|
Post by skyship on Nov 10, 2012 18:09:23 GMT -5
Metazoan cells? Intermediate filaments (IFs) are cytoskeletal components found in metazoan cells. " Intermediate filament organization in metazoan cells In the hypothetical epithelial cell depicted, the three key filament systems of the cytoskeleton, microfilaments (MFs), microtubules (MTs) and intermediate filaments (IFs), are connected to each other by dimeric complexes of plakin-type molecules such as plectin and BPAG1. In addition, a multitude of MT-associated proteins and actin-binding proteins, including motor proteins, are thought to increase the complexity of these interactions. IFs are coupled to IF-anchoring plaques of cell–cell junctions (desmosomes) by desmoplakin, a prototype plaque molecule (plakin), and to those of cell–matrix junctions (hemidesmosomes) by plectin and BPAG1. The transmembrane proteins that mediate the contact with the neighbouring cells and with the extracellular matrix (ECM) are desmosomal cadherins and integrins, respectively. IFs are furthermore coupled to the outer nuclear membrane (ONM) by plectin and nesprin-3, whereas nesprin-2 anchors the MF system to the nucleus. On the inner side of the nuclear envelope, a layer of nuclear IF proteins (lamins) is attached to pores and inner nuclear membrane (INM) proteins as well as to chromatin. The membrane proteins of the INM might be linked to those of the ONM and thereby provide a mechanical continuum reaching from the ECM to chromatin. The number of newly identified INM and ONM proteins is increasing steadily and is represented here only in a schematic manner. ER, endoplasmic reticulum; MTOC, microtubule-organizing centre; NPC, nuclear pore complex.FROM THE FOLLOWING ARTICLE: Intermediate filaments: from cell architecture to nanomechanics Harald Herrmann, Harald Bär, Laurent Kreplak, Sergei V. Strelkov & Ueli Aebi Nature Reviews Molecular Cell Biology 8, 562-573 (July 2007) doi:10.1038/nrm2197 '' php.med.unsw.edu.au/cellbiology/images/2/23/Intermediate_filament_organization_cartoon.jpgphp.med.unsw.edu.au/cellbiology/index.php?title=File:Intermediate_filament_organization_cartoon.jpgvimentin? php.med.unsw.edu.au/cellbiology/index.php?title=File:IF-vimentin-cartoon.jpgIF Desmin mutants: from metazoan cells? ? php.med.unsw.edu.au/cellbiology/index.php?title=File:IF_desmin_mutants.jpgMonomer.....dimer......tetramer........... form organic to nano? en.wikipedia.org/w/index.php?title=File:Intermediate_filament.svg&page=1en.wikipedia.org/wiki/Intermediate_filamentWhere do the Metazoan cells come from?
|
|
|
Post by skyship on Nov 10, 2012 18:10:41 GMT -5
What Metazoan cells are used? all kinds of types exist: Types I and II - Acidic and Basic Keratins keratin intermediate filaments (stained red) For more details on this topic, see cytokeratin. These proteins are the most diverse among IFs and constitute type I (acidic) and type II (basic) IF proteins. The many isoforms are divided in two groups: epithelial keratins (about 20) in epithelial cells (image to right) trichocytic keratins (about 13) (hair keratins), which make up hair, nails, horns and reptilian scales.Regardless of the group, keratins are either acidic or basic. Acidic and basic keratins bind each other to form acidic-basic heterodimers and these heterodimers then associate to make a keratin filament.Type III There are four proteins classed as type III IF proteins, which may form homo- or heteropolymeric proteins. Desmin IFs are structural components of the sarcomeres in muscle cells. GFAP (glial fibrillary acidic protein) is found in astrocytes and other glia. Peripherin found in peripheral neurons. Vimentin, the most widely distributed of all IF proteins, can be found in fibroblasts, leukocytes, and blood vessel endothelial cells. They support the cellular membranes, keep some organelles in a fixed place within the cytoplasm, and transmit membrane receptor signals to the nucleus. Type IV α-Internexin Neurofilaments - the type IV family of intermediate filaments that is found in high concentrations along the axons of vertebrate neurons. Synemin Syncoilin Type V - Nuclear Lamins Lamins Lamins are fibrous proteins having structural function in the cell nucleus. I n metazoan cells, there are A and B type lamins, which differ in their length and pI. Human cells have three differentially regulated genes. B-type lamins are present in every cell. B type lamins, B1 and B2, are expressed from the LMNB1 and LMNB2 genes on 5q23 and 19q13, respectively. A-type lamins are only expressed following gastrulation. Lamin A and C are the most common A-type lamins and are splice variants of the LMNA gene found at 1q21. These proteins localize to two regions of the nuclear compartment, the nuclear lamina—a proteinaceous structure layer subjacent to the inner surface of the nuclear envelope and throughout the nucleoplasm in the nucleoplasmic "veil".Comparison of the lamins to vertebrate cytoskeletal IFs shows that lamins have an extra 42 residues (six heptads) within coil 1b. The c-terminal tail domain contains a nuclear localization signal (NLS), an Ig-fold-like domain, and in most cases a carboxy-terminal CaaX box that is isoprenylated and carboxymethylated (lamin C does not have a CAAX box). Lamin A is further processed to remove the last 15 amino acids and its farnesylated cysteine. During mitosis, lamins are phosphorylated by MPF, which drives the disassembly of the lamina and the nuclear envelope. Type VI Nestin[12] Unclassified Beaded Filaments-- Filensin, Phakininl en.wikipedia.org/wiki/Intermediate_filament
|
|
|
Post by skyship on Nov 10, 2012 18:18:39 GMT -5
metazoan cells come from nematodes, molluscs etc.
which ones were used for human IFAP?
|
|
|
Post by skyship on Nov 10, 2012 21:14:45 GMT -5
Wonder what these are? Okay so 1968, they found the Intermediate filaments? Synemin Syncoilin and these? Beaded Filaments-- Filensin, Phakininl and Extracellular Matrix 2Basal Lamina Introduction This second lecture on ECM will cover the glycoprotein components of ECM and specialized epithelial ECM. Finally I will discuss some key experiments exploring the role and function of the ECM of epitheilia (basement membrane) and connective tissues. With the epithelial ECM the term "basement membrane" is used with light microscopy and "basal lamina" is used with electron microscopy. Archive Objectives Understanding of the localisation and origin of extracellular matrix Understanding of the 3 major components fibers, proteoglycans (matrix), adhesive lycoproteins Broad understanding of structure and function fibronectin laminin basement membrane Broad understanding of some key extracellular matrix experiments History Below are some example historical research finding related to cell junctions from the JCB Archive. 1978 Basal lamina instructs innervation Joshua Sanes and Jack McMahan show that regenerating nerve axons take their cues for new synapse formation from the extracellular matrix (ECM) of muscle cells and not from the muscle cells themselves. ".." Fibronectin Structure dimer connected at C-terminus Mr 550 kDa nearly identical subunits composed of types I (F1), II (F2), and III (F3) fibronectin modules S-S linkages rigid and flexible domains fibronectin fibrils have elastic properties and can stretch fibrils up to four-fold their relaxed length. fibrillogenesis - transformation from the compact (soluble) form to the extended fibrillar (insoluble) form of fibronectin, requires application of mechanical forces generated by cells. "Notice the monomer is soluble, but the other is not. Fibronectin Function Fibronectin (fl) soluble protein in blood plasma (200–250 kDa monomer) blood clotting process, link to fibrin insoluble protein in extracellular matrix (ECM) ECM fibronectin differs from plasma fibronectin by the presence of additional polypeptide segments and in altering morphology of transformed cells and hemagglutination. Additional polypeptide segments which alters morphology of transformed cells ......Okay, below tells us what this extracellular II does. it is an extra system in the Cytoskeletal cells, as I have mentioned many years ago. =========== " ECM ReorganisationReorganisation can occur through proteolytic degradation changes to ECM proteins (collagen, laminin, and fibronectin). Their activity can be regulated locally by inhibitors. The proteases form 2 main classes:Matrix Metalloproteases (MMPs) dependent upon bound Ca2+ or Zn2+ for activity. family of enzymes MMP-2 (Gelatinase A, 72 kDa type IV collagenase) is the most widely distributed collagenases can specifically cleave proteins at a small number of sites. inhibited by tissue inhibitors of metalloproteases (TIMPs). MMP-2 appears to be associated with early breast carcinoma and cervical neoplasia Serine Proteases have a highly reactive serine in their active site. inhibited by serpins. role in metastasis Links: SOMS Ocular Immunology Group | Expression of MMPs and TIMPs in breast tumours ECM Scaffold - Tissue Engineering “Decellularized tissues and organs have been successfully used in a variety of tissue engineering/regenerative medicine applications, … Each of these treatments affect the biochemical composition, tissue ultrastructure, and mechanical behavior of the remaining extracellular matrix (ECM) scaffold, which in turn, affect the host response to the material.”
Reference: Decellularization of tissues and organs. Biomaterials. 2006 Jul;27(19):3675-83. Epub 2006 Mar 7. ' php.med.unsw.edu.au/cellbiology/index.php?title=Extracellular_Matrix_2=========================== It is the Neuromuscular junction where damage is occurring, These bundles are accumulating there, and they adhere there, sticking their noses where they do not belong.So, this extracellular matrix II is the one we are after, it is insoluble. Does not dissolve, but travels around in ECM.================= so, what is this made of this polypeptide that does not dissolve? very complicated..... php.med.unsw.edu.au/cellbiology/index.php?title=Extracellular_Matrix_2
|
|
|
Post by skyship on Nov 10, 2012 21:45:07 GMT -5
Pancreas cell desmosome: php.med.unsw.edu.au/cellbiology/index.php?title=File:5pancreas.jpg============================ Are these the filaments that wrapped around Karen's pancreas in the ECM II? could be...these cause breast and other cancers as well. So, the MMPs and TIMPs from Proteases, the new proteins in the non coding RNA? probably!==============
"The proteases form 2 main classes:
Matrix Metalloproteases (MMPs)dependent upon bound Ca2+ or Zn2+ for activity. family of enzymes MMP-2 (Gelatinase A, 72 kDa type IV collagenase) is the most widely distributed collagenases can specifically cleave proteins at a small number of sites. inhibited by tissue inhibitors of metalloproteases (TIMPs). MMP-2 appears to be associated with early breast carcinoma and cervical neoplasia Serine Proteases have a highly reactive serine in their active site. inhibited by serpins. role in metastasis " Extracellular matrix II php.med.unsw.edu.au/cellbiology/index.php?title=Extracellular_Matrix_2en.wikipedia.org/wiki/Extracellular_matrix========================= Somewhere between these two we can find the integration of the "special ECM proteins".............. MMP2? definition:===========
|
|
|
Post by skyship on Nov 10, 2012 23:30:21 GMT -5
MMP2 definition: "What is the official name of the MMP2 gene? The official name of this gene is “matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase).” MMP2 is the gene's official symbol. The MMP2 gene is also known by other names, listed bel" What is the normal function of the MMP2 gene? From Entrez GeneThis link leads to a site outside Genetics Home Reference.: Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes an enzyme which degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. Mutations in this gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] From UniProtThis link leads to a site outside Genetics Home Reference.: Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro.PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels. How are changes in the MMP2 gene related to health conditions? UniProtThis link leads to a site outside Genetics Home Reference. provides the following information about the MMP2 gene's known or predicted involvement in human disease. Defects in MMP2 are the cause of Torg-Winchester syndrome (TWS)[1]This link leads to a site outside Genetics Home Reference.; also known as multicentric osteolysis nodulosis and arthropathy (MONA). TWS is an autosomal recessive osteolysis syndrome. It is severe with generalized osteolysis and osteopenia. Subcutaneous nodules are usually absent. Torg-Winchester syndrome has been associated with a number of additional features including coarse face, corneal opacities, patches of thickened, hyperpigmented skin, hypertrichosis and gum hypertrophy. However, these features are not always present and have occasionally been observed in other osteolysis syndromes. Entrez GeneThis link leads to a site outside Genetics Home Reference. lists the following diseases or traits (phenotypes) known or believed to be associated with changes in the MMP2 gene. Torg Winchester syndrome[1]This link leads to a site outside Genetics Home Reference. UniProt and Entrez Gene cite these articles in OMIM, a catalog designed for genetics professionals and researchers that provides detailed information about genetic conditions and genes. Article Number Main Topic [1] 259600This link leads to a site outside Genetics Home Reference. TORG-WINCHESTER SYNDROME 120360This link leads to a site outside Genetics Home Reference. MATRIX METALLOPROTEINASE 2 Where is the MMP2 gene located? Cytogenetic Location: 16q13-q21 Molecular Location on chromosome 16: base pairs 55,513,080 to 55,540,585 ...........more here: ghr.nlm.nih.gov/gene/MMP2If MMP2 causes neoplasms, then that causes many issues similar to Morgellons?
|
|
|
Post by skyship on Nov 11, 2012 0:20:40 GMT -5
What the heck does this mean? "matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase).” gelatinase A Type IV collagenase?============================== Gelatinase:"gelatinase is a proteolytic enzyme that allows a living organism to hydrolyse gelatin[1] into its sub-compounds (polypeptides, peptides, and amino acids) that can cross the cell membrane and be used by the organism. It is not a pepsin. Forms of gelatinases are expressed in several bacteria including Pseudomonas aeruginosa and Serratia marcescens. In humans, the gelatinases are matrix metalloproteinases MMP2 and MMP9.".en.wikipedia.org/wiki/Gelatinase========================== ========= Gelatinase A: Remember when glue came from horse hooves?"http://www.laminitisresearch.org/downloads/chrispollitt_MungallPollittCollins1998.pdf How did it become pathogenic? Disease called "Laminitis"....... how relates to humans?================================ " Our results indicate that MMPs, mainly MMP9, play a role in the release of biologically active VEGF and consequently in the formation of ascites. "......... cancerres.aacrjournals.org/content/63/17/5224.full=========== So, if Dr. Fry says this is vegetative, could it be this that causes the Cancers? VEGF?? Causes diabetes.eurekamag.com/keyphrase/h/164/hybridization-vegf.php#.UJ8vGGdWpSo================================= How many diseases does it create?............================= "VEGF in diseaseVEGFxxx has been implicated with poor prognosis in breast cancer. Numerous studies show a decreased overall survival and disease-free survival in those tumors overexpressing VEGF. The overexpression of VEGFxxx may be an early step in the process of metastasis, a step that is involved in the "angiogenic" switch. Although VEGFxxx has been correlated with poor survival, its exact mechanism of action in the progression of tumors remains unclear. VEGFxxx is also released in rheumatoid arthritis in response to TNF-α, increasing endothelial permeability and swelling and also stimulating angiogenesis (formation of capillaries). VEGFxxx is also important in diabetic retinopathy (DR). The microcirculatory problems in the retina of people with diabetes can cause retinal ischaemia, which results in the release of VEGFxxx, and a switch in the balance of pro-angiogenic VEGFxxx isoforms over the normally expressed VEGFxxxb isoforms. VEGFxxx may then cause the creation of new blood vessels in the retina and elsewhere in the eye, heralding changes that may threaten the sight.VEGFxxx plays a role in the disease pathology of the wet form age-related macular degeneration (AMD), which is the leading cause of blindness for the elderly of the industrialized world. The vascular pathology of AMD shares certain similarities with diabetic retinopathy, although the cause of disease and the typical source of neovascularization differs between the two diseases. VEGF-D serum levels are significantly elevated in patients with angiosarcoma.[6] Once released, VEGFxxx may elicit several responses. It may cause a cell to survive, move, or further differentiate. Hence, VEGF is a potential target for the treatment of cancer. The first anti-VEGF drug, a monoclonal antibody named bevacizumab, was approved in 2004. Approximately 10-15% of patients benefit from bevacizumab therapy; however, biomarkers for bevacizumab efficacy are not yet known. Current studies show that VEGFs are not the only promoters of angiogenesis. In particular FGF2 and HGF are potent angiogenic factors.Patients suffering from pulmonary emphysema have been found to have decreased levels of VEGF in the pulmonary arteries. In the kidney, increased expression of VEGFxxx in glomeruli directly causes the glomerular hypertrophy that is associated with proteinuria.[7] VEGF alterations can be predictive of early-onset pre-eclampsia.[8]"........ en.wikipedia.org/wiki/Vascular_endothelial_growth_factor======== OKay, so what is it made of?
here are 3 isoforms........========================= "Three VEGFR isoforms have been identified in humans: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1) and VEGFR-3 (Flt-4) "........www.tocris.com/pharmacologicalBrowser.php?ItemId=187901&Information=True&Pathway=vegf&PathwayTitle=VEGF#.UJ8x32dWpSoThey are called Mitogens...............
|
|
|
Post by skyship on Nov 11, 2012 0:31:09 GMT -5
Mitogens.
"A mitogen is a chemical substance that encourages a cell to commence cell division, triggering mitosis. A mitogen is usually some form of a protein.Mitogenesis is the induction (triggering) of mitosis, typically via a mitogen. Mitogens trigger signal transduction pathways in which mitogen-activated protein kinase (MAPK) is involved, leading to mitosis." Lipopolysaccharide toxin from gram-negative bacteria is thymus-independent. They may directly activate B cells, regardless of their antigenic specificity.Plasma cells are terminally [[Cellular differentiation|] and, therefore, cannot undergo mitosis. Memory B cells can proliferate to produce more memory cells or plasma B cells. This is how the mitogen works, that is, by inducing mitosis in memory B cells to cause them to divide, with some becoming plasma cells. en.wikipedia.org/wiki/Mitogen====================== We are back to the poisonous plant: I destroyed mine!========================== "Parts of this plant are highly toxic to livestock and humans, and it is considered a major pest by farmers. Nonetheless, some parts can be used as food, medicine or poison."....... en.wikipedia.org/wiki/Phytolacca_americana========================= so, what gram negative bacteria is this derived from? other than the poisonous protein from the pokeweed? ================ Mitogens in human physiology Insulin-like Growth Factor 1 mediates the major growth-promoting effect of Human Growth Hormone as a paracrine agent at growth plates in the skeletal system. another example for mitogen agent is G-CSF. =========== What is mitogen agent G-CSF?
|
|
|
Post by skyship on Nov 11, 2012 1:01:14 GMT -5
Wait a minute........... History and phylogeny of intermediate filaments: Now in insectsreally? .. ......"From hair to nuclear organizationBiological specimens enriched in intermediate filament (IF) proteins were among the first to be placed into an x-ray beam for structural analysis, back in the 1930s by William Astbury. He used hair, in its non-stretched and stretched form, rightly deducing that such extended, stable and flexible rods are made from highly ordered proteins. However, it took the thesis work of a graduate student several years later to explain fully these first, surprisingly simple diffraction patterns. The student was Francis Crick. He realized that the keratin α-helices in hair are packed as “simple coiled coils”, remarking later, in his 1988 autobiography, that at that time “helices were in the air”. This excitement was partly due to the discovery of the α-helical fold by Linus Pauling and his group as a fundamental structural principle embodied in the muscle proteins myosin and tropomyosin; and in the years that followed, more α-helix-rich proteins were discovered and grouped together as fibrous proteins. Years later the excitement of biochemists was gone. The second edition of classical textbook Biological Chemistry by Mahler and Cordes (1971) lists them simply under scleroproteins together with collagen and gelatin, without further mention. "................ This scenario changed when in 1968 the group of Howard Holtzer discovered IFs as a further independent filament system in cells obtained from chicken muscle in addition to the well established actin and myosin filaments, highly abundant in myocytes. By conventional electron microscopy, the diameter of these new filaments was determined to be intermediate between that of actin and myosin filaments, hence intermediate filaments or 10-nm filaments (see [1]). Within the next 10 years these new filaments were found in all vertebrate tissues and cultured cell lines investigated, and in many other animals too; and subsequently, the massive DNA sequencing efforts of the 1980s produced two major insights into this protein class. First, IF proteins from various tissues all exhibit a conserved central α-helical rod domain, organized so that two chains can form a parallel in-register coiled coil (Figure 1; [1]]), and which is flanked by non-α-helical domains of very different character and size. Second, they are only found in metazoan species and appear to be absent from plants and fungi. It came as a great surprise when the cell nucleus was found to contain fibrillar substructures - the nuclear lamina - composed of specialized IF proteins, the lamins. As so often in science, these entities, discovered last, turned out to be the evolutionary ancestors of the whole intermediate filament multigene family. Simple metazoans such as Hydra attenuata were found to express at least nuclear IF proteins, and a comparative analysis of their lamin sequences and the other known lamin and IF protein sequences led to the conclusion that IFs originated in an ur-lamin [2]. The simple invertebrate Caenorhabditis elegans, which has a single nuclear lamin, also harbors eleven genes coding for cytoplasmic IF proteins, four of which have been demonstrated to be essential for viability [3]; but the fruit fly Drosophila melanogaster, which expresses the two nuclear lamins - lamin A and lamin B - characteristic of mammalian species, does not exhibit any cytoplasmic IF protein. T his led to the conclusion that insects lack cytoplasmic IFs - a conclusion that is now challenged by Mencarelli et al. [4], who detected abundant cytoplasmic structures in the mid-gut cells of the hexapod Isotomurus maculatus (commonly known as the springtail), and have isolated the protein, cloned the DNA from the deduced sequence, compared the sequence with those of known IFs, reassembled filaments from the expressed protein in vitro, and conclude that the protein, which they call isomin, is an intermediate filament protein. ......"What makes a bona fide intermediate filament?Coiled-coil forming parts within protein sequences can be identified relatively easily by looking for heptad repeats - amino-acid sequence motifs that, first, allow the formation of an α-helix and second, have apolar residues periodically at positions a and d within the seven amino-acid repeat (abcdefg)n. It is the long-range regular disposition of hydrophobic residues that forces two α-helices into a superhelix, that is, a coiled-coil dimer, and their hydrophobic character also determines the strength of the interaction of the α-helices within the coiled coil [7]. Charged amino acids within the coiled coil serve as ‘trigger motifs’, essential for dimerization.
Why dimers are important in this new found IF.................. insects too? ======= So what about isomin?We would suggest that isomin may have a distinct tissue-specific role in Isotomurus that is not necessarily restricted to generating structural order and support. For this reason, its sequence may have drifted away from the standard IF pattern, especially if isomin is in fact a ‘co-assembler’ analogous to other IF proteins such as synemin, nestin or the high molecular weight neurofilament triplet protein, with a hitherto unrecognized partner. It seems possible from this case that Isotomurus may harbor more IF proteins, unrecognized until now, and isomin may herald the discovery of much greater IF complexity in hexapoda. www.biomedcentral.com/1741-7007/9/16==========
|
|
|
Post by skyship on Nov 11, 2012 1:17:26 GMT -5
It appears that IFs are quite primary, then.
Intermediate filaments: primary determinants of cell architecture and plasticity Was it desmin mutants that caused these new diseases???Intermediate filaments: primary determinants of cell architecture and plasticity "Mutations in the genes encoding the epidermal K5 and K14 were the first to be identified to cause disease (reviewed in refs. 50–52). In the basal cell layer of the epidermis, the mutated keratin filaments aggregate heavily and lose their normal connection to desmosomes and hemidesmosomes. Hence, these mutations in K5 and K14 interfere with the proper generation of a functional cytoskeleton and, as a consequence, with the stress-absorbing functions of IFs. Both the loss of normal connection to desmosomes and hemidesmosomes and the defect in stress-absorption are evidently central to the tissue fragility observed in individuals carrying these mutations in K5 and K14, although other processes, such as signaling and protein turnover, may well be affected and contribute to the pathophysiology (95). As a consequence, the skin of people born with defective K14 is highly fragile (103). One of the most recent examples of mutations in IF protein–encoding genes that contribute to tissue malfunction relates to the eye lens: a mutation in coil 1B of vimentin, Glu151Lys, has recently been demonstrated to underlie the formation of cataract (104). This glutamic acid is absolutely conserved in vimentins from sharks to humans, and its change to lysine results in a strong kinetic in vitro assembly defect without, however, having a gross effect on the morphology of the mature IF (104). Desmin mutations affect IF assembly. The muscle-specific IF protein desmin is, in evolutionary terms, rather old, as highly conserved homologs are found in muscle cells from the invertebrate Styela to mammals including humans (49, 105). Moreover, all these desmins, including the Styela protein, follow the ULF-type assembly pathway, as demonstrated by in vitro studies with recombinant proteins (27). This conserved assembly behavior indicates that structural and functional aspects coevolved early on, even before vertebrate development started. The first disease-associated mutation in the human desmin-encoding gene was identified about ten years ago (106). Analysis of the effects of the mutation, which led to a deletion of seven amino acids in coil 1B, demonstrated that it compromised desmin IF assembly both in vitro and in transfected cells. This observation provided a molecular explanation for the huge sarcoplasmic desmin aggregates found in patient muscle and the concomitant severe disturbance in the ordered parallel alignment of sarcomeres within individual myofibers. Interestingly, at about the same time, a mutation in the gene encoding a small heat shock protein known as αB-crystallin was identified and found to cause a desmin-related myopathy, pointing to a direct functional relationship between desmin networks and these chaperone proteins (107). Ever since, more than 40 desmin disease-associated mutations have been described, and a recent survey of patients with a dilated cardiomyopathy phenotype has revealed desmin to be quite frequently mutated, in approximately 1%–2% of these patients (108). "............. I think these desmin mutants are what was introduced into the IFs."As the first reported desmin mutant, introduced in the previous paragraph (106), was unable to form regular IFs in vitro but only short irregular filaments, it was of interest to see whether all desmin disease-associated mutations would impair its ability to assemble into bona fide IFs. As expected, with the study of a larger number of desmin disease-associated mutants, a more complex picture emerged: about half of the mutant desmins were able to form extended filaments, whereas the others deviated from the normal assembly pathway at distinct stages by forming various non-IF structures (109, 110). Most interestingly, the patient mutations taught structural biologists an important lesson: the introduction of a proline into a central position of the coiled coil does not necessarily impede the ordered organization of the tetramer, ULF, or even the filament. The A360P mutation, which is situated in an a position of the heptad pattern, introduces a change from the typical coiled coil–mediating amino acid alanine to proline, which is supposed to be a “helix breaker.” Its occurrence in a coiled coil is therefore highly unusual but, remarkably enough, long regular filaments still formed (Figure 6A). As a result of the mutation, however, the A360P mutant IFs exhibit a diameter of 14.5 nm as compared with 12.6 nm for wild-type desmin IFs, and correspondingly harbor 56 subunits per IF cross-section instead of 48, as determined by mass measurements using scanning transmission electron microscopy (110). Furthermore, the extended filaments observed after 1 hour of in vitro assembly exhibit alterations in their networking ability, indicating a defect in their higher order organization (110). Among the mutants in the second group, which are unable to form extended filaments, some (such as R406W) still associate into regular ULF-like structures. Hence, it is their ability to longitudinally anneal that is affected (Figure 6B). In the case of R406W, the inter-helical salt bridge formed by the highly conserved aspartate and arginine residues at the end of coil 2B (residues 401 and 406, respectively, in human desmin) is destroyed as a consequence of the mutation (Figure 6C). Some mutant desmins form short IFs that eventually convert into sheet-like assemblies, whereas others convert into small ball-like aggregates (109). These mutants deviate from the normal desmin assembly pathway at distinct steps, indicating they are unable to perform the appropriate subunit reorganizations needed to reach the next assembly stage. Interestingly, mutations located very close to one another within the molecule can give rise to entirely different in vitro assembly phenotypes. "...... www.jci.org/articles/view/38214 This is long but, does get into how the IFs is where the mutants came in, creating all kinds of human syndromes and effects.
|
|
|
Post by skyship on Nov 11, 2012 1:50:04 GMT -5
So was this new multicell made from metazoan proteins from IFs of metazoans and if so which ones, this could help determine the Protomyxzoa............. So are we looking at metazoan cells? and the proto would be the blueprint model? Model of mixed zoans............ there we go........ Again: lets look at this: and related references........." AbstractIntermediate filaments (IFs) are major constituents of the cytoskeleton and nuclear boundary in animal cells. They are of prime importance for the functional organization of structural elements. Depending on the cell type, morphologically similar but biochemically distinct proteins form highly viscoelastic filament networks with multiple nanomechanical functions. Besides their primary role in cell plasticity and their established function as cellular stress absorbers, recently discovered gene defects have elucidated that structural alterations of IFs can affect their involvement both in signaling and in controlling gene regulatory networks. ........
Seems like the "alterations" could not handle the IFs in "signalling and controlling the gene ...... networks"....... references:Related research Intermediate filaments: a role in epithelial polarity. Andrea S Oriolo, Flavia A Wald, Victoria P Ramsauer, Pedro J I Salas in Experimental Cell Research (2007) Save reference to library · Related research 19 readers The membranome and membrane heredity in development and evolution Thomas Cavalier-Smith in An Evolutionary Synthesis in the Age of Genomics (2004) Cell evolution and Earth history: stasis and revolution Thomas Cavalier-Smith in Philosophical Transactions of the Royal Society of London - Series B: Biological Sciences (2006) Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus. Ning Wang, Jessica D Tytell, Donald E Ingber in Nature Reviews Molecular Cell Biology (2009) Geometric control of tissue morphogenesis. Celeste M Nelson in Biochimica et Biophysica Acta (2009) www.mendeley.com/research/intermediate-filaments-primary-determinants-cell-architecture-plasticity/ Wasn't it the TT who said that this involved tissue morphogenesis or tissue engineering?Okay, if we can find the multicellular progeny of the IFs then we can find the filament producers. not in fungi or ?....... but in Metazoans.
|
|
|
Post by skyship on Nov 11, 2012 2:17:03 GMT -5
WE are as close as we are ever going to get to Dr. Fry's Protomyxozoa............... Holy....Holy.....Holy......
Remember Skizit and Nicole King? okay then........Choanoflagellate are the closest to human multicell....... ======= MAPK cascades in the choanoflagellate, Monosiga brevicollis MAP Kinase (MAPK) cascades are an almost universal eukaryotic signaling pathway, of critical importance to growth and stress responses. Humans have several such parallel pathways, which emerged from a single common ancestor. Now, using the genome of Monosiga brevicollis, one of the closest unicellular relatives of the animal kingdom, we see some of the early steps in the evolution of multiple MAPK cascades, including some surprises.MAPK signaling The typical MAPK cascade consists of a MAPK kinase such as Erk, Jnk or p38, which is activated by phosphorylation from an upstream kinase called MAP2K, MEK or Ste7. This in turn is phosphorylated and activated by a MAP3K (MEKK, MKK, Ste11), and that sometimes by a MAP4K (Ste20 family). Erk MAPKs largely transduce growth signals downstream from receptor tyrosine kinases and other extracellular signals, while Jnk and p38 MAPKs respond to various stresses.Most animals have p38 and Jnk pathways, and several variants of the Erk pathway, and there is some cross-talk between the different pathway genes. In fungi, there is one main Erk-like pathway, and some poorly classified related genes, so we looked at the Monosiga genome to see if we could find an intermediate state, where maybe some of these pathways had emerged, but not all of them. This was done in collaboration with Matthew Good from the Lim lab at UCSF, and coordinated by Nicole King of UC Berkeley. The results were published as part of the Monosiga genome paper in 2008. The genome of the choanoflagellate Monosiga brevicollis and the origins of metazoan multicellularity. King, N, Westbrook, MJ, Young, SL, Kuo, A, Abedin, M, Chapman, J, Fairclough, S, Hellsten, U, Isogai, Y, Letunic, I, Marr, M, Pincus, D, Putman, N, Rokas, A, Wright, KJ, Zuzow, R, Dirks, W, Good, M, Goodstein, D, Lemons, D, Li, W, Lyos, J, Morris, A, Nichols, S, Richter, DJ, Salamov, A, JGI Sequencing, Bork, P, Lim, WA, Manning, G, Miller, WT, McGinnis, W, Shapiro, H, Tijan, R, Grigoriev, IV, Rokhsar, D. Nature 451, 783-788 (Medline, PDF) Monosiga does indeed have an intermediate MAPK system between that of fungi and metazoans. A clear Erk pathway is found (MKK1 -> MEK1 -> Erk), and, surprisingly, a complete Erk5 cascade is also present (MEKK2 -> MKK4 -> Erk5). Up to recently, this was thought to be vertebrate-specific, since these genes are absent from Drosophila and C. elegans, but now are found in the sea urchin and the sea anemone, Nematostella, to which Monosiga now extends it further. This cascade is not well studies, but in mammals it is primarily activated by stress stimuli, and can also be activated by traditional Erk stimuli such as nerve growth factor (NGF) and Erk5 can also be directly activated by PI3 Kinase downstream of the insulin receptor. kinase.com/monosiga/mapk.htmlSo the sea urchin, sea aneme and nematostella. link to human kinase: kinase.com/monosiga/Mbre_genome_Table_S9.pdf
|
|
|
Post by skyship on Nov 11, 2012 3:29:26 GMT -5
When real med history is available, one finds many things.Where the Isomin came from:================ Isomin: a novel cytoplasmic intermediate filament protein from an arthropod speciesMencarelli C, Ciolfi S, Caroti D, Lupetti P, Dallai R - BMC Biol. (2011) Bottom Line: Only lamins, the nuclear IF proteins, have so far been identified in the model organisms analysed; on this basis, it has been considered that arthropods do not express cytoplasmic IFs.Here, we report the first evidence for the expression of a cytoplasmic IF protein in an arthropod - the basal hexapod Isotomurus maculatus.Sequence analysis indicates that isomin is mostly related to the Intermediate Filament protein C (IFC) subfamily of Caenorhabditis elegans IF proteins, which are molecular constituents of the nematode intestinal terminal web.Interestingly, the coil 1a domain of isomin appears to have been influenced by a substantial molecular drift and only the aminoterminal part of this domain, containing the so-called helix initiation motif, has been conserved.Our results set a new basis for the analysis of IF protein evolution during arthropod phylogenyMentions: Collembolan species belonging to the genus Isotomurus express, in their midgut epithelium, a peculiar terminal web- consisting of a dense belt-like layer of closely intertwined filaments of about 8-10 nm in diameter, which crosses the apical cytoplasm and contacts laterally the membrane at the septate junction level where filaments adhere to and reinforce the cytoplasmic face of the junction (Figure 1a and 1b). This cytoskeletal array appears to act as an anchoring structure for the microfilament bundles descending from microvilli and segregates the cytoplasm into an apical and a basal region that are structurally distinct, the latter containing most part of the cellular organelles. The web is not continuous but shows several fenestrations which appear to be somehow reinforced at their edges (Figure 1a and 1b). openi.nlm.nih.gov/detailedresult.php?img=3065449_1741-7007-9-17-1&query=the&fields=all&favor=none&it=none&sub=none&uniq=0&sp=none&req=4&simCollection=1976895_brjcancer00108-0048-a&npos=89&prt=3Maybe not the collembolan but the IF from the collembolan? openi.nlm.nih.gov/detailedresult.php?img=3065449_1741-7007-9-17-1&query=the&fields=all&favor=none&it=none&sub=none&uniq=0&sp=none&req=4&simCollection=1976895_brjcancer00108-0048-a&npos=89&prt=3
|
|
|
Post by skyship on Nov 11, 2012 3:48:12 GMT -5
Finally found something that forms Polimers.............Isomin.......from yup......the collembola. Now on molecular basis. The Isomin molecule. It can form filaments........ "Isomin is able to form filaments in vitroA hallmark feature of IF proteins is their capability to renature after solubilization by urea treatment and to undergo a spontaneous re-assembly process in appropriate conditions. Thus, we preliminarily tested the capability of recombinant isomin to assemble in vitro into filaments, using the standard re-assembly conditions described for other IF proteins [24]. Following this protocol, we observed the formation of morphologically distinct filaments (Figure (Figure4a);4a); parallel electrophoretic analysis showed them to consist essentially of the 40 kDa isomin band (Figure (Figure4b).4b). Most reconstituted filaments were about 9-12 nm in diameter but some unwoven filaments also occurred, revealing the presence of thinner, 2-4 nm protofilaments (see arrowheads in Figure Figure4a,4a, inset). The in-vitro formation of such 'loose' filaments could result from suboptimal reassembly conditions. The requirement for peculiar reassembly conditions might be related to the unusual structure of the isomin molecule, which is characterized by an extremely short head domain and by a modified coil 1a segment. In addition, we do not know whether, in vivo, isomin forms homopolimers or is, instead, part of a heteropolimeric IF system, requiring a partner to correctly assemble into stable filament...............Isomin filament image: europepmc.org/articles/PMC3065449?figure=F4/europepmc.org/articles/PMC3065449So, does IF protein from this particular collembola create the 'vimentin filaments we are finding, if that is what they are? Seems to create a web of sorts, just the protein.
|
|
|
Post by skyship on Nov 11, 2012 4:17:33 GMT -5
Evidence of IF diseases: Keywords: database; intermediate filament; keratin; desmin; lamin; GFAP; neurofilament; epidermolysis bullosa; laminopathy Abstract We describe a revised and expanded database on human intermediate filament proteins, a major component of the eukaryotic cytoskeleton. The family of 70 intermediate filament genes (including those encoding keratins, desmins, and lamins) is now known to be associated with a wide range of diverse diseases, at least 72 distinct human pathologies, including skin blistering, muscular dystrophy, cardiomyopathy, premature aging syndromes, neurodegenerative disorders, and cataract. To date, the database catalogs 1,274 manually-curated pathogenic sequence variants and 170 allelic variants in intermediate filament genes from over 459 peer-reviewed research articles. Unrelated cases were collected from all of the six sequence homology groups and the sequence variations were described at cDNA and protein levels with links to the related diseases and reference articles. The mutations and polymorphisms are presented in parallel with data on protein structure, gene, and chromosomal location and basic information on associated diseases. Detailed statistics relating to the variants records in the database are displayed by homology group, mutation type, affected domain, associated diseases, and nucleic and amino acid substitutions. Multiple sequence alignment algorithms can be run from queries to determine DNA or protein sequence conservation. Literature sources can be interrogated within the database and external links are provided to public databases. The database is freely and publicly accessible online at www.interfil.org (last accessed 13 September 2007). Users can query the database by various keywords and the search results can be downloaded. It is anticipated that the Human Intermediate Filament Database (HIFD) will provide a useful resource to study human genome variations for basic scientists, clinicians, and students alike. Hum Mutat 29(3), 351–360, 2008. © 2007 Wiley-Liss, Inc. The Human Intermediate Filament Database: comprehensive information on a gene family involved in many human diseases† onlinelibrary.wiley.com/doi/10.1002/humu.20652/abstract
|
|
|
Post by skyship on Nov 11, 2012 4:25:07 GMT -5
the eukaryotic cytoskeleton: Invasion of Eukaryotic cells into Human cytoskeleton............ The reorganization of the Cytoskelton. www.bms.ed.ac.uk/research/others/smaciver/Bacteria%20Inv.htmmore later............. we are back where we were a few years back in this and the collembola protein rears its little head again, and so does the cytoskeletal cell, filled with all kinds of things.
|
|
|
Post by lilsissy on Nov 12, 2012 11:55:55 GMT -5
Fibro is this the same muscle casing that is diseased in fibro, sky said, It is the Neuromuscular junction where damage is occurring, These bundles are accumulating there, and they adhere there, sticking their noses where they do not belong. So, this extracellular matrix II is the one we are after, it is insoluble. Does not dissolve, but travels around in ECM. en cut, then the lymh nodes can not carry off the waste products. Uploaded with ImageShack.uswww.etoims.com/blogs/?p=196In neuromuscular pain such as fibromyalgia the mediate cause of pain is muscle shortening and/or spasm under the control of neuromuscular junctions or trigger points. This muscle shortening and/or spasm results in focal ischemia (lack of blood supply) to intramuscular nerves and blood vessels and also produce a traction effect on pain sensitive structures such as tendons, bones and joints. Electrical Twitch Obtaining Intramuscular Stimulation (eToims® Twitch Relief Method), is a new anatomical and physiological approach to treat neuromuscular pain such as myofascial pain and fibromyalgia. It is a markedly innovative discovery in medicine as common pain therapies do not attempt to stimulate the neuromuscular junctions of muscles which mediate the pain processes.
|
|
|
Post by lilsissy on Nov 12, 2012 12:12:51 GMT -5
So if the article below is right, and I know vibrations cause pain for me and certain lighting conditions are know to then the increase the pain in fibro. Then it could come from the phosphorlation of our D.N.A. to form nano-tubes. , 7 of them horizontal, 7 of them vertical that re-son-ate at various frequencies. Antennas in us. I learned years ago we fibros are like people who have extra receptors for various stimuli. chronicfatigue.about.com/b/2009/07/20/weird-things-that-cause-fibromyalgia-pain.htmPeople without fibromyalgia just don't get it -- and really, how could they? A lot of things about it just make no sense. Among the bizarre, confusing aspects of this condition is the things that cause pain. People around me can understand that I wake up with stiff muscles; that even gentle pressure can cause pain in some place; and that my pain is artificially heightened by my brain. What they can't understand is the truly weird things that cause pain. Here's a list of some of my more unusual fibromyalgia-pain triggers: •The car turning a corner too fast •Vibrations •Loud or repetitive noises, especially high pitched ones •Bright or flashing lights •Busy patterns •Being startled •Anxiety Those are things that shouldn't cause pain but do. It would be reasonable, for instance, if the noises or lights caused a headache. They don't -- they give me abdominal pain. We've had to make some rules at my house: noisy toys have time limits, no one is to jump out and scare me, and (most recently) my husband needs to take corners a little more slowly. Do any of these pain triggers sound familiar? What other odd things cause you pain? Share your experience by leaving a comment below!
|
|
|
Post by lilsissy on Nov 12, 2012 12:20:47 GMT -5
searching, EJC Search Results: authorExact:"Dario, Paolo"
journals.ohiolink.edu/ejc/search.cgi?q=authorExact...Share
Records 1 - 30 – Defining brain–machine interface applications by matching interface performance ... Interaction with machines is mediated by human–machine interfaces (HMIs). ... of tendon hysteresis from adaptive recruitment of collagen type I fibrils. .... of a new algorithm for pattern recognition in machine vision, the Least ...
|
|
|
Post by lilsissy on Nov 12, 2012 12:32:52 GMT -5
Karen's granddaughter could move her eyes independent of her other at will something mentioned about the white matter that separated the left and right hemisphere of the brain going on in my family en.wikipedia.org/wiki/Ciliopathyresults affect maybe also what i have empty Sella syndrome My sister Debbie told me her tests had indicated a problem with the Grey and white matter at the base of the brain where it connects to the spine. White matter is being affected by waves? Waves that can bring our hemispheres to connect during sleep? Sleepwalking Waves reorganizing us?
|
|
|
Post by lilsissy on Nov 12, 2012 12:35:54 GMT -5
|
|
|
Post by lilsissy on Nov 12, 2012 12:43:39 GMT -5
|
|
|
Post by skyship on Nov 12, 2012 15:46:42 GMT -5
searching, EJC Search Results: authorExact:"Dario, Paolo" journals.ohiolink.edu/ejc/search.cgi?q=authorExact...Share Records 1 - 30 – Defining brain–machine interface applications by matching interface performance ... Interaction with machines is mediated by human–machine interfaces (HMIs). ... of tendon hysteresis from adaptive recruitment of collagen type I fibrils. .... of a new algorithm for pattern recognition in machine vision, the Least ... Many with fibro were the first to notice this, I believe, and this was just a name given to put people off the track, like it was a real Mendelian disease. However, these folks never got help either. Rheumatica. So, it was lumped into rheumatism diseases, as was the other unexplained phenomena. But, Dr. Fry has isolated the biofilm, which most likely consists of the forming elements. So if non coding, as in a film I just saw from a Stanford scientist, is the issue, he says it is a microRNA transposon, that they have now isolated from some prokaryotes, which should not have had them. So, what he is saying is this non coding transposon, whether the origin as he says it true or not, we do not know, but, it is those transposons that remain in junk dna, in what they call dark matter DNA. When the new agers talk of the 12 strands being activated, what they mean is those implanted or microRNA cells, which usually are dormant will be activated. Just like a computer? Because they have the seed? or monomer or protocell for activation. I have been looking again at the protocells. If we can see that the RNAs in Reverse transcriptase, can activate the new strands put in. Those run along the CNS or the neurojunctions Fox who came up with a protocell, which he also called the ProtoNerve, so it would be along tendons, nerve junctions, the muscular nerve junctions, and that would be why Fibromyalgia is part of Morgellons or is really Morgellons as well. This fibromyalgia involves the IFs or the neurofilaments in the filament groups. So, as I wandered through the IF info, a long read, but, you can get the idea of how the IFs could have easily been manipulated to put these quantum strands in. They would begin as protocells, which could be released into the environment, for they can replicate whereever the correct signals are found or vibrations and EM are increased. It would be this action that would set them to replicate along with heat. Sidney Fox came up with what he called the "thermal protocell". It would be activated by heat, yet the cell would have to be available in the environment in some form. So, I set out looking for different protocells and how they were created. The Protomyxzoa would be a consecutive or following cell to be used for another purpose and that could be what the myxzoa is. A metazoan or protozoan was able to grow from the Protocell, which would be different than the original protocell, it would have morphed to make the zoan. But, it had to have zoan like metazoan rna and virus to make it repeat itself. Not reproduce, but replicate its cell once it reached its capacity. So, that means a phage was involved, but, a bacteria and heat had to trigger it off. That bacteria, fungi cells from environment would recognize its Pheromones, whether from animal or plant. Once past the organic stage, that same ECM cell could replicate its form, whatever bacteria or heat stage would set it off. There has to be a signal, and that could just simply be EM or vibrations, sounds: RF.....etc. So, the body's electric system would alter its normal function and become part of the network. Geez, don't know if that makes sense or not, but if this is Protomyxzoa, that means a minicell, or minimal cell or protocell had to be involved to have the right genes, proteins, chemicals to mix together to make a form that would replicate only under certain conditions. Heat, RF, EM, microwave, quantum photons, electrons etc. Even mention of the bodies filaments being as "fiber optics". So those IFs could be the fiber optics. Found where they can tear at the ends, I have seen these in the black ones. If dark matter is involved than melanin has to be part of it. Sigma Aldrich seem to be the ones who constructed these filaments. They were involved in dendrons, dimers, dendrimers, etc, oligomers which are melanin based, fungi is melanin based etc. These could make the hybrid monomers that would actually be a form of microRNA. So, a protocell that would be multicellular, that could make anything it was programmed to do. like this ribozyme, which is the rRNA. Seems to be the core. This would be the way in. These microspheres, and that would tell us what the sphere is, it replicates and then forms and goes to the RNA most likely to achieve its effect. The Cytoskeleton is the only place this can take place, and the cytoskeleton has been compromised. That would involve the neuromuscular junctions, and smooth muscle action. These get tangled in those junctions, thereby, the fibromyalgia, the myalgia forms the biofilms? Maybe?
|
|
|
Post by skyship on Nov 12, 2012 16:06:25 GMT -5
Lil Sis posted: "karns granddaughter could move her eyes independent of her other at will something mentioned about the white matter that speratered the left and right hemisphere of the brain going on in my family en.wikipedia.org/wiki/Ciliopathyresults affect maybe also what i have empty sella syndrome My sister Debbie told me her tests had indicated a problem with the grey and white matter at the base of the brain where it connects to the spine. White matter is being affected by waves? Waves that can bring our hemispheres to coonect during sleep? Sleepwaliking Waves reorgaining us? ------------------------------------------------------ I have one slow eye now, so the muscles in the eye are involved. However, in my junk DNa there is a silencer for the "duchenne type muscular dystrophy", and again this could have been activated, so that would mean that a form of this would try to overpower my muscles, but, this is different, the one we have, it involves the "lamins" of the IFs, I believe, so different musculature proteins involved. Still at the neuromus junction, though. But, it is the junk DNA they wish to activate this so called quantum consc. Which means that some form of electrical signal sets it off. How did these get in us? From your link, Lil Sis, that would mean the "melanin" is the issue, it is being destroyed. That is why we have the scars, from the protocells that formed on skin with the filaments. These filaments are not organic, they are polymer, vinyl of sorts, depending on the creation of them. I have seen the "telechelic polymers" they are fat on the ends, like connectors, and they are short, they hook the other filaments to each other and this is all in the ECM, extracellular matrix, part of the IFs, the MTs and the MFs of the musculature, since they are what move, and muscles are electrical as Giavonni and Duchennne discovered years ago. This may be why Dr. H. says it is a form of muscular dystrophy, but in this case is more laminopathies, involving the fibromyalgias, the involuntary muscles, the ones least used, the places where the new filaments could go, without being detected. However, you feel the pain in those areas where those muscles are, usually you would feel it in voluntary muscles. These are in "resting muscle". so a different form of dystrophy. Our old proteins as in dystrophin or dynein. HHM was looking at dynein and desmein, and this appears to be where these filaments could enter into the musculature. This is also where the "morpholinos" or oligomers could be, the created peptides and polymer peptides, the artificial ones. Here this shows that the rhizome is involved. the rRNA which could be part of the "reverse transposons"....... It is in the membrane where the changes begin, the membrane of the cells? So these are protocells that would hybridize, and done through the Chromatin and Histones. That dark matter would be there. Somehow our histones have been modified with methylation. those processes again come in, including glycosylation, phosphorylation, ubiquination, methylation and acetylation. so glyco: PEG Phos: Pyrophosphatase Ubiq: universal cell Methy: intro of methanococcus or Archaea Acetylation: the CoA My take so far. ================ The emergence of ribozymes synthesizing membrane components in RNA-based protocells. Abstract A significant problem of the origin of life is the emergence of cellular self-replication. In the context of the "RNA world", a crucial concern is how the RNA-based protocells could achieve the ability to produce their own membrane. Here we show, with the aid of a computer simulation, that for these protocells, there would be "immediately" a selection pressure for the emergence of a ribozyme synthesizing membrane components. The ribozyme would promote the enlargement of cellular space and favor the incoming (by permeation) of RNA's precursors, thus benefit the replication of inner RNA, including itself. Via growth and division, protocells containing the ribozyme would achieve superiority and spread in the system, and meanwhile the ribozyme would spread in the system. The present work is inspiring because it suggests that the transition from molecular self-replication to cellular self-replication might have occurred naturally (and necessarily) in the origin of life, leading to the emergence of Darwinian evolution at the cellular level. www.researchgate.net/publication/40448889_The_emergence_of_ribozymes_synthesizing_membrane_components_in_RNA-based_protocellsSo if we concentrate on the RNA based protocell, we may find the RNA based Protomyxzoa. S
|
|
|
Post by skyship on Nov 12, 2012 16:10:37 GMT -5
From your post above Lil Sis:
"n neuromuscular pain such as fibromyalgia the mediate cause of pain is muscle shortening and/or spasm under the control of neuromuscular junctions or trigger points. This muscle shortening and/or spasm results in focal ischemia (lack of blood supply) to intramuscular nerves and blood vessels and also produce a traction effect on pain sensitive structures such as tendons, bones and joints. Electrical Twitch Obtaining Intramuscular Stimulation (eToims® Twitch Relief Method), is a new anatomical and physiological approach to treat neuromuscular pain such as myofascial pain and fibromyalgia. It is a markedly innovative discovery in medicine as common pain therapies do not attempt to stimulate the neuromuscular junctions of muscles which mediate the pain processes. ".......
I have jumping bottom lip, jumping twitches in arms and spasms. They are awful. But, you can tell that something triggers them off. It is the protonerve cell. or the protocell in actions somehow. It is un nerving for sure, but, it tells us something at the same time. Jumping in eye often, means a signal from somewhere is triggering it. EM is only one I can think of. Or Light waves........... possible.
|
|
|
Post by skyship on Nov 12, 2012 16:17:32 GMT -5
Cilia: from "tetrahymena thermophiles"? That is an Archaean. So, this protocell has to have an archaean cell in it. Was the tetra used for this Tetrahedron? Cold Spring Harbor is who is pushing Epigenetics and all the processes mentioned above, glycosylation, ubiq, phosphor, acetylation, methylation and histone modification. This is the protocell created by Szostak........ beyond Fox's? or a different form?=============== The Origins of Cellular Life Jason P. Schrum, Ting F. Zhu and Jack W. Szostak+ Author Affiliations Howard Hughes Medical Institute, Department of Molecular Biology and the Center for Computational and Integrative Biology, Massachusetts General Hospital, Boston, Massachusetts 02114 Abstract Understanding the origin of cellular life on Earth requires the discovery of plausible pathways for the transition from complex prebiotic chemistry to simple biology, defined as the emergence of chemical assemblies capable of Darwinian evolution. We have proposed that a simple primitive cell, or protocell, would consist of two key components: a protocell membrane that defines a spatially localized compartment, and an informational polymer that allows for the replication and inheritance of functional information. Recent studies of vesicles composed of fatty-acid membranes have shed considerable light on pathways for protocell growth and division, as well as means by which protocells could take up nutrients from their environment. Additional work with genetic polymers has provided insight into the potential for chemical genome replication and compatibility with membrane encapsulation. The integration of a dynamic fatty-acid compartment with robust, generalized genetic polymer replication would yield a laboratory model of a protocell with the potential for classical Darwinian biological evolution, and may help to evaluate potential pathways for the emergence of life on the early Earth. Here we discuss efforts to devise such an integrated protocell model. cshperspectives.cshlp.org/content/2/9/a002212.long======== Figure 1. A simple protocell model based on a replicating vesicle for compartmentalization, and a replicating genome to encode heritable information. A complex environment provides lipids, nucleotides capable of equilibrating across the membrane bilayer, and sources of energy (left), which leads to subsequent replication of the genetic material and growth of the protocell (middle), and finally protocellular division through physical and chemical processes (right). (Reproduced from Mansy et al. 2008 and reprinted with permission from Nature Publishing ©2008.) cshperspectives.cshlp.org/content/2/9/a002212/F1.expansion.htmlSo, this was created for other uses than just to prove the origin of life. Even the former Pope was interested in Fox's model of protocell. So, you know this has some significance. Why the interest in that? Also Szostak took it a step further. This RNA protocell? The Integrated Protocell? S
|
|
|
Post by skyship on Nov 12, 2012 16:37:59 GMT -5
What would an information polymer be? " We have proposed that a simple primitive cell, or protocell, would consist of two key components: a protocell membrane that defines a spatially localized compartment, and an informational polymer that allows for the replication and inheritance of functional information. "........ Protocell membrane Informational polymer Going back to 1973: something called Ufasomes? ? Now we are getting to the LIPIDS: "Model Protocells from Single-Chain Lipids" Model Protocells from Single-Chain Lipids Sheref S. Mansy Author information ► Article notes ► Copyright and License information ► This article has been cited by other articles in PMC. Go to: Abstract Significant progress has been made in the construction of laboratory models of protocells. Most frequently the developed vesicle systems utilize single-chain lipids rather than the double-chain lipids typically found in biological membranes. Although single-chain lipids yield less robust vesicles, their dynamic characteristics are highly exploitable for protocellular functions. Herein the advantages of using single-chain lipids in the construction of protocells are discussed. Keywords: Origin of life, prebiotic, vesicle, synthetic biology, fatty acid www.ncbi.nlm.nih.gov/pmc/articles/PMC2672004/========================== Remember, Lil Sis, we kept saying this involved the "fatty acids"? I think these polymers wrap around them and use them as energy. We have found dimers, pseudovesicles, plaque on skin where biofilms are. We have muscle twitching, we have scaling, we have excessive calcium deposits, we have jolts, we have formed organisms, unrecognizable as organic or biological, we have filaments of different sizes, spheres, hexagons(dimers), monomers of polymer and of rna particles, nanoparticles, bottom up assembly of protocells. Membranes, so the Transmembrane is involved. The membrane of cells has been infiltrated. Especially in the Cytoskeletal cells. So, we come round again to the "reorganization of the Cytoskeleton, again". The Aarp2/3, the RHO, the new protofilaments, which are implicit in Alzheimers, they really are Oligomers which are melanin based?
|
|
|
Post by skyship on Nov 12, 2012 16:48:49 GMT -5
Back to the Ufasomes: It seems the 'created things" are called "somes"...... or zymes" Unidentified Flying Airs in some people. Dark matter airs? ah....yes..... the dark aether airs? from the mists? Infilitrating the Histones.......His Tones........... Couldn't leave "well enough, alone", could they? Because "They" need the Energy. It is stolen from us, so we become immobile. Bad enough, they steal our land, our gold, our titles, and then to steal our energies? Naw, what are Ufasomes, really? ============== Ufasomes: A vesicular drug delivery www.sysrevpharm.org/article.asp?issn=0975-8453;year=2011;volume=2;issue=2;spage=72;epage=78;aulast=PatelFigure 6: Mechanism of fusion of cationic vesicles and ufasomes www.sysrevpharm.org/viewimage.asp?img=SystRevPharm_2011_2_2_72_86290_f6.jpg======================== At the height of my accomplishments, was my destruction. We were never to cross the line were we? However, my thoughts are still my own. Remember that, folks. "your thoughts are your own" and they have meaning. God does not make "junk".(my personal note)............will get into that later, names mean a lot. or maybe just ignore, and put the science out there.
|
|
|
Post by skyship on Nov 12, 2012 19:29:12 GMT -5
|
|
|
Post by skyship on Nov 12, 2012 19:48:30 GMT -5
Metabolic materials are able to carry out their dynamic functions without the need for DNA, which is the information processing system that biology uses. One specific example of agents that are capable of generating functional metabolic materials is protocells. These are dynamic oil in water droplets that are chemically programmable and exhibit some of the properties of living systems. Protocell oil droplets are able to move around their environment, sense it, modify it and undergo complex behaviours, some of which are architectural. The architectural properties of protocells include the shedding of skins, altering the chemistry of an environment through their ‘waste’ products, the precipitation of solids, population based interactions, light sensitivity and responsiveness to vibration. Protocells can be ‘programmed’ chemically to achieve particular outcomes. For example, is possible to create a ‘carbonate’ shell from insoluble carbonate crystals that are produced by protocells when they come in contact with dissolved carbon dioxide. Protocells can therefore produce a limestone like substance and artificially extend the development of this material (created by the accretion of the skeletons of tiny marine organisms), which can continue to grow, self-repair and even respond to changes in the environment. We are developing a coating for building exteriors based on this principle. www.nextnature.net/2010/06/self%E2%80%93repairing-architecture/=========== Protocells are tiny, self-organizing, evolving entities that spontaneously assemble and continuously regenerate themselves from simple organic and inorganic sub- strates in their environment. A number of scientifi c teams around the world are racing to create protocells, and success is expected within a few years. Protocells will raise a number of social and ethical issues, involving benefi ts to individuals and to society, risks to human health and the environment, and trans- gressions of cultural and moral prohibitions. This volume contains the thoughts of a diverse group of experts who explore the prospect of protocells from a variety of perspectives. These perspectives include applied ethics in analytical philosophy, continental philosophy, and anthropology as well as political and social commen- tary. The book raises broad questions for a broad audience, without necessarily drawing fi nal conclusions. We produced this book because we believe the social and ethical issues raised by the prospect of protocells are complex, and involve many interesting open questions. We hope that this volume will contribute to fi nding responsible solutions to these issues. Our aim is to engage and inform all stakeholders and to prepare them for navigating the uncharted waters ahead. www.wosco.org/books/Philosophy/EthicsProtocells.pdfSo, there is concern. S
|
|