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Post by skyship on Dec 31, 2009 16:40:03 GMT -5
I have been looking at how A and B blood is being changed to O, Universal O blood, One blood for all of humanity? and the bacterial enzymes used.
Elizabethkingia.....and b. fragilis..........
in e-coli, the vector..........yeast with prion, and neurospora crassa fusions and fissions and many other enzymes, polypeptides from other organisms.
but, here is where we start with the blood; posted on another board but, will bring over here because until we see the physical changes we will not get there.
I am concerned about those suffering from calcium deposits, and from blockages and from bacteria forming symbiosis and creating objects in us that do not belong there.
By finding and challenging the studies of those who experiment with those who are trying to solve issues has been a demanding one on my part.
Many things have been overlooked, but many things are being exposed as well.=================== There is fusion with e-coli, yeast, and neurospora crassa. This seems to have been a great discovery many years ago. ==================== Amyloid - Any of a group of chemically diverse proteins that appear microscopically homogeneous, but are composed of linear nonbranching aggregated fibrils arranged in sheets when seen under the electron microscope. Occurs characteristically as pathologic extracellular deposits. ============================ chemicial diverse proteins> would include agrobacterium as well, but am finding that homogenous means like proteins, so we are getting proteins that are like what we used to get, like in gmo foods, but are not the same substance. In other words archaea was used in heat shock proteins put in tomato and other plants. genes from other organisms enzymes and proteins, were put in plants. Just found the chlamydia link to this thing. And the "tissue tropis" was mentioned. epithelial cells, intestine wall, pancreas, duodenum, small intestine, lungs etc. ======================== Chlamydial Infection Induces Pathobiotype-Specific Protein Tyrosine Phosphorylation in Epithelial Cells"Chlamydiae are obligate intracellular bacteria that exhibit remarkable diversity in host species, tissue tropism and disease pathogenicity (Table 1). Chlamydiae have two distinct developmental forms: the extracellular, infectious, metabolically inactive elementary body (EB) and the intracellular, noninfectious, metabolically active reticulate body (RB) (20). Early attachment of the EB and commencement of infection is mediated by binding of the chlamydial major outer membrane protein (MOMP) to heparin or heparin sulfate glycosaminoglycan moieties on the host cell surface (1, 4, 5, 22, 24-26). After attachment, a second uncharacterized step is required for entry of the EB into host cells (7, 28). Upon completion of the attachment and entry steps, chlamydiae promote actin-cytoskeletal rearrangement that facilitates their final entry into nonlysosomal fusogenic phagosomes where the pathogen replicates (6, 9, 20). Attachment and/or entry of chlamydiae into host cells induces protein tyrosine phosphorylation (2, 9, 10, 14). The identity and source of these phosphorylated proteins remains controversial. Birkelund et al. (2) first reported that infection of host cells with Chlamydia trachomatis serovar L2 induces protein tyrosine phosphorylation of several proteins: a triplet of ~64, 66, and 68 kDa and polypeptides with masses of 97 and 140 kDa, respectively; however, in a subsequent study, C. pneumoniae VR1310 failed to induce tyrosine phosphorylation in either HeLa 229 or Henle 407 host cells (14). Fawaz et al. (10) later extended these findings by demonstrating that L2 and the mouse strain C. muridarum (MoPn) induced different patterns of phosphorylation in HeLa cells. More recently, Clifton et al. reported that a protein tyrosine-phosphorylated during chlamydial infection (Tarp) was of chlamydial origin (9). They suggested that Tarp was translocated into the host cytosol by a chlamydial type III secretion mechanism and that secreted Tarp facilitated actin rearrangement during entry into host cells. Altogether, these results, using a limited number of strains suggested that tyrosine phosphorylation may be critical to early chlamydia-host interaction and might vary among chlamydial strains of differing host and tissue tropism in vivo."iai.asm.org/cgi/content/full/73/4/1939=========================== I do not know if you can glean anything from this, but this appears to relate to placque and maybe calcium deposits, or calculini as they call it.
protein tyrosine phosphorylation============================== Cellular Signalling and Human Disease LaboratoryA cell's ability to respond to its extracellular environment involves a complex and highly organised series of events referred to as cellular signalling. Signalling processes regulate fundamental cellular responses and abrogation of these processes can lead to the development of various human diseases. Protein tyrosine phosphorylation controls a diverse array of cellular responses including growth, proliferation, differentiation, migration, metabolism and survival. Tyrosine phosphorylation is a reversible, dynamic process controlled by the activities of the protein tyrosine kinases (PTKs) and the competing actions of the protein tyrosine phosphatases (PTPs). The laboratory's general research interest is in understanding the role of tyrosine phosphorylation-dependent signalling in physiological and pathological processes. Our overall goal is to provide a basis from which rational, mechanism-based strategies can be developed for modulating tyrosine phosphorylation-dependent signalling in diseased states such as cancer, inflammation and diabetes. To date, the laboratory's research has concentrated on understanding the regulation and function of PTPs, key regulatory enzymes that serve to coordinate fundamental cellular responses to varied extracellular and intracellular inputs. Much of the work has focussed on the widely expressed phosphatase known as TCPTP, but we also work on other PTPs including the prototypic PTP1B as well as Ser/Thr and lipid phosphatases. We use wide array of in vitro cell-based (immortalized/transformed and primary cells) and in vivo (knockout mice and mutant Drosophila strains) approaches to systematically dissect the role of PTPs in varied signalling pathways and biological responses. www.med.monash.edu.au/biochem/research/projects/protein.html======================== I try to do ankle circles, and then step exercises and stretching and exercises that help with strengthening little used muscles. wrist circling helps my hands, small leg lifts and you can work up to larger leg lifts, also lifting weights, start with nothing go through motions as if you are lifting weigts, then go to 1 lb can of something, then 2 lbs, seems to be helping me some. cranberry juice good for kidneys. there are more than just blood changes, but, will get to that later. ------------------------------------- will bring over bit by bit...... skyship
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Post by skyship on Dec 31, 2009 16:41:38 GMT -5
next copy;================ GlycosaminoglycanFor other uses of GAGs see Gag (disambiguation) Chondroitin sulfate Hyaluronan (-4GlcUAβ1-3GlcNAcβ1-)n Glycosaminoglycans[1] (GAGs) or mucopolysaccharides[2] are long unbranched polysaccharides consisting of a repeating disaccharide unit. The repeating unit consists of a hexose (six-carbon sugar) or a hexuronic acid, linked to a hexosamine (six-carbon sugar containing nitrogen). Production Protein cores made in the rough endoplasmic reticulum are posttranslationally modified by glycosyltransferases in the Golgi apparatus, where GAG disaccharides are added to protein cores to yield proteoglycans; the exception is the GAG hyaluronan, which is uniquely synthesized without a protein core and is "spun out" by enzymes at the cell surface directly into the extracellular space. en.wikipedia.org/wiki/Glycosaminoglycan-------------------------- Glycosyltransferase Peptidoglycan biosynthesis glycosyltransferase MurG (1f0k). Blue plane shows hydrocarbon boundary of the lipid bilayer Glycosyltransferases are enzymes (EC 2.4) that act as a catalyst for the transfer of a monosaccharide unit from an activated nucleotide sugar (also known as the "glycosyl donor") to an Glycosyl acceptor molecule, usually an alcohol. The result of glycosyl transfer can be a carbohydrate, glycoside, oligosaccharide, or a polysaccharide. Some glycosyltransferases catalyse transfer to inorganic phosphate or water. Glycosyl transfer can also occur to protein residues, usually to tyrosine, serine, or threonine to give O-linked glycoproteins, or to asparagine to give N-linked glycoproteins. Mannosyl groups may be transferred to tryptophan to generate C-mannosyl tryptophan, which is relatively abundant in eukaryotes. Transferases may also use lipids as an acceptor, forming glycolipids, or even lipid-linked sugar phosphate donors, such as dolichol phosphates. en.wikipedia.org/wiki/Glycosyltransferase================================ Now this may be indication of how this relates to blood groups, and the application of making everyone's blood Universal O.=================== Determinant of blood type The ABO blood group system is determined by what type of glucosyltransferases are expressed in the body. The ABO gene locus expressing the glucosyltransferases has three main alleleic forms: A, B, and O. The A allele encodes a glycosyltransferase that bonds α-N-acetylgalactosamine to D-galactose end of H antigen, producing the A antigen. The B allele encodes a glycosyltransferase that joins α-D-galactose bonded to D-galactose end of H antigen, creating the B antigen. In case of O allele the exon 6 contains a deletion that results in a loss of enzymatic activity. The O allele differs slightly from the A allele by deletion of a single nucleotide - Guanine at position 261. The deletion causes a frameshift and results in translation of an almost entirely different protein that lacks enzymatic activity. This results in H antigen remaining unchanged in case of O groups. The combination of glucosyltransferases by both alleles present in each person determines whether there is a AB, A, B or O blood type. .........."The deletion causes a frameshift and results in translation of an almost entirely different protein that lacks enzymatic activity"............ ===================== so enzymes stop working, this frame shift could be present in Karen and us. People with O type blood remain unchanged, this could be the blood link issue!
what is the H antigen?======================== No antibodies are formed against the H antigen, except in those individuals with the Bombay phenotype.In ABH secretors, ABH antigens are secreted by most mucus-producing cells of the body interfacing with the environment, including lung, skin, liver, pancreas, stomach, intestines, ovaries and prostate.[16] ========================= interesting bit here??
are we of this descent? a and b or ab?
======================" "In the UK, the distribution of blood type frequencies through the population still shows some correlation to the distribution of placenames and to the successive invasions and migrations including Vikings, Danes, Saxons, Celts, and Normans who contributed the morphemes to the placenames and the genes to the population.[18] There are six common alleles in white individuals of the ABO gene that produce one's blood type:[19][20] A
* A101 (A1) * A201 (A2) B
* B101 (B1)O
* O01 (O1) * O02 (O1v) * O03 (O2)Many rare variants of these alleles have been found in human populations around the world. Some evolutionary biologists theorize that the IA allele evolved earliest, followed by O (by the deletion of a single nucleotide, shifting the reading frame) and then IB.[citation needed] This chronology accounts for the percentage of people worldwide with each blood type. It is consistent with the accepted patterns of early population movements and varying prevalent blood types in different parts of the world: for instance, B is very common in populations of Asian descent, but rare in ones of Western European descent.) Another theory states that there are four main lineages of the ABO gene and that mutations creating type O have occurred at least three times in humans.[21] From oldest to youngest, these lineages comprise the following alleles: A101/A201/O09, B101, O02 and O01. The continued presence of the O alleles is hypothesized to be the result of balancing selection.[21] Both theories contradict the previously-held theory that type O blood evolved earliest, supported by the fact that all human beings (except Type hh) can receive it.[citation needed] The British National Blood Transfusion Service states this to be the case (see the web-link under External Links below) and says that originally all human beings were type O."======================== the artificial blood created involves glycolysis!------------------------------------------- Universal blood created from other types, and artificial bloodIn April 2007 an international team of researchers announced in the journal Nature Biotechnology an inexpensive and efficient way to convert types A, B and AB blood into type O.[31] This is done by using glycosidase enzymes from specific bacteria to strip the blood group antigens from red blood cells. The removal of A and B antigens still does not address the problem of the Rhesus blood group antigen on the blood cells of Rhesus positive individuals, and so blood from Rhesus negative donors must be used. Patient trials will be conducted before the method can be relied on in live situations. Another approach to the blood antigen problem is the creation of artificial blood which could act as a substitute in emergencies. BBC. en.wikipedia.org/wiki/ABO_blood_group_system========================== so by trying to make us all type universal O, the pancreas is affected and other epithelials.
it is made from bacterial enzymes. I do think the chlamydia comes in here.------------------------------- skyship
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Post by skyship on Dec 31, 2009 16:46:11 GMT -5
Continuing with the blood business, this does relate to Morgellons and the pancreas, diabetis, and liver, lungs, gastrointestinal, and skin.
Do many of you notice that you get bruise like things on skin, yet you did not bump yourself, is symtom of lupus, I believe.
Here is how they made this Univiversal O blood and/or the glycotransferase used to change A B antigen and blood to O.==================== " Bacterial glycosidases for the production of universal red blood cellsQiyong P Liu1,9, Gerlind Sulzenbacher2,9, Huaiping Yuan1, Eric P Bennett3, Greg Pietz1,3, Kristen Saunders1, Jean Spence1, Edward Nudelman1, Steven B Levery4, Thayer White1, John M Neveu5, William S Lane5, Yves Bourne2, Martin L Olsson6,7, Bernard Henrissat2 & Henrik Clausen3,8 Abstract Enzymatic removal of blood group ABO antigens to develop universal red blood cells (RBCs) was a pioneering vision originally proposed more than 25 years ago. Although the feasibility of this approach was demonstrated in clinical trials for group B RBCs, a major obstacle in translating this technology to clinical practice has been the lack of efficient glycosidase enzymes. Here we report two bacterial glycosidase gene families that provide enzymes capable of efficient removal of A and B antigens at neutral pH with low consumption of recombinant enzymes. The crystal structure of a member of the alpha-N-acetylgalactosaminidase family reveals an unusual catalytic mechanism involving NAD+. The enzymatic conversion processes we describe hold promise for achieving the goal of producing universal RBCs, which would improve the blood supply while enhancing the safety of clinical transfusions. 1. ZymeQuest Inc., 100 Cummings Center, Suite 436H, Beverly, M" www.nature.com/nbt/journal/v25/n4/abs/nbt1298.html================== What bacterial glycosidase did they use? Lets look further.============ Here is proof folks!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!========================= Expression of gp130 in Tumors and Inflammatory Disorders of the Skin: Formal Proof of its Identity as CD146 (MUC18, Mel-CAM)Margarete Schön*, Thilo Kähne†, Harald Gollnick‡ and Michael P Schön* 1. *Rudolf Virchow Center, DFG Research Center for Experimental Biomedicine and Department of Dermatology, Julius Maximilians University, Würzburg, Germany 2. †Institute for Experimental Internal Medicine, Otto von Guericke University, Magdeburg, Germany 3. ‡Department of Dermatology, Otto von Guericke University, Magdeburg, Germany Correspondence: Michael P. Schön, MD, Rudolf Virchow Center, DFG Research Center for Experimental Biomedicine and Department of Dermatology, Julius Maximilians University, Versbacher Str. 9, 97078 Würzburg, Germany. Email: michael.schoen@virchow.uni-wuerzburg.de Received 28 November 2004; Revised 1 March 2005; Accepted 16 March 2005. Top of page Abstract Two antibodies, BT14 and L101, detect a tumor-associated cell surface glycoprotein (gp130) whose properties in normal and diseased skin were assessed, and whose molecular identity was determined in this study. In normal skin, gp130 was constitutively expressed on dermal blood vessels and epidermal appendages, but not in interfollicular epidermis. Marked induction was detected within benign and malignant tumors of various origins including viral warts, basal cell carcinomas, squamous cell carcinomas, metastatic melanomas, and cutaneous T cell lymphomas. In vitro studies confirmed the general upregulation of gp130 expression in malignantly transformed cells. Surprisingly, gp130 was also induced in inflammatory skin diseases including psoriasis and allergic contact dermatitis. Halting proliferation of transformed keratinocytes through cytostatic drugs or increasing the Ca2+ concentration in the medium resulted in increased gp130 expression. In addition, overexpression of Bcl-2 led to upregulation of gp130. When the protein was purified and analyzed by peptide mass fingerprinting, we could demonstrate that it is MUC18 (Mel-CAM, CD146). Sequential immunoprecipitations and western blot analyses confirmed the identity of the antigen. Thus, both expression pattern and regulation characteristics of the now-known glycoprotein gp130 extended beyond previously published data regarding MUC18, thus shedding some new light on a supposedly well-known antigen. Keywords: tumor-associated antigen, CD146, MUC18, skin tumor, inflammation Abbreviations: FCS, fetal calf serum; mAb, monoclonal antibody; MALDI-TOF, matrix-assisted laser desorption/ionization-time of flight; PBL, peripheral blood lymphocytes; SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis MORE ARTICLES LIKE THIS These links to content published by NPG are automatically generated. RESEARCH Expression of Basal-Cell Adhesion Molecule (B-CAM) is Associated with Immature States of Human Keratinocytes Journal of Investigative Dermatology Letter Death Receptor-Independent Apoptosis in Malignant Melanoma Induced by the Small-Molecule Immune Response Modifier Imiquimod Journal of Investigative Dermatology Original Article www.nature.com/jid/journal/v125/n2/abs/5603489a.html================== now next post will dissect.....................................skyship
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Post by skyship on Dec 31, 2009 16:49:21 GMT -5
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Post by skyship on Dec 31, 2009 16:50:25 GMT -5
Okay, they know about this, and many are bringing it forward. No small matter! ======================== CD146 is a 118 kDa integral transmembrane glycoprotein, also known as MUC18, S-Endo, MCAM, and Mel-CAM (melanoma cell adhesion molecule). It belongs to the immunoglobulin superfamily. CD146 is expressed on melanoma cells, epithelial cells, endothelial cells, fibroblasts, activated T cells, multipotent mesenchymal stromal cells, and activated keratinocytes. CD146 mediates heterophilic cell adhesion and regulates monocyte transendothelial migration. The ligand of CD146 remains to be identified.www.biolegend.com/pe-anti-human-cd146-muc18-mel-cam-antibody-5874.html============================ antihuman??
okay then................
keratinocytes:
skyship
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Post by skyship on Dec 31, 2009 16:54:30 GMT -5
seems they made an antibody for the antibody? in last post. but the"Bacterial glycosidases" is what we need to find. I see they cannot find the ligand. so I will help them. ======================== antibodies, BT14 and L101, detect a tumor-associated cell surface glycoprotein (gp130) whose properties in normal and diseased skin were assessed, and whose molecular identity was determined in this study.... =========================== so antibodies BT 14 and L101 detect "tumor-associated cell surface glycoprotein (gp130)" =============== "Glycoprotein 130 Interleukin 6 signal transducer (gp130, oncostatin M receptor) Gp130 extracellular domain crystal structure from PDB 1p9m. Available structures 1bj8, 1bqu, 1i1r, 1p9m, 1pvh Identifiers Symbols IL6ST; CD130; CDw130; GP130; GP130-RAPS; IL6R-beta External IDs OMIM: 600694 MGI: 96560 HomoloGene: 1645 GeneCards: IL6ST Gene [show]Gene ontology Molecular function • receptor activity • interleukin-6 receptor activity • oncostatin-M receptor activity • protein binding Cellular component • plasma membrane • integral to plasma membrane Biological process • immune response • cell surface receptor linked signal transduction • positive regulation of cell proliferation • regulation of Notch signaling pathway Orthologs Species Human Mouse Entrez 3572 16195 Ensembl n/a ENSMUSG00000021756 UniProt n/a Q3TDT5 RefSeq (mRNA) NM_002184 NM_010560 RefSeq (protein) NP_002175 NP_034690 Location (UCSC) n/a Chr 13: 113.58 - 113.63 Mb PubMed search [1] [2] Glycoprotein 130 (also known as gp130, IL6ST, IL6-beta or CD130) is a transmembrane protein which is the founding member of the class of all cytokine receptors. It forms one subunit of type I cytokine receptors within the IL-6 receptor family. It is often referred to as the common gp130 subunit, and is important for signal transduction following cytokine engagement. As with other type I cytokine receptors, gp130 possesses a WSXWS amino acid motif that ensures correct protein folding and ligand binding. It interacts with Janus kinases to elicit an intracellular signal following receptor interaction with its ligand. Structurally, gp130 is composed of five fibronectin type-III domains and one immunoglobulin-like C2-type (immunoglobulin-like) domain in its extracellular portion." =================== see picture of crystals. ======================== ww2.cnrs.fr/en/870.htm?debut=224Group O blood for everyone ? A general view of the molecular structure of Elizabethkingia meningosepticum N-acetylgalactosaminidase in complex with the NAD+ cofactor (in yellow) and the A antigen on the surface of A type red blood cells. The N-acetylgalactosamine molecule recognized and hydrolyzed by the enzyme appears in red please see crystals, sure look wicked! ============================ Flavobacterium meningosepticum (Chryseobacterium meningosepticum) (Elizabethkingia meningoseptica) "Bacterial glycosidases for the production of universal red blood cells." Liu Q.P., Sulzenbacher G., Yuan H., Bennett E.P., Pietz G., Saunders K., Spence J., Nudelman E., Levery S.B., White T., Neveu J.M., Lane W.S., Bourne Y., Olsson M.L., Henrissat B., Clausen H. Nat. Biotechnol. 25:454-464(2007) [PubMed: 17401360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, BIOTECHNOLOGY, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). Strain: ATCC 33958. www.uniprot.org/uniprot/A4Q8F7======================== Remember the B. subtilis? skyship
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Post by skyship on Dec 31, 2009 16:56:13 GMT -5
How many here have O blood?
most of us have A or B right?
it is the antigen on the A and B.
antigen bt14 and L101:
here some to chew on:============================ www.copewithcytokines.de/cope.cgi?key=gp130%20antigen======================= back later. more reading in Spanish and German.
this is so involved. but others are looking.....
skyship
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Post by skyship on Dec 31, 2009 17:03:11 GMT -5
good link here, thanks lil sissy!======================== www.godlikeproductions.com/forum1/message455569/pg1========================== I think the different colored fibers give it away.
The red fibers I am thinking are related to blood or ragged red fibers The blue lines we see maybe some relation to oxygen, since the aerosol operations, we have had lowered oxygen levels, and since the magnetic forces from sun causing warming, and the magnetic force of earth, have lowered our magnetism, however, more positive magnetism is not the answer, it should be more magnetism for human body, but, it should be negative, this is why the magnetic pads work good for us. If the wrong polarity in the magnetism is present in us, it causes electrical electrolyte problems, dizziness, vertigo, etc.
I notice that the construction of these used to change blood have Mn manganese or magnesium or other metal and that is where the ligand comes in. Ligands mentioned, copper, cobalt, and others and are related to the NAD. that I will study some more.
But, yes agro and b subtilis at the beginning of this were used together and b subtilis is the walking dna.
Now, here is how they set about doing this, they started with enzyme from green coffee bean, but, then went on to the Elizabethkia.... and b gragilis.========================= Enzymes convert all donor blood to group O* 18:00 01 April 2007 by Peter Aldhous You're rushed into hospital and need a blood transfusion - but what is your blood group? In future, it may not matter, thanks to enzymes that scrub antigens from red blood cells, turning all donated blood into group O - which can be given safely to anyone. The A and B antigens, which give blood groups their name, are sugars carried on the surface of red blood cells. Human red blood cells can carry one of these antigens, both, or neither; giving four blood groups: A, B, AB and O, respectively. Receiving mismatched blood can cause a life-threatening reaction, and errors are made in 1 in every 15,000 transfusions, on average. In the 1980s, a team in New York, US, showed that an enzyme from green coffee beans could remove the B antigen from red blood cells. It proved too inefficient for practical use, but Henrik Clausen at the University of Copenhagen in Denmark and colleagues have now screened bacteria and fungi for more powerful enzymes. "The diversity you get in the bacterial kingdom is much higher," Clausen explains.
The researchers homed in on two enzymes. One, from a gut bacterium called Bacteroides fragilis, removes the B antigen. The other, from Elizabethkingia meningosepticum - which causes opportunistic infections in people - targets the A antigen. The purified enzymes are highly efficient. For example, the B. fragilis enzyme is used up at only one-thousandth the rate of the coffee bean enzyme.
Clausen's team is working with a company called ZymeQuest in Beverly, Massachusetts, US, which plans clinical trials to test whether the treated blood is safe and effective. If so, the technology should be in hot demand, because group O blood - the only safe option if there is any doubt about the recipient's blood group - is a precious commodity. "We're always in a shortage," says Richard Benjamin, chief medical officer with the American Red Cross in Washington DC, US. www.newscientist.com/article/dn11....to-group-o.html========================== They are in a shortage because the blood taken was used for experimentation rather than for use. How much was doled out for experimentation in a project this big?
--------------------------------- skyship
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Post by skyship on Dec 31, 2009 17:09:43 GMT -5
This is donor blood, but, could this have been introduced into gmo foods?
I bet, just like the agro changing our intestinal flora.
This is done on enzyme level which has everything to do with the pancreas.
The pancreas begins to lose the ability to help break food down because it gets blocked or the glycosidases change and cannot process, an accumulation of fibronectin or micelles occurs, but calcium forms and then forms the stones. Many people are getting stones in kidney as well as colon, stomach, pancreas tubes are blocked, etc. This accumulation of calcium is prevalent.
Biomineralization is going on as well, a chemical reaction that forms calcium and this calcium is sclerosing. It scleroses the liver as well.
Prednisone seems to help break this up in blood, because same thing happens to arteriosclerosis. I think Dr. Marshall has the key.
Do you remember his studies?
Much of his work has been challenged, I believe. But, he did have a protocol called the Marshall Protocol.
Here is an example of sclerosing, in this case the liver:======================= en.wikipedia.org/wiki/Primary_sclerosing_cholangitisskyship
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Post by skyship on Dec 31, 2009 17:11:10 GMT -5
If this is scerosing material, then one help for me with the excess calcium is vinegar, I take a tablespoon a day.
This will break up the calcium, and grape juice or wine/hydrogen peroxide swish will get it out from under teeth.
If your teeth hurt, swish with grape juice, spit out and you will see the fungal form. and your teeth will feel better. Any biomineralization will come from teeth, or bone anywhere in the body, but, if more is being formed because of lack of digestion of the enzmes, more calcium will form in soft matter.
www.carnicom.com
This is on enzyme level.=========================== Marshall Protocol:www.marshallprotocol.com/skyship
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Post by skyship on Dec 31, 2009 17:14:24 GMT -5
Knowing that the antigen called the H antigen from blood type A and B is being converted to O blood only, makes one wonder how this was done, and why those with O blood are not affected, seems they have the H antigen?
what antigen from A and B is being removed?
I do believe is related to mucin???============================ ......"I nitiation of mucin-type O-glycosylation is controlled by a large family of UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). Most GalNAc-transferases contain a ricin-like lectin domain in the C-terminal end, which may confer GalNAc-glycopeptide substrate specificity to the enzyme. We have previously shown that the lectin domain of GalNAc-T4 modulates its substrate specificity to enable unique GalNAc-glycopeptide specificities and that this effect is selectively inhibitable by GalNAc; however, direct evidence of carbohydrate binding of GalNAc-transferase lectins has not been previously presented. Here we report the direct carbohydrate binding of two GalNAc-transferases, GalNAc-T4 and GalNAc-T2, and their isolated lectins domains, representing isoforms reported to have distinct glycopeptide activity (GalNAc-T4) and isoforms without apparent distinct GalNAc-glycopeptide specificity (GalNAc-T2). Both lectins exhibited specificity for binding of free GalNAc. Kinetic and time-course analysis of GalNAc-T2 demonstrated that the lectin domain did not affect transfer to initial glycosylation sites, but selectively modulated velocity of transfer to subsequent sites and affected the number of acceptor sites utilized. The results suggest that GalNActransferase lectins serve to modulate the kinetic properties of the enzymes in the late stages of the initiation process of O-glycosylation to accomplish dense or complete O-glycan occupancy. Key words: GalNAc / transferases / lectins / glycans / mucins" glycob.oxfordjournals.org/cgi/content/short/cwl082v1======================= O-glycosylation
is this intentional or did they just appear in the gut?
symbiosis with what? ======================= ..."A General O-Glycosylation System Important to the Physiology of a Major Human Intestinal SymbiontC. Mark Fletcher1, Michael J. Coyne1, Otto F. Villa2, 3, Maria Chatzidaki-Livanis1 and Laurie E. Comstock1, Go To Corresponding Author, 1 Channing Laboratory, Brigham & Women's Hospital, Harvard Medical School, 181 Longwood Avenue, Boston, MA 02115, USA 2 Pulmonary Critical Care and Sleep Division, Department of Medicine, Mount Sinai School of Medicine, 1468 Madison Avenue, New York, NY 10029, USA Corresponding author 3 Present address: Memorial Hospital of Rhode Island, 111 Brewster Street, Pawtucket, RI 02860, USA SummaryThe Bacteroides are a numerically dominant genus of the human intestinal microbiota. These organisms harbor a rare bacterial pathway for incorporation of exogenous fucose into capsular polysaccharides and glycoproteins. The infrequency of glycoprotein synthesis by bacteria prompted a more detailed analysis of this process. Here, we demonstrate that Bacteroides fragilis has a general O-glycosylation system. The proteins targeted for glycosylation include those predicted to be involved in protein folding, protein-protein interactions, peptide degradation as well as surface lipoproteins. Protein glycosylation is central to the physiology of B. fragilis and is necessary for the organism to competitively colonize the mammalian intestine. We provide evidence that general O-glycosylation systems are conserved among intestinal Bacteroides species and likely contribute to the predominance of Bacteroides in the human intestine. Jobs from the Cell Career Network" www.cell.com/abstract/S0092-8674(09)00255-4=============================== b. fragilis is one of the enzymes used to change the A and B antigens.
discovering coverups, saying symbiosis has gone on for a long time is a lie. and I will call it that. We see the science where they intentionally used both b. fragilis glycogen or enzyme and the Elizabethkia..... to change A and B blood antigens to present O Blood only.
So, to say that this is already there, like the Achaean from the heat shock protein, many Jews are suffering from diseases related to this as are Asians from the pancreas problems, Japan has found many incidents of enzyme and auto immune pancreas diseases as well as in Asians here. Many with intestinal issues.
In fact, president of North Korea is now suffering from Pancreas Cancer.
Many here in US are dying from this cancer. blocked tubes with calculus or as they say particulate matter, excessive calcium in my opinion blocking not digested and symbiosis through e-coli transmutations.
Vector of this? e-coli in air, in water, in insects, in mammals, in humans, in plants etc.
The way in carrying the load of dna altering ingredients is e - coli.
The blood was first, I believe, than, muscle fibers, nerve fibers, you name it. The created sup35 and sup45 takes us into the protein folding, unfolding, use of prion for amyloid formation and then electrifying the package.
I do believe jj and I had arrived here once, but, we were not certain about what we were looking at.
Now, it is beginning to make sense.
One blood, wonder if this means insect blood, mammal blood, human blood etc? plant enzymes, etc. Molecular level crosses all species?
This is hard to take in, knowing this is being done, by gmo foods, aerosol operations and recombinations of H1N1 and H5N1 and so on.
But, we are aiming to be more specific and find out the rest of the story.
skyship
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Post by skyship on Dec 31, 2009 17:17:35 GMT -5
.......
We feel the pain, and the blockage sometimes, so here is where they do say that increased Oxygen is beneficial.
Opaline or Allicin C may be of help to us all.
I have been chewing garlic again, eating black licorice and a tablespoon of vinegar, seems to help break this calcium deposits up.
just my opinion there, but they do say vinegar helps with arthritis and osteo or bone changes. More vinegar or acid is the only thing I can see that would attack that.
And if ph is high meaning toward 1 acid that is, and we are accumulating toward 11 on the ph scale, that means we are too akaline, rather than too much acid, acid breaks down things.
what do you think?
skyship
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Post by aqt on Jan 1, 2010 12:22:13 GMT -5
I think you never cease to amaze me.
It will take me all day to digest this page of work, but I think you are truly on to something here..LOL
amyloid fibers, prions, ect....piece by piece
The vinegar is a good idea.
aqt
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Post by lilsissy on Jan 1, 2010 16:05:52 GMT -5
From your link skytrool, www.cazy.org/I asked my daughter ELIZABETH , to write to you and tell you want has been going on with her blood . It is changing blood groups and I think we can verify it. Her dog went missing last night but as soon as she is able I will get her on the board . Her blood has actually shown up three different blood types. Jen I am really studying this thread today, seeing so much on the way, First Skytrool , did you see the Stanford University video about how they used Chlamydiae , Archebacteria gene inserts to provide a on and off switch to the membrane of the brain to activate the neurons by light through ions? Bet that is why we find Chlamydiae, ya think? Also 1q42 F.H. deficiency . Also wonder if this is a part, wsmcsn.s5.com/understandci.htmSomething I have noticed is some of the foods I do not tolerate are the same ones you should not feed dogs , Dogs are now getting viral cancer? I thought about that tonight as I shared my Delicious Ham on Rye with my dog Titan , I think I remember dogs should not eat rye or wheat nor should I, . I am wheat intolerant . Same foods too, like chocolate ,beer , mushrooms and certain breads , forgot why though. My memory is scary , I want to believe it is overload but ....... O.K. took a minute here it is ,, hops ¡<!--[if !supportLists]--> <!--[endif]-->Hops, a primary beer ingredient, can cause a condition called malignant hyperthermia in dogs, usually with fatal results. Hops should be kept away from all dogs. Even small amounts of hops can trigger a potentially deadly reaction Oh my it is that yeast you where talking about , I seem to have trouble with it, www.wisegeek.com/what-is-brewers-yeast.htmtinyurl.com/yzwp5y8I won't let that dog take another bite but I love rye bread . I only eat it maybe every few months. Jen This is one thing that I think is really coming into play with us, en.wikipedia.org/wiki/AcetylcholineNotice the irreversible damage that can be done by insecticides to certain people , that would be us I think . Watch the Vinegar though , I show you why. I have seen this in morgellons samples , it is probably a co-infection . I started a new thread on it so not to get off tract here, www.morgboard.proboards.com/index.cgi?action=display&board=general&thread=378Jen Also , you are right about the fibers , colors and proteins, I read an article on this. They used protein fibers to stop the inflammation response of tissues to Pedot by use of protein fibers. As you can see , I am really studying your material, Here the protein core is called Viral hmmmm..... www.path.utah.edu/research/cbi/ila-singh-md-phdHow would the F.H. defiency fit into this equasion? I really think we have this at least Karen and I because of Uterine Fibroids well have fibroids everywhere it seems, Glycosaminoglycan chondrotin sulfat Hyaluronan but we have a defiency of F.H.
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Post by lilsissy on Jan 1, 2010 22:30:33 GMT -5
Also my daughter Elizabeth gained weight rapidly and has had two miscarriages. She began having stomach trouble at about 13 , pain and ulcer type bleeding off and on since. I did once have to pry out of her salvillary gland in he back of her throat a yeast like cheese ball that seemed to grow in it. She was so embarassed by this . They had a terrible smell and would occasional be expelled. She also has a cyst on one of her ovaries. www.pnas.org/content/104/25/10643.full
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Post by skyship on Jan 1, 2010 23:14:18 GMT -5
Now if looking at CD146(Muc18)mel-cam what shall we behold? ============================== Outside-in Signaling Pathway Linked to CD146 Engagement in Human Endothelial Cells* CD146 (S-Endo 1 Ag or MUC18) is a transmembrane glycoprotein expressed on endothelial cells on the whole vascular tree. CD146 is located at the intercellular junction where it plays a role in the cohesion of the endothelial monolayer. CD146 engagement initiates an outside- in signaling pathway involving the protein tyrosine kinases FYN and FAK as well as paxillin. Here we report that CD146 engagement by its specific monoclonal antibody in human umbilical vein endothelial cells induces a Ca21 influx that is sensitive to thapsigargin and EGTA treatment, indicating that CD146 engagement initiates a store-operated calcium mobilization. In addition, biochemical and pharmacological analysis revealed that CD146 engagement initiates the tyrosine phosphorylation of phospholipase C-g, Pyk2, and p130Cas. Pharmacological inhibition of Ca21 flux with 1,2-bis(o-aminophenoxy) ethane-N,N,N*,N*-tetraacetic acetoxymethyl ester and EGTA indicated that an increase in Ca21 is required for Pyk2 and p130Cas tyrosine phosphorylation. Moreover, a complex association was observed between Pyk2, p130Cas, and paxillin. These results indicate that CD146 is coupled to a FYN-dependent pathway that triggers Ca21 flux via phospholipase C-g activation leading subsequently to the tyrosine phosphorylation of downstream targets such as Pyk2, p130Cas, FAK, and paxillin. In addition to its role in cell-cell adhesion, CD146 is a signaling molecule involved in the dynamics of actin cytoskeleton rearrangement." www.jbc.org/content/276/2/1564.full.pdf+html================ Pretty much says it. ================ Now, piece by piece, each acronym represents genes from other organisms etc. Gene constructions. Outside in signaling pathway: "CD146 engagement initiates an outside- in signaling pathway involving the protein tyrosine kinases FYN and FAK as well as paxillin" skeletal rearrangement. skyship FAK Human endothelial cells:
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Post by lilsissy on Jan 2, 2010 0:29:03 GMT -5
Sky , I am trying so hard to keep up with you or at least run behind you shall I say,
The gag gene fromm X.M.R.V. do you think ,X.M.R.V. is what they are using on us
I see how imporatant gleaning this from your link,
This family of carbohydrates is essential or important for life.
GAGs form an important component of connective tissues. GAG chains may be covalently linked to a protein to form proteoglycans. Water sticks to GAGs, this is where the resistance to pressure comes from. The density of sugar molecules and the net negative charges attract cations. Ex: Na+, and after the sodium binds it attracts water molecules. Water does not compress, unlike gas.
Some examples of glycosaminoglycan uses in nature include heparin as an anticoagulant, hyaluronan as a component in the synovial fluid lubricant in body joints, and chondroitins which can be found in connective tissues, cartilage and tendons.
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Post by lilsissy on Jan 2, 2010 2:08:53 GMT -5
Yes the garlic is great I believe and I agree with this, acid breaks down things.
Jen
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Post by skyship on Jan 2, 2010 13:54:39 GMT -5
it involves carbohydrates, but, I do not know if the fibronectin matrix and the xmrv are related. somehow, more studies are indicating a slight connection. ========================= ......"integration of XMRV shows a strong preference for transcription start sites, CpG islands, gene-dense regions, and DNase-hypersensitive sites. In prostate cancer tissues, in addition to the aforementioned chromosomal features, XMRV integration sites are associated with frequent cancer breakpoints, common fragile sites, microRNA (miRNA), and cancer-related genes. These associations in prostate cancer tissues may represent a selection event for particular XMRV integration sites and suggest that XMRV may play a role in prostate cancer development." tinyurl.com/yfo5ulqjvi.asm.org/cgi/content/full/82/20/9964?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&fulltext=ranked&searchid= 1&FIRSTINDEX=110&resourcetype=HWFIG fragile sites..microRNA. CpG islands: =============== Comprehensive analysis of CpG islands in human chromosomes 21 and 22. Takai D, Jones PA. Department of Biochemistry and Molecular Biology, University of Southern California/Norris Comprehensive Cancer Center, Keck School of Medicine of the University of Southern California, Los Angeles, CA 90033, USA. takai_d@ccnt.hsc.usc.edu CpG islands are useful markers for genes in organisms containing 5-methylcytosine in their genomes. In addition, CpG islands located in the promoter regions of genes can play important roles in gene silencing during processes such as X-chromosome inactivation, imprinting, and silencing of intragenomic parasites. The generally accepted definition of what constitutes a CpG island was proposed in 1987 by Gardiner-Garden and Frommer [Gardiner-Garden, M. & Frommer, M. (1987) J. Mol. Biol. 196, 261-282] as being a 200-bp stretch of DNA with a C+G content of 50% and an observed CpG/expected CpG in excess of 0.6. Any definition of a CpG island is somewhat arbitrary, and this one, which was derived before the sequencing of mammalian genomes, will include many sequences that are not necessarily associated with controlling regions of genes but rather are associated with intragenomic parasites. We have therefore used the complete genomic sequences of human chromosomes 21 and 22 to examine the properties of CpG islands in different sequence classes by using a search algorithm that we have developed. Regions of DNA of greater than 500 bp with a G+C equal to or greater than 55% and observed CpG/expected CpG of 0.65 were more likely to be associated with the 5' regions of genes and this definition excluded most Alu-repetitive elements. We also used genome sequences to show strong CpG suppression in the human genome and slight suppression in Drosophila melanogaster and Saccharomyces cerevisiae. This finding is compatible with the recent detection of 5-methylcytosine in Drosophila, and might suggest that S. cerevisiae has, or once had, CpG methylation." www.ncbi.nlm.nih.gov/pubmed/11891299?dopt=Abstract================ Chromosome 21 and 22 triple helix w/down's syndrome, related to ALZ and amyloids and dystrophy gene. Notice the relationship to X related autosomal. ================== and they say xmrv and prostate cancer could involve a paracrine mechanism, and this could involve fibronectin. ======================= Additionally, XMRV integration sites in cancer tissues were associated with cancer breakpoints, common fragile sites, microRNA, and cancer-related genes, suggesting a selection process that favors certain chromosomal integration sites. In both acutely infected cells and cancer tissues, no common integration site was detected within or near proto-oncogenes or tumor suppressor genes. These results are consistent with a model in which XMRV may contribute to tumorigenicity via a paracrine mechanism. tinyurl.com/ybynsk6www.biomedexperts.com/Abstract.bme/18684813/Integration_site_preference_of_xenotropic_murine_leukemia_virus-related_virus_a_ new_human_retrovirus_associated_with_pr ======================== am looking for link now with paracrine mechanism and CpG islands, this seems all related to the XMRV. The information will expell itself when I find this link to the fibronectin. Discover as we go. This is big, because our whole genetic systems are being revamped. Skyship
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Post by aqt on Jan 2, 2010 18:50:17 GMT -5
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Post by skyship on Jan 2, 2010 19:06:17 GMT -5
Let me first put in what cytoskeleton means: Image: Cytoskeleton The eukaryotic cytoskeleton. Actin filaments are shown in red, microtubules in green, and the nuclei are in blue. The cytoskeleton (also CSK) is a cellular "scaffolding" or "skeleton" contained within the cytoplasm that is made out of protein. The cytoskeleton is present in all cells; it was once thought this structure was unique to eukaryotes, but recent research has identified the prokaryotic cytoskeleton. It is a dynamic structure that maintains cell shape, protects the cell, enables cellular motion (using structures such as flagella, cilia and lamellipodia), and plays important roles in both intracellular transport (the movement of vesicles and organelles, for example) and cellular division. The concept and the term (cytosquelette, in French) was first introduced by French embryologist Paul Wintrebert in 1931.[1] en.wikipedia.org/wiki/Cytoskeleton================== skyship
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Post by skyship on Jan 2, 2010 20:04:20 GMT -5
aqt, from that link, found this, woah Nellie! www.sciencemag.org/sciencexpress/recent.dtl================ 300 years old concept? ======================== Recurring views on the structure and function of the cytoskeleton: A 300-Year Epic Eugenio Frixione * Departamento de Biología Celular and Departamento de Fisiología, Biofísica y Neurociencias, Centro de Investigacíon y de Estudios Avanzados del IPN, México email: Eugenio Frixione (frixione@cell.cinvestav.mx) *Correspondence to Eugenio Frixione, Dept. Biología Celular, CINVESTAV del IPN, Apartado Postal 14-740, México, D.F. 07000 Funded by: CONACYT (México); Grant Number: 980201 Keywords actin filaments; filament sliding; history; microtubules; motility; movement; neurofilaments Abstract Some unnoticed or seldom remembered precedents of current views on biological motion and its structural bases are briefly outlined, followed by a concise recapitulation of how the present theory has been constructed in the last few decades. It is shown that the evolution of the concept of fibers as main constituents of living matter led to hypothesizing microscopic structures closely resembling microtubules in the 18th century. At the beginning of this period, fibers sliding over each other and driven by interposed moving elements were envisioned as the cause of muscle contraction. In the following century, an account of the mechanism of myofibril contraction visualized longitudinal displacements of myosin-containing submicroscopic rodlets. The existence of fibrils in the protoplasm of non-muscle cells, a subject of long debate in the second half of the 19th century, was virtually discarded as irrelevant or fallacious 100 years ago. The issue resurfaced in the early 1930s as a theoretical notion - the cytosquelette - nearly two decades before intracellular filamentous structures were first observed with electron microscopy. The role originally assumed for such fibrils as signal conductors is nowadays being reappraised, although under new interpretations with a much wider significance including modulation of gene expression, morphogenesis, and even consciousness. Since all of the above ancestral conceptions were eventually abandoned, the corresponding current views are, to a certain extent, recurrent. Cell Motil. Cytoskeleton 46:73-94, 2000 © 2000 Wiley-Liss, Inc. Received: 8 October 1999; Accepted: 24 March 2000 www3.interscience.wiley.com/journal/72510621/abstract==================== wow.............. have to share this with everyone! www.wiley.com/legacy/wileyblackwell/images/cytoskeleton_flyernew for 2010 skyship
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Post by skyship on Jan 4, 2010 1:12:58 GMT -5
.1 Background information CD146 (also known as MUC18, MCAM, Mel-CAM, and S-Endo-1) is a transmembrane glycoprotein belonging to the immunoglobulin superfamily and contains 5 extracellular immunoglobulin (Ig)-like domains.¹,² CD146 possesses a limited tissue distribution, including endothelial cells, smooth muscle cells, follicular dendritic cells, melanoma cells, and a sub-population of activated T lymphocytes.¹,³ CD146 is also expressed on circulating endothelial cells (cECs) and a subpopulation of endothelial progenitor cells (cEPCs)⁴ as well as on marrow stromal cells (MSCs)⁵. CD146 functions as a Ca2+-independent cell adhesion molecule that is involved in heterophilic cell-cell interactions⁶, and may be involved in the extravasion and/or homing of activated T cells³. CD146 expression in melanoma is also directly associated with tumor growth and metastasis.⁷,⁸ www.miltenyibiotec.com/download/datasheets/985/DS130-092-849-850-851-852-853.pdf================ subpopulation of endothelial progenitor cells (cEPCs)⁴ as well as on marrow stromal cells (MSCs)⁵. skyship
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Post by lilsissy on Jan 4, 2010 1:42:06 GMT -5
This is Elizabeth Miracle, Jennifer's daughter. i am writing because strangely, my blood type has changed twice. when i was born, my blood type was B positive. then about a year ago, i was getting my blood checked, and they said i was O negative. then last February, i had a miscarriage and the doctors did blood work on me, and came to the conclusion that i could have miscarried because i was a rare blood type... AB positive. so I'm not sure what has happened, but it is definitely weird.
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Post by lilsissy on Jan 4, 2010 3:20:45 GMT -5
Hair growth is activated , this certainly seems to be a factor, abnormal hair growth.
Two Proteins Enable Skin Cells To Regenerate
Never mind facial masks and exfoliating scrubs, skin takes care of itself. Stem cells located within the skin actively generate differentiating cells that can ultimately form either the body surface or the hairs that emanate from it. In addition, these stem cells are able to replenish themselves, continually rejuvenating skin and hair. Now, researchers at Rockefeller University have identified two proteins that enable these skin stem cells to undertake this continuous process of self-renewal.
The work, published in Nature Genetics, brings new details to the understanding of how stem cells maintain — and lose — their status as stem cells and are able to specialize into various types of cells. It also further dissects a ubiquitous Rube Goldberg-like pathway whose molecular gears and levers play an important role in activating stem cells to divide and transform into tissue-making cells.
Lead researcher Elaine Fuchs, head of the Laboratory of Mammalian Cell Biology and Development, and first author Hoang Nguyen, a former postdoc in the lab, worked with mice engineered to lack the proteins TCF3 and TCF4, which reside in the nucleus of skin stem cells, where they bind to DNA to turn genes off that would otherwise cause the stem cells to differentiate. They found that without TCF3 and TCF4, all of the layers of the mice’s skin still develop properly, but they cannot be maintained.
“The epidermal stem cells — one of the types of stem cells in the skin — lose their capacity to self-renew and replace skin cells that have died,” says Nguyen, who is now an assistant
professor at Baylor College of Medicine in Houston, Texas. “We show that the epidermis cannot be maintained long-term without these two proteins. And that’s what we see in the Petri dish as well as our skin-grafting experiments.”
The TCF proteins (there is a family of four) are found in many stem cells of the body. Their ability to turn genes on depends on signals they receive from their molecular environment that result in the stabilization of a partner molecule called â-catenin.
Fuchs, who is a Howard Hughes Medical Institute investigator and Rebecca C. Lancefield Professor at Rockefeller, and Nguyen have now learned that TCF3 and TCF4 can also work in skin stem cells by keeping off genes when nuclear â-catenin is not around. “In the hair follicles, TCF3 and TCF4 are required to maintain the stem cells as stem cells when â-catenin is not around, but when â-catenin is there, hair growth is activated,” says Fuchs. “In the skin epidermis, TCF3 and TCF4 apparently maintain the epidermal stem cells all by themselves, without â-catenin.”
“If the TCF proteins always act through â-catenin in the skin, then you would always see the same failures whenever â-catenin or TCF3 and TCF4 are missing,” says Nguyen. “But you don’t. The epidermis seems to rely more on TCF3 and TCF4 while hair follicles require TCF3 and TCF4 and â-catenin. This means that there is an arm of this pathway that has never been explored.”
Although the finding is new for mammalian stem cells, it has parallels in other organisms, including worms. “TCFs have ancient origins and the worm field has long believed that TCFs have functions that are not dependent upon â-catenin,” says Fuchs. The parallels between worms and mammalian skin opens new avenues of research into regenerative therapies that could illuminate how to trigger skin growth for burn victims or hair growth for those suffering from hair loss.
“Skin stem cells hold great promise for regenerative medicine,” says Fuchs. “And the more we know about what makes a stem cell a stem cell and the different cocktail of molecules that give these cells their properties, the more sophisticated we can be about understanding their basic biology and using them for the benefit of society.”
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