Many scientists are finding that melanin issues can be related to Neurological conditions. I think we need to look at this. This is what can possibly be the "dumbed down", drug related SSRIs and the substituted melanin causing issues of Dementia. Alzheimers is a fancy word named after Altos Alzheimer. He did not name it, those after him did. The way in to control the human brain, could be from melanin, this substitute for Tyrosine.
Melanin is found in several areas of the human body including:
Skin where it provides skin color Hair Pupils or irises of the eyes Stria vascularis of the inner ear Areas of the brain, the substantia nigra and locus coeruleus The medulla and zona reticularis of the adrenal gland
Types of melanin
Some of the different types of melanin include eumelanin, pheomelanin and neuromelanin. Eumelanin is found in the hair, skin and dark areas around the nipples. It is particularly abundant among black populations and provides black and brown pigment to the hair, skin and eyes.
When eumelanin is present only in small amounts, hair may be blonde.
Pheomelanin is also found in the hair and skin. This type of melanin provides pink and red colors and is the main pigment found among red-haired individuals. This type of melanin is not as protective against UV- radiation induced cancer as eumelanin.
Neuromelanin is a form of melanin found in different areas of the brain and loss of this melanin may cause several neurological disorders.
This natural loss of melanin could be what is behind the skin, ear, brain fog, hair issues and lesions which have plaque involved. The oligomers are the substituted melanins, I believe. This involves the neurological dendrites.
Melanin: the organizing molecule. Barr FE. Abstract
The hypothesis is advanced that (neuro)melanin (in conjunction with other pigment molecules such as the isopentenoids) functions as the major organizational molecule in living systems. Melanin is depicted as an organizational "trigger" capable of using established properties such as photon-(electron)-phonon conversions, free radical-redox mechanisms, ion exchange mechanisms, and semiconductive switching capabilities to direct energy to strategic molecular systems and sensitive hierarchies of protein enzyme cascades. Melanin is held capable of regulating a wide range of molecular interactions and metabolic processes primarily through its effective control of diverse covalent modifications. To support the hypothesis, established and proposed properties of melanin are reviewed (including the possibility that (neuro)melanin is capable of self-synthesis). Two "melanocentric systems"--key molecular systems in which melanin plays a central if not controlling role--are examined: 1) the melanin-purine-pteridine (covalent modification) system and 2) the APUD (or diffuse neuroendocrine) system. Melanin's role in embryological organization and tissue repair/regeneration via sustained or direct current is considered in addition to its possible control of the major homeostatic regulatory systems--autonomic, neuroendocrine, and immunological.
"Melanin's role in embryological organization and tissue repair/regeneration via sustained or direct current is considered in addition to its possible control of the major homeostatic regulatory systems--autonomic, neuroendocrine, and immunological.".....
The interaction of L-DOPA melanin with p-tert-butylcatechol. Menter JM, Willis I. Abstract
The interaction between the skin depigmenter 4-tert-butylcatechol (tBC) and L-DOPA melanin was qualitatively studied by means of spectroscopically monitoring the binding of tBC melanin as well as the oxidation of tBC in the presence and absence of melanin. Additionally, we assessed the quantitative effect of tBC on melanin's chemical reactivity by using the reduction of potassium ferricyanide as a redox marker. The kinetics of ferricyanide reduction in the ternary (melanin/tBC/ferricyanide) system are essentially different from those in each of the binary components (i.e., melanin/ferricyanide and tBC/ferricyanide). The experiments indicate that tBC can bind to melanin (KB = 3.8 X 10(3) M-1) and that melanin can act as a "catalyst-like" electron transfer agent which couples ferricyanide reduction with tBC oxidation (k' = 1.3 X 10(-6) mole min-1). These kinetic and thermodynamic parameters may provide a means of quantitatively comparing melanins obtained from different biological and pathological situations, and they may make possible an understanding of cutaneous depigmentation processes on the molecular level.
A 1980 paper. They knew where they were going with this. It had to have a name like Alzheimers, Parkinson, Huntingtons, Paniculitis, even Pellegra are more descriptive.
....."The experiments indicate that tBC can bind to melanin (KB = 3.8 X 10(3) M-1) and that melanin can act as a "catalyst-like" electron transfer agent which couples ferricyanide reduction with tBC oxidation (k' = 1.3 X 10(-6) mole min-1). These kinetic and thermodynamic parameters may provide a means of quantitatively comparing melanins obtained from different biological and pathological situations, and they may make possible an understanding of cutaneous depigmentation processes on the molecular level.".....
Last Edit: Apr 15, 2014 12:50:33 GMT -5 by skyship
"melanin can act as a "catalyst-like" electron transfer agent"..
skin depigmenter 4-tert-butylcatechol (tBC) and L-DOPA melanin
Hyperpigmentation of the treatment site was observed in 80–100% of animals in all groups (with the exception of HQMME-treated animals, treated for only 3 weeks), which may be attributable to the use of hydrophilic ointment as the vehicle, the application procedure, or simply clipping hair from the skin. Thus, this study showed that TBHQ causes depigmentation in black guinea pigs at concentrations of 1% or greater, but that a no-effect threshold for this endpoint exists at a concentration between 0.1 and 1.0%. Keywords
This Is What Happens In Your Stomach When You Consume Packaged Ramen Noodles With a Deadly Preservative
Ramen noodles contain Tertiary-butyl hydroquinone (TBHQ), which is a by-product of the petroleum industry and food additive frequently to preserve cheap processed foods. It is one of those chemicals that is neither digestible or beneficial in any way for your body. A gastrointestinal specialist conducted an experiment with a time lapse video inside the stomach, comparing both fresh and preserved ramen noodles. After two hours of digestion, the results were staggering.
The first-of-its-kind experiment by Dr. Braden Kuo of Massachusetts General Hospital wanted to find out exactly what happens to food in the stomach and digestive tract after consuming ramen noodles.
SSo Mr. Natural Foods could not find the filament in the McNuggets? Really? It is first on the list~!
You can find TBHQ in McDonald’s chicken Mcnuggets across the United States, however Mcdonalds European chicken nuggets do not contain the toxic preservative. This is interesting since both the European Food Safety Authority (EFSA) and the FDA have evaluated TBHQ and determined that it is safe to consume at the concentration allowed in foods. The EFSA considers TBHQ to be non-carcinogenic, so why do they not allow it in chicken mcnuggets?
Other Food Products Containing TBHQ:
Mcdonalds chicken nuggets and french fries CHEEZ-IT Crackers made by Kelloggs Butterfinger chocolate and Reese’s Peanut butter cups Nestle Crunch Wheat Thins Microwave popcorn Pam cooking spray Aldi products Keebler Club crackers Kellogs eggo frozen waffles and many other kellog products Taco bell beans and some taco shells Teddy Grahams Red Barron frozen pizza Keebler Cookies TastyKake Little Debbie Kellog’s Pop-Tarts Homestyle Peanut butter cookies Some forms of soymilk Different breads cerals and crackers could contain TBHQ Crisco oil Some pet foods Many cosmetic products and baby products Some hair dyes lipsticks and eyeshadows Wrigley’s gum Little Debbies nutty bars and some M&M products KFC beans and fried chicken
There are many more processed foods not listed above which contain TBHQ. A conclusion that is now quickly reaching vast numbers is that all processed food in general, has far too many problems to be considered safe. Our regulatory agencies are not responsibly catering to the problems and instead of removing these toxins from the food supply, are claiming that safe levels exist. Since when did safe levels exist of any poison entering the body?
Effects of Hydroquinone on Cytoskeletal Organization and Intracellular Transport in Cultured Xenopus laevis Melanophores and Fibroblasts
Hydroquinone (HQ) is a synthetically produced and naturally occurring chemical that is used for example in cosmetics as a skin-lightening agent, as a reagent in photographic developers, and in rubber manufacture . It is also present in significant levels in cigarette smoke . Genomic and proteomic analyses have shown that HQ treatment induces changes in proteins that are involved in for instance oxidative stress, focal adhesion, cellular signalling, and cytoskeleton reconstruction [1–3].
...Melatonin, α-MSH, and phenylthiocarbamide were from Sigma (St. Louis, MO, USA). HQ was from Fluka (Buchs, Switzerland). Stock solutions of melatonin and α-MSH were stored at −20°C and diluted to the experimental concentrations in fresh medium just before use. Fresh stock solution of HQ was made just before each experiment. The α-tubulin antibody was from Sigma, the rhodamin marked phalloidin and the Alexa Fluor 594-conjugated secondary antibodies were from Molecular Probes (Eugene, OR, USA)..........
..........2. Cell Culture Xenopus laevis fibroblasts and melanophores were generously provided by Michael Lerner, Arena Pharmaceuticals. The fibroblasts were cultured in 0.7-x Leibovitz L-15 medium at 27°C. The medium was diluted with sterile water and supplemented with 20% fetal bovine serum, 2 mM L-glutamine, 100 IU/ml penicillin, and 100 μg/ml streptomycin. Medium that had been conditioned by fibroblasts for 3 to 4 days was then used in the melanophore culture. For depigmentation, melanophores were cultured in phenylthiocarbamide diluted in conditioned medium (900 μM) for at least six weeks. Cell culture reagents were obtained from Life Technologies (Renfrewshire, Scotland) and cell culture......
...3.3. HQ Affects Cytoskeletal Morphology
The light microscopy results indicate that HQ has an impact on the melanophore cytoskeleton, and we used antibodies directed against tubulin and rhodamin-labelled phalloidin to study the effects of HQ on melanophore microtubules and actin filaments.It has been previously implied that sensitivity to the cytotoxic effects of HQ is associated with the presence of tyrosinase activity , and in order to investigate whether pigment-containing cells are more sensitive we also imaged the cytoskeleton in fibroblasts and depigmented melanophores. Depigmented melanophores have no active pigment production, and fibroblasts lack the ability to produce melanin. The black melanosomes quench some fluorescence, and therefore the pigmented melanophores were preaggregated with melatonin before incubation with drugs and immunostaining. Due to their reduced adhesion to the substrate, effects on the cytoskeleton could not be studied in cells treated with 100 μM HQ. They detached from the cover slips during the staining procedure.
In untreated melanophores, pigmented as well as depigmented microtubules radiate from the cell centre to the periphery in a complicated network (Figures 3(a) and 3(d)). After incubation with 10 μM HQ, the microtubules were mostly unaffected, but in some cells microtubules were bundled in the central parts of the cell but remained individual in the periphery (Figures 3(b) and 3(e)). The cellular organization of microtubules was severely affected in pigmented melanophores treated with 50 μM HQ (Figure 3(c)). The microtubules appeared to be bundled and were thicker than in control cells. The microtubules in depigmented melanophores were much less affected and no bundles were observed (Figure 3(f)). Microtubules in fibroblasts also radiate from the cell centre to the periphery, and HQ did not affect the α-tubulin distribution in any of the concentrations tested (Figures 3(g)–3(i)).
fig3 Figure 3: Distribution of microtubules in cultured melanophores and fibroblasts, revealed by immunoreactivity. Scale bar = 50 μm. (a–c): pigmented melanophores with aggregated pigment. (d–f): depigmented melanophores. (g–i): fibroblasts.........
Chlorination of hydroquinone US 4439595 A Abstract Chlorination of hydroquinone by reacting sulfuryl chloride with hydroquinone in an alkyl ester solvent having 2-8 carbon atoms yields a mixture containing a major proportion of monochlorohydroquinone.
Each of these known processes is economically or technically disadvantageous in that it requires the use of superatmospheric conditions, employs benzoquinone as the starting material, produces an unacceptably high amount of polychlorinated hydroquinone, produces tar-like by-products which cause the product to be discolored, or gives poor conversion of hydroquinone. Thus, these prior art processes are not entirely suitable for preparing monochlorohydroquinone containing relatively low amounts of starting material and polychlorohydroquinone.
We have discovered that monochlorohydroquinone can be prepared by treating hydroquinone with chlorine in hydrochloric acid at a temperature of 100° to 105° C. Carrying out the reaction at 100° to 105° C. is important since the use of lower temperatures results in the formation of a black, tarry material of no practical utility. We have also found that the hydrochloric acid reaction material should contain at least one mole of hydrogen chloride per mole of hydroquinone reactant. While a molar excess of hydrogen chloride, e.g. a hydrogen chloride:hydroquinone ratio as high as five, may be used there normally is no advantage to do so.
Tyrosine Aminotransferase (TAT, Richner-Hanhart syndrome): TAT converts tyrosine into p-hydroxyphe- nylpyruvate. Glucocorticoid hormones induce it. TAT deficiency occurs rarely in humans and is controlled by a recessive gene (ca. 11 kb, 12 exons) in human chromosome 16q22.1-q22.3 (and mouse in chromosome 8). The condition involves elevated level of tyrosine and in some cases an increased urinary excretion of p-hydroxyphenylpyruvate and hydroxy- phenylacetate. The disease generally involves corneal ulcer, palm keratosis (callous skin), and mental and physical retardation. The mitochondrial enzyme is under the control of another gene. A TAT regulator gene may be located in the human X-chromosome and glutamic oxaloacetic transaminase (16q21) also regulates its activity. ►tyrosine, ►tyrosinemia
Tyrosine Hydroxylase (TYH): TYH is encoded in human chromosome 11p15 (mouse chromosome 7), which controls the synthesis of dopamine from phenylalanine. Dopamine is a hormone involved with adrenergic neurons, the sympathetic nerve fibers that liberate norepinephrine when an impulse passes the nerve synapse. This enzyme may play a key role in fetal development and in manic depression. The microsatellite sequence in the first intron serves normally as a transcriptional enhancer of the gene. ►tyrosine, ►manic depression, ►DOPA; Albanese V et al 2001 Hum Mol Genet 10:1785.
\ dopamine from phenylalanine. Dopamine is a hormone involved with adrenergic neurons, the sympathetic nerve fibers that liberate norepinephrine when an impulse passes the nerve synapse.
"Trosine Kinases (protein tyrosine kinase): Tyrosine kinase activity is essential for many processes of the signal transduction, tissue differentiation involving oncogenesis, and signaling to immunoreceptors. The most frequently activated proteins are phospholipase C-y, phosphatidylinositol 3-kinase, and GTPase activating kinase. ►oncogenes ABL, ►ARG, ►Blk,
An update on oxidative stress-mediated organ pathophysiology
Research in this area is essential as the knowledge on cellular survival and death would help in designing effective therapeutic strategies that are needed for the maintenance of the normal physiological functions of the body. In this regard, naturally occurring bio-molecules can be considered as potential therapeutic targets as they are normally available in commonly consumed foodstuffs and are thought to have minimum side effects. This review article describes the detailed mechanisms of oxidative stress-mediated organ pathophysiology and the ultimate fate of the cells either to survive or to undergo necrotic or apoptotic death. The mechanisms underlying the beneficial role of a number of naturally occurring bioactive molecules in oxidative stress-mediated organ pathophysiology have also been included in the review. The review provides useful information about the recent progress in understanding the mechanism(s) of various types of organ pathophysiology, the complex cross-talk between these pathways, as well as their modulation in stressed conditions. Additionally, it suggests possible therapeutic applications of a number of naturally occurring bioactive molecules in conditions involving oxidative stress. Abbreviations
Yu Chen, University of Washington, Seattle, Washington, USA Gabriele Varani, University of Washington, Seattle, Washington, USA
Published online: June 2010
Full Article on Wiley Online Library
Abstract Images References
Ribonucleic acid (RNA) molecules perform their function in living cells by adopting specific and highly complex 3‐dimensional structures. Like proteins, RNA structure can be described in terms of its primary (sequence), secondary (hairpins, bulges and internal loops), tertiary (A‐minor motif, 3‐way junction, pseudoknot, etc.) and quaternary structure (supermolecular organisation). Watson–Crick base pairs as well as other noncanonical base interactions are the basic building blocks of RNA secondary and tertiary structures. Metal ions are essential for the stabilisation of RNA tertiary structures and for catalytic function. In the past decade, there has been a tremendous advance in RNA structure determination, with the successful determination of the ribosome structures, as well as many other folded large RNAs. These studies have given us a unique new opportunity to understand the structure–function relationship of RNA molecules to an unprecedented level of insight. Key Concepts:
Double helical tracts separated by single‐stranded nucleotides represent the basic building block of RNA structure.
Hairpins (or stem–loops) are the most common element of RNA secondary structure.
RNA secondary structure can generally be predicted successfully from sequence analysis and thermodynamic calculation.
RNA secondary structure is generally more stable than its tertiary structure.
RNA three‐dimensional structures form by joining together the different secondary structure elements through the formation of long‐range tertiary interactions.
Coaxial stacking between double‐stranded helices at junctions where helices come together is a major determinant of higher order RNA tertiary structure.
Multivalent ions are often important for thermodynamic stabilisation and catalytic activities of RNA tertiary structures.
tRNA secondary structureAll tRNAs have similar sequences of 73 to 93 nucleotides 3' end always terminates with the sequence CCA, with the 3' hydroxyl of the ribose of the terminal A being the point of covalent attachment of the amino acid Contain a number (7-15%) of unique/modified bases. These are post-transcriptionally modified after synthesis by RNA polymerase. In particular, adenosine (A) in first or 5' position of the anticodon (corresponding to the third or 3' position of the codon) is always modified to inosine (I) which lacks the amino group on the purine ring. Inosine can base-pair with A, U or C and thus accounts for much of the degeneracy of the Genetic Code ("Wobble Theory"). tRNAs have cloverleaf secondary structure due to four base-paired stems The cloverleaf contains three non-base-paired loops: D, anticodon, and TpsiC loop
Nucleic acid tertiary structure From Wikipedia, the free encyclopedia (Redirected from RNA Tertiary Structure) Example of a large catalytic RNA. The self-splicing group II intron from Oceanobacillus iheyensis.
The tertiary structure of a nucleic acid is its precise three-dimensional structure, as defined by the atomic coordinates. RNA and DNA molecules are capable of diverse functions ranging from molecular recognition to catalysis. Such functions require a precise three-dimensional tertiary structure. While such structures are diverse and seemingly complex, they are composed of recurring, easily recognizable tertiary structure motifs that serve as molecular building blocks. Some of the most common motifs for RNA and DNA tertiary structure are described below, but this information is based on a limited number of solved structures. Many more tertiary structural motifs will be revealed as new RNA and DNA molecules are structurally characterized. en.wikipedia.org/wiki/RNA_Tertiary_Structure
Last Edit: Apr 15, 2014 18:21:53 GMT -5 by skyship
Molecular Biology of Small Heat Shock Proteins associated with Peripheral Neuropathies
Anne Holmgren, Neurogenetics Laboratory, Institute Born Bunge, Antwerpen, Belgium Delphine Bouhy, Neurogenetics Laboratory, Institute Born Bunge, Antwerpen, Belgium Vincent Timmerman, Neurogenetics Laboratory, Institute Born Bunge, Antwerpen, Belgium
Published online: November 2012
Full Article on Wiley Online Library
Abstract Images References
Heat‐shock proteins (HSPs) are molecular chaperones that protect the cell from various types of stress. Although regulated by stress, some of these proteins are constitutively expressed and responsible for quality control and protein folding. Based on their molecular weight, the HSP family mainly consists of two groups: large and small HSPs. The large HSPs require adenosine triphosphate (ATP) for their functioning, whereas the small HSPs (HSPBs) are ATP independent. The latter bind improperly folded proteins and assist in the targeting process for refolding or degradation. These HSPBs are not only molecular chaperones but they are also involved in many essential cellular processes such as apoptosis, autophagy, splicing, cytoskeleton dynamics and neuronal survival. This review focusses on the small HSPs HSPB1, HSPB3 and HSPB8, as mutations in these proteins are causative for Charcot–Marie–Tooth (CMT) disease and distal hereditary motor neuropathies (dHMN). Moreover, this review discusses the functional consequences of these mutations and their role in the length‐dependent neurodegeneration typical of CMT diseases. Key Concepts:
The molecular signature of the small HSPs is the conserved α‐crystallin domain.
Mutations in HSPB1, HSPB3 and HSPB8 are associated with dHMN and CMT subtypes.
Mutant HSPB1 causes instability of the cytoskeletal elements and therefore disorganisation of the neuronal cytoskeleton could underlie the peripheral neuropathies.
Mutant HSPB8 may induce pathomechanisms leading to CMT diseases through a loss of autophagy function, rather than a toxic gain of function.
The HSPB3 protein differs considerably from the other members regarding sequence similarity such as the poor conservation in the N‐terminal region and the very short C‐terminal domain.
It remains fragmentary how mutations in these small HSPs initiate a molecular cascade leading to progressive axonal degeneration.
Keywords: HSPB1; HSPB3; HSPB8; mutation; neurodegeneration; Charcot–Marie–Tooth disease; dHMN; apoptosis; autophagy Related Sub-Topics: Neurobiology of Disease | Mutational Mechanisms of Genetic Disease | Specific Genetic Disorders | Protein Folding, Evolution and Degradation
That type IV secretion is the crystallized protein. Radiobacter........ so must be loaded with melanin? That phoney goo.
this is why ALZ and even Lymes is chronic, the repeat units.
Based on this, we speculate that amoeba favor the transfer of genes as phagocytic protists, which allows for intraphagocytic survival and, as a consequence, promotes the creation of potential pathogenic organisms.
A perpetual cycle.
the amoeba fits nicely into the the area of the pineal gland. Then they went to artificial melanin for the AI. Amoeboes look like the neurojunctions. So, they used form instead of design. Create the form than synthesize it into AI medium, right?
Last Edit: Apr 15, 2014 18:30:44 GMT -5 by skyship
A putative (nasty) protein for the devoluton or to devolve the human species. Supposedly done before the New Human Species is introduced. Those proteins that conform will integrate the amoeba or geo/bio/chem/photon form, particle, wave or bioilluminance, just to keep track of our reactions
I think our DNA is speaking for itself. so, rejecting these would say "we do not participate" in this evil amoeba from hades.
Last Edit: Apr 15, 2014 18:58:11 GMT -5 by skyship
tash: Hi skizit, I have watched all your videos on youtube and cant thank you enough for all you have educated me on. I cry for you alot and a bit for me. I was wanting to send you photos of what is raining down everyday here in Australia in hope you can tell me
Dec 11, 2019 23:28:22 GMT -5
tash: not sure where to send them as hush mail and rocket mail bounced back
Dec 11, 2019 23:30:03 GMT -5