Amyloid III: Amyloids/Filaments All Over the Body (Morgellons?)

In most of my Morgellons research, I have crossed paths with amyloid issues.  Morgellons and Alzheimers  do have many characteristics in common.  Morgellons sufferers have been diagnosed with prions, they have fibrils, filaments and particulate matter, calculini, calcium deposits similar to Amyloid Deposits.  When Amyloid precursors are used as templates for Nanotech and other applications of  SuperMolecular Structures,  these artifacts are becoming more prominent and often cannot be separated from pathological amyloids and prions.


Image: Amyloid fibrils as templates for inorganic nanomaterials.

Protein Aggregation: From Inclusion Bodies to Amyloid and Biomaterials



When most Alzheimers studies only concern the brain, they are missing the formers of the Amyloid and many of its constituents in other areas of the body. Why cannot scientists see that amyloid, folding proteins and prions, whether from CJD, TSE or BSE, involves encephalitis and calculini and particulate matter deposition? This sees very clear. Why create amyloids when one has no idea if they will be pathogenic? Especially amyloid spherocysts covered in metallic coats. This hides the amyloid, like a Trojan Horse, or could that have been the plan? If not, then  stupidity surely reigns in the minds of these “anything goes” scientists. The path is wide, and many travel it with their “eyes wide shut”. For example, Sup35 and chaperonin Heat Shock Protein 90 and 104 were used as what is called an “evolutionary capacitor”. It was argued that it was not Evo Devo, but in truth it appears to be the opposite. It was meant to alter or transform the human condition. Humans are simply left to adapt. Also PNA’s (peptide nucleic acids) are involved. Amyloids are being found inside many body organs, Lysosome variations are apparent, Amyloids that form are related to oligomers, and dimers and monomers. Below are articles on how Amyloids. part of other diseases, are causing other proteins to misfold. Is it the pentamer units or monomer units of this altered amyloid with its “coats of many colors, metals and polymers” causing more amyloids which are often misdiagnosed as “calcium deposits”?


Insoluble amyloid-like aggregations are a common pathological characteristic in human neurodegenerative conditions such as Alzheimer’s disease and Parkinson’s disease. In the case of prion diseases such as Creutzfeld-Jacob disease, amyloidogenic forms of Prion-Protein propagate the disease by seeding the conformational changes to the non-pathogenic form. The authors of the paper do not call the Orb2 oligomers prions, as the mechanisms underlying oligomerisation are not understood. However, in the case of ApCPEB, multimerisation was shown to be self-sustaining, and hence prion-like.Is there a link between the preponderance of amyloid associated neurodegenerative diseases and the role of amyloid-like oligomers in memory? It is probably unwise to extrapolate too far from these results. However, one could postulate that if this is a widespread mechanism of memory formation, amyloid associated diseases could be more likely to affect the brain. Likewise, if amyloid-like protein multimerisation has normal physiological roles in the brain, it could be a more permissive environment for amyloid formation than other tissues. http://biobabel.wordpress.com/tag/prion/


The HET-s Prion of Podospora anserina

Podospora anserina is a filamentous fungus. Genetically compatible colonies of this fungus can merge together and share cellular contents such as nutrients and cytoplasm. A natural system of protective “incompatibility” proteins exists to prevent promiscuous sharing between unrelated colonies. One such protein, called HET-S, adopts a prion-like form in order to function properly.[2] The prion form of HET-S spreads rapidly throughout the cellular network of a colony and can convert the non-prion form of the protein to a prion state after compatible colonies have merged.[3] However, when an incompatible colony tries to merge with a prion-containing colony, the prion causes the “invader” cells to die, ensuring that only related colonies obtain the benefit of sharing resources.

 Prions of Yeast  [PSI+] & [URE3]

In 1965, Brian Cox, a geneticist working with the yeast Saccharomyces cerevisiae, described a genetic trait (termed [PSI+]) with an unusual pattern of inheritance. The initial discovery of [PSI+] was made in a strain auxotrophic for adenine due to a nonsense mutation.[4] Despite many years of effort, Cox could not identify a conventional mutation that was responsible for the [PSI+] trait. In 1994, yeast geneticist Reed Wickner correctly hypothesized that [PSI+] as well as another mysterious heritable trait, [URE3], resulted from prion forms of certain normal cellular proteins.[5] The names of yeast prions are frequently placed within brackets to indicate that they are non-mendelian in their passage to progeny cells, much like plasmid and mitochondrial DNA.

It was soon noticed that heat shock proteins (which help other proteins fold properly) such as Hsp104 were intimately tied to the inheritance and transmission of [PSI+] and many other yeast prions. Since then, researchers have unravelled how the proteins that code for [PSI+] and [URE3] can convert between prion and non-prion forms, as well as the consequences of having intracellular prions.

When exposed to certain adverse conditions, in some genetic backgrounds [PSI+] cells actually fare better than their prion-free siblings;[6] this finding suggests that the ability to adopt a [PSI+] prion form may result from positive evolutionary selection.[7] It has been speculated that the ability to convert between prion-infected and prion-free forms acts as an evolutionary capacitor to enable yeast to quickly and reversibly adapt in variable environments. Nevertheless, Wickner maintains that URE3 and [PSI+] are diseases,[8] although this claim has been challenged using theoretical population genetic models.[9]

Further investigation found that [PSI+] is the result of a self-propagating misfolded form of Sup35p, which is an important factor for translation termination during protein synthesis.[10] In [PSI+] yeast cells the Sup35 protein forms filamentous aggregates known as amyloid. The amyloid conformation is self-propagating and represents the prion state. It is believed that suppression of nonsense mutations in [PSI+] cells is due to a reduced amount of functional Sup35 because much of the protein is in the amyloid state. The Sup35 protein assembles into amyloid via an amino-terminal prion domain. The structure is based on the stacking of the prion domains in an in-register and parallel beta sheet confirmation.[11]



Fungal Proteins and Fungal Prions

A heritable switch in carbon source utilization driven by an unusual yeast prion.

Brown JC, Lindquist S.


Whitehead Institute for Biomedical Research and Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02142, USA.


Several well-characterized fungal proteins act as prions, proteins capable of multiple conformations, each with different activities, at least one of which is self-propagating. Through such self-propagating changes in function, yeast prions act as protein-based elements of phenotypic inheritance. We report a prion that makes cells resistant to the glucose-associated repression of alternative carbon sources, [GAR(+)] (for “resistant to glucose-associated repression,” with capital letters indicating dominance and brackets indicating its non-Mendelian character). [GAR(+)] appears spontaneously at a high rate and is transmissible by non-Mendelian, cytoplasmic inheritance. Several lines of evidence suggest that the prion state involves a complex between a small fraction of the cellular complement of Pma1, the major plasma membrane proton pump, and Std1, a much lower-abundance protein that participates in glucose signaling. The Pma1 proteins from closely related Saccharomyces species are also associated with the appearance of [GAR(+)]. This allowed us to confirm the relationship between Pma1, Std1, and [GAR(+)] by establishing that these proteins can create a transmission barrier for prion propagation and induction in Saccharomyces cerevisiae. The fact that yeast cells employ a prion-based mechanism for heritably switching between distinct carbon source utilization strategies, and employ the plasma membrane proton pump to do so, expands the biological framework in which self-propagating protein-based elements of inheritance operate. http://www.ncbi.nlm.nih.gov/pubmed/19797769


Evidence:  Amyloids are being found inside body organs.

Abdominal Amyloidosis: Spectrum of Radiological Findings

Received: 8 January 2003 Revised: 27 January 2003 Accepted: 1 February 2003

Amyloidosis is a disease characterized by the deposition of fibrillar protein amyloid of b-structure in organs or tissues. It is usually classified as either a primary disease or secondary to a co-existent condition, such as rheumatoid arthritis, tuberculosis, or neoplasm (particularly multiple myeloma or renal cell carcinoma). Amyloid protein deposition can be seen in a variety of organs though it occurs with higher frequency in the gastrointestinal tract, kidney, and heart. Amyloidosis can have a wide spectrum of manifestations in nearly every abdominal organ. Some of these, for example, multiple cystic submucosal masses of the stomach, amyloidosis of the gallbladder, and dirty soft tissue infiltration of the subcutaneous fat, have not yet been covered in the radiological literature. The combination of various imaging techniques and the identification of characteristic computed tomography (CT) hepatic features may help in the differentiation of amyloidosis from other infiltrative diseases; however, confirmative diagnosis can usually only be achieved by tissue biopsy. Kim, S. H. et al. (2003). Clinical Radiology 58: 610–620. http://www.mdtodate.com/mdtodate/EL_BAUL_files/Abdominal%20amyloidosis.pdf


 Amyloidosis types

December 2009

This is a duodenal biopsy specimen showing subtle amyloid deposition in the basal lamina of duodenal glands. In the upper left panel, Congo red stain gives pale orange-red reactivity with the amyloid deposits. In the upper right panel, under polarized light the deposits show characteristic apple-green birefringence. Similarly  immunohistochemistry for serum amyloid P component (SAP) labels the amyloid deposited in the basal lamina of the glands. By electron microscopy (EM), the amyloid is composed of nonbranching fibrils. http://www.mayomedicallaboratories.com/articles/hottopics/transcripts/2009/2009-12a-amyloidosis/12a-4.html



Subtypes Historical Context:

December 2009

Before the protein constituents of amyloidosis were known, the amyloidosis was classified according to clinical presentation. Those cases with no apparent cause were called primary amyloidosis. We now know that these were mostly AL (light chain) amyloidosis caused by an underlying plasma cell proliferative disorder. The amyloidoses developing secondary to underlying chronic inflammatory disorder such as tuberculosis or rheumatoid arthritis was called secondary amyloidosis. We now know that most of these were caused by abnormal deposition of an acute phase reactant, serum amyloid A (SAA) protein, and are now termed as AA amyloidosis. The other important systemic amyloid type is caused by accumulation by transthyretin or prealbumin, now called ATTR. ATTR amyloidosis can be seen sporadically in advanced age, so-called senile amyloidosis, or as part of a germline mutation affecting the TTR gene, so-called hereditary amyloidosis. http://www.mayomedicallaboratories.com/articles/hottopics/transcripts/2009/2009-12a-amyloidosis/12a-5.html


 Amyloids and Panniculitis


History of Biochemistry. Amyloids etc…


Human Serum Amyloid P component:



Peptide Nucleic Acids (PNAs)


PNA monomers











Cutaneous Lichen Amyloidosis





From  the Department  of Ophthalmology,  College  of Physicians  and  Surgeons,  Columbia University,  and  the  Institute  of Ophthalmology,  Presbyterian  Hospital,  New  York. Received  for  publication,  February  23,  1946:

Our  knowledge  of  lysozyme,  the  bacteriolytic  and  mucolytic  enzyme found  in egg white  and  in many  tissues and body  fluids,  is almost entirely based  on the  properties of  the  enzyme  obtained  from egg white.  The wide distribution  of  an  ag$nt  which  is  bacteriolytic  for  certain  micrococci, Sarcinae,  and  other  air-borne  organisms, was recognized  by  Fleming  who also  reported  its occurrence in some  plants, especially  the  turnip  (1). The  occurrence  of  a  lysozyme-like  enzyme  in  samples of  papain  was detected  when  it  was observed  that  the  high  viscosity  of  a solution  containing  a mucopolysaccharide  fraction  isolated from  Micrococcus  lysodeikticus  disappeared on  incubation  with  papain-HCN.  Bacteriological  tests showed the  presence of  a  lytic  enzyme  in  the  papain  preparation  used. http://www.jbc.org/content/163/3/733.full.pdf

Nonsense Suppression in Yeast Cells Overproducing Sup35 (eRF3) Is Caused by Its Non-heritable Amyloids. http://www.jbc.org/content/280/10/8808


From conversion to aggregation: Protofibril formation of the prion protein:


Fig. 4.

Dimensions of our PrP protofibril and higher-order oligomers. (a) A diglycosylated PrPSc-like trimer with circumferences (dashed circles) of the β-/extended core (magenta), all protein atoms (gray), and the diglycosylated protofibril (cyan). (b) Same view as in a of a 48-mer protofibril with the protein surface shown gray and the sugars shown in cyan. (c) Side view of a 48-mer protofibril. Bars at the top indicate diameters of the 35-Å extended β-core (magenta), 65-Å protein diameter (gray), and a 110-Å diglycosylated protofibril (cyan). http://ww.pnas.org/content/101/8/2293.abstract


Fundamental Patterns of Protein Structure

More than a half century ago, evidence began to accumulate that a major part of most proteins’ foldedstructure consists of two regular, highly periodic arrangements, designated  α and β.  In 1951 researchersworked out the precise nature of these arrangements.The key to both structures is the hydrogen bond.  A hydrogen atom is nothing more than a proton witha surrounding electron cloud.  When one of these atoms is chemically bonded to an electron-withdrawing atom such as nitrogen or oxygen, much of the electron cloud ves toward the nitrogen or oxygen. http://www.faseb.org/portals/0/pdfs/opa/protfold.pdf



Masel group

Ecology & Evolutionary Biology, University of Arizona

Evolutionary capacitance: theory

Biological systems have a tendency to become robust or canalized to perturbation during evolution. This leads to a buildup of cryptic genetic variation. Cryptic genetic variation may not be 100% hidden, and low residual levels of selection may act as a form of pre-screening. This removes the most deleterious alleles and leaves the remaining variation pre-enriched for potential adaptations (Masel 2006). This enrichment means that the majority of adaptations are likely to stem from cryptic genetic variation, making it of fundamental importance in evolution.

Evolutionary capacitors provide a window into cryptic genetic variation, facilitating its study. Evolutionary capacitors are molecular mechanisms that are able to tap into stocks of cryptic genetic variation. Just as an electronic capacitor stores and releases charge, an evolutionary capacitor stores and releases genetic variation. Examples include the yeast prion [PSI+], regulators of alternative splicing, phase variation and gene conversion. In fact, any complex network can have evolutionary capacitance properties, so capacitance is likely to be widespread.

The main example we study as a model system for evolutionary capacitance is the yeast prion [PSI+]. [PSI+] taps into cryptic stocks of variation beyond stop codons by causing elevated rates of readthrough translation. This can lead to faster adaptation: [PSI+] can lead to faster growth rates in stressful environments (True & Lindquist 2000). Evolutionary capacitors may therefore promote evolvability.

When variation is revealed all at once, most of it is likely to be deleterious, while only a small subset is likely to be adaptive. Selection will act to genetically assimilate this subset. For example, [PSI+] may act as a stopgap mechanism, buying yeast time to find the appropriate stop codon mutation (Giacomelli et al. 2007). Once this has occurred, capacitors such as [PSI+] are reversible, and simply disappear. This leaves the organism with a brand new adaptation but no load of other, deleterious mutations, since these disappear with [PSI+]. This reversibility is one of the factors that make evolutionary capacitance a much more potent promoter of evolvability than elevated mutation rates.

It is one thing for capacitors to promote evolvability, but another for this increased evolvability to itself be the product of natural selection. The evolution of evolvability is difficult, because natural selection acts on present costs, not future benefits. We have constructed stochastic mathematical models that balance the weak constant deleterious effects of capacitance through revealing variation at inappropriate times, the rare strongly advantageous effects of capacitance at times of environmental change, and genetic drift. We found both that evolutionary capacitance is favored by natural selection (Masel 2005; King & Masel 2007; Masel, King & Maughan 2007) and that this is by far the most likely explanation for how the ability to form [PSI+] evolved in the first place (Masel & Bergman 2003).

Our goal in this work is to understand evolutionary capacitance, and the biology of the [PSI+] prion is our guide, but along the way our theoretical models have had broader application to other related areas of evolutionary theory. These have included phenotypic plasticity, epigenetic inheritance systems, bet-hedging, and the mutational degradation of complex traits.

People most actively involved in this:  Meredith Trotter Grant Peterson,    Etienne Rajon, Yilu Wang. http://eebweb.arizona.edu/faculty/masel/research/popgen/


 For  Amyloid issues, filament formations and other Alz or Morgellons and even Lymes issues this  may be beneficial.

Power of Mustard, Cranberries, Mustard Family… Cabbage,  etc.


Please stay tuned as we gather more information and find the cause or causes of Morgellons.   Many other diseases seem to be involved with Morgellons as well. At some point we will be able to separate the organic issues from inorganic issues and find appropriate treatment. In the meantime, my motto is:

“Less Is Better”

The less antibiotics, the less artificial foods, the less gmo, sugar, the less amyloid formers the better.

The less anxiety, the less stress, the less anger, hate, the better we all are.

Whole foods, correct minerals, exercise and fun are needed. 

We need to Recreate ourselves through Recreation Now and Then.



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