Doxycycline stops Prion Protein Infections

Topics with scientific, medical or general health related information and discussion that is not specifically related to Lyme disease.
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Re: Doxycycline stops Prion Protein Infections

Postby Pandora » Sun 24 Aug 2014 3:23

Wow! Two new Winners!
At this rate it won't be no time before the people suffering neurological sindumbs, psych, and cancers are afforded more than 10 days of antibiotics according to the guidelines for the infections that cause it and treatment for the immune suppression the infections cause....
Cell Mol Biol Lett. 2014 Aug 20. [Epub ahead of print]
The role of advanced glycation end products in various types of neurodegenerative disease: a therapeutic approach.
Salahuddin P1, Rabbani G, Khan RH.
Mol Neurobiol. 2014 Aug 21. [Epub ahead of print]
Potential of Cellular and Animal Models Based on a Prion-Like Propagation of α-Synuclein for Assessing Antiparkinson Agents.
Sato H1, Kato T, Arawaka S.

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Re: Doxycycline stops Prion Protein Infections

Postby Pandora » Sat 13 Sep 2014 19:25

An Isoprenylation and Palmitoylation Motif Promotes Intraluminal Vesicle Delivery of Proteins in cells

from different species...

PLoS One. 2014 Sep 10;9(9):e107190. doi: 10.1371/journal.pone.0107190. eCollection 2014.

Oeste CL1, Pinar M2, Schink KO3, Martínez-Turrión J1, Stenmark H3, Peñalva MA2, Pérez-Sala D1. ... ne.0107190


The C-terminal ends of small GTPases contain hypervariable sequences

which may be posttranslationally modified by defined lipid moieties.

The diverse structural motifs generated direct proteins towards specific cellular membranes or organelles.

However, knowledge on the factors that determine these selective associations is limited.

Here we show, using advanced microscopy, that the isoprenylation and palmitoylation motif of human RhoB (–CINCCKVL) targets chimeric proteins to intraluminal vesicles of endolysosomes in human cells,

displaying preferential co-localization with components of the late endocytic pathway.

Moreover, this distribution is conserved in distant species, including cells from amphibians, insects and fungi.

Blocking lipidic modifications results in accumulation of CINCCKVL chimeras in the cytosol, from where they can reach endolysosomes upon release of this block.

Remarkably, CINCCKVL constructs are sorted to intraluminal vesicles in a +++++cholesterol-dependent process.+++++

In the lower species, neither the C-terminal sequence of RhoB, nor the endosomal distribution of its homologs are conserved;

in spite of this, CINCCKVL constructs also reach endolysosomes in Xenopus laevis and insect cells.

Strikingly, this behavior is prominent in the filamentous ascomycete fungus Aspergillus nidulans,

in which GFP-CINCCKVL is sorted into endosomes and vacuoles in a lipidation-dependent manner and allows monitoring endosomal movement in live fungi.

In summary, the isoprenylated and palmitoylated CINCCKVL sequence constitutes a specific structure which delineates an endolysosomal sorting strategy

operative in phylogenetically diverse organisms.

PS: It's Not Cholesterol ... index.html
Last edited by Pandora on Fri 21 Nov 2014 3:48, edited 1 time in total.

Posts: 252
Joined: Tue 20 Mar 2012 14:58

Re: Doxycycline stops Prion Protein Infections

Postby Pandora » Mon 15 Sep 2014 10:16

J Biol Chem. 2014 Sep 12. pii: jbc.M114.559450. [Epub ahead of print]
Acid-induced Molten Globule State of a Prion Protein: Crucial Role of Strand 1-Helix 1-Strand 2 Segment.
Honda RP1, Yamaguchi KI1, Kuwata K2.
Author information

The conversion of a cellular prion protein (PrPC) to its pathogenic isoform (PrPSc) is a critical event in the pathogenesis of prion diseases.

Pathogenic conversion is usually associated with the oligomerization process; therefore, the conformational characteristics of the pre-oligomer state may provide insights into the conversion process.

Previous studies indicate that PrPC is prone to oligomer formation at low pH, but the conformation of the pre-oligomer state remains unknown.

In this study, we systematically analyzed the acid-induced conformational changes of PrPC and discovered a unique acid-induced molten globule state at pH 2.0 termed ″ A-state″.

We characterized the structure of the A-state using far/near-UV CD, 1-anilino-8-naphthalene sulfonate (ANS)-fluorescence, size exclusion chromatography, and NMR.

Deuterium exchange experiments with NMR detection revealed its unique structure ever reported thus far,

i.e., the Strand 1-Helix 1-Strand 2 segment at the N-terminal was preferentially unfolded,

while the Helix 2-Helix 3 segment at the C-terminal remained marginally stable.

This conformational change could be triggered by the protonation of Asp144, Asp147, and Glu196 followed by disrupture of key salt bridges in PrPC.

Moreover, the initial population of the A-state at low pH (2.0-5.0) was well correlated with the rate of the β-rich oligomer formation,

suggesting that the A-state is the pre-oligomer state.

Thus, the specific conformation of the A-state would provide crucial insights into the mechanisms of oligomerization

and further pathogenic conversion, as well as facilitate the design of novel medical chaperones for treating prion diseases.
I really like the name--A-state! LOL

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Re: Doxycycline stops Prion Protein Infections

Postby Pandora » Thu 6 Nov 2014 22:17

All you PARENTS with Vaccine damaged kids..THIS IS THE NIH ADMITTING IT......The infections they gave you cause it...We'll worry bout them doctors and nurses they continue to infect later---they'll figure it out when there are none!

Lipolysaccharide-Induced Neuroinflammation Is Associated with Alzheimer-Like Amyloidogenic Axonal Pathology and Dendritic Degeneration in Rats

The bacterial endotoxin lipopolysaccharide (LPS) can induce chronic neuroinflammation in rodents [36]–[38]. LPS administration also causes learning and memory deficits in the animals, providing an excellent model system for studying cognitive dysfunction associated with chronic neuroinflammation [39]–[41]. Neuroinflammation is considered to play an early or inductive role in the development of AD pathologies, although the anatomic evidence remains to be better formulated. Therefore, the present study was set to address whether intracerebral LPS injection in adult rats may induce axonal and dendritic pathologies similar to that seen in AD [32]
Now them rats didn't get the infectious vaccines we got for decades......
They have been told many times in many ways but for som reason the Congress cannot see fit to give US a Surgeon General who will have authority over the NIH/CDC.....LOL

Vaccine damaged kids.----------Syndrome sufferers and Morgellons sufferers-----
Exogenous amyloidogenic proteins function as seeds in amyloid β-protein aggregation
April 2014
Kenjiro Ono | Ryoichi Takahashi | Tokuhei Ikeda | Mineyuki Mizuguchi | Tsuyoshi Hamaguchi | Masahito Yamada

Abstract: Amyloid β-protein (Aβ) aggregation is considered to be a critical step in the neurodegeneration of Alzheimer's disease (AD).

In addition to Aβ, many proteins aggregate into the amyloid state,

in which they form elongated fibers with spines comprising stranded β-sheets.

However, the cross-seeding effects of other protein aggregates on Aβ aggregation pathways are not completely clear. To investigate the cross-seeding effects of exogenous and human non-CNS amyloidogenic proteins on Aβ aggregation pathways, we examined whether and how sonicated fibrils of casein, fibroin, sericin, actin, and islet amyloid polypeptide affected Aβ40 and Aβ42 aggregation pathways using the thioflavin T assay and electron microscopy.

Interestingly, the fibrillar seeds of all amyloidogenic proteins functioned as seeds.

The cross-seeding effect of actin was stronger but that of fibroin was weaker than that of other proteins.

Furthermore, our nuclear magnetic resonance spectroscopic studies identified the binding sites of Aβ with the amyloidogenic proteins.

Our results indicate that the amyloidogenic proteins,

+++including those contained in foods and cosmetics,+++

contribute to Aβ aggregation by binding to Aβ, suggesting their possible roles in the propagation of Aβ amyloidosis.
Page 2.....
Pulse-field electrophoresis indicates full-length Mycoplasma chromosomes range widely in size. ... 22/?page=1

Antigenic variable as your Ana.....

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Re: Doxycycline stops Prion Protein Infections

Postby Pandora » Tue 23 Dec 2014 9:59

The junk infectious DNA they have growing in us recombining in the prion synergy of spirochetal prion proteins is much worse than anyone imagined------NOT so called "Failure to Prune Synapses" that they would like for you to believe----
Int J Cardiol. 2015 Jan 15;178:55-62. doi: 10.1016/j.ijcard.2014.10.133. Epub 2014 Oct 23.
Infectious agents and inflammation in donated hearts and dilated cardiomyopathies related to cardiovascular diseases, Chagas' heart disease, primary and secondary dilated cardiomyopathies.

Sci Rep. 2014 Dec 3;4:7301. doi: 10.1038/srep07301.
Prion protein- and cardiac troponin T-marked interstitial cells from the adult
myocardium spontaneously develop into beating cardiomyocytes.
Omatsu-Kanbe M1, Nishino Y1, Nozuchi N1, Sugihara H2, Matsuura H1.
Author information
Atypically-shaped cardiomyocytes (ACMs) constitute a novel subpopulation of beating heart cells
found in the cultures of cardiac myocyte-removed crude fraction cells obtained from adult mouse cardiac ventricles.

Although ~500 beating ACMs are observed under microscope in the cell
cultures obtained from the hearts of either male or female mice, the
origin of these cells in cardiac tissue has yet to be elucidated due to
the lack of exclusive markers.
In the present study, we demonstrate the efficacy of cellular prion protein (PrP) as a surface marker of ACMs.

Cells expressing PrP at the plasma membrane in the culture of the
crude fraction cells were found to develop into beating ACMs

or fuse with each other to become larger multinuclear beating ACMs.

Combining PrP with a cardiac-specific contractile protein cardiac
troponin T (cTnT) allowed us to identify native ACMs in the mouse
cardiac ventricles as either clustered or solitary cells.
and cTnT-marked cells were also found in the adult, even aged, human
cardiac ventricles.

These findings suggest that interstitial cells
marked by PrP and cTnT, native ACMs,

exhibit life-long survival in the cardiac ventricles of both mice and humans.
Stealth Infected Parasites

Borrelia Seeks Vectors ... JY-W_8AAOc

At the current rate of the infected they call Autism by 2025--every second child will be severely infected.
By 2050 there will be no one with half a brain to fix you. Simply because they refuse to stop and treat the cause they gave us for decades and the immune suppression those infections always caused.

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Re: Doxycycline stops Prion Protein Infections

Postby Pandora » Sat 26 Sep 2015 20:38
In this study, we were able to extract cellular PrP (PrPC)

from plasma-derived exosomes

by a simple, fast method without the use of differential ultracentrifugation and to visualize it by Western blotting, reducing the presence of most plasma proteins. This result confirms

that blood is capable of releasing PrP in association with exosomes

and could be useful to better study its role in TSEs pathogenesis.

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Re: Doxycycline stops Prion Protein Infections

Postby Pandora » Sat 26 Sep 2015 20:44

Conventional immunohistochemistry (IHC) identified 3/19 CWD positive dams, whereas a more sensitive assay - the serial protein misfolding cyclic amplification (sPMCA) - detected CWD prion seeding activity (PrPCWD) in 15/19 dams.

PrPCWD distribution in tissues was widespread and included the central nervous system (CNS), lymphoreticular system (LRS), reproductive, secretory, excretory and adipose tissues. Interestingly, five of fifteen sPMCA positive dams showed no evidence of PrPCWD in either CNS or LRS, sites typically assessed in diagnosing CWD.

Analysis of fetal tissues harvested from the fifteen sPMCA positive dams revealed PrPCWD in 80% of fetuses (12/15), regardless of gestational stage.

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Re: Doxycycline stops Prion Protein Infections

Postby Pandora » Mon 28 Sep 2015 6:48

Still trying to figure out how they give vaccines with 95% of the pop's already infected.....
Structural and functional analysis of BB0689 from Borrelia burgdorferi, a member of the bacterial CAP superfamily.

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Re: Doxycycline stops Prion Protein Infections

Postby Pandora » Tue 29 Sep 2015 6:25

We have, for the first time, systematically analyzed samples of Aβ 42 peptide supplied by five different companies (Anaspec, Invitrogen, Enzo, Sigma-Aldrich, and SynthAssist) and obtained evidence of significant variability, including lot to lot variations.

"""All studied samples formed amyloid-like fibrils at pH3-6,'"'

and the fibrils contained cross-β structures.

Samples from Anaspec, Invitrogen, and Enzo formed one particular type of amyloid-like fibrils,

while the samples from Sigma-Aldrich and SynthAssist formed another distinct type of fibrils.

The observed polymorphism emphasizes the capacity of the Aβ 42 peptide to act as a prion agent with varying structural characteristics. The presented data have allowed us to propose a possible mechanism of formation of amyloid-like fibrils.

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