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From: TSS ()
Subject: Re: Association between Deposition of Beta-Amyloid and Pathological Prion Protein in Sporadic Creutzfeldt-Jakob Disease
Date: March 27, 2008 at 11:45 am PST

In Reply to: Re: Association between Deposition of Beta-Amyloid and Pathological Prion Protein in Sporadic Creutzfeldt-Jakob Disease posted by TSS on March 27, 2008 at 10:57 am:

Subject: CJD or Alzheimer's, THE PA STUDY...full text
Date: May 7, 2001 at 10:24 am PST

Diagnosis of dementia:
Clinicopathologic correlations

Francois Boller, MD, PhD; Oscar L. Lopez, MD; and John Moossy, MD

Article abstract--Based on 54 demented patients consecutively autopsied at the University of Pittsburgh, we studied the accuracy of clinicians in predicting the pathologic diagnosis. Thirty-nine patients (72.2%) had Alzheimer's disease, while 15 (27.7%) had other CNS diseases (four multi-infarct dementia; three Creutzfeldt-Jakob disease; two thalamic and subcortical gliosis; three Parkinson's disease; one progressive supranuclear palsy; one Huntington's disease; and one unclassified). Two neurologists independently reviewed the clinical records of each patient without knowledge of the patient's identity or clinical or pathologic diagnoses; each clinician reached a clinical diagnosis based on criteria derived from those of the NINCDS/ADRDA. In 34 (63 %) cases both clinicians were correct, in nine (17%) one was correct, and in 11 (20%) neither was correct. These results show that in patients with a clinical diagnosis of dementia, the etiology cannot be accurately predicted during life.

NEUROLOGY 1989;39:76-79


full text ;


http://www.vegsource.com/talk/madcow/messages/9249.html


From: TSS (216-119-130-151.ipset10.wt.net)
Subject: Evaluation of Cerebral Biopsies for the Diagnosis of Dementia
Date: May 8, 2001 at 6:27 pm PST

Subject:
Evaluation of Cerebral Biopsies for the Diagnosis of Dementia
Date:
Tue, 8 May 2001 21:09:43 -0700
From:
"Terry S. Singeltary Sr."
Reply-To:
Bovine Spongiform Encephalopathy
To:
BSE-L@uni-karlsruhe.de


######### Bovine Spongiform Encephalopathy #########

Evaluation of Cerebral Biopsies for the
Diagnosis of Dementia

Christine M. Hulette, MD; Nancy L. Earl, Md; Barbara J. Crain, MD, Phd

∑ To identify those patients most likely to benefit from a cerebral
biopsy to diagnose dementia, we reviewed a series of 14 unselected
biopsies performed during a 9-year period (1980 through 1989) at Duke
University Medical Center, Durham, NC. Pathognomonic features allowed a
definitive diagnosis in seven specimens. Nondiagnostic abnormalities but
not diagnostic neuropathologic changes were seen in five additional
specimens, and two specimens were normal. Creutzfeldt-Jakob disease was
the most frequent diagnosis. One patient each was diagnosed as having
Alzheimer's disease, diffuse Lewy body disease, adult-onset Niemann-Pick
disease, and anaplastic astrocytoma. We conclude that a substantial
proportion of patients presenting clinically with atypical dementia are
likely to receive a definitive diagnosis from a cerebral biopsy.
However, in those with coexisting hemiparesis, chorea, athetosis, or
lower motor neuron signs, cerebral biopsies are less likely to be
diagnostic.
(Arch Neurol. 1992;49:28-31)


full text ;


http://www.vegsource.com/talk/madcow/messages/9254.html

From: TSS (216-119-138-130.ipset18.wt.net)
Subject: CJD or Alzheimer's or the same ???
Date: April 29, 2001 at 11:53 am PST

Subject:
CJD or Alzheimer's or the same ???
Date:
Sun, 29 Apr 2001 12:45:28 -0700
From:
"Terry S. Singeltary Sr."
Reply-To:
Bovine Spongiform Encephalopathy
To:
BSE-L@uni-karlsruhe.de


######### Bovine Spongiform Encephalopathy #########

Greetings List,

thought some might be interested in this. I
have always wondered if CJD and or all TSEs
and Alzheimer's could be linked. i have been
of the opinion that Alzheimer's is a TSE for
a long time, just at the low end of the titre
of infectivity scale. i also believe in the accumulation theory. by dose, you could be killed by one sitting, or one injection, or one whatever, depending on the titre of infectivity of that whatever. on the other hand, if the dose is not a lethal dose, over a period of time, the accumulation will become lethal (if
consumption continued), and i believe the route/source/titre of infectivity, will be a key roll to the incubation period, and symptoms.

just my opinion...

Prusiner has spent the last 18 years trying to distance himself from a joint paper with GG
Glenner in which prion diseases were recognized
as just another amyloid. The recent keynote
speech was especially amusing/annoying in that
now he is completely turning the tables, trying
to adsorb some strains of Alzheimer etc into "prions." The fact is, cross-recruitment has
been a standard topic in amyloidoses since the
late 70's.

Who would want plasma from someone with the ApoA2 mutation below, given that it can recruit the normal protein?

-=-=-

The context of the paper below is systemic hereditary amyloidosis, by which they mean an inherited condition with amyloid spread far and wide by the circulatory system. Damage from cross-beta fibril deposition occurs in kidneys, heart, periferal neurons, liver, or cornea. in contrast to CNS amyloid like CJD or AD.

The first was observed in 1950 by Ostertag,
though it wasn't until 1978 that a constituent protein was identified (transthyretin, today 77 known mutational forms). Table I of the paper
lists cystatin C (1 mutation), gelsolin (2), apolipoprotein A1 (9), lysozyme (2), and fibrinogen Aalpha (4).

None of these proteins are related. There are no sequence similarities or shared motifs. Most
have alpha helix; large semi-speculative literature has these destablized by mutation or amphipathic with respect to beta sheet, or
kinetically trapped during folding.

About a quarter of the mutations are frameshifts
or stop codon read-thrus, ie mutations that generate random, unadapted polypeptide stretches. They are generally autosomal dominant,
indicative of toxic gain-of-function, eg fibril formation. This means heterozygous; sometimes the normal product is recruited to amyloid, the
mutant product is always there.

In some amyloids, the entire protein is present;
in others just a proteolytic fragment. In the
case here, the entire normal protein, as well as the extended read-through product, was found in amyloid. The patient studied spent 9 years on hemodialysis during which considerable
readsorption of amyloid occurred, ie amyloid formation is balanced against amyloid
degradation.

The most interesting observation in this paper is that there are now 4 lipid binding proteins seen
in amyloid, serum amyloid A, ApoA1, ApoE, and
now ApoA2.

"As a class, these proteins exist in a partly folded state in solution. The helical content is increased and stabilized upon binding to lipid
...
any change in lipid metabolism or mutation in the protein that alters lipid binding will favor aggregatin and fibrillogenesis." That suggests that some apoA2 cases will appear sporadic, eg, be attributable to the disruption of lipid metabolism rather than be a mutation in this gene.

A New Human Hereditary Amyloidosis: The Result of
a Stop-Codon Mutation in the Apolipoprotein AII Gene Genomics pp. 272-277 (doi:10.1006/geno.2000.6499) published electronically April 02,
2001

Merrill D. Benson1, ... Barbara Kluve-Beckerman
Telephone: (317) 278-3428. E-mail: mdbenson@iupui.edu.

Hereditary systemic amyloidosis may be caused by mutations in a number of plasma proteins including transthyretin, apolipoprotein AI, fibrinogen
A-chain, lysozyme, and gelsolin. Each type of amyloidosis is inherited as an autosomal dominant disease and is associated with a structurally
altered protein that aggregates to form amyloid fibrils. Here we report that the amyloid protein
in a family with previously uncharacterized hereditary renal amyloidosis is apolipoprotein AII (apoAII) with a 21-residue peptide extension on
the carboxyl terminus. Sequence analysis of the apoAII gene of affected individuals showed heterozygosity for a single base substitution in the apoAII stop codon. The mutation results in extension of translation to the next in-frame stop codon 60 nucleotides downstream and is predicted to give a 21-residue C-terminal extension of the apoAII protein identical to that found in the amyloid. This mutation produces a novel Bst NI restriction site that can be used to identify individuals with this gene by restriction fragment length polymorphism analysis. This is the first report of apoAII amyloid in humans and the first
mutation identified in apoAII protein. Amyloid fibril formation from apoAII suggests that this lipoprotein, which is predicted to have an
amphipathic helical structure, must undergo a transition to a beta -pleated sheet by a mechanism shared by other lipoproteins that form amyloid.


=-=-=-=-=
This can't be studied in the human genome because it lies in a wholly unsequenced region.
987696512-14444-6374


MKLLAATVLLLTICSLEGALVRRQAKEPCVESLVSQYFQTVTDYGKDLMEKVKSPELQAEAKSYFEKSKEQLTPLIKKAGTELVNFLSYFVELGTQPATQ

1 aggcacagac accaaggaca gagacgctgg ctaggccgcc ctccccactg ttaccaacat

61 gaagctgctc gcagcaactg tgctactcct caccatctgc agccttgaag gagctttggt

121 tcggagacag gcaaaggagc catgtgtgga gagcctggtt tctcagtact tccagaccgt

181 gactgactat ggcaaggacc tgatggagaa ggtcaagagc ccagagcttc aggccgaggc

241 caagtcttac tttgaaaagt caaaggagca gctgacaccc ctgatcaaga aggctggaac

301 ggaactggtt aacttcttga gctatttcgt ggaacttgga acacagcctg ccacccagtg

361 aagtgtccag accattgtct tccaacccca gctggcctct agaacaccca ctggccagtc

421 ctagagctcc tgtccctacc cactctttgc tacaataaat gctgaatgaa tcc

kind regards,
Terry S. Singeltary Sr., Bacliff, Texas USA

############ http://mailhost.rz.uni-karlsruhe.de/warc/bse-l.html ############


http://www.vegsource.com/talk/madcow/messages/9198.html

Clinico-Pathological Correlation in Dementias

F. TeixeiraI, E. Alonso2, V. Romerol, A. Ortiz', C. Martinez3, E. Otero4
'Departnents of Experimental Neuropathology and 2Genetics, and the 3Division
of Psychology and
4Neurology, National Institute of Neurology and Neurosurgery, Mexico City,
Mexico

Submitted: February 22, 1994
Accepted: February 9, 1995

The object of this study is to investigate whether or not there are clinical signs and symptoms in patients with dementia that, by themselves or jointly, can be associated with the pathological diagnosis of Alzheimer's disease. Twelve patients with dementia were studied, in whom the clinical diagnosis of Alzheimer's disease was made according to established criteria. A sample of leptomeninges, cortex and subcortical white matter was obtained from each patient and was processed for light and electron microscopy. In the cases in whom neuritic plaques and neurofibrilary
tangles were present, pathological changes were quantified. The diagnosis of Alzheimer's disease was confirmed in 5 cases, whereas in 3 patients spongiform encephalopathy was present. In the remaining patients, the number of neuritic plaques was within normal limits for the age of the subjects. Comparison of the data in Alzheimer (n = 5) and non-Alzheimer (n =7) groups showed an increased, statistically significant incidence of acalculia, abnormalities of judgment, impairment of abstraction and primitive reflexes in the former. Although good fitting models were obtained, none achieved perfect discrimination. The model that included alterations of judgment and acalculia gave the best fit.

Key Words: Alzheimer's disease, dementia

INTRODUCTION

snip...see full text ;


http://www.vegsource.com/talk/madcow/messages/9911293.html


Subject: Transmissibility of mouse AApoAII amyloid fibrils: inactivation by physical and chemical methods
Date: March 22, 2006 at 6:31 am PST

The FASEB Journal Express Article doi:10.1096/fj.fj.05-4890fje
Published online March 20, 2006


Transmissibility of mouse AApoAII amyloid fibrils: inactivation by physical and chemical methods

Huanyu Zhang, Jinko Sawash!ta, Xiaoying Fu, Tatsumi Korenaga, Jingmin Yan, Masayuki Mori, and Keiichi Higuchi

E-mail contact: khiguchi@sch.md.shinshu-u.ac.jp


AApoAII amyloid fibrils have exhibited prion-like transmissibility in mouse senile amyloidosis. We have demonstrated that AApoAII is extremely active and can induce amyloidosis following doses less than 1 pg. We tested physical and chemical methods to disrupt AApoAII fibrils in vitro as determined by thioflavin T binding and electron microscopy (EM) as well as inactivating the transmissibility of AApoAII fibrils in vivo. Complete disruption of AApoAII fibrils was achieved by treatment with formic acid, 6 M guanidine hydrochloride, and autoclaving in an alkaline solution. Injection of these disrupted AApoAII fibrils did not induce amyloidosis in mice. Disaggregation with 6 M urea, autoclaving, and alkaline solution was incomplete, and injection of these AApoAII fibrils induced mild amyloidosis. Treatment with formalin, delipidation, freeze-thaw, and RNase did not have any major effect. A distinct correlation was obtained between the amounts of amyloid fibrils and the transmissibility of amyloid fibrils, thereby indicating the essential role of fibril conformation for transmission of amyloidosis. We also studied the inactivation of AApoAII fibrils by several organic compounds in vitro and in vivo.

AApoAII amyloidosis provides a valuable system for studying factors that may prevent transmission of amyloid disease as well as potential novel therapies.


http://www.fasebj.org/cgi/content/abstract/fj.05-4890fjev1

another transmissible protein amyloidosis? what does this implicate with Alzheimer's? thought alzheimer's was not suppose to be transmissible either? low level TSE maybe?


http://www.vegsource.com/talk/madcow/messages/1000569.html

http://betaamyloidcjd.blogspot.com/

http://betaamyloidcjd.blogspot.com/2008/03/10-million-baby-boomers-to-have.html

http://betaamyloidcjd.blogspot.com/2008/03/association-between-deposition-of-beta.html

tss



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