Suppression of in Vivo -Amyloid Peptide Toxicity by Overexpression of the HSP-16.2 Small Chaperone Protein.

Suppression of in Vivo -Amyloid Peptide Toxicity by Overexpression of the HSP-16.2 Small Chaperone Protein. Research Abstract Details 

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Suppression of in Vivo -Amyloid Peptide Toxicity by Overexpression of the HSP-16.2 Small Chaperone Protein. Abstract Text:

Virginia Fonte,D Randal Kipp,John Yerg,David Merin,Margaret Forrestal,Eileen Wagner,Christine M Roberts,Christopher D Link,Virginia Fonte,D Randal Kipp,John Yerg,David Merin,Margaret Forrestal,Eileen Wagner,Christine M Roberts,Christopher D Link,

Expression of the human beta-amyloid peptide (Abeta) in a transgenic Caenorhabditis elegans Alzheimer disease model leads to the induction of HSP-16 proteins, a family of small heat shock-inducible proteins homologous to vertebrate alphaB crystallin. These proteins also co-localize and co-immunoprecipitate with Abeta in this model (Fonte, V., Kapulkin, V., Taft, A., Fluet, A., Friedman, D., and Link, C. D. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 9439-9444). To investigate the molecular basis and biological function of this interaction between HSP-16 and Abeta, we generated transgenic C. elegans animals with high level, constitutive expression of HSP-16.2. We find that constitutive expression of wild type, but not mutant, HSP-16.2 partially suppresses Abeta toxicity. Wild type Abeta-(1-42), but not Abeta single chain dimer, was observed to become sequestered in HSP-16.2-containing inclusions, indicating a conformation-dependent interaction between HSP-16.2 and Abeta in vivo. Constitutive expression of HSP-16.2 could reduce amyloid fibril formation, but it did not reduce the overall accumulation of Abeta peptide or alter the pattern of the predominant oligomeric species. Studies with recombinant HSP-16.2 demonstrated that HSP-16.2 can bind directly to Abeta in vitro, with a preferential affinity for oligomeric Abeta species. This interaction between Abeta and HSP-16.2 also influences the formation of Abeta oligomers in in vitro assays. These studies are consistent with a model in which small chaperone proteins reduce Abeta toxicity by interacting directly with the Abeta peptide and altering its oligomerization pathways, thereby reducing the formation of a minor toxic species.

Suppression of in Vivo -Amyloid Peptide Toxicity by Overexpression of the HSP-16.2 Small Chaperone Protein. Publishing Authors By Initials

V Fonte,DR Kipp,J Yerg,D Merin,M Forrestal,E Wagner,CM Roberts,CD Link,V Fonte,DR Kipp,J Yerg,D Merin,M Forrestal,E Wagner,CM Roberts,CD Link,

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Suppression of in Vivo -Amyloid Peptide Toxicity by Overexpression of the HSP-16.2 Small Chaperone Protein. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: The Journal of biological chemistry

VOLUME: 283

Page Numbers: 784-91

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 9

MONTH: 11

YEAR: 2007

Suppression of in Vivo -Amyloid Peptide Toxicity by Overexpression of the HSP-16.2 Small Chaperone Protein. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

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Grant and Affiliation Information for Suppression of in Vivo -Amyloid Peptide Toxicity by Overexpression of the HSP-16.2 Small Chaperone Protein.

AFFILIATION: Institute for Behavioral Genetics, University of Colorado, Boulder, Colorado 80309.

Country: United States

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MEDLINETA: J Biol Chem

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