Interaction of intracellular beta amyloid peptide with chaperone proteins.

Interaction of intracellular beta amyloid peptide with chaperone proteins. Research Abstract Details 

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Interaction of intracellular beta amyloid peptide with chaperone proteins. Abstract Text:

Virginia Fonte,Vadim Kapulkin,Andrew Taft,Amy Fluet,David Friedman,Christopher D Link,

Expression of the human beta amyloid peptide (A beta) in transgenic Caenorhabditis elegans animals can lead to the formation of intracellular immunoreactive deposits as well as the formation of intracellular amyloid. We have used this model to identify proteins that interact with intracellular A beta in vivo. Mass spectrometry analysis of proteins that specifically coimmunoprecipitate with A beta has identified six likely chaperone proteins: two members of the HSP70 family, three alpha B-crystallin-related small heat shock proteins (HSP-16s), and a putative ortholog of a mammalian small glutamine-rich tetratricopeptide repeat-containing protein proposed to regulate HSP70 function. Quantitative reverse transcription-PCR analysis shows that the small heat shock proteins are also transcriptionally induced by A beta expression. Immunohistochemistry demonstrates that HSP-16 protein closely colocalizes with intracellular A beta in this model. Transgenic animals expressing a nonaggregating A beta variant, a single-chain A beta dimer, show an altered pattern of coimmunoprecipitating proteins and an altered cellular distribution of HSP-16. Double-stranded RNA inhibition of R05F9.10, the putative C. elegans ortholog of the human small glutamine-rich tetratricopeptide-repeat-containing protein (SGT), results in suppression of toxicity associated with A beta expression. These results suggest that chaperone function can play a role in modulating intracellular A beta metabolism and toxicity.

Interaction of intracellular beta amyloid peptide with chaperone proteins. Publishing Authors By Initials

V Fonte,V Kapulkin,A Taft,A Fluet,D Friedman,CD Link,

For similar genetic phenomena: variation (genetics) research abstracts see: genetic phenomena: variation (genetics) research

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Interaction of intracellular beta amyloid peptide with chaperone proteins. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Proceedings of the National Academy of Sciences of

VOLUME: 99

Page Numbers: 9439-44

Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.

ISSN: 0027-8424

DAY: 27

MONTH: 06

YEAR: 2002

Interaction of intracellular beta amyloid peptide with chaperone proteins. Information

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LANGUAGE: eng

NlmUniqueID: 7505876

Interaction of intracellular beta amyloid peptide with chaperone proteins. Keywords Mesh Terms:

KEYWORDS: Variation (Genetics)

MESH TERMS: metabolism

Chemical & Substance for Abstract: Interaction of intracellular beta amyloid peptide with chaperone proteins. Information

Substance Name: amyloid beta-protein (1-42)

Registry Number: 0

Grant and Affiliation Information for Interaction of intracellular beta amyloid peptide with chaperone proteins.

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

Country: United States

AGENCY: United States NIA

GRANT: AG-12423

ACRONYM: AG

MEDLINETA: Proc Natl Acad Sci U S A

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