Science Links Japan | Small heat shock proteins participate in the regulation of cellular aggregates of misfolded protein.

Small heat shock proteins participate in the regulation of cellular aggregates of misfolded protein.

Accession number;03A0113865

Title;Small heat shock proteins participate in the regulation of cellular aggregates of misfolded protein.

Author; ITO HIDENORI (Aichi Prefectural Colony Welfare Center for Peresons with Dev. Disabilities, Inst. Dev. Res., JPN) INAGUMA YUTAKA (Aichi Prefectural Colony Welfare Center for Peresons with Dev. Disabilities, Inst. Dev. Res., JPN) KATO KANEFUSA (Aichi Prefectural Colony Welfare Center for Peresons with Dev. Disabilities, Inst. Dev. Res., JPN)

Journal Title;Folia Pharmacologica Japonica

Journal Code:G0740A

ISSN:0015-5691

VOL.121;NO.1;PAGE.27-32(2003)

Figure&Table&Reference;FIG.3, REF.28

Pub. Country;Japan

Language;Japanese

Abstract;Molecular chaperones participate in folding of many proteins and several families are known to exist in mammalian cells including the small heat shock protein (sHSP) family. sHSPs have a molecular mass of 15-30 kDa and are known to be induced and phosphorylated in response to various stimuli. There are several reports describing the correlation between sHSPs and degenerative diseases. We have been reported that Hsp27 and .ALPHA.B-crystallin were recruited to aggresome when cells were treated with proteasome inhibitors. Expression of Hsp27 suppresses the cell death induced by expression of expanded polyglutamine via down regulation of the oxidative stress pathway. Recently, a missense mutation in .ALPHA.B-crystallin, R120G, has been found in a French family suffering from desmin-related myopathy. Moreover, transgenic mice expressing R120G.ALPHA.B-crystallin exhibit symptoms similar to desmin-related myopathy. We recently examined the interaction of R120G.ALPHA.B-crystallin and Hsp27 in mammalian cells and found that expression of R120G.ALPHA.B-crystallin caused formation of inclusion bodies and co-expression of Hsp27 inhibited this formation of inclusion bodies. Clarification of physiological roles of sHSPs in degenerative diseases may lead to the development of new therapy. (author abst.)

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