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HSP-1/2, a major protein of equine seminal plasma, exhibits chaperone-like activity.

Abstract：

:The major bovine seminal plasma protein, PDC-109 exhibits chaperone-like activity (CLA) against a variety of target proteins. The present studies show that the homologous protein from equine seminal plasma, HSP-1/2 also exhibits CLA and inhibits the thermal aggregation of target proteins such as lactate dehydrogenase, and DTT-induced aggregation of insulin in a concentration-dependent manner. Phosphorylcholine binding inhibited the CLA of HSP-1/2, suggesting that aggregation state of the protein is important for this activity. These results demonstrate that HSP-1/2 functions as a molecular chaperone in vitro, and suggest that it may protect other proteins of equine seminal plasma from unfolding/misfolding or aggregation. These results suggest that homologous proteins from the seminal plasma of other mammals also exhibit CLA, which will be physiologically relevant.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Sankhala RS,Kumar CS,Singh BP,Arangasamy A,Swamy MJ

doi

10.1016/j.bbrc.2012.08.120

subject

Has Abstract

pub_date

2012-10-12 00:00:00

pages

18-23

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(12)01688-9

journal_volume

427

pub_type

杂志文章

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