HSP-1/2, a major protein of equine seminal plasma, exhibits chaperone-like activity.
Biochem Biophys Res Commun
; 427(1): 18-23, 2012 Oct 12.
Article
em En
| MEDLINE
| ID: mdl-22982540
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Sêmen
/
Glicoproteínas
/
Proteínas de Transporte
/
Chaperonas Moleculares
/
Proteínas de Plasma Seminal
/
Cavalos
Limite:
Animals
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article