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Heat shock protein 27: its potential role in vascular disease
Author(s) -
Ferns Gordon,
Shams Sedigheh,
Shafi Shahida
Publication year - 2006
Publication title -
international journal of experimental pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.671
H-Index - 72
eISSN - 1365-2613
pISSN - 0959-9673
DOI - 10.1111/j.1365-2613.2006.00484.x
Subject(s) - heat shock protein , hsp27 , chaperone (clinical) , microbiology and biotechnology , hsp70 , protein aggregation , co chaperone , hsp90 , hspa4 , shock (circulatory) , apoptosis , biology , chemistry , biochemistry , medicine , pathology , gene
Summary Heat shock proteins are molecular chaperones that have an ability to protect proteins from damage induced by environmental factors such as free radicals, heat, ischaemia and toxins, allowing denatured proteins to adopt their native configuration. Heat shock protein‐27 (Hsp27) is a member of the small Hsp (sHsp) family of proteins, and has a molecular weight of approximately 27 KDa. In addition to its role as a chaperone, it has also been reported to have many additional functions. These include effects on the apoptotic pathway, cell movement and embryogenesis. In this review, we have focused on its possible role in vascular disease.