Heat shock protein 27: its potential role in vascular disease.
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.
Ferns
Gordon
G
Centre for Clinical Science and Measurement, School of Biomedical Science, University of Surrey, Guildford Surrey, UK. g.ferns@surrey.ac.uk
Shams
Sedigheh
S
Shafi
Shahida
S
D000818:Animals; D017209:Apoptosis / Q000502:physiology; D042783:Endothelial Cells / Q000378:metabolism; D004730:Endothelium, Vascular / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000502:physiology*; D006801:Humans; D007249:Inflammation; D023421:Models, Animal; D018832:Molecular Chaperones / Q000502:physiology*; D009369:Neoplasms / Q000378:metabolism; D020033:Protein Isoforms / Q000502:physiology*; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction / Q000502:physiology; D014652:Vascular Diseases / Q000378:metabolism*
D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D020033:Protein Isoforms