The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.