The heat shock proteins were discovered, as the name suggests, since they are heavily upregulated when cells are stressed by temperatures above the normal physiological range. They are expressed in unstressed cells also and have a normal function as chaperones, helping other proteins to fold correctly, and are required in much greater amounts if the cell or tissue is stressed by heat. The increased levels are generated transcriptionally under the influence of a powerful transcription factor, the heat shock factor 1 (HSF1).
The different heat shock proteins were originally named based on their SDS-PAGE mobility, so HSP60 has an apparent molecular weight of 60 kDa. It is an abundant protein in mitochondria and is typically responsible for the transportation and refolding of proteins from the cytoplasm into the mitochondrial matrix. HSP60 aids in the folding and conformation maintenance of approximately 15-30% of all cellular proteins. In addition to its role as a heat shock protein, HSP60 plays an important role in the transport and maintenance of mitochondrial proteins as well as the transmission and replication of mitochondrial DNA. HSP60 has been implicated in the initiation and/or progression of some subtypes of Cardiovascular Disease (CVD), implying its potential as a biomarker with applications for diagnosis, assessing prognosis and response to treatment, as well as for preventing and treating CVD. The HGNC name for this protein is HSBD1.