Interactions of heat shock protein 47 with collagen and the stress response: an unconventional chaperone model?
Heat shock proteins (HSPs) are upregulated and manifested upon cellular stress and possess chaperoning functions. HSP47 is an endoplasmic reticulum (ER)-resident, collagen-specific chaperone and plays a key role in collagen biosynthesis and its structural assembly. The collagen scaffold is a primary structural target of recent interest due to its applications in tissue engineering and drug delivery and in treatment of clinical disorders. This review highlights the fundamental aspects of HSPs in protein folding and quality control, in the elicitation of a stress response in connective tissue and in the characterization of HSP47 in collagen folding and assembly. The significant features of HSP47 which are distinct in its cellular capabilities are discussed. We propose that targeting the stress response is a key factor in identifying connective tissue biomarkers. We also address the issues and strategies involved in the stress response of connective tissue diseases. In conclusion, we describe the prospects of collagen biochemistry in correlation to the science of HSPs.
Mala
J Geraldine Sandana
JG
Department of Biotechnology, Central Leather Research Institute, Council of Scientific and Industrial Research (CSIR), Chennai-600020, India.
Rose
C
C
D000818:Animals; D015415:Biomarkers / Q000378:metabolism; D003094:Collagen / Q000378:metabolism*; D003238:Connective Tissue / Q000378:metabolism; D003240:Connective Tissue Diseases / Q000473:pathology*; D004721:Endoplasmic Reticulum / Q000378:metabolism; D050958:HSP47 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism; D017510:Protein Folding
D015415:Biomarkers; D050958:HSP47 Heat-Shock Proteins; D018832:Molecular Chaperones; D003094:Collagen