Expression and function of heat shock protein 47: a collagen-specific molecular chaperone in the endoplasmic reticulum.
Heat shock protein (HSP) 47 is a collagen-binding stress protein localized in the endoplasmic reticulum (ER). In addition to stress-inducibility through heat shock element-heat shock factor interaction, the expression of HSP47 under normal conditions always correlates with that of collagens in various cell types and tissues. Both HSP47 and types I and III collagens are also dramatically induced under pathophysiological conditions such as liver fibrosis. HSP47 transiently associates with procollagen in the ER and dissociates from it in the cis-Golgi compartment. Possible functions of HSP47 as a molecular chaperone specific for procollagen are discussed: prevention of nascent procollagen chains from forming aggregates, effect on the modification of procollagen, inhibition of intracellular degradation of procollagen, quality control mechanisms under stress conditions, and effect on the secretion from the ER to the Golgi compartment.
Nagata
K
K
Department of Cell Biology, Kyoto University, Japan.
D000818:Animals; D003094:Collagen / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D050958:HSP47 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008956:Models, Chemical; D011347:Procollagen / Q000378:metabolism; D013329:Structure-Activity Relationship
D050958:HSP47 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D011347:Procollagen; C494660:SERPINH1 protein, human; D003094:Collagen