title: Hsp47: a collagen-specific molecular chaperone.
abstract: Hsp47 is a novel stress protein in the endoplasmic reticulum that binds specifically to various types of collagens and procollagens. Hsp47 transiently associates with procollagen and is involved in collagen processing and/or secretion under normal conditions. Under conditions of stress, Hsp47 is part of the quality control system for procollagen, including the prevention of the secretion of procollagen with abnormal conformation. In addition to its role as a molecular chaperone, Hsp47 synthesis always parallels that of collagen in developing tissues and various cell lines, and in collagen-related pathological conditions such as fibrosis.
authors.affiliation: Department of Cell Biology, Kyoto University, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Nagata
mesh_terms: D000818:Animals; D003094:Collagen / Q000378:metabolism*; D050958:HSP47 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism*
chemical_list: D050958:HSP47 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; C494660:SERPINH1 protein, human; D003094:Collagen