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A Chaperone Complex Formed by HSP47, FKBP65, and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen
Author(s) -
Duran Ivan,
Martin Jorge H,
Weis Mary Ann,
Krejci Pavel,
Konik Peter,
Li Bing,
Alanay Yasemin,
Lietman Caressa,
Lee Brendan,
Eyre David,
Cohn Daniel H,
Krakow Deborah
Publication year - 2017
Publication title -
journal of bone and mineral research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.882
H-Index - 241
eISSN - 1523-4681
pISSN - 0884-0431
DOI - 10.1002/jbmr.3095
Subject(s) - procollagen peptidase , hydroxylation , type i collagen , chemistry , biology , microbiology and biotechnology , endocrinology , biochemistry , enzyme
Lysine hydroxylation of type I collagen telopeptides varies from tissue to tissue, and these distinct hydroxylation patterns modulate collagen cross‐linking to generate a unique extracellular matrix. Abnormalities in these patterns contribute to pathologies that include osteogenesis imperfecta (OI), fibrosis, and cancer. Telopeptide procollagen modifications are carried out by lysyl hydroxylase 2 (LH2); however, little is known regarding how this enzyme regulates hydroxylation patterns. We identified an ER complex of resident chaperones that includes HSP47, FKBP65, and BiP regulating the activity of LH2. Our findings show that FKBP65 and HSP47 modulate the activity of LH2 to either favor or repress its activity. BiP was also identified as a member of the complex, playing a role in enhancing the formation of the complex. This newly identified ER chaperone complex contributes to our understanding of how LH2 regulates lysyl hydroxylation of type I collagen C‐telopeptides to affect the quality of connective tissues. © 2017 American Society for Bone and Mineral Research.