2009
DOI: 10.1074/jbc.m109.007070
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Biochemical Characterization of the Prolyl 3-Hydroxylase 1·Cartilage-associated Protein·Cyclophilin B Complex

Abstract: The rough endoplasmic reticulum-resident protein complex consisting of prolyl 3-hydroxylase 1 (P3H1), cartilage-associated protein (CRTAP), and cyclophilin B (CypB) can be isolated from chick embryos on a gelatin-Sepharose column, indicating some involvement in the biosynthesis of procollagens. Prolyl 3-hydroxylase 1 modifies a single proline residue in the ␣ chains of type I, II, and III collagens to (3S)-hydroxyproline. The peptidyl-prolyl cistrans isomerase activity of cyclophilin B was shown previously to … Show more

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Cited by 108 publications
(101 citation statements)
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“…HSP47/SERPINH1 specifically and transiently binds to various types of collagen in the ER and is believed to facilitate the triple-helical structure of collagen (Nagata 2003). The P4H complex, consisting of a2b2 tetramers, in which the b-subunits are identical to PDI, and the P3H complex, containing cartilage-associated protein (CRTAP), prolyl 3-hydroxylase 1 (P3H1), and cyclophilin B, are also known to be essential assembling factors and collagen chaperones (Ishikawa et al 2009;Gorres and Raines 2010;Morello and Rauch 2010). Mutation or knockout of these factors results in embryonic lethality or osteogenesis imperfecta, which clearly shows their importance for productive procollagen folding and maturation (Nagai et al 2000;Morello et al 2006;Cabral et al 2007;Choi et al 2009).…”
Section: Other Specific Chaperonesmentioning
confidence: 99%
“…HSP47/SERPINH1 specifically and transiently binds to various types of collagen in the ER and is believed to facilitate the triple-helical structure of collagen (Nagata 2003). The P4H complex, consisting of a2b2 tetramers, in which the b-subunits are identical to PDI, and the P3H complex, containing cartilage-associated protein (CRTAP), prolyl 3-hydroxylase 1 (P3H1), and cyclophilin B, are also known to be essential assembling factors and collagen chaperones (Ishikawa et al 2009;Gorres and Raines 2010;Morello and Rauch 2010). Mutation or knockout of these factors results in embryonic lethality or osteogenesis imperfecta, which clearly shows their importance for productive procollagen folding and maturation (Nagai et al 2000;Morello et al 2006;Cabral et al 2007;Choi et al 2009).…”
Section: Other Specific Chaperonesmentioning
confidence: 99%
“…The complex is involved in the hydroxyl ation of proline 986 of the collagen α1(I) chain and α1(II) chain and proline 707 of the α2(I) chain 13,[19][20][21] , which are thought to be important for supramolecular assembly of collagen fibrils and to serve as binding sites for chaperones or small leucine rich proteoglycans 22 . Beyond its prolyl 3 hydroxylase activity, the com plex functions as a PPIase and chaperone for collagen folding 13,19,23 . Indeed, the fast propagation of the triple helix requires the isomerization of cis peptide bonds that convert proline residues into trans configuration, mainly by PPIase B 24 (FIG.…”
Section: Mechanisms/pathophysiologymentioning
confidence: 99%
“…Alternatively the non-A1 3Hyp sites may not require the same enzyme complex as site A1. The latter site is normally hydroxylated by a trimeric protein complex of P3H1, CRTAP protein, and cyclophilin B (32). Without CRTAP, P3H1 fails to hydroxylate site A1 in collagen ␣1(I) and ␣1(II) from studies on the crtap null mouse (6) and human CRTAPnull OI patients (9).…”
Section: Comparison Of A-clade and B-clade 3hypmentioning
confidence: 99%