Article
Substitution of murine type I collagen A1 3-hydroxylation site alters matrix structure but does not recapitulate osteogenesis imperfecta bone dysplasia.
Matrix biology : journal of the International Society for Matrix Biology - 1 Aug 2020
Cabral Wayne A, Fratzl-Zelman Nadja, Weis MaryAnn, Perosky Joseph E, Alimasa Adrienne, Harris Rachel, Kang Heeseog, Makareeva Elena, Barnes Aileen M, Roschger Paul, Leikin Sergey, Klaushofer Klaus, Forlino Antonella, Backlund Peter S, Eyre David R, Kozloff Kenneth M, Marini Joan C
Abstract excerpt
Null mutations in CRTAP or P3H1, encoding cartilage-associated protein and prolyl 3-hydroxylase 1, cause the severe bone dysplasias, types VII and VIII osteogenesis imperfecta. Lack of either protein prevents formation of the ER prolyl 3-hydroxylation complex, which catalyzes 3Hyp modification of types I and II collagen and also acts as a collagen chaperone. To clarify the role of the A1 3Hyp substrate site in...
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