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Article

Crtap and p3h1 knock out zebrafish support defective collagen chaperoning as the cause of their osteogenesis imperfecta phenotype.

Matrix biology : journal of the International Society for Matrix Biology - 1 Aug 2020

Tonelli F, Cotti S, Leoni L, Besio R, Gioia R, Marchese L, Giorgetti S, Villani S, Gistelinck C, Wagener R, Kobbe B, Fiedler I A K, Larionova D, Busse B, Eyre D, Rossi A, Witten P E, Forlino A

Abstract excerpt

Prolyl 3-hydroxylation is a rare collagen type I post translational modification in fibrillar collagens. The primary 3Hyp substrate sites in type I collagen are targeted by an endoplasmic reticulum (ER) complex composed by cartilage associated protein (CRTAP), prolyl 3-hydroxylase 1 (P3H1) and prolyl cis/trans isomerase B, whose mutations cause recessive forms of osteogenesis imperfecta with impaired levels of...

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PMID: 32173581
DOI: 10.1016/j.matbio.2020.03.004

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Crtap and p3h1 knock out zebrafish support defective collagen chaperoning as the cause of their osteogenesis imperfecta phenotype.PMID 32173581Read ↗

Components of the Collagen Prolyl 3-Hydroxylation Complex are Crucial for Normal Bone DevelopmentSemantic proximity Read ↗

CRTAP is required for prolyl 3- hydroxylation and mutations cause recessive osteogenesis imperfecta.Semantic proximity Read ↗

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Deficiency of CRTAP in non-lethal recessive osteogenesis imperfecta reduces collagen deposition into matrix.Semantic proximity Read ↗

Null mutations in LEPRE1 and CRTAP cause severe recessive osteogenesis imperfecta.Semantic proximity Read ↗

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