Proteomics

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Lysyl hydroxylase 3 mediated post-translational modifications are required for proper biosynthesis of collagen a1a1a2(IV)


ABSTRACT: We performed proteomic identification of type IV collagen gel bands from wild-type and lysyl hydroxylase 3 knockout cells by LC-MS after trypsin digestion.

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Yoshihiro Ishikawa 

PROVIDER: PXD035051 | JPOST Repository | Mon Nov 21 00:00:00 GMT 2022

REPOSITORIES: jPOST

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Lysyl hydroxylase 3-mediated post-translational modifications are required for proper biosynthesis of collagen α1α1α2(IV).

Ishikawa Yoshihiro Y   Taga Yuki Y   Coste Thibault T   Tufa Sara F SF   Keene Douglas R DR   Mizuno Kazunori K   Tournier-Lasserve Elisabeth E   Gould Douglas B DB  

The Journal of biological chemistry 20221117 12


Collagens are the most abundant proteins in the body and among the most biosynthetically complex. A molecular ensemble of over 20 endoplasmic reticulum resident proteins participates in collagen biosynthesis and contributes to heterogeneous post-translational modifications. Pathogenic variants in genes encoding collagens cause connective tissue disorders, including osteogenesis imperfecta, Ehlers-Danlos syndrome, and Gould syndrome (caused by mutations in COL4A1 and COL4A2), and pathogenic varia  ...[more]

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