Dataset Information

Proline hydroxylation of collagens in prolyl 4-hydroxylase mutant mice

ABSTRACT: Collagen from the skin of wild type and prolyl 4-hydroxylase mutant mice was extracted and proline hydroxylation of the collagen-derived peptides were analyzed by LC-MS/MS.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Skin

SUBMITTER: Pekka Rappu

LAB HEAD: Jyrki Heino

PROVIDER: PXD008802 | Pride | 2018-04-10

REPOSITORIES: Pride

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Publications

Proline hydroxylation in collagen supports integrin binding by two distinct mechanisms.

Sipilä Kalle H KH Drushinin Kati K Rappu Pekka P Jokinen Johanna J Salminen Tiina A TA Salo Antti M AM Käpylä Jarmo J Myllyharju Johanna J Heino Jyrki J

The Journal of biological chemistry 20180403 20

Collagens are the most abundant extracellular matrix proteins in vertebrates and have a characteristic triple-helix structure. Hydroxylation of proline residues is critical for helix stability, and diminished prolyl hydroxylase activity causes wide-spread defects in connective tissues. Still, the role of proline hydroxylation in the binding of collagen receptors such as integrins is unclear. Here, we isolated skin collagen from genetically modified mice having reduced prolyl 4-hydroxylase activi ...[more]

PMID: 29615493

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			Action	DRS
	150612_C1-nr1.msf	Msf
	150612_C1-nr1.raw	Raw
	150612_C1-nr2.msf	Msf
	150612_C1-nr2.raw	Raw
	150612_C10-nr1.msf	Msf