Reduced Bone Mass in Collagen Prolyl 4-Hydroxylase P4ha1 ^+/-; P4ha2 ^-/- Compound Mutant Mice.

ABSTRACT: Proper deposition of the extracellular matrix and its major components, the collagens, is essential for endochondral ossification and bone mass accrual. Collagen prolyl 4-hydroxylases (C-P4Hs) hydroxylate proline residues in the -X-Pro-Gly- repeats of all known collagen types. Their product, 4-hydroxyproline, is essential for correct folding and thermal stability of the triple-helical collagen molecules in physiological body temperatures. We have previously shown that inactivation of the mouse P4ha1 gene, which codes for the catalytic α subunit of the major C-P4H isoform, is embryonic lethal, whereas inactivation of the P4ha2 gene produced only a minor phenotype. Instead, mice with a haploinsufficiency of the P4ha1 gene combined with a homozygous deletion of the P4h

SUBMITTER: Tolonen JP 

PROVIDER: S-EPMC9189910 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature