A procollagen C-proteinase inhibitor diminishes collagen and lysyl oxidase processing but not collagen cross-linking in osteoblastic cultures

Journal of Cellular Physiology
Nicole PischonPhilip C Trackman

Abstract

The deposition of insoluble functional collagen occurs following extracellular proteolytic processing of procollagens by procollagen N- and C-proteinases, fibril formation, and lysyl oxidase dependent cross-linking. Procollagen C-proteinases in addition process and activate lysyl oxidase. The present study evaluates a possible role for procollagen C-proteinases in controlling different aspects of collagen deposition in vitro. Studies determine whether inhibition of procollagen C-proteinase activity with a specific BMP-1 inhibitor results in perturbations in lysyl oxidase activation, and in collagen processing, deposition, and cross-linking in phenotypically normal cultured murine MC3T3-E1 cells. Data show that BMP-1 Inhibitor dose dependently inhibits lysyl oxidase activation by up to 50% in undifferentiated proliferating cells. In differentiating cultures, BMP-1 inhibitor decreased collagen processing but did not inhibit the accumulation of mature collagen cross-links. Finally, electron microscopy studies show that collagen fibril diameter increased. Thus, inhibition of procollagen C-proteinases results in perturbed collagen deposition primarily via decreased collagen processing.

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Citations

Jul 30, 2016·Circulation. Heart Failure·Karl T Weber, Javier Díez
Sep 17, 2005·Journal of Cellular Biochemistry·Philip C Trackman
May 18, 2010·American Journal of Physiology. Heart and Circulatory Physiology·Begoña LópezJavier Díez
Dec 14, 2018·FEBS Open Bio·Maya TalantikiteCatherine Moali
Sep 11, 2019·Cardiovascular Research·Doa'a Al-U'dattStanley Nattel
May 27, 2021·Expert Opinion on Drug Discovery·Marialucia Gallorini, Simone Carradori

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