A procollagen C-proteinase inhibitor diminishes collagen and lysyl oxidase processing but not collagen cross-linking in osteoblastic cultures.
A procollagen C-proteinase inhibitor diminishes collagen and lysyl oxidase processing but not collagen cross-linking in osteoblastic cultures.
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前胶原 C 蛋白酶抑制剂可减少成骨细胞培养物中胶原蛋白和赖氨酰氧化酶的加工，但不会减少胶原蛋白交联。
DOI：
10.1002/jcp.20206
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发表时间：
2005
期刊：
影响因子：
--
通讯作者：
Trackman,PhilipC
中科院分区：
文献类型：
--
作者：
Pischon,Nicole;Babakhanlou-Chase,Hermik;Darbois,Laurent;Ho,Wen-Bin;Brenner,MitchellC;Kessler,Efrat;Palamakumbura,AmithaH;Trackman,PhilipC
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. © 2004 Wiley‐Liss, Inc.
