FURTHER-STUDIES ON ACTIVATION OF PROCOLLAGENASE, LATENT PRECURSOR OF BONE COLLAGENASE - EFFECTS OF LYSOSOMAL CATHEPSIN-B, PLASMIN AND KALLIKREIN, AND SPONTANEOUS ACTIVATION
FURTHER-STUDIES ON ACTIVATION OF PROCOLLAGENASE, LATENT PRECURSOR OF BONE COLLAGENASE - EFFECTS OF LYSOSOMAL CATHEPSIN-B, PLASMIN AND KALLIKREIN, AND SPONTANEOUS ACTIVATION
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DOI:
10.1042/bj1660021
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发表时间:
1977-01-01
影响因子:
4.1
通讯作者:
VAES, G
中科院分区:
文献类型:
--
作者:
EECKHOUT, Y;VAES, G
Cathepsin B, [EC 2.4.22.1] a tissue (lysosomal) proteinase, and 2 humoral proteinases, plasmin [EC 3.4.21.7] and kallikrein, [EC 3.4.21.8] activate the latent collagenase [EC 3.4.24.3] (procollagenase) which is released by mouse bone explants in culture. Other lysosomal proteinases (carboxypeptidase B, cathepsin C and D) and thrombin did not activate the procollagenase. Dialysis of the culture fluids against 3 M-NaSCN at 4.degree. C and, for some culture fluids, prolonged preincubation at 25.degree. C also caused the activation of procollagenase. In all these cases, activation of procollagenase involved at least 2 successive steps: the activation of an endogenous latent activator present in the culture fluids and the activation of procollagenase itself. An assay method was developed for the endogenous activator. Human serum, bovine serum albumin, casein and cysteine inhibited the endogenous activator at concentrations that did not influence the collagenase activity. N-Ethylmaleimide and 4-hydroxymercuribenzoate stimulated the endogenous activator, but iodoacetate had no effect. It is proposed that cathepsin B, kallikrein and plasmin may play a role in the physiological activation of latent collagenase and thus initiate degradation of collagen in vivo. This may occur whatever the molecular nature of procollagenase (zymogen or enzyme-inhibitor complex) might be.