Nethery A, O'Grady R L
Department of Pathology, University of Sydney, Australia.
Invasion Metastasis. 1991;11(5):241-8.
Functional characteristics of the interstitial collagenase purified from the BCl rat mammary carcinoma cell line were examined and compared with literature reports of the corresponding characteristics of collagenase from non-neoplastic cells. BCl collagenase degraded soluble collagen types I, II and III at the same rate and degraded fibrillar tendon collagen with an activation energy of 75 kcal/mol; these characteristics were identical to collagenase from normal rat uterine smooth muscle cells. Degradation of fibrillar collagen by BCl collagenase was completely inhibited by rat alpha 2-macroglobulin which was concomitantly cleaved into half-fragments. BCl collagenase was also inhibited by native and recombinant tissue inhibitor of metalloproteinases, a synthetic peptide collagenase inhibitor (Z-pro-leugly-NHOH), and Zn2+. In all functional characteristics examined, BCl collagenase was the same as interstitial collagenases from non-neoplastic sources.
对从BCl大鼠乳腺癌细胞系中纯化出的间质胶原酶的功能特性进行了检测，并与来自非肿瘤细胞的胶原酶相应特性的文献报道进行了比较。BCl胶原酶以相同速率降解可溶性I、II和III型胶原，并以75千卡/摩尔的活化能降解纤维状肌腱胶原；这些特性与正常大鼠子宫平滑肌细胞的胶原酶相同。BCl胶原酶对纤维状胶原的降解被大鼠α2-巨球蛋白完全抑制，同时α2-巨球蛋白被裂解成半片段。BCl胶原酶也被天然和重组金属蛋白酶组织抑制剂、一种合成肽胶原酶抑制剂（Z-脯-亮甘-氨醇）和Zn2+抑制。在所有检测的功能特性方面，BCl胶原酶与来自非肿瘤来源的间质胶原酶相同。
