Kluve B, Merrick W C, Gershman H
Biochem J. 1983 Jun 15;212(3):641-7. doi: 10.1042/bj2120641.
A collagenase previously reported to accumulate in the medium of cultures of BALB/c 3T3 cells on infection with Mycoplasma orale [Kluve, Merrick, Stanbridge & Gershman (1981) Nature (London) 292, 855-857] was partially purified and characterized. With regard to purification properties, activation, sensitivity to inhibitors and relative molecular mass the enzyme was similar to previously reported vertebrate collagenases, but could not be unequivocally distinguished from bacterial collagenases. With regard to substrate-specificity and reaction products, however, the collagenase was typical of vertebrate collagenases and distinct from bacterial collagenases. Specifically, the enzyme displayed a preference for type III collagen and type I collagen, a somewhat decreased ability to degrade type II collagen, and a very limited ability to degrade type IV collagen. The initial products of the action of the collagenase on type I collagen were characterized as fragments one-quarter and three-quarters of the length of the intact collagen molecule. Because the properties of the collagenase produced by cultures of mycoplasma-infected BALB/c 3T3 cells are those of a mammalian-type (vertebrate-type) enzyme, we have concluded that the collagenase is a product of the mouse (BALB/c 3T3) genome, and is not produced by the mycoplasma. Therefore it appears that infection of BALB/c 3T3 mouse fibroblasts with Mycoplasma orale induces the mouse cells to produce and secrete collagenase.
一种先前报道在口腔支原体感染BALB/c 3T3细胞的培养物培养基中积累的胶原酶[Kluve、Merrick、Stanbridge和Gershman(1981年),《自然》(伦敦)292, 855 - 857]得到了部分纯化和表征。就纯化特性、激活、对抑制剂的敏感性和相对分子质量而言,该酶与先前报道的脊椎动物胶原酶相似,但无法与细菌胶原酶明确区分。然而,就底物特异性和反应产物而言,该胶原酶是典型的脊椎动物胶原酶,与细菌胶原酶不同。具体而言,该酶对III型胶原和I型胶原表现出偏好,降解II型胶原的能力略有下降,降解IV型胶原的能力非常有限。胶原酶作用于I型胶原的初始产物被表征为完整胶原分子长度的四分之一和四分之三的片段。由于支原体感染的BALB/c 3T3细胞培养物产生的胶原酶具有哺乳动物型(脊椎动物型)酶的特性,我们得出结论,该胶原酶是小鼠(BALB/c 3T3)基因组的产物,而非支原体产生。因此,口腔支原体感染BALB/c 3T3小鼠成纤维细胞似乎会诱导小鼠细胞产生并分泌胶原酶。