Murphy G, Cockett M I, Ward R V, Docherty A J
Strangeways Research Laboratory, Worts' Causeway, Cambridge, U.K.
Biochem J. 1991 Jul 1;277 ( Pt 1)(Pt 1):277-9. doi: 10.1042/bj2770277.
The abilities of the matrix metalloproteinases 95 kDa and 72 kDa gelatinases (type IV collagenases), stromelysins-1 and -2 and punctuated metalloproteinase (PUMP) to degrade insoluble elastin, type IV collagen films and proteoglycan have been compared. The gelatinases and PUMP were markedly more active in the degradation of elastin than were the stromelysins. PUMP and the stromelysins were more potent proteoglycan-degrading enzymes. All of the enzymes studied degraded soluble native type IV collagen, but the gelatinases were more effective at higher temperatures. These quantitative data allow an analysis of the potential relative roles of these metalloproteinases in the breakdown of the key components of connective tissue matrices.
已对95 kDa和72 kDa基质金属蛋白酶(IV型胶原酶)、基质溶解素-1和-2以及点状金属蛋白酶(PUMP)降解不溶性弹性蛋白、IV型胶原膜和蛋白聚糖的能力进行了比较。与基质溶解素相比,明胶酶和PUMP在弹性蛋白降解方面活性明显更高。PUMP和基质溶解素是更强效的蛋白聚糖降解酶。所有研究的酶都能降解可溶性天然IV型胶原,但明胶酶在较高温度下更有效。这些定量数据有助于分析这些金属蛋白酶在结缔组织基质关键成分分解中的潜在相对作用。