Studies on uterine collagenase in tissue culture. I. Relationship of enzyme production to collagen metabolism.
Studies on uterine collagenase in tissue culture. I. Relationship of enzyme production to collagen metabolism.
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组织培养子宫胶原酶的研究。
DOI：
10.1016/0304-4165(71)90101-2
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发表时间：
1971
期刊：
影响因子：
--
通讯作者：
A. Eisen
中科院分区：
文献类型：
--
作者：
J. Jeffrey;R. Coffey;A. Eisen
培养的产后大鼠子宫组织产生特异性胶原酶，在pH和离子强度的生理条件下对天然胶原具有活性。活跃产生胶原酶的组织在培养物中持续长达10天。在分娩后的第一个72小时内从动物体内取出子宫时，培养基中的胶原酶活性最大。在此时间之后，酶活性不可检测。这段时间对应于胶原蛋白在子宫内体内快速降解的时间。酶的产生也与培养物中的胶原降解密切相关。伴随着活性胶原酶合成的是85%的组织胶原损失到培养基中，主要是以小于50 000 mol的含羟脯氨酸的肽的形式。重量，表明胶原蛋白在产后退化过程中大量蛋白水解降解。通过嘌呤霉素或冻融抑制培养物中的酶产生也可防止组织中的胶原降解，表明这种酶是子宫中正常胶原代谢所需的。
Post-partum rat uterine tissue in culture produces a specific collagenase, active against native collagen under physiologic conditions of pH and ionic strength. Tissue which actively produces collagenase does so for up to 10 days in culture. Collagenase activity in the medium of cultures in maximal when the uterus is removed from the animal within the first 72 h after parturition. After this time, enzyme activity is undetectable. This period corresponds to the time during which collagen is rapidly degraded in the uterusin vivo. Enzyme production is closely correlated with collagen degradation in culture as well. Concomittant with active collagenase synthesis is the loss of 85% of the tissue collagen into the medium, mostly in the form of hydroxyproline-containing peptides of less than 50 000 mol. wt., indicating that collagen is largely proteolytically degraded during post-partum involution. Inhibition of enzyme production in the cultures by puromycin or freeze-thawing also prevents collagen degradation in the tissue, suggesting that this enzyme is required for normal collagen metabolism in the uterus.