Human fibroblast collagenase: glycosylation and tissue-specific levels of enzyme synthesis.
Human fibroblast collagenase: glycosylation and tissue-specific levels of enzyme synthesis.
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人成纤维细胞胶原酶：糖基化和酶合成的组织特异性水平。
DOI：
10.1073/pnas.83.11.3756
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发表时间：
1986
影响因子：
11.1
通讯作者：
Goldberg,G
中科院分区：
文献类型：
--
作者：
Wilhelm,SM;Eisen,AZ;Teter,M;Clark,SD;Kronberger,A;Goldberg,G
人皮肤成纤维细胞分泌胶原酶有两种形式(57 kDa和52 kDa)。次要的(57 KDa)酶原形式是主要的(52 KDa)酶原通过添加N-连接的复合寡糖进行部分翻译后修饰的结果。人的内皮细胞以及来自人的结肠、角膜、牙龈和肺的成纤维细胞也以两种与皮肤成纤维细胞酶相似的形式分泌胶原酶。体外组织培养研究表明，这种成纤维细胞类型的间质胶原酶的组成合成水平是组织特异性的，变化很大，并与单个胶原酶特异的2.5kb碱基的mRNA的稳定水平相关。肿瘤促进剂佛波酯12-肉豆蔻酸酯13-乙酸酯显然阻止了胶原酶合成的控制，导致所有受检细胞中胶原酶的表达水平类似地高(大约相当于每10(6)个细胞每24小时3-7微克胶原酶)。28 kDa胶原酶抑制剂的合成组成水平与酶的合成水平没有相关性。佛波醇12-肉豆蔻酸酯13-醋酸酯刺激这种抑制物的产生，进而调节条件培养液中胶原酶的活性。因此，存在于培养液中的酶的表观活性不能准确地反映其合成和分泌的速度。
Human skin fibroblasts secrete collagenase as two proenzyme forms (57 and 52 kDa). The minor (57-kDa) proenzyme form is the result of a partial posttranslational modification of the major (52-kDa) proenzyme through the addition of N-linked complex oligosaccharides. Human endothelial cells as well as fibroblasts from human colon, cornea, gingiva, and lung also secrete collagenase in two forms indistinguishable from those of the skin fibroblast enzyme. In vitro tissue culture studies have shown that the level of constitutive synthesis of this fibroblast-type interstitial collagenase is tissue specific, varies widely, and correlates with the steady-state level of a single collagenase-specific mRNA of 2.5 kilobases. The tumor promoter, phorbol 12-myristate 13-acetate, apparently blocks the control of collagenase synthesis resulting in a similarly high level of collagenase expression (approximately equal to 3-7 micrograms of collagenase per 10(6) cells per 24 hr) in all examined cells. The constitutive level of synthesis of a 28-kDa collagenase inhibitor does not correlate with that of the enzyme. Phorbol 12-myristate 13-acetate stimulates the production of this inhibitor that in turn modulates the activity of collagenase in the conditioned media. As a result, the apparent activity of the enzyme present in the medium does not accurately reflect the rate of its synthesis and secretion.