Human keratinocytes express EMMPRIN, an extracellular matrix metalloproteinase inducer
Human keratinocytes express EMMPRIN, an extracellular matrix metalloproteinase inducer
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DOI：
10.1111/1523-1747.ep12348959
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发表时间：
1996-06-01
影响因子：
6.5
通讯作者：
Biswas, C
中科院分区：
文献类型：
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作者：
DeCastro, R;Zhang, Y;Biswas, C
基质金属蛋白酶水平的增加与肿瘤侵袭和创伤愈合过程中的组织降解和重塑有关。在这两个过程中，有证据表明成纤维细胞与肿瘤细胞或角质形成细胞之间的细胞相互作用导致金属蛋白酶产生的增加。（细胞外基质金属蛋白酶诱导剂），其刺激成纤维细胞产生间质胶原酶、明胶酶A和基质溶解素-1，我们已经从LX-1人肺癌细胞中获得了编码EMMPRIN蛋白的cDNA克隆。在这项研究中，我们报告了EMMPRIN在体外和体内人角质形成细胞表面的免疫定位，和从人角质形成细胞文库中分离编码EMMPRIN的整个开放阅读框的cDNA，通过核苷酸序列分析比较来自正常人角质形成细胞和LX-1人Turner细胞的EMMPRIN cDNA，重组蛋白的表达，和使用来自两种来源的cDNA的体外翻译表明它们表达非常相似形式的EMMPRIN，天然EMMPRIN直接从角质形成细胞提取物中分离，然而，与LX-1肿瘤细胞相比，EMMPRIN的大小略小，浓度较低。这些结果证实了EMMPRIN在正常表皮中的存在，并提高了其参与调节表皮-真皮界面基质重塑的可能性。
Increased levels of matrix metalloproteinases are associated with tissue degradation and remodeling during tumor invasion and wound healing, In both processes, there is evidence that cell interactions between fibroblasts and tumor cells or keratinocytes lead to increases in metalloproteinase production, We have previously isolated and purified a tumor cell surface protein, EMMPRIN (extracellular matrix metalloproteinase inducer), which stimulates production of interstitial collagenase, gelatinase A, and stromelysin-1 by fibroblasts, and we have obtained cDNA clones that encode the EMMPRIN protein from LX-1 human lung carcinoma cells, In this study we report immunolocalization of EMMPRIN around the surface of human keratinocytes in vitro and in vivo, and isolation of cDNAs that encode the entire open reading frame for EMMPRIN from a human keratinocyte library, Comparison of the EMMPRIN cDNAs from normal human keratinocytes and LX-1 human turner cells by nucleotide sequence analysis, expression of the recombinant proteins, and in vitro translation using the cDNAs from the two sources indicate that they express very similar forms of EMMPRIN, Native EMMPRIN isolated directly from extracts of keratinocytes, however, is slightly smaller in size and is present at a lower concentration compared with that from LX-1 tumor cells, These results establish the presence of EMMPRIN in the normal epidermis and raise the possibility of its involvement in regulation of matrix remodeling at the epidermal-dermal interface.