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人肿瘤细胞衍生的胶原酶刺激因子(重新命名为EMMPRIN)是免疫球蛋白超家族的一员。

The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily.

作者信息

Biswas C, Zhang Y, DeCastro R, Guo H, Nakamura T, Kataoka H, Nabeshima K

机构信息

Department of Anatomy and Cellular Biology, Tufts University School of Medicine, Boston, Massachusetts 02111.

出版信息

Cancer Res. 1995 Jan 15;55(2):434-9.

PMID:7812975
Abstract

Tumor cell-derived collagenase stimulatory factor, renamed extracellular matrix metalloproteinase inducer (EMMPRIN), is a M(r) approximately 58,000 glycoprotein which is located on the outer surface of human tumor cells and which interacts with fibroblasts to stimulate expression of several matrix metalloproteinases in the fibroblasts. In this study, we have used several approaches to isolate a complementary DNA encoding EMMPRIN. Several peptide sequences obtained from the isolated M(r) 58,000 glycoprotein are found in the translated complementary DNA clone, verifying its identity. Computer database searches indicate that EMMPRIN is a member of the immunoglobulin superfamily and that the deduced amino acid sequence of EMMPRIN is identical to that recently reported for human basigin and M6 antigen, molecules of previously undetermined biological function.

摘要

肿瘤细胞衍生的胶原酶刺激因子,现更名为细胞外基质金属蛋白酶诱导因子(EMMPRIN),是一种分子量约为58,000的糖蛋白,位于人类肿瘤细胞的外表面,它与成纤维细胞相互作用,刺激成纤维细胞中几种基质金属蛋白酶的表达。在本研究中,我们采用了多种方法来分离编码EMMPRIN的互补DNA。从分离出的分子量为58,000的糖蛋白中获得的几个肽序列在翻译后的互补DNA克隆中被发现,证实了其身份。计算机数据库搜索表明,EMMPRIN是免疫球蛋白超家族的成员,并且EMMPRIN推导的氨基酸序列与最近报道的人类基底膜蛋白和M6抗原相同,这两种分子的生物学功能以前尚未确定。

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