CHARACTERIZATION OF HUMAN-SKIN FIBROBLAST EXTRACELLULAR PROTEINS BY TWO-DIMENSIONAL POLYACRYLAMIDE-GEL ELECTROPHORESIS
CHARACTERIZATION OF HUMAN-SKIN FIBROBLAST EXTRACELLULAR PROTEINS BY TWO-DIMENSIONAL POLYACRYLAMIDE-GEL ELECTROPHORESIS
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DOI：
10.1002/elps.1150090711
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发表时间：
1988-07-01
期刊：
影响因子：
2.9
通讯作者：
NEVIN, NC
中科院分区：
文献类型：
--
作者：
GRAHAM, CA;MCLEAN, WHI;NEVIN, NC
人类皮肤成纤维细胞分泌50多种蛋白质到培养基中。在本文中，这些特征是使用二维聚丙烯酰胺凝胶电泳和肽图的蛋白质代谢标记在存在和不存在霉素。其中30种已被证明是n -糖苷，4种是o -糖苷，10种没有糖基化。在主要蛋白质中，1-4组先前已被证明是成纤维细胞特异性的。肽图谱和tunicamycin治疗已经确定，第1组和第2组、第3组和第4组密切相关，第1组和第3组分别由第2组和第4组的n -糖基化产生。其他几种蛋白质的未糖基化前体形式也已被确定。这种分析蛋白质分泌的方法同时提供了许多蛋白质的丰富信息，可用于评估与发育相关的蛋白质分泌的变化，并确定细胞外生长因子和其他调节蛋白。
Human skin fibroblasts secrete over 50 proteins into the culture medium. In this paper these are characterised using two-dimensional polyacrylamide gel electrophoresis and peptide mapping of proteins metabolically labelled in the presence and absence of tunicamycin. Thirty of these proteins have been shown to be N-glycosides, 4 are O-glycosides and 10 are not glyciosylated. Of the major proteins, groups 1-4 have previously been shown to be fibroblast specific. Peptide mapping and tunicamycin treatment has identified that groups 1 and 2, and 3 and 4 are closely related and that groups 1 and 3 arise by N-glycosylation of 2 and 4, respectively. The unglycosylated precursor forms of several other proteins have also been identified. This approach to the analysis of protein secretion provides an abundance of information on many proteins simultaneously and can be used to assess the changes in protein secretion associated with development, and to identify extracellular growth factors and other regulatory proteins.