IDENTIFICATION AND PURIFICATION OF A CELL-SURFACE GLYCOPROTEIN MEDIATING INTERCELLULAR-ADHESION IN EMBRYONIC AND ADULT TISSUE
IDENTIFICATION AND PURIFICATION OF A CELL-SURFACE GLYCOPROTEIN MEDIATING INTERCELLULAR-ADHESION IN EMBRYONIC AND ADULT TISSUE
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DOI:
10.1016/0092-8674(83)90379-3
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发表时间:
1983-01-01
期刊:
影响因子:
64.5
通讯作者:
BUCK, CA
中科院分区:
文献类型:
--
作者:
DAMSKY, CH;RICHA, J;BUCK, CA
An antiserum against material shed into serum-free medium by MCF-7 human mammary carcinoma cells (anti-SFM II) disrupts cell-cell interactions in murine mammary tumor epithelial cells (MMTE). An 80 kd [kilodalton] glycoprotein (GP80) was purified from SEM of MCF-7 mammary carcinoma cells that blocks the activity of anti-SFM II. Anti-SFM II also inhibits compaction of 8-cell mouse embryos, and purified GP80 blocks this reaction. An antiserum against purified GP80 (anti-GP80) has all adhesion-disrupting activities displayed by anti-SFM II. It recognizes one band at 80 kd in SFM and a 120 kd band in detergent extracts of epithelial but not fibroblastic cells. In immunofluorescence studies it is restricted to sites of cell-cell interaction in cultured epithelial cells. A cell surface glycoprotein of 120 kd, the medium form of which is .apprx. 80 kd, which is neither species nor tissue specific, is expressed at early stages of mammalian development and is found on epithelia.