Heparin-binding EGF-like growth factor, which acts as the diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which up-regulates functional receptors and diphtheria toxin sensitivity
作者： R. Iwamoto , S. Higashiyama , T. Mitamura , N. Taniguchi , M. Klagsbrun
DOI: 10.1002/J.1460-2075.1994.TB06516.X
关键词:
摘要: DRAP27, the monkey homolog of human CD9 antigen (DRAP27/CD9) and diphtheria toxin receptor (DTR) were expressed in mouse L cells. cells transfected transiently with both DRAP27/CD9 DTR cDNA bound approximately 10 times more (DT) than alone. Stable cell transfectants expressing (LCH-1 cells) had 15 surface DT-binding sites 20 sensitive to DT stable alone (LH-1 cells). Increased sensitivity not due increased transcription or protein. Co-immunoprecipitation chemical cross-linking suggest a tight association these membrane-bound proteins. In addition, identity growth factor (HB-EGF) was established. Immobilized specifically adsorbed HB-EGF precursor solubilized from [125I]DT immobilized recombinant HB-EGF. We conclude that associates tightly DTR/HB-EGF up-regulates number functional DTRs sensitivity, is identical DTR.
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