Portal de Periódicos da CAPES

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.

1994; Springer Nature; Volume: 13; Issue: 10 Linguagem: Inglês

10.1002/j.1460-2075.1994.tb06516.x

1460-2075

Ryo Iwamoto, Shigeki Higashiyama, T. Mitamura, Naoyuki Taniguchi, Michael Klagsbrun, Eisuke Mekada,

Monoclonal and Polyclonal Antibodies Research

Research Article15 May 1994free access 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. R. Iwamoto R. Iwamoto Institute of Life Science, Kurume University, Fukuoka, Japan. Search for more papers by this author S. Higashiyama S. Higashiyama Institute of Life Science, Kurume University, Fukuoka, Japan. Search for more papers by this author T. Mitamura T. Mitamura Institute of Life Science, Kurume University, Fukuoka, Japan. Search for more papers by this author N. Taniguchi N. Taniguchi Institute of Life Science, Kurume University, Fukuoka, Japan. Search for more papers by this author M. Klagsbrun M. Klagsbrun Institute of Life Science, Kurume University, Fukuoka, Japan. Search for more papers by this author E. Mekada E. Mekada Institute of Life Science, Kurume University, Fukuoka, Japan. Search for more papers by this author R. Iwamoto R. Iwamoto Institute of Life Science, Kurume University, Fukuoka, Japan. Search for more papers by this author S. Higashiyama S. Higashiyama Institute of Life Science, Kurume University, Fukuoka, Japan. Search for more papers by this author T. Mitamura T. Mitamura Institute of Life Science, Kurume University, Fukuoka, Japan. Search for more papers by this author N. Taniguchi N. Taniguchi Institute of Life Science, Kurume University, Fukuoka, Japan. Search for more papers by this author M. Klagsbrun M. Klagsbrun Institute of Life Science, Kurume University, Fukuoka, Japan. Search for more papers by this author E. Mekada E. Mekada Institute of Life Science, Kurume University, Fukuoka, Japan. Search for more papers by this author Author Information R. Iwamoto1, S. Higashiyama1, T. Mitamura1, N. Taniguchi1, M. Klagsbrun1 and E. Mekada1 1Institute of Life Science, Kurume University, Fukuoka, Japan. The EMBO Journal (1994)13:2322-2330https://doi.org/10.1002/j.1460-2075.1994.tb06516.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info DRAP27, the monkey homolog of human CD9 antigen (DRAP27/CD9) and diphtheria toxin receptor (DTR) were expressed in mouse L cells. L cells transfected transiently with both DRAP27/CD9 and DTR cDNA bound approximately 10 times more diphtheria toxin (DT) than cells transfected with DTR alone. Stable L cell transfectants expressing both DTR and DRAP27/CD9 (LCH-1 cells) had 15 times more cell surface DT-binding sites and were 20 times more sensitive to DT than were stable L cell transfectants expressing DTR alone (LH-1 cells). Increased DT-binding and DT sensitivity were not due to increased DTR transcription or increased cell surface DTR protein. Co-immunoprecipitation of DRAP27/CD9 with DTR and chemical cross-linking suggest a tight association of these membrane-bound proteins. In addition, the identity of DTR and a growth factor (HB-EGF) was established. Immobilized DT specifically adsorbed HB-EGF precursor solubilized from transfected L cells and [125I]DT bound to immobilized recombinant HB-EGF. We conclude that DRAP27/CD9 associates tightly with DTR/HB-EGF and up-regulates the number of functional DTRs and DT sensitivity, and that HB-EGF is identical to DTR. Previous ArticleNext Article Volume 13Issue 101 May 1994In this issue RelatedDetailsLoading ...