NDF/HEREGULIN STIMULATES THE PHOSPHORYLATION OF HER3/ERBB3

被引:72
作者
KITA, YA
BARFF, J
LUO, Y
WEN, DZ
BRANKOW, D
HU, S
LIU, NL
PRIGENT, SA
GULLICK, WJ
NICOLSON, M
机构
[1] AMGEN INC, AMGEN CTR, DEPT MAMALIAN CELL MOLEC BIOL, THOUSAND OAKS, CA 91320 USA
[2] AMGEN INC, AMGEN CTR, DEPT PROC DEV, THOUSAND OAKS, CA 91320 USA
[3] UNIV CALIF SAN DIEGO, CTR CANC, SCH MED, DEPT MED, LA JOLLA, CA 92093 USA
[4] UNIV CALIF SAN DIEGO, CTR CANC, SCH MED, DEPT PHARMACOL, LA JOLLA, CA 92093 USA
[5] HAMMERSMITH HOSP, IMPERIAL CANC RES FUND, INCOL UNIT, LONDON W12 0NN, ENGLAND
来源
FEBS LETTERS | 1994年 / 349卷 / 01期
关键词
HER3; ERBB3; NDF; HEREGULIN; TYROSINE KINASE; EGF RECEPTOR FAMILY;
D O I
10.1016/0014-5793(94)00644-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Her3/erbB3 has been identified as a third member of the epidermal growth factor receptor (EGFR) family [(1989) Proc. Natl. Acad. Sci. USA 86, 9193-9197; (1990) Proc. Natl. Acad. Sci. USA 87, 4905-4909]. The natural ligand for Her3 has not been identified. Although recently NDF has been proposed as a specific ligand for Her4 [(1993) Nature 366, 473-475; (1993) J. Biol. Chem. 268, 18407-18410], we report here that Her3 was phosphorylated on tyrosine not only in three breast carcinoma cell lines, MDAMB453, MDAMB468 and SKBR3, but also in Her3-transfected CHO cells in response to NDF stimulation. In further studies, cells were reacted with I-125-labeled NDF and then chemically crosslinked. Immunoprecipitation with anti-Her3 revealed a dense high M(W) band, greater than 400 kDa. The results suggest that NDF may be a ligand of Her3 and induces receptor hetero-oligomerization.
引用
收藏
页码:139 / 143
页数:5
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