INTERLEUKIN-6-INDUCED TYROSINE PHOSPHORYLATION OF MULTIPLE PROTEINS IN MURINE HEMATOPOIETIC LINEAGE CELLS

被引：33

作者：

MATSUDA, T ^{[1
]}

YAMANAKA, Y ^{[1
]}

HIRANO, T ^{[1
]}

机构：

[1] OSAKA UNIV, SCH MED, BIOMED RES CTR, SUITA, OSAKA 565, JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 200卷 / 02期

关键词：

D O I：

10.1006/bbrc.1994.1525

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：

Interleukin-6 (IL-6) is a multifunctional cytokine playing various roles in the immune system, hematopoiesis and acute phase reactions. To elucidate the intracellular signal transduction mechanism through the IL-6 receptor, we investigated IL-6-induced protein tyrosine phosphorylation in murine hematopoietic cell lines, BAFm130 and Y6. IL-6 stimulated tyrosine phosphorylation of multiple cellular proteins, such as gp130, an IL-6 signal transducer; Jak family of the cytoplasmic tyrosine kinases; and the latent cytoplasmic signal transducer and activator of transcription. We showed that the pattern of these tyrosine-phosphorylated molecules was different between BAFm130 and Y6 cells on which IL-6 exhibited different biological activities. (C) 1994 Academic Press, Inc.

引用

页码：821 / 828

页数：8

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