Altered regulation of protein tyrosine phosphorylation in anikis-resistant tumor cells
文献类型：期刊论文
| 作者 | Zhang, LN; Zha, XL; Yu, Q
|
| 刊名 | PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS
 |
| 出版日期 | 2005-11 |
| 卷号 | 32期号:11页码:1047-1054 |
| 关键词 | anoikis src homologue 2 tyrosine phosphorylation tumor cell |
| ISSN号 | 1000-3282 |
| 文献子类 | Article |
| 英文摘要 | Anoikis is a type of apoptosis that results from cell detachment from the extracellular matrix. Resistance to anoikis may allow survival of cancer cells during metastasis. It has been found that PI3K-PKB/Akt and MAPK pathways confer anoikis resistance to cancer cells. However, the tyrosine kinase pathways upstream of PI3K-PKB/Akt and MAPK have not been adequately explored. In an attempt to identify specific phosphotyrosine-containing proteins and potential tyrosine kinase pathways involved in anoikis resistance, a functional screening method based on the specific interaction between src homologue 2 (SH(2)) domains and phosphotyrosine (p-Tyr) containing proteins was designed. Cell detachment rendered normal MDCK cells to undergo anoikis. However, the survival and proliferation of tumor cells was anchorage-independent. Consistent with this phenomenon, cell detachment induced rapid decrease in SH(2)s-binding tyrosine phosphorylated proteins in MDCK cells, while tyrosine phosphorylation of SH(2)-binding proteins in tumor cells was anchorage-independent. It was also found that tyrosine phosphorylation levels of Abl SH(2)-associated proteins decreased in detached MDCK cells. However, the tyrosine phosphorylation levels of Abl SH(2)-associated proteins in H460 lung tumor cells increased after a transient decrease, and the levels increased in H1792 lung tumor cells upon detachment. Using this functional screening method, some of the Fyn SH(2) and Crk SH(2)-binding proteins were identified as FAK and p130Cas respectively, which are critical in mediating cell-matrix interactions. The present data suggest that multiple phosphotyrosine-containing proteins and potential tyrosine kinase pathways may act to support the anoikis resistance of tumor cells. The SH(2)-domain screening method may be an efficient way to explore anoikis-resistance-related phosphotyrosine-containing proteins and potential tyrosine kinase pathways in tumor cells. |
| WOS关键词 | LUNG ADENOCARCINOMA CELLS ; FOCAL ADHESION KINASE ; GROWTH-FACTOR RECEPTOR ; SIGNALING PATHWAYS ; EPITHELIAL-CELLS ; SH2 DOMAIN ; ANOIKIS ; SURVIVAL ; SRC ; ACTIVATION |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
| 语种 | 中文 |
| WOS记录号 | WOS:000233534300008 |
| 出版者 | CHINESE ACAD SCIENCES, INST BIOPHYSICS |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/273787]  |
| 专题 | 药理学第一研究室 |
| 通讯作者 | Zha, XL |
| 作者单位 | 1.Fudan Univ, Shanghai Med Coll, Key Lab Glycoconjugate Res, Dept Biochem & Mol Biol, Shanghai 200032, Peoples R China 2.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China 3.Boston Univ, Ctr Med, Dept Biochem, Boston, MA 02118 USA 4.Boston Univ, Ctr Med, Ctr Pulm, Boston, MA 02118 USA |
| 推荐引用方式 GB/T 7714 | Zhang, LN,Zha, XL,Yu, Q. Altered regulation of protein tyrosine phosphorylation in anikis-resistant tumor cells[J]. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS,2005,32(11):1047-1054. |
| APA | Zhang, LN,Zha, XL,&Yu, Q.(2005).Altered regulation of protein tyrosine phosphorylation in anikis-resistant tumor cells.PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS,32(11),1047-1054. |
| MLA | Zhang, LN,et al."Altered regulation of protein tyrosine phosphorylation in anikis-resistant tumor cells".PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS 32.11(2005):1047-1054. |
入库方式： OAI收割
来源：上海药物研究所
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