NMR structure and regulated expression in APL cell of human SH3BGRL3

被引:24
作者
Xu, C
Zheng, PZ
Shen, SH
Xu, YQ
Wei, L
Gao, HJ
Wang, SN
Zhu, CR
Tang, YJ
Wu, JH
Zhang, QH [1 ]
Shi, YY
机构
[1] Shanghai Med Univ 2, Ruijin Hosp, Shanghai Inst Hematol, State Key Lab Med Genom, Shanghai 20025, Peoples R China
[2] Univ Sci & Technol China, Sch Life Sci, Hefei Natl Lab Phys Sci Mircoscale, Anhua 230026, Peoples R China
[3] Natl Engn Ctr Biochip Shanghai, Shanghai 201203, Peoples R China
[4] Fujian Med Univ, Union Hosp, Dept Clin Lab, Fujian 350001, Peoples R China
来源
FEBS LETTERS | 2005年 / 579卷 / 13期
基金
中国国家自然科学基金;
关键词
SH3 domain binding glutamic acid-rich protein like 3; nuclear magnetic resonance structure; leukemia; all-trans retinoic acid; differentiation; localization;
D O I
10.1016/j.febslet.2005.04.011
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
SH3 domain binding glutamic acid-rich protein like 3 (SH3BGRL3) is the new member of thioredoxin (TRX) super family, whose posttranslational modified form was identified as tumor necrosis factor alpha (TNF-alpha) inhibitory protein, TIP-B1. In this paper, we determined its solution structure by multidimensional nuclear magnetic resonance spectroscopy. The overall structure of human SH3BGRL3 conformed to a TRX-like fold. To understand its function in vivo, the upregulated expression in acute promyelocytic leukemia cell line NB4 at both mRNA and protein level was elucidated. Immunofluorescence and immunohistochemistry staining with monoclonal antibody against SH3BGRL3 demonstrated that it was a cytoplasmic protein in both NB4 cell and human tissues. These results, as a whole, indicate that SH3BGRL3 may function as a regulator in all-trans retinoic acid-induced pathway. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:2788 / 2794
页数:7
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