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The apoptosis‐associated protein BNIPL interacts with two cell proliferation‐related proteins, MIF and GFER
Author(s) -
Shen Li,
Hu Jian,
Lu Hong,
Wu Ming,
Qin Wenxin,
Wan Dafang,
Li Yu-Yang,
Gu Jianren
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00229-1
Subject(s) - immunoprecipitation , cell growth , macrophage migration inhibitory factor , apoptosis , saccharomyces cerevisiae , microbiology and biotechnology , biology , yeast , chemistry , biochemistry , gene , immunology , cytokine
Bcl‐2/adenovirus E1B 19 kDa interacting protein 2‐like, BNIP‐2‐like (BNIPL) is a recently cloned and characterized apoptosis‐associated protein that shares 72% homology with BNIP‐2. It is highly expressed in human placenta and lung. A yeast two‐hybrid system was used to obtain two BNIPL‐interacting proteins, MIF (macrophage migration inhibitory factor) and GFER (growth factor erv1 ( Saccharomyces cerevisiae )‐like). The interactions were confirmed by glutathione S ‐transferase pull‐down assay in vitro and co‐immunoprecipitation assay in vivo. Colony formation assay and cell proliferation test suggest that overexpression of BNIPL could inhibit the growth of BEL‐7402 cells. These findings suggest that BNIPL may physically bind to cell proliferation‐related proteins, MIF and GFER.