s100a6 protein negatively regulates cacybpsip-mediated inhibition of gastric cancer cell proliferation and tumorigenesiss100a6蛋白负调节cacybpsip-mediated抑制胃癌细胞增殖和肿瘤发生.pdfVIP
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s100a6 protein negatively regulates cacybpsip-mediated inhibition of gastric cancer cell proliferation and tumorigenesiss100a6蛋白负调节cacybpsip-mediated抑制胃癌细胞增殖和肿瘤发生
S100A6 Protein Negatively Regulates CacyBP/SIP-
Mediated Inhibition of Gastric Cancer Cell Proliferation
and Tumorigenesis
1 . 2. 4 3 1 1 1
Xiaoxuan Ning * , Shiren Sun , Kun Zhang , Jie Liang , Yucai Chuai , Yuan Li *, Xiaoming Wang *
1 Department of Geriatrics, Xijing Hospital, Fourth Military Medical University, Xi’an, Shaanxi, China, 2 Department of Nephrology, Xijing Hospital, Fourth Military Medical
University, Xi’an, Shaanxi, China, 3 State Key Laboratory of Cancer Biology and Institute of Digestive Diseases, Xijing Hospital, Fourth Military Medical University, Xi’an,
Shaanxi, China, 4 College of Life Science, Shaanxi Normal University, Xi’an, Shaanxi, China
Abstract
Calcyclin-binding protein (CacyBP/SIP), identified on the basis of its ability to interact with S100 proteins in a calcium-
dependent manner, was previously found to inhibit the proliferation and tumorigenesis of gastric cancer cells in our
laboratory. Importantly, the effects of S100 proteins on the biological behavior of CacyBP/SIP in gastric cancer remain
unclear. Herein, we report the construction of eukaryotic expression vectors for wild-type CacyBP/SIP and a truncated
mutant lacking the S100 protein binding domain (CacyBP/SIPDS100). The expressions of the wild-type and truncated
recombinant proteins were demonstrated by transfection of MKN45 gastric cancer cells. Co-immunoprecipitation assays
demonstrated interaction between S100A6 and wild-type CacyBP/SIP in MKN45 cells. Removal of the S100 protein binding
domain dramatically reduced the affinity of CacyBP/SIP for S100 proteins as indicated by reduced co-immunoprecipitation
of S100A6 by CacyBP/SIPDS100. The MTT a
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