THE HUMAN HIP GENE, OVEREXPRESSED IN PRIMARY LIVER-CANCER ENCODES FOR A C-TYPE CARBOHYDRATE-BINDING PROTEIN WITH LACTOSE BINDING-ACTIVITY
THE HUMAN HIP GENE, OVEREXPRESSED IN PRIMARY LIVER-CANCER ENCODES FOR A C-TYPE CARBOHYDRATE-BINDING PROTEIN WITH LACTOSE BINDING-ACTIVITY
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DOI：
10.1016/0014-5793(94)80640-3
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发表时间：
1994-01-03
期刊：
影响因子：
3.5
通讯作者：
SEVE, AP
中科院分区：
文献类型：
--
作者：
CHRISTA, L;FELIN, M;SEVE, AP
HIP 最初被确定为在原发性肝癌以及胰腺和小肠等正常组织中表达的基因。根据基因数据库同源性，HIP 蛋白应由连接到单个碳水化合物识别域的信号肽组成。为了检验这一假设，HIP 和由最后 138 个 C 端氨基酸编码的推定碳水化合物识别域被表达为谷胱甘肽-S-转移酶蛋白（分别为 GST-HIP 和 GST-HIP-142）。两种重组蛋白均通过单一亲和纯化步骤从细菌裂解物中纯化，并测试了它们结合与 trisacryl GF 2000M 偶联的糖的能力。我们的结果表明，HIP 和 HIP-142 蛋白与乳糖结合，而且这种结合需要二价阳离子。因此，HIP蛋白是一种乳糖结合凝集素，其C端区域具有138个氨基酸的C型碳水化合物识别结构域的特征。
HIP was originally identified as a gene expressed in primary liver cancers, and in normal tissues such as pancreas and small intestine. Based on gene data base homologies, the HIP protein should consist of a signal peptide linked to a single carbohydrate recognition domain. To test this hypothesis HIP and the putative carbohydrate recognition domain encoded by the last 138 C-terminal amino acids, were expressed as glutathione-S-transferase proteins (GST-HIP and GST-HIP-142, respectively). Both recombinant proteins were purified by a single affinity purification step from bacterial lysates and their ability to bind saccharides coupled to trisacryl GF 2000M were tested. Our results show that HIP and HIP-142 proteins bind to lactose, moreover the binding requires divalent cations. Thus the HIP protein is a lactose-binding lectin with the characteristics of a C-type carbohydrate recognition domain of 138 amino acids in the C-terminal region.