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The human HIP gene, overexpressed in primary liver cancer encodes for a C‐type carbohydrate binding protein with lactose binding activity
Author(s) -
Christa Laurence,
Felin Murielle,
Morali Olivier,
Simon Marie-Thérèse,
Lasserre Chantal,
Brechot Christian,
Sève Annie-Pierre
Publication year - 1994
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 - 10.1016/0014-5793(94)80640-3
Subject(s) - biochemistry , carbohydrate responsive element binding protein , gene , amino acid , carbohydrate , biology , chemistry , transcription factor
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.