Molecular cloning of human and bovine LECT2 having a neutrophil chemotactic activity and its specific expression in the liver

Biochim Biophys Acta. 1998 Mar 4;1396(1):105-13. doi: 10.1016/s0167-4781(97)00181-4.


We previously reported the purification and amino acid sequence of a novel neutrophil chemotactic protein termed LECT2 (leukocyte cell-derived chemotaxin 2). In this paper we report molecular cloning of human and bovine LECT2 cDNAs based on the amino acid sequence of the purified protein. The deduced amino acid sequence of human LECT2 (hLECT2) shows an 86% identity to bovine LECT2 (bLECT2). The deduced primary structures of LECT2 were highly homologous to the repeated units of Mim-1 protein (myb induced myeloid protein-1). The mim-1 gene is one of the known myb target genes and is specifically expressed in normal and transformed immature granulocytes in the chicken. Northern blot analysis of normal human tissues demonstrated that the hLECT2 gene is specifically expressed in the adult and fetal livers. In addition, several human hepatoma cell lines also expressed LECT2 mRNA, suggesting that hepatic cells in the liver produce LECT2 protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cattle
  • Chemotactic Factors / biosynthesis*
  • Chemotactic Factors / genetics*
  • Chemotaxis, Leukocyte
  • Cloning, Molecular
  • DNA, Complementary / isolation & purification
  • Gene Expression
  • Humans
  • Intercellular Signaling Peptides and Proteins*
  • Liver / metabolism*
  • Molecular Sequence Data
  • Neutrophils / immunology*
  • Protein Biosynthesis*
  • Proteins / genetics*
  • RNA, Messenger / biosynthesis
  • Tumor Cells, Cultured


  • Chemotactic Factors
  • DNA, Complementary
  • Intercellular Signaling Peptides and Proteins
  • LECT2 protein, Bos taurus
  • LECT2 protein, human
  • Proteins
  • RNA, Messenger

Associated data

  • GENBANK/AB001350
  • GENBANK/D63521