Purification and primary amino acid sequence of a novel neutrophil chemotactic factor LECT2

Immunol Lett. 1996 Aug;52(1):9-13. doi: 10.1016/0165-2478(96)02572-2.


We purified a neutrophil chemotactic factor from a culture fluid of the PHA-activated human T-cell leukemia SKW-3 cells. The factor showed a 16-kDa basic protein by Tricin-SDS-polyacrylamide gel electorophoresis and analysis of amino acid composition. The primary amino acid sequence revealed that the chemotactic factor was significantly different from other known chemotactic factors, indicating a novel protein designated LECT2. The sequence revealed homology with the myb-induced myeloid protein-1 (Mim-1), which is expressed from gene in immature and normal granulocytes of chicken. Its biological function had not yet been identified. LECT2 and Mim-1 may be involved in the regulation of neutrophil functions in an as yet unidentified way.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Biological Assay
  • Chemotaxis, Leukocyte*
  • Humans
  • Intercellular Signaling Peptides and Proteins*
  • Molecular Sequence Data
  • Neutrophils / drug effects*
  • Proteins / chemistry*
  • Proteins / pharmacology*
  • Sequence Analysis
  • Sequence Homology, Amino Acid
  • T-Lymphocytes / chemistry*
  • Tumor Cells, Cultured


  • Amino Acids
  • Intercellular Signaling Peptides and Proteins
  • LECT2 protein, human
  • Proteins