Purification and primary amino acid sequence of a novel neutrophil chemotactic factor LECT2.
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.
Yamagoe
S
S
Department of Bioactive Molecules, National Institute of Health, Tokyo, Japan.
Yamakawa
Y
Y
Matsuo
Y
Y
Minowada
J
J
Mizuno
S
S
Suzuki
K
K
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001681:Biological Assay; D002634:Chemotaxis, Leukocyte; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000187:drug effects*; D011506:Proteins / Q000737:chemistry* / Q000494:pharmacology*; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D013601:T-Lymphocytes / Q000737:chemistry*; D014407:Tumor Cells, Cultured
D000596:Amino Acids; D036341:Intercellular Signaling Peptides and Proteins; C103468:LECT2 protein, human; D011506:Proteins