Molecular cloning and expression of a cDNA encoding NGAL: a lipocalin expressed in human neutrophils

Biochem Biophys Res Commun. 1994 Aug 15;202(3):1468-75. doi: 10.1006/bbrc.1994.2096.

Abstract

NGAL, a protein recently isolated from human neutrophils, is a novel member of the lipocalins. NGAL binds a derivative of the bacterial chemotactic peptide formylmethionyl-leucyl-phenylalanine and may have important immunomodulatory functions. We here report the cloning of a cDNA for NGAL covering a 63 bp 5' untranslated region and the coding region of 591 bp. The cDNA encodes a protein of 197 amino acids, with a 19 amino acid leader sequence and a mature protein of 178 amino acids. Alignment of the cDNA sequence of NGAL to the rat analogue, alpha 2-microglobulin related protein, demonstrates a very high degree of conservation of this lipocalin. Northern blotting of a variety of tissues revealed that NGAL is mainly expressed in myeloid cells, where a signal of approximately 850 bp is observed. A faint signal was observed in fetal and adult human lung tissue. The molecular cloning of the NGAL cDNA allowed the recombinant production of NGAL in E. coli.

MeSH terms

  • Acute-Phase Proteins*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Carrier Proteins / genetics*
  • Cloning, Molecular
  • DNA, Complementary
  • Escherichia coli / genetics
  • Humans
  • Lipocalin-2
  • Lipocalins
  • Molecular Sequence Data
  • Neutrophils / metabolism*
  • Oncogene Proteins*
  • Proto-Oncogene Proteins
  • RNA, Messenger / metabolism
  • Sequence Homology, Amino Acid

Substances

  • Acute-Phase Proteins
  • Carrier Proteins
  • DNA, Complementary
  • LCN2 protein, human
  • Lipocalin-2
  • Lipocalins
  • Oncogene Proteins
  • Proto-Oncogene Proteins
  • RNA, Messenger

Associated data

  • GENBANK/X83006