Jr. Bundgaard et al., MOLECULAR-CLONING AND EXPRESSION OF A CDNA-ENCODING NGAL - A LIPOCALIN EXPRESSED IN HUMAN NEUTROPHILS, Biochemical and biophysical research communications, 202(3), 1994, pp. 1468-1475
NGAL, a protein recently isolated from human neutrophils, is a novel m
ember of the lipocalins. NGAL binds a derivative of the bacterial chem
otactic peptide formylmethionyl-leucyl-phenylalanine and may have impo
rtant immunomodulatory functions. We here report the cloning of a cDNA
for NGAL covering a 63 bp 5' untranslated region and the coding regio
n 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. Al
ignment of the cDNA sequence of NGAL to the rat analogue, alpha(2)-mic
roglobulin related protein, demonstrates a very high degree of conserv
ation of this lipocalin. Northern blotting of a variety of tissues rev
ealed that NGAL is mainly expressed in myeloid cells, where a signal o
f approximately 850 bp is observed. A faint signal was observed in fet
al and adult human lung tissue. The molecular cloning of the NGAL cDNA
allowed the recombinant production of NGAL in E. Coil. (C) 1994 Acade
mic Press, Inc.