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.
| Original language | English |
|---|---|
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 202 |
| Issue number | 3 |
| Pages (from-to) | 1468-75 |
| Number of pages | 8 |
| ISSN | 0006-291X |
| DOIs | |
| Publication status | Published - 15 Aug 1994 |
| Externally published | Yes |
Keywords
- 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
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