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PMID: 2775493 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The human neutrophil elastase gene. Analysis of the nucleotide sequence reveals three distinct classes of repetitive DNA.

Biological chemistry Hoppe-Seyler ·Vol. 370 ·No. 7 ·1989-07-00 ·Pages 737-44

Farley D, Travis J, Salvesen G

Abstract

DNA sequence analysis reveals the gene encoding human neutrophil elastase to be contained on a 6-kb EcoRI fragment. The gene contains five exons and closely resembles rat mast cell proteinase II and mouse adipsin in its exon structure and intron splice phase. Non-coding regions are very rich in repetitive DNA, containing seven Alu-like segments, three distinct clustered direct repeats with monomer lengths of 53 (six repeats), 23 (three repeats) and 41 (ten repeats) nucleotides, and a 200-nucleotide AT-rich region. Protein sequence analysis, inferred from the coding regions of the gene, indicates that neutrophil elastase may contain an unusual activation peptide similar to that found in the other major neutrophil serine proteinase, cathepsin G.

MeSH Terms
DNA/analysis DNA, Recombinant Humans Molecular Sequence Data Neutrophils/enzymology Pancreatic Elastase/biosynthesis,genetics Repetitive Sequences, Nucleic Acid
Chemicals
DNA, Recombinant DNA Pancreatic Elastase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Farley D
Department of Biochemistry, University of Georgia, Athens.
Travis J
Salvesen G
Article Info
Journal
Biological chemistry Hoppe-Seyler
Abbr.
Biol Chem Hoppe Seyler
ISSN
0177-3593
Published
1989-07-00
Pages
737-44
Language
English
Region
Germany
NLM ID
8503054
Subset
IM
Grants
NCI NIH HHS · CA29589 · United States
NHLBI NIH HHS · HL26887 · United States
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