Isolation and sequence of a human gene encoding a potent inhibitor of leukocyte proteases.
We report the isolation of the human gene encoding an inhibitor of neutrophil elastase and cathepsin G. We have sequenced the gene and a cDNA clone isolated from human parotid tissue. The protein encoded by this gene appears to contain two functional domains, one having a trypsin inhibitory site and the other an elastase inhibitory site. The two-domain structure of the protein is reflected in the organization of the gene, with each domain represented by a separate exon. We have also noted that the intervening sequence separating the trypsin-inhibitor-exon and the elastase-inhibitor-exon is flanked by eleven base-pair direct repeats, suggesting that this intron may have been generated by a transposition-type event.
D001483:Base Sequence; D056649:Cathepsin G; D002403:Cathepsins / Q000037:antagonists & inhibitors*; D005091:Exons; D005796:Genes; D006801:Humans; D007438:Introns; D007962:Leukocytes / Q000201:enzymology*; D009841:Oligonucleotides / Q000138:chemical synthesis / Q000235:genetics; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D010306:Parotid Gland / Q000502:physiology; D011480:Protease Inhibitors / Q000235:genetics* / Q000378:metabolism; D011487:Protein Conformation; D012697:Serine Endopeptidases; D013329:Structure-Activity Relationship
D009841:Oligonucleotides; D011480:Protease Inhibitors; D002403:Cathepsins; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G; D010196:Pancreatic Elastase