Elafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence.
A potent inhibitor of human leukocyte elastase (EC 3.4.21.37) and porcine pancreatic elastase (EC 3.4.21.36) was purified to homogeneity from human horny layers. It inhibits human leukocyte elastase and porcine pancreatic elastase in a 1:1 molar ratio and shows equilibrium dissociation constants of 6 x 10(-10) M and 1 x 10(-9) M, respectively. Inhibition of plasmin, trypsin, alpha-chymotrypsin, and cathepsin G was not observed. This inhibitor proved to be an acid stable basic peptide with an isoelectric point of 9.7. The complete amino acid sequence appears to be unique with 38% homology to the C-terminal half of antileukoprotease. The sequence shows that the inhibitor is composed of 57 amino acids and predicts a Mr of 7017. The high affinity as well as the apparent specificity for elastases suggests a functional role in preventing elastase-mediated tissue proteolysis. It is suggested that the term "elafin" be used to designate this inhibitor.
Department of Dermatology, University of Kiel, Federal Republic of Germany.
O
O
Wiedow
J M
JM
Schröder
H
H
Gregory
J A
JA
Young
E
E
Christophers
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007962:Leukocytes / Q000201:enzymology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors* / Q000097:blood; D053491:Proteinase Inhibitory Proteins, Secretory; D011506:Proteins; D012689:Sequence Homology, Nucleic Acid; D015842:Serine Proteinase Inhibitors / Q000235:genetics / Q000302:isolation & purification* / Q000494:pharmacology; D012867:Skin / Q000378:metabolism*
D053491:Proteinase Inhibitory Proteins, Secretory; D011506:Proteins; D015842:Serine Proteinase Inhibitors; D010196:Pancreatic Elastase