Elastase inhibition by the C-terminal domains of alpha-crystallin and small heat-shock protein.
alpha-Crystallin, an abundant eye-lens protein and a stress protein in other tissues, shows structural and functional similarities with the small heat-shock proteins. One of the properties in common is the inhibition of elastase. We now report that the separated subunits of alpha-crystallin, alpha A and alpha B, also exhibit elastase inhibition, whereas phosphorylation of these subunits apparently has no influence on the inhibitory capacity. Furthermore, for both alpha A-crystallin and mouse HSP25 the putative C-terminal structural domain, comprising the major region of homology between these proteins, is sufficient to give elastase inhibition. With database search no homology could be found between the three proteins under investigation and any of the known consensus sequences of proteinase inhibitor families.
Voorter
C E
CE
Department of Biochemistry, University of Nijmegen, The Netherlands.
de Haard-Hoekman
W
W
Merck
K B
KB
Bloemendal
H
H
de Jong
W W
WW
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D051379:Mice; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000737:chemistry / Q000494:pharmacology*; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D013552:Swine
D003459:Crystallins; D009363:Neoplasm Proteins; D010196:Pancreatic Elastase