Abstract
Jararafibrase I is a hemorrhagic metalloproteinase purified from Bothrops jararaca venom, which induces local hemorrhage by degrading the basement membrane components. The present study was undertaken to investigate the inhibition of jararafibrase I by human and rat serum proteinase inhibitors. The proteolytic activity of jararafibrase I was completely inhibited by human and rat sera. In particular, rat serum displayed a greater inhibitory capacity. The inhibitory capacities of both sera were dependent on α-macroglobulins. SDS-PAGE analysis revealed that jararafibrase I formed complexes with α-macroglobulins that were present in normal sera. The proteolytic activity of jararafibrase I was completely inhibited by α1-macroglobulin and murinoglobulin in rat serum, and by human α2-macroglobulin. The inhibition molar ratios of α-macroglobulin/jararafibrase I were 1.5 for rat α1-macroglobulin and human α2-macroglobulin, and 2.4 for rat murinoglobulin. SDS-PAGE under reducing conditions demonstrated that the bait region of human α2-macroglobulin and rat murinoglobulin was cleaved by jararafibrase I. The bait region cleavage sites were identified as being situated at the 696Arg– 697Leu peptide bond in human α2-macroglobulin, and at the 686Ala– 687Val peptide bond in rat murinoglobulin.
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