Literature DB >> 15110752

High molecular mass kininogen inhibits metalloproteinases of Bothrops jararaca snake venom.

Luís Roberto de Camargo Gonçalves1, Ana Marisa Chudzinski-Tavassi.   

Abstract

High molecular mass kininogen (HK) purified from Bothrops jararaca (Bj) plasma was tested on activities of the Bj venom in vivo and in vitro. Results showed that, when incubated with BjHK, the Bj venom presented inhibition on hemorrhagic, edema forming, myotoxic, and coagulant activities. It is well known that metalloproteinases are directly or indirectly involved in these activities. Similarly, human HK inhibits the hemorrhagic effect of the Bj venom as well as hemorrhagic and enzymatic effects of jararhagin, a hemorrhagic metalloproteinase isolated from Bj venom. Complex between HK and jararhagin was not detected by gel filtration. Nevertheless, the inhibitory effect of the hemorrhagic activity of the venom was only partial when HK was pre-incubated with 0.4mM ZnCl(2) or with 0.45mM CaCl(2). These data suggest that the inhibitory effect depends, at least partially, on the competition for ions between kininogen and metalloproteinases of the venom.

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Year:  2004        PMID: 15110752     DOI: 10.1016/j.bbrc.2004.03.182

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  1 in total

Review 1.  The modular nature of bradykinin-potentiating peptides isolated from snake venoms.

Authors:  Juliana Mozer Sciani; Daniel Carvalho Pimenta
Journal:  J Venom Anim Toxins Incl Trop Dis       Date:  2017-10-26
  1 in total

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