Source:http://linkedlifedata.com/resource/pubmed/id/14757212
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2004-2-3
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pubmed:abstractText |
Snake Venom Metalloproteinases (SVMPs) are synthesized as zymogens and undergo proteolytic processing resulting in a variety of multifunctional proteins. Jararhagin is a P-III SVMP, isolated from the venom of Bothrops jararaca, comprising metalloproteinase, disintegrin-like and cysteine-rich domains. The catalytic domain is responsible for the hemorrhagic activity. The disintegrin-like/cysteine-rich domains block alpha2beta1 integrin binding to collagen and apparently enhance the hemorrhagic activity of SVMPs. The relevance of disintegrin-like domain is described in this paper using a series of mouse anti-jararhagin monoclonal antibodies (MAJar 1-7). MAJar 3 was the only antibody able to completely neutralize jararhagin hemorrhagic activity. Neutralization of catalytic activity was partial by incubation with MAJar 1. MAJars 1 and 3 efficiently neutralized jararhagin binding to collagen with IC50 of 330 and 8.4 nM, respectively. MAJars 1 and 3 recognized the C-terminal portion of the disintegrin domain, which is apparently in conformational proximity with the catalytic domain according to additivity tests. These data suggest that disintegrin-like domain epitopes are in close contact with catalytic site or functionally modulate the expression of hemorrhagic activity in SVMPs.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Crotalid Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloproteases,
http://linkedlifedata.com/resource/pubmed/chemical/jararhagin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0041-0101
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
801-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14757212-Animals,
pubmed-meshheading:14757212-Antibodies, Monoclonal,
pubmed-meshheading:14757212-Antibody Specificity,
pubmed-meshheading:14757212-Bothrops,
pubmed-meshheading:14757212-Collagen,
pubmed-meshheading:14757212-Crotalid Venoms,
pubmed-meshheading:14757212-Hemorrhage,
pubmed-meshheading:14757212-Metalloendopeptidases,
pubmed-meshheading:14757212-Metalloproteases,
pubmed-meshheading:14757212-Mice,
pubmed-meshheading:14757212-Mice, Inbred BALB C,
pubmed-meshheading:14757212-Structure-Activity Relationship
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pubmed:year |
2003
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pubmed:articleTitle |
Snake venom metalloproteinases: structure/function relationships studies using monoclonal antibodies.
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pubmed:affiliation |
Laboratório de Imunopatologia, Instituto Butantan, Av. Vital Brasil, 1500, CEP 05503-900, São Paulo, SP, Brazil.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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