Abstract
Three main collagen binding proteins from trophozoites of E. histolytica have been isolated: 105 kDa, 56 kDa and 30 kDa. They display a type I collagenolytic activity. The enzyme behaves as a mammalian collagenase regarding to its activity, collagen degradation products and inhibitors. Antibodies against affinity-purified molecules inhibit the binding of trophozoites to collagen substrates. Indirect evidence suggests that the 30 kDa molecule is the putative collagen receptor. These surface molecules may be necessary for attachment and migration of the parasite into solid tissue.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Chromatography, Affinity
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Collagen / metabolism
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Collagenases / isolation & purification*
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Entamoeba histolytica / chemistry*
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Entamoeba histolytica / growth & development
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Integrins / isolation & purification*
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Matrix Metalloproteinase Inhibitors
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Membrane Proteins / isolation & purification*
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Molecular Weight
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Protozoan Proteins / antagonists & inhibitors
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Protozoan Proteins / isolation & purification*
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Receptors, Collagen
Substances
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Integrins
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Matrix Metalloproteinase Inhibitors
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Membrane Proteins
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Protozoan Proteins
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Receptors, Collagen
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Collagen
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Collagenases