Entamoeba histolytica collagen binding proteins.
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.
Rosales-Encina
J L
JL
Departamento de Patología Experimental, CINVESTAV-IPN, México, DF.
Campos-Salazar
M S
MS
Rojkind Matluk
M
M
D000818:Animals; D002846:Chromatography, Affinity; D003094:Collagen / Q000378:metabolism; D017364:Collagenases / Q000302:isolation & purification*; D004748:Entamoeba histolytica / Q000737:chemistry* / Q000254:growth & development; D016023:Integrins / Q000302:isolation & purification*; D061965:Matrix Metalloproteinase Inhibitors; D008565:Membrane Proteins / Q000302:isolation & purification*; D008970:Molecular Weight; D015800:Protozoan Proteins / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D038981:Receptors, Collagen
D016023:Integrins; D061965:Matrix Metalloproteinase Inhibitors; D008565:Membrane Proteins; D015800:Protozoan Proteins; D038981:Receptors, Collagen; D003094:Collagen; D017364:Collagenases