| http://purl.uniprot.org/citations/7639679 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7639679 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7639679 | http://www.w3.org/2000/01/rdf-schema#comment | "A potent platelet aggregation inducer, aggretin, was purified from Malayan-pit-viper (Calloselasma rhodostoma) venom by ionic-exchange chromatography, gel-filtration chromatography and HPLC. It is a heterodimeric protein (29 kDa) devoid of esterase, phospholipase A and thrombin-like activity. Aggretin (> 5 nM) elicited platelet aggregation with a lag period in both human platelet-rich plasma and washed platelet suspension. EDTA (5 mM), prostaglandin E1 (1 microM) and 3,4,5-trimethoxybenzoic acid 8-(diethylamino)octyl ester ('TMB-8'; 100 microM) abolished its aggregating activity, indicating that exogenous bivalent cations and intracellular Ca2+ mobilization are essential for aggretin-induced platelet aggregation. Neomycin (4 mM) and mepacrine (50 microM) completely inhibited aggretin (33 nM)-induced aggregation; however, creatine phosphate/creatine phosphokinase (5 mM, 5 units/ml) and indomethacin (50 microM) did not significantly affect its aggregating activity. Aggretin caused a significant increase of [3H]InsP formation in [3H]Ins-loaded platelets, intracellular Ca2+ mobilization and thromboxane B2 formation. Neomycin, a phospholipase C inhibitor, completely inhibited both the increase of [3H]InsP and intracellular Ca2+ mobilization of platelets stimulated by aggretin. A monoclonal antibody (6F1) directed against glycoprotein Ia/IIa inhibited platelet shape change and aggregation induced by aggretin. 125I-aggretin bound to platelets with a high affinity (Kd = 4.0 +/-1.1 nM), and the number of binding sites was estimated to be 2119 +/-203 per platelet. It is concluded that aggretin may act as a glycoprotein Ia/IIa agonist to elicit platelet aggregation through the activation of endogenous phospholipase C, leading to hydrolysis of phosphoinositides and subsequent intracellular Ca2+ mobilization."xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj3091021"xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj3091021"xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/author | "Yang S.-H."xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/author | "Yang S.-H."xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/author | "Huang T.-F."xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/author | "Huang T.-F."xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/author | "Liu C.-Z."xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/author | "Liu C.-Z."xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/pages | "1021-1027"xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/pages | "1021-1027"xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/title | "Aggretin, a novel platelet-aggregation inducer from snake (Calloselasma rhodostoma) venom, activates phospholipase C by acting as a glycoprotein Ia/IIa agonist."xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/title | "Aggretin, a novel platelet-aggregation inducer from snake (Calloselasma rhodostoma) venom, activates phospholipase C by acting as a glycoprotein Ia/IIa agonist."xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/volume | "309"xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://purl.uniprot.org/core/volume | "309"xsd:string |
| http://purl.uniprot.org/citations/7639679 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7639679 |
| http://purl.uniprot.org/citations/7639679 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7639679 |
| http://purl.uniprot.org/citations/7639679 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7639679 |
| http://purl.uniprot.org/citations/7639679 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7639679 |