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Literature summary for 3.4.24.87 extracted from

  • Davis, A.K.; Makar, R.S.; Stowell, C.P.; Kuter, D.J.; Dzik, W.H.
    ADAMTS13 binds to CD36: a potential mechanism for platelet and endothelial localization of ADAMTS13 (2009), Transfusion, 49, 206-213.
    View publication on PubMed
Search for more literature for 3.4.24.87

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
-
 Homo sapiens 9986
-
extracellular
-
 Homo sapiens
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens ADAMTS13 contains eight thrombospondin type 1 repeats and binds to CD36, a transmembrane protein present on endothelial cells and platelets. CD36 also binds to thrombospondin-2 via three thrombospondin type 1 repeats in a manner competitive to ADAMTS13, overview ?
-
 ?
von Willebrand factor + H2O Homo sapiens ADAMTS13 cleaves ultra-large von Willebrand factor multimers ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
blood platelet ADAMTS13 associates to the platelet surface via binding of membrane-integrated CD36 Homo sapiens
-
endothelial cell ADAMTS13 associates to the cell surface via binding of membrane-integrated CD36 Homo sapiens
-
plasma
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ADAMTS13 contains eight thrombospondin type 1 repeats and binds to CD36, a transmembrane protein present on endothelial cells and platelets. CD36 also binds to thrombospondin-2 via three thrombospondin type 1 repeats in a manner competitive to ADAMTS13, overview Homo sapiens ?
-
 ?
von Willebrand factor + H2O ADAMTS13 cleaves ultra-large von Willebrand factor multimers Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
ADAMTS13
-
 Homo sapiens

General Information

General Information Comment Organism
additional information binding of ADAMTS13 to CD36 on cell surfaces might be involved in ADAMTS13 regulation and regulation of von Willebrand cleavage Homo sapiens
physiological function ADAMTS13 plays a significant role in vascular biology and thrombotic thrombocytopenic purpura Homo sapiens