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Literature summary for 3.4.24.87 extracted from

  • De Cock, E.; Hermans, C.; De Raeymaecker, J.; De Ceunynck, K.; De Maeyer, B.; Vandeputte, N.; Vandenbulcke, A.; Deckmyn, H.; Rottensteiner, H.; De Maeyer, M.; De Meyer, S.F.; Vanhoorelbeke, K.
    The novel ADAMTS13-p.D187H mutation impairs ADAMTS13 activity and secretion and contributes to thrombotic thrombocytopenic purpura in mice (2015), J. Thromb. Haemost., 13, 283-292.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D187H mutation identified in a patient with pregnancy-onset thrombotic thrombocytopenic purpura. Mutation is located in the high affinity Ca2+-binding site in the metalloprotease domain of ADAMTS13. The homozygous mutation down-regulates ADAMTS13 activity in vitro. Impaired proteolytic activity is linked to unstable Ca2+ binding. In addition, the D187H mutation affects protein secretion in vitro Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q76LX8
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leukocyte
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Homo sapiens
-

General Information

General Information Comment Organism
physiological function in Adamts13-/- mice, the transfection with homozygous mutant D187H leads to reduced ADAMTS13 secretion and activity and contributes to thrombotic thrombocytopenic purpura when these mice are triggered with recombinant human von Willebrand factor Homo sapiens