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Literature summary for 3.4.21.47 extracted from

  • Martinez-Barricarte, R.; Heurich, M.; Valdes-Canedo, F.; Vazquez-Martul, E.; Torreira, E.; Montes, T.; Tortajada, A.; Pinto, S.; Lopez-Trascasa, M.; Morgan, B.P.; Llorca, O.; Harris, C.L.; Rodriguez de Cordoba, S.
    Human C3 mutation reveals a mechanism of dense deposit disease pathogenesis and provides insights into complement activation and regulation (2010), J. Clin. Invest., 120, 3702-3712.
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
medicine mutation 923DELTADG in complement factor 3 gene is identified in patients with dense deposit disease. Mutant C3923DELTADG, which lacks 2 amino acids, cannot be cleaved to C3b by the alternative pathway C3-convertase and is therefore the predominant circulating C3 protein in the patients. Upon activation to C3b by proteases, or to C3(H2O) by spontaneous thioester hydrolysis, mutant C3 generates an active C3-convertase that is regulated normally by decay accelerating factor but is resistant to decay by factor H. Activated C3b923DELTADG and C3(H2O)923DELTADG are resistant to proteolysis by factor I in the presence of factor H, but are efficiently inactivated in the presence of membrane cofactor protein, causing a fluid phase-restricted alternative pathway dysregulation in the patients that continuously activates and consumes C3 produced by the normal C3 allele Homo sapiens

Protein Variants

Protein Variants Comment Organism
923DELTADG mutation in complement factor 3 gene identified in patients with dense deposit disease. Mutant C3923DELTADG, which lacks 2 amino acids, cannot be cleaved to C3b by the alternative pathway C3-convertase and is therefore the predominant circulating C3 protein in the patients. Upon activation to C3b by proteases, or to C3(H2O) by spontaneous thioester hydrolysis, mutant C3 generates an active C3-convertase that is regulated normally by decay accelerating factor but is resistant to decay by factor H. Activated C3b923DELTADG and C3(H2O)923DELTADG are resistant to proteolysis by factor I in the presence of factor H, but are efficiently inactivated in the presence of membrane cofactor protein, causing a fluid phase-restricted alternative pathway dysregulation in the patients that continuously activates and consumes C3 produced by the normal C3 allele Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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