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factor C
acts as an LPS-responsive C3 convertase on the surface of invading Gram-negative bacteria in the initial phase of horseshoe crab complement activation. The proteolytic activity of factor C on the surface of Escherichia coli is essential for the deposition of C3b
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formyl-methionyl-leucylphenylalanine
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treatment of whole blood leads to stimulation of neutrophils resulting in activation of the alternative complement pathway and release of C5 fragments, which further amplify proinflammatory responses
human complement factor H-related protein 4
CFHR 4, two isozymes A and B of 86 and 45 kDa from plasma, domain structure, overview. The protein belongs to the factor H family of plasma glycoproteins that are composed of short consensus repeat (SCR) domains. It activates complement by serving as a platform for the assembly of alternative pathway C3 convertase via its interaction with C3b protein. CFHR4 binds C3b via its C-terminus, and it lacks SCRs homologous to the complement inhibitory domains of factor H and has no significant complement regulatory activities. In contrast to the complement inhibitor factor H, CFHR4 acts as an enhancer of opsonization by promoting complement activation
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LPS
proteolytic conversion of C3 to C3b in hemocyanin-depleted plasma is strongly induced by LPS
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phorbol myristate acetate
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treatment of whole blood leads to stimulation of neutrophils resulting in activation of the alternative complement pathway and release of C5 fragments, which further amplify proinflammatory responses
tumor necrosis factor-alpha
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treatment of whole blood leads to stimulation of neutrophils resulting in activation of the alternative complement pathway and release of C5 fragments, which further amplify proinflammatory responses
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zymosan
it is capable of activating the classical pathway as well as the alternative pathway, when the classical pathway is blocked, mechanism, overview
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factor B
generation of the AP C3-convertase initiates by the binding of factor B to C3b to form the proconvertase, C3bB. Factor B undergoes a dramatic conformational change upon binding to C3b, it binds near the C345C domain in C3b. Factor B-D279G mutant promotes high-affinity C3b-binding and is correctly cleaved by factor D in the C3bB proenzyme to generate a very stable, functionally-active, AP C3-convertase C3bBb
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factor B
the classical C5 convertase requires factor D and factor B for activation and complex assembly
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factor D
the proconvertase C3bB is cleaved by factor D at a single site in factor B, producing Ba and Bb fragments. Ba dissociates from the complex, while Bb remains bound to C3b, forming the active AP C3-convertase C3bBb
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factor D
the classical C5 convertase requires factor D and factor B for activation and complex assembly
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mannan-binding lectin
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binding to O antigen-specific oligosaccharides derived from Salmonella sp. corresponding to serogroup C, and efficient support of component C3 deposition in the absence of C2, C4, or the associated serine protease 2
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mannan-binding lectin
mannan-binding lectin (MBL) promotes activation of complement component C3 through the combined action of MBL-associated serine proteases MASP-1 and MASP-2 without appreciable involvement of the alternative pathway, experimental conditions described
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mannan-binding lectin
mannan-binding lectin (MBL) promotes activation of complement component C3 through the combined action of MBL-associated serine proteases MASP-1 and MASP-2 without appreciable involvement of the alternative pathway
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properdin
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surface plasmon resonance assays, properdin promotes the association of C3b with factor B and provides a focal point for the assembly of enzyme on a surface. Properdin can use its unoccupied C3b-binding sites as receptors and form a lattice of properdin-C3b, -C3bB and C3bBb complexes leading to in situ assembly of enzyme
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properdin
facilitates AP complement activation by stabilizing the C3 convertase C3bBb, essential for AP complement activation induced by bacterial lipopolysacharide (LPS) and lipooligosacharide (LOS) and other AP complement activators
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properdin
positive regulator of the alternative pathway, no direct interaction with the decay-accelerating factor DAF determined
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properdin
properdin (Factor P) binding to the erythrocyte membranes is necessary for C3b to attach and initiate alternative pathway activation
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properdin
facilitates AP complement activation by stabilizing the C3 convertase C3bBb, essential for AP complement activation induced by bacterial lipopolysacharide (LPS) and lipooligosacharide (LOS) and other AP complement activators
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additional information
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complement activation via the lectin pathway on zymosan particles is at least 4times more efficient than via the classical pathway on sheep erythrocytes coated with antibody. Every C4b deposited via the lectin pathway is capable of forming a convertase in contrast to only one of four C4b molecules deposited via the classical pathway. Rate of formation of lectin pathway C3/C5 convertases depends on the activation of C4 and C2 by MASP-2
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additional information
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high surface density of complement component C3b is critical for the enzyme activity
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additional information
proteolytic conversion of C3 to C3b in hemocyanin-depleted plasma is not induced by zymosan, peptidoglycan, or laminarin
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