Literature summary for 3.4.21.43 extracted from

Braunschweig, A.; Jozsi, M.
Human pentraxin 3 binds to the complement regulator c4b-binding protein (2011), PLoS ONE, 6, e23991.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

General Information

General Information	Comment	Organism
physiological function	soluble recognition molecule PTX3, i.e. long pentraxin 3, displays multiple functions including innate immune defense against certain microbes and the clearance of apoptotic cells. In addition to complement activators, PTX3 interacts with complement inhibitors including C4BP. This balanced interaction on extracellular matrix and on apoptotic cells may prevent excessive local complement activation that would otherwise lead to inflammation and host tissue damage. PTX3 binds to the classical and lectin pathway regulator C4b-binding protein C4BP. A PTX3-binding site lies within short consensus repeats 1-3 of the C4BP a-chain. PTX3 does not interfere with the cofactor activity of C4BP in the fluid phase and C4BP maintains its complement regulatory activity when bound to PTX3 on surfaces. PTX3 binds to human fibroblast- and endothelial cell-derived extracellular matrices and recruits functionally active C4BP to these surfaces. Whereas PTX3 enhances the activation of the classical/lectin pathway and causes enhanced C3 deposition on extracellular matrix, deposition of terminal pathway components and the generation of the inflammatory mediator C5a are not increased. PTX3 enhances the binding of C4BP to late apoptotic cells, which resultes in an increased rate of inactivation of cell surface bound C4b and a reduction in the deposition of C5b-9	Homo sapiens

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Release 2023.1 (January 2023)