Literature summary for 3.4.21.B7 extracted from

Jani, P.K.; Kajdacsi, E.; Megyeri, M.; Dobo, J.; Doleschall, Z.; Futosi, K.; Timar, C.I.; Mocsai, A.; Mako, V.; Gal, P.; Cervenak, L.
MASP-1 induces a unique cytokine pattern in endothelial cells: a novel link between complement system and neutrophil granulocytes (2014), PLoS ONE, 9, e87104.

Search for more literature for 3.4.21.B7

Cloned(Commentary)

Cloned (Comment)	Organism
expression oof MASP-1 catalytic fragments in Escherichia coli	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
plasmaprotease C1-inhibitor	-	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P48740	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
endothelial cell	human umbilical vein endothelial cells	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
MASP-1	-	Homo sapiens

General Information

General Information	Comment	Organism
metabolism	human umbilical vein endothelial cells, activated by recombinnat MASP-1, secrete interleukin-6 and interleukin-8, but not interleukin-1alpha, interleukin-1ra, TNFalpha and MCP-1. rMASP-1 induces interleukin-6 and interleukin-8 production with different kinetics. Enzyme-triggered interleukin-6 and interleukin-8 production is regulated predominantly by the p38-MAPK pathway. The supernatant of rMASP-1-stimulated cells activates the chemotaxis of neutrophil granulocytes as an integrated effect of cytokine production	Homo sapiens
physiological function	MASP-1, the most abundant enzyme of the complement lectin pathway, can induce p38-MAPK activation, NFkappaB signaling, and Ca2+-mobilization in endothelial cells and induces a unique cytokine pattern in endothelial cells linking complement system and neutrophil granulocytes. Besides initializing the complement lectin pathway, MASP-1 may activate neutrophils indirectly, via the endothelial cells, which link these effective antimicrobial host defense mechanisms	Homo sapiens

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Release 2023.1 (January 2023)