EC Number   |
General Information |
Reference |
|---|
   3.4.21.B7 | malfunction |
enzyme-deficient mice lack alternative pathway activation because factor D remains as a proenzyme in the serum |
731099 |
| 3.4.21.B7 | malfunction |
increased MASP-1 plasma levels in patients in the suba-cute phase of myocardial infarction, but decreased levels of MASP-1 in patients withacute ischemic stroke |
732520 |
| 3.4.21.B7 | malfunction |
N-terminal parts of MASP-1 enzyme which only contain non-enzymatic domains, and a stable zymogen mutant form of enzyme MASP-1 are ineffective to stimulate endothelial cells |
732519 |
| 3.4.21.B7 | malfunction |
presence of a functional alternative pathway in a human patient with Malpuech-Michels-Mingarelli-Carnevale (3MC) syndrome caused by a genetic defect in the MASP1 gene, which abolishes the production of all three splice products of this gene: mannan-binding lectin-associated serine proteases 1 and 3, and MBL-associated protein of 44 kDa, a human complement |
732271 |
| 3.4.21.B7 | metabolism |
among the components of the mannose-binding lectinMASPs complexes only enzyme MASP-1 is able to trigger response in human umbilical vein endothelial cells and the proteolytic activity of MASP-1 is essential |
732519 |
| 3.4.21.B7 | metabolism |
both MASP-1 and MASP-2 are essential for lectin pathway activation in normal human serum |
732520 |
| 3.4.21.B7 | 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 |
732779 |
| 3.4.21.B7 | metabolism |
influence of buffer composition on the activity of the alternative pathway of complement activation in mice in the presence and the absence of the Masp1 gene products: MASP-1, MASP-3, and MAp44 |
732271 |
| 3.4.21.B7 | metabolism |
MASP-1 is a protease of the lectin pathway of complement |
732869 |
| 3.4.21.B7 | metabolism |
target binding of pattern recognition molecules leads to the activation of zymogen mannan-binding lectin-associated serine proteases and triggers the lectin pathway, an antibody-independent activation route of the complement system, which provides immediate defense against pathogens and altered self-cells, but also causes severe tissue damage after stroke, heart attack, and other ischemia reperfusion injuries. MASP-2 and MASP-1 are both essential pathway components |
732057 |
