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Literature summary for 3.4.21.B7 extracted from

  • Megyeri, M.; Jani, P.K.; Kajdacsi, E.; Dobo, J.; Schwaner, E.; Major, B.; Rigo, J.; Zavodszky, P.; Thiel, S.; Cervenak, L.; Gal, P.
    Serum MASP-1 in complex with MBL activates endothelial cells (2014), Mol. Immunol., 59, 39-45.
    View publication on PubMed
Search for more literature for 3.4.21.B7

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant MASP-1 catalytic fragments encoding the complement control protein domains 1 and 2, CCP1-CCP2-SP, region (rMASPcf) in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information generation of a MASP-1 catalytic fragment encoding the CCP1-CCP2-SP region (rMASPcf) Homo sapiens
R448Q site-directed mutagenesis Homo sapiens
S646A site-directed mutagenesis Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Homo sapiens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required, enzyme-bound Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P48740
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant MASP-1 catalytic fragments encoding the complement control protein domains 1 and 2, CCP1-CCP2-SP, region from Escherichia coli by repeated anion exchange chromatography and gel filtration Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
blood plasma
-
 Homo sapiens
-
endothelial cell
-
 Homo sapiens
-

Synonyms

Synonyms Comment Organism
MASP-1
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Homo sapiens

General Information

General Information Comment Organism
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 Homo sapiens
metabolism among the components of the mannose-binding lectin–MASPs 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 Homo sapiens
physiological function enzyme MASP-1 plays a central role in the early innate immune response. The initiation complexes of the lectin pathway, consisting of mannose-binding lectin and associated serine proteases (MASPs) elicit Ca2+-signaling in cultured endothelial cells. The recombinant catalytic fragment of MASP-1 activates endothelial cells by cleaving protease activated receptor 4. Mannose binding lectin-mannan-binding lectin-associated serine protease 1 complexes trigger intracellular Ca2+-signaling in human umbilical vein endothelial cells, overview Homo sapiens