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Literature summary for 3.4.21.76 extracted from

  • Mirea, A.M.; Toonen, E.J.M.; van den Munckhof, I.; Munsterman, I.D.; Tjwa, E.T.T.L.; Jaeger, M.; Oosting, M.; Schraa, K.; Rutten, J.H.W.; van der Graaf, M.; Riksen, N.P.; de Graaf, J.; Netea, M.G.; Tack, C.J.; Chavakis, T.; Joosten, L.A.B.
    Increased proteinase 3 and neutrophil elastase plasma concentrations are associated with non-alcoholic fatty liver disease (NAFLD) and type 2 diabetes (2019), Mol. Med., 25, 16 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
alpha-1 antitrypsin AAT Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P24158
-
-

Source Tissue

Source Tissue Comment Organism Textmining
blood plasma PR3 plasma concentrations are increased in patients with liver steatosis Homo sapiens
-
neutrophil
-
Homo sapiens
-

Synonyms

Synonyms Comment Organism
neutrophil serine protease
-
Homo sapiens
PR3
-
Homo sapiens
proteinase 3
-
Homo sapiens

Expression

Organism Comment Expression
Homo sapiens PR3 plasma concentrations are increased in patients with liver steatosis. PR3 concentration is upregulated in patients with type 2 diabetes when compared to lean and obese controls up

General Information

General Information Comment Organism
malfunction ratios between neutrophil serine proteases and their natural inhibitor are altered in non-alcoholic fatty liver disease (NAFLD) and type 2 diabetes when compared to healthy controls Homo sapiens
metabolism increased proteinase 3 and neutrophil elastase (EC 3.4.21.37) plasma concentrations are associated with non-alcoholic fatty liver disease (NAFLD) and type 2 diabetes, potential role for the neutrophil serine proteases (NSPs), proteinase-3 (PR3) and neutrophil elastase (NE), in NAFLD as well as an imbalance between NSPs and their natural inhibitor alpha-1 antitrypsin (AAT). Circulating levels of NSPs associate with obesity-related metabolic disorders Homo sapiens
physiological function the neutrophil serine protease proteinase-3 (PR3) is able to process interleukin-1beta to its bioactive form independently of caspase-1-NLRP3 inflammasome complex Homo sapiens