Intracardiac administration of neutrophil protease cathepsin G activates noncanonical inflammasome pathway and promotes inflammation and pathological remodeling in non-injured heart

SERPINA3C ameliorates adipose tissue inflammation through the Cathepsin G/Integrin/AKT pathway

“…Because adipose SERPINA3C was found to play protective role against insulin resistance in our study, the involvement and mechanism of β1 Integrin in the regulation of adipose tissue metabolism by SERPINA3C was then investigated. β1 Integrin is known to form heterodimers with α5 Integrin to activate AKT signaling [ 44 , [46] , [47] , [48] , [49] , [50] , [51] ]. We examined α5 Integrin and β1 Integrin protein expressions in KO and AAV-SERPINA3C mice.…”

“…Cathepsin G has the ability to cleave and activate IL-36γ and aggravate imiquimod-induced mouse psoriatic lesions [ 48 ]. Intracardiac administration of Cathepsin G promotes inflammation and pathological remodeling in the non-injured heart [ 49 ]. However, most of these studies concentrated on non-adipose tissues.…”

Hindrance of the Proteolytic Activity of Neutrophil-Derived Serine Proteases by Serine Protease Inhibitors as a Management of Cardiovascular Diseases and Chronic Inflammation

“…These results indicate cardioprotective effects when both CatG and chymase are inhibited ( Hooshdaran et al, 2017 ). Intracardial administration of CatG into rats marks high levels of pro-inflammatory cytokines and recruitment of neutrophils as well as macrophages to the myocardium ( Miller et al, 2019 ). Additionally, neutrophil activation triggers the release of neutrophil extracellular traps (NETs), which encompass DNA and cytoplasmic granular proteins, like CatG, in order to catch and trap microorganisms in the extracellular space ( Ma et al, 2019 ), resulting in enhanced inflammation, endothelial dysfunction, and induced thrombogenicity in a process depending on IL-1α precursor processing by CatG ( Folco et al, 2018 ).…”