Angiotensin II Triggers NLRP3 Inflammasome Activation by a Ca Signaling-Dependent Pathway in Rat Cardiac Fibroblast Ang-II by a Ca-Dependent Mechanism Triggers NLRP3 Inflammasome in CF.

Angiotensin II (Ang-II) is a widely studied hypertensive, profibrotic, and pro-inflammatory peptide. In the heart, cardiac fibroblasts (CF) express type 1 angiotensin II receptors (AT1R), Toll-like receptor-4 (TLR4), and the NLRP3 inflammasome complex, which play important roles in pro-inflammatory processes. When activated, the NLRP3 inflammasome triggers proteolytic cleavage of pro-IL-1, resulting in its activation.

NLRP3 Inflammasome in Vascular Disease: A Recurrent Villain to Combat Pharmacologically.

Despite the great advances in medicine, mortality from cardiovascular diseases keeps on growing. This tendency is not likely to change considering the pandemic proportions of obesity and diabetes. Besides, the global population is more aged as life expectancy increases, and vascular aging plays a key role in the increased risk of vascular disease.

Pathways responsible for apoptosis resulting from amadori-induced oxidative and nitrosative stress in human mesothelial cells.

Background: Apoptosis and inflammatory/oxidative stress have been associated with hyperglycemia in human peritoneal mesothelial cells (HPMCs) and other cell types. We and others have highlighted the role of early products of non-enzymatic protein glycation in inducing proinflammatory conditions and increasing apoptotic rates in HPMCs. Loss of HPMCs seems to be a hallmark of complications associated with peritoneal membrane dysfunction.

[Therapeutic targets in diabetic vasculopathy].

Vascular complications are the main cause of morbidity and mortality in long-term diabetes mellitus. Endothelial dysfunction appears as an initial pathological mechanism leading to diabetic vasculopathy, which is associated with sustained high glucose levels and enhanced oxidative stress. Non-enzymatic protein glycosylation, through the formation of so-called advanced glycosylation end-products, appears as one of the mechanisms involved in diabetes-associated endothelial dysfunction.