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In islets from db/db (show LEPR Proteins) mice, ACE2 over-expression increased intracellular calcium influx and restored impaired mitochondrial oxidation, potentially causing an increase in GSIS. These results shed light on the potential roles of ACE2 in mitochondrial metabolism, moreover, may improve our understanding of diabetes.
ACE2 may have a role in silent atherosclerosis in patients with chronic kidney disease; it counterbalances the vasoconstrictor adverse effects of angiotensin II by its conversion
This study reveals an elevated serum concentration of ACE2 and independent associations between serum ACE2 and echocardiographic parameters in hypertensive patients.
The findings of this study indicate that ACE-2 activity is reduced in AD and is an important regulator of the central classical ACE-1 (show ACE Proteins)/Ang II (show AGT Proteins)/AT1R (show AGTR1 Proteins) axis of renin (show REN Proteins)-angiotensin system, and also that dysregulation of this pathway likely plays a significant role in the pathogenesis of Alzheimer's disease.
Overexpression of ACE2 ameliorates Abeta (show APP Proteins)-induced inflammatory response by activating the ACE2/Ang-(1 (show ANGPT1 Proteins)-7)/Mas (show MAS1 Proteins) axis in human RPE (show RPE Proteins) cells.
Although further studies are required to determine how clusterin (show CLU Proteins) suppresses non-specific cellular uptake in phagocytes, our data suggest that clusterin (show CLU Proteins) plays a key role in the stealth effect of not only pegylated nanoparticles but also non-pegylated nanoparticles.
The ACE2 G8790A polymorphism in type 2 diabetes mellitus patients was correlated with cerebral stroke, and the A allele might be a risk factor of type 2 diabetes mellitus combined with cerebral stroke.
ollectrin, an ACE2 homolog with no catalytic activity, regulates blood pressure through an NO-dependent mechanism. Large body of experimental data confirmed sustained beneficial effects of ACE2/Ang-(1 (show ANGPT1 Proteins)-7)/Mas (show MAS1 Proteins) receptor axis activation on hypertension and vascular injury.
The potential contribution of the ACE2 to cardiovascular disease progression was addressed.
Serum ACE2 activity was significantly lower in acute ischemic stroke as compared to both control and stroke-alert patients, followed by an increase to control levels at three days.
Ultra-high doses did not influence the ACE2/AT2R (show AGTR2 Proteins)/Mas (show MAS1 Proteins) axis and promoted renal injury with increased renal ERK1/2 activation and exaggerated fibronectin (show FN1 Proteins) expression in db/db (show LEPR Proteins) mice. Our study demonstrates dose-related effects of candesartan in diabetic nephropathy: intermediate-high dose candesartan is renoprotective, whereas ultra-high dose candesartan induces renal damage.
Altogether, our study demonstrates that HFD feeding increases RAS activity and mediates glycemic dysregulation likely through loss of ACE2 present outside the islets but independently of changes in islet ACE2.
Results suggest that angiotensin converting enzyme 2 may reduce anxiety-like behavior by activating central Mas (show MAS1 Proteins) receptor that facilitate GABA release onto pyramidal neurons within the basolateral amygdala.
These findings demonstrate that ACE2 plays a critical role in preventing RSV-induced lung injury, and suggest that ACE2 is a promising potential therapeutic target in the management of RSV-induced lung disease.
ACE2 overexpression significantly reduced the myocardial infarction-induced increase in apoptosis, macrophage infiltration, and HMGB1 (show HMGB1 Proteins) and proinflammatory cytokine expression.
ACE2 regulates vascular function by modulating nitric oxide release.
MAS (show MAS1 Proteins) receptors mediate vasoprotective and atheroprotective effects of candesartan upon the recovery of vascular ACE2-angiotensin-(1-7)-MAS (show MAS1 Proteins) axis functionality
ACE2 plays a novel role in heart disease associated with obesity wherein ACE2 negatively regulates obesity-induced epicardial adipose tissue inflammation and cardiac insulin (show INS Proteins) resistance.
a Mas (show MAS1 Proteins) receptor-mediated mechanism may stimulate pancreatic cell development
The objective of this study was to characterize the profiles of Ang-(1-7), MAS receptor, ACE(2), NEP and PEP during the ovulatory process in cattle.
sporadic non-synonymous substitutions reduced the level of rh-ACE2 protein expression and did not support severe acute respiratory syndrome coronavirus entry effectively
In a pig model of acute pulmonary embolism leading to cardiac arrest, captopril infusion was associated with less mean right ventricular pressure overload after resuscitation, compared with saline infusion. The reduction in systemic and pulmonary vascular resistance associated with captopril may be by inhibiting the ACE (show ACE Proteins)-Ang II (show AGT Proteins)-AT1R (show AGTR1 Proteins) axis and activating the ACE2/Ang-(1 (show ANGPT1 Proteins)-7)/Mas (show MAS1 Proteins) axis.
This study produced the full-length porcine ACE2 cDNA sequence and found polyunsaturated fatty acids could downregulate the expression of ACE2.
activation of the central rennin (show CYM Proteins)-angiotensin system in animals with chronic heart failure involves an imbalance of ACE (show ACE Proteins) and ACE2 in regions of the brain that regulate autonomic function.
Overexpression of ACE2 inhibited atherosclerotic plaque inflammation response in hypercholesterolemic rabbits.
The protein encoded by this gene belongs to the angiotensin-converting enzyme family of dipeptidyl carboxydipeptidases and has considerable homology to human angiotensin 1 converting enzyme. This secreted protein catalyzes the cleavage of angiotensin I into angiotensin 1-9, and angiotensin II into the vasodilator angiotensin 1-7. The organ- and cell-specific expression of this gene suggests that it may play a role in the regulation of cardiovascular and renal function, as well as fertility. In addition, the encoded protein is a functional receptor for the spike glycoprotein of the human coronaviruses SARS and HCoV-NL63.
, angiotensin I converting enzyme (peptidyl-dipeptidase A) 2
, angiotensin-converting enzyme 2
, angiotensin-converting enzyme homolog
, metalloprotease MPROT15
, peptidyl-dipeptidase A
, angiotensin I converting enzyme 2
, anigotensin-converting enzyme-related carboxypeptidase
, renal angiotensin-converting enzyme 2