[The role of SIRT6 in nonalcoholic steatohepatitis].

SIRT6, a member of the silencing information regulatory protein family, is a nicotinamide adenine dinucleotide-dependent histone deacetylase and an ADP-ribose transferase enzyme. It plays an important role in fundamental physiological and pathological processes, including lipid metabolism, inflammation, oxidative stress and fibrosis, and is considered as a potential therapeutic target for metabolic syndrome. SIRT6 knockout mice displayed severe fatty liver, and the expression of SIRT6 in the liver of nonalcoholic steatohepatitis (NASH) mice was significantly lower than that of normal mice.

Irisin alleviates pressure overload-induced cardiac hypertrophy by inducing protective autophagy via mTOR-independent activation of the AMPK-ULK1 pathway.

In hypertrophic hearts, autophagic flux insufficiency is recognized as a key pathology leading to maladaptive cardiac remodeling and heart failure. This study aimed to illuminate the cardioprotective role and mechanisms of a new myokine and adipokine, irisin, in cardiac hypertrophy and remodeling. Adult male wild-type, mouse-FNDC5 (irisin-precursor)-knockout and FNDC5 transgenic mice received 4 weeks of transverse aortic constriction (TAC) alone or combined with intraperitoneal injection of chloroquine diphosphate (CQ).

SIRT6 protects cardiomyocytes against ischemia/reperfusion injury by augmenting FoxO3α-dependent antioxidant defense mechanisms.

SIRT6, a member of the NAD(+)-dependent class III deacetylase sirtuin family, has been revealed to play important roles in promoting cellular resistance against oxidative stress. The formation of reactive oxygen species (ROS) and oxidative stress are the crucial mechanisms underlying cellular damage and dysfunction in cardiac ischemia/reperfusion (I/R) injury, but the role of SIRT6 in I/R-induced ROS and oxidative stress is poorly understood. In this study, by using heterozygous SIRT6 knockout (SIRT6(+/-)) mice and cultured neonatal cardiomyocyte models, we investigated how SIRT6 mediates oxidative stress and myocardial injury during I/R.

Patients Aged 80 Years or Older are Encountered More Potentially Inappropriate Medication Use.

Background: Polypharmacy and potentially inappropriate medications (PIMs) are prominent prescribing issues in elderly patients. This study was to investigate the different prevalence of PIM use in elderly inpatients between 65-79 years of age and 80 years or older, who were discharged from Geriatric Department in West China Hospital.

Methods: A large-scale cohort of 1796 inpatients aged 65 years or over was recruited.

Ghrelin inhibits doxorubicin cardiotoxicity by inhibiting excessive autophagy through AMPK and p38-MAPK.

Doxorubicin (DOX) is a wide spectrum antitumor drug, but its clinical application is limited by the cardiotoxicity. Ghrelin, a multi-functional peptide hormone with metabolic regulation in energy homeostasis, plays important roles in cardiovascular protection. Now, the underlying mechanisms of ghrelin against DOX-induced cardiomyocyte apoptosis and atrophy are still not clear.

[The mechanisms of stimulated lipolysis by high concentration of glucose in primary rat adipocytes].

Objective: To investigate the cellular mechanisms of adipocyte lipolytic response to a high concentration of glucose, which liberates free fatty acids (FFA) efflux from adipose cells to plasma.

Methods: Adipocytes were isolated from epididymal fat pads of Sprague-Dawley (SD) rats, and were incubated in the presence or absence of excess glucose (25 mmol/L). Glycerol released in the culture medium was determined by use of a colorimetric assay and served as an index of lipolysis.

[Perilipin associated with lipid droplets regulates lipolysis].

Perilipins are the proteins associating with the lipid droplets in adipocytes and steroidogenic cells. Unphosphorylated perilipins coat the surface of intracellular lipid droplets to form a barrier that prevents lipase from accessing to triacylglycerol core, thus suppressing lipolysis. Upon activation of protein kinase A (PKA), two proteins, hormone-sensitive lipase (HSL) and perilipins, are phosphorylated.