Adipocyte chemerin release is induced by insulin without being translated to higher levels <i>in vivo</i>

Bauer, Sabrina; Bala, Margarita; Kopp, Andrea; Eisinger, Kristina; Schmid, Andreas; Schneider, Silvia; Neumeier, Markus; Buechler, Christa

doi:10.1111/j.1365-2362.2012.02713.x

Cited by 28 publications

(17 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our data suggest that insulin and chemerin exert antagonistic roles at cardiac level, which could participate in the mechanisms involved in insulin resistance in cardiomyocytes, in view of the negative effects of chemerin on glucose uptake recently reported by Zhang et al (2014) and confirmed by our observations (data not shown) [59]. Two previous studies found however that insulin upregulated chemerin levels and secretion by human and murine adipocytes [73,74], highlighting the tissue-dependent nature of chemerin biology.…”

Section: Cellular Physiology and Biochemistry Cellular Physiology Andsupporting

confidence: 59%

The Adipokine Chemerin Induces Apoptosis in Cardiomyocytes

Rodríguez-Penas¹,

Feijóo‐Bandín²,

García-Rúa³

et al. 2015

Cell Physiol Biochem

View full text Add to dashboard Cite

Background: The adipokine chemerin has been associated with cardiovascular disease. We investigated the effects of chemerin on viability and intracellular signalling in murine cardiomyocytes, and the effects of insulin and TNF-α on cardiomyocyte chemerin production. Methods: Hoechst dye vital staining and cell cycle analysis were used to analyse the viability of murine cardiac cells in culture. Western blot was used to explore the phosphorylation of AKT and caspase-9 activity in neonatal rat cardiomyocytes and HL-1 cells. Finally, RT-qPCR, ELISA and western blot were performed to examine chemerin and CMKLR1 expression after insulin and TNF-α treatment in cardiac cells. Results: Chemerin treatment increased apoptosis, reduced phosphorylation of AKT at Thr308 and increased caspase-9 activity in murine cardiomyocytes. Insulin treatment lowered chemerin and CMKLR1 mRNA and protein levels, and the amount of chemerin in the cell media, while TNF-α treatment increased chemerin mRNA and protein levels but decreased expression of the CMKLR1 gene. Conclusion: Chemerin induces apoptosis, reduces AKT phosphorylation and increases the cleavage of caspase-9 in murine cardiomyocytes. The expression of chemerin is regulated by important metabolic (insulin) and inflammatory (TNF-α) mediators at cardiac level. Our results suggest that chemerin could play a role in the physiopathology of cardiac diseases.

show abstract

Section: Cellular Physiology and Biochemistry Cellular Physiology Andsupporting

confidence: 59%

The Adipokine Chemerin Induces Apoptosis in Cardiomyocytes

Rodríguez-Penas¹,

Feijóo‐Bandín²,

García-Rúa³

et al. 2015

Cell Physiol Biochem

View full text Add to dashboard Cite

show abstract

“…Insulin upregulates adipocyte chemerin whereas mRNA expression is not enhanced in PHH [4,35,36]. Chemerin was reported to enhance insulin-stimulated glucose uptake and insulin receptor substrate-1 tyrosine phosphorylation, suggesting that chemerin increases insulin sensitivity [13].…”

Section: Discussionmentioning

confidence: 99%

Hepatic chemerin mRNA in morbidly obese patients with nonalcoholic fatty liver disease

Kajor¹,

Kukla²,

Waluga³

et al. 2017

pjp

View full text Add to dashboard Cite

The aim of this study was to investigate hepatic chemerin mRNA, serum chemerin concentration, and immunohistochemical staining for chemerin and and chemokine receptor-like 1 (CMKLR1) in hepatic tissue in 56 morbidly obese women with nonalcoholic fatty liver disease (NAFLD) and to search for a relationship with metabolic and histopathological features. Chemerin mRNA was assessed by quantitative real-time PCR, chemerin, and CMKLR1 immunohistochemical expression with specific antibodies, while serum chemerin concentration was assessed with commercially available enzyme-linked immunosorbent assays. Serum chemerin concentration reached 874.1 ±234.6 ng/ml. There was no difference in serum chemerin levels between patients with BMI < 40 kg/m 2 and ≥ 40 kg/m 2 . Serum chemerin concentration tended to be higher in patients with hepatocyte ballooning, greater extent of steatosis, and definite nonalcoholic steatohepatitis (NASH). Liver chemerin mRNA was observed in all included patients and was markedly, but insignificantly, higher in those with BMI ≥ 40 kg/ m 2 , hepatocyte ballooning, greater extent of steatosis, and definite NASH. Hepatic chemerin mRNA might be a predictor of hepatic steatosis, hepatocyte ballooning, and NAFLD activity score (NAS) but seemed not to be a primary driver regulating liver necroinflammatory activity and fibrosis. The lack of association between serum chemerin and hepatic chemerin mRNA may suggest that adipose tissue but not the liver is the main source of chemerin in morbidly obese women.

show abstract

“…Hepatic chemerin expression is not affected by food restriction and food restrictionrefeeding [23]. Adipocyte chemerin synthesis is upregulated by insulin but whether this contributes to higher serum chemerin levels is still a matter of debate [23][24][25]. Glucagon and insulin have no effect on hepatocyte chemerin expression [21].…”

Section: Regulating Of Hepatocyte Chemerin and Cmklr1mentioning

confidence: 99%

Chemerin in Liver Diseases

2014

Endocrinol Metab Synd

View full text Add to dashboard Cite

Chemerin is a chemoattractant protein and moreover has a role in adipogenesis, angiogenesis and glucose homeostasis. Chemerin is primarily synthesized and secreted by adipocytes and hepatocytes. Chemerin receptors chemokine-like receptor 1 (CMKLR1), G-protein coupled receptor 1 (GPR1) and CC-motif chemokine receptorlike 2 (CCRL2) are all expressed in the liver suggesting that chemerin may be relevant in liver physiology and pathophysiology. Non-alcoholic fatty liver disease (NAFLD) is associated with obesity and is the most common cause of chronic liver injury. NAFLD and chronic hepatitis C virus infection are risk factors for hepatocellular carcinoma. Hepatic and serum chemerin have been analyzed in human and rodent NAFLD, in patients with chronic hepatitis C and patients with hepatocellular carcinoma. Chemerin, GPR1 and CMKLR1 deficient mice have been used to elucidate the role of these proteins in body weight gain and glucose homeostasis. The regulation of chemerin and CMKLR1 by adipokines, hormones and cytokines relevant in liver diseases has been studied in hepatocytes. The data published so far are briefly summarized herein. Current experimental findings do not provide evidence for a crucial role of chemerin in chronic liver diseases and further research is needed to evaluate a possible protective function of this protein in hepatocellular carcinoma.

show abstract

Adipocyte chemerin release is induced by insulin without being translated to higher levels in vivo

Abstract: Post-prandial hyperinsulinaemia does not contribute to higher chemerin levels in nondiabetic individuals.

Cited by 28 publications

References 20 publications

The Adipokine Chemerin Induces Apoptosis in Cardiomyocytes

The Adipokine Chemerin Induces Apoptosis in Cardiomyocytes

Hepatic chemerin mRNA in morbidly obese patients with nonalcoholic fatty liver disease

Chemerin in Liver Diseases

Contact Info

Product

Resources

About