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Expression of human chemerin induces insulin resistance in the skeletal muscle but does not affect weight, lipid levels, and atherosclerosis in LDL receptor knockout mice on high-fat diet.

Becker M, Rabe K, Lebherz C, Zugwurst J, Göke B, Parhofer KG, Lehrke M, Broedl UC - Diabetes (2010)

Bottom Line: Chemerin reduced insulin-stimulated Akt1 phosphorylation and activation of 5'AMP-activated protein kinase (AMPK) in the skeletal muscle, but had no effect on Akt phosphorylation and insulin-stimulated AMPK activation in the liver and gonadal adipose tissue.Chemerin induces insulin resistance in the skeletal muscle in vivo.Chemerin is involved in the cross talk between liver, adipose tissue, and skeletal muscle.

View Article: PubMed Central - PubMed

Affiliation: Department of Internal Medicine II, University of Munich, Munich, Germany.

ABSTRACT

Objective: Chemerin is a recently discovered hepatoadipokine that regulates adipocyte differentiation as well as chemotaxis and activation of dendritic cells and macrophages. Chemerin was reported to modulate insulin sensitivity in adipocytes and skeletal muscle cells in vitro and to exacerbate glucose intolerance in several mouse models in vivo. In humans, chemerin was shown to be associated with multiple components of the metabolic syndrome including BMI, triglycerides, HDL cholesterol, and hypertension. This study aimed to examine the effect of chemerin on weight, glucose and lipid metabolism, as well as atherosclerosis in vivo.

Research design and methods: We used recombinant adeno-associated virus to express human chemerin in LDL receptor knockout mice on high-fat diet.

Results: Expression of chemerin did not significantly alter weight, lipid levels, and extent of atherosclerosis. Chemerin, however, significantly increased glucose levels during the intraperitoneal glucose tolerance test without affecting endogenous insulin levels and the insulin tolerance test. Chemerin reduced insulin-stimulated Akt1 phosphorylation and activation of 5'AMP-activated protein kinase (AMPK) in the skeletal muscle, but had no effect on Akt phosphorylation and insulin-stimulated AMPK activation in the liver and gonadal adipose tissue.

Conclusions: Chemerin induces insulin resistance in the skeletal muscle in vivo. Chemerin is involved in the cross talk between liver, adipose tissue, and skeletal muscle.

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Related in: MedlinePlus

A: Western blot analysis of chemerin expression in serum samples of LDLRKO mice 16 weeks after injection with 1 × 1013 particles of AAV.lacZ or AAV.chemerin and a healthy human volunteer. B: Expression of chemerin in LDLRKO mice 16 weeks after injection with 1 × 1013 particles of AAV.lacZ or AAV.chemerin (n = 12 per group) and in 3 healthy human volunteers as assessed by ELISA. C: Murine chemerin levels in LDLRKO mice 16 weeks after injection with 1 × 1013 particles of AAV.lacZ or AAV.chemerin (n = 12 per group) as assessed by ELISA.
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Figure 1: A: Western blot analysis of chemerin expression in serum samples of LDLRKO mice 16 weeks after injection with 1 × 1013 particles of AAV.lacZ or AAV.chemerin and a healthy human volunteer. B: Expression of chemerin in LDLRKO mice 16 weeks after injection with 1 × 1013 particles of AAV.lacZ or AAV.chemerin (n = 12 per group) and in 3 healthy human volunteers as assessed by ELISA. C: Murine chemerin levels in LDLRKO mice 16 weeks after injection with 1 × 1013 particles of AAV.lacZ or AAV.chemerin (n = 12 per group) as assessed by ELISA.

Mentions: To examine the effect of chemerin expression on body weight, glucose and lipid metabolism, as well as atherosclerosis in vivo, LDLRKO mice on HFD were injected with 1 × 1013 particles of AAV.chemerin or control (AAV.lacZ). Injection of AAV.chemerin resulted in specific and sustained chemerin expression over the course of the study with serum levels comparable with those seen in healthy human volunteers (Fig. 1A and B). Expression of human chemerin did not alter murine chemerin serum levels (Fig. 1C).


Expression of human chemerin induces insulin resistance in the skeletal muscle but does not affect weight, lipid levels, and atherosclerosis in LDL receptor knockout mice on high-fat diet.

Becker M, Rabe K, Lebherz C, Zugwurst J, Göke B, Parhofer KG, Lehrke M, Broedl UC - Diabetes (2010)

A: Western blot analysis of chemerin expression in serum samples of LDLRKO mice 16 weeks after injection with 1 × 1013 particles of AAV.lacZ or AAV.chemerin and a healthy human volunteer. B: Expression of chemerin in LDLRKO mice 16 weeks after injection with 1 × 1013 particles of AAV.lacZ or AAV.chemerin (n = 12 per group) and in 3 healthy human volunteers as assessed by ELISA. C: Murine chemerin levels in LDLRKO mice 16 weeks after injection with 1 × 1013 particles of AAV.lacZ or AAV.chemerin (n = 12 per group) as assessed by ELISA.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2963549&req=5

Figure 1: A: Western blot analysis of chemerin expression in serum samples of LDLRKO mice 16 weeks after injection with 1 × 1013 particles of AAV.lacZ or AAV.chemerin and a healthy human volunteer. B: Expression of chemerin in LDLRKO mice 16 weeks after injection with 1 × 1013 particles of AAV.lacZ or AAV.chemerin (n = 12 per group) and in 3 healthy human volunteers as assessed by ELISA. C: Murine chemerin levels in LDLRKO mice 16 weeks after injection with 1 × 1013 particles of AAV.lacZ or AAV.chemerin (n = 12 per group) as assessed by ELISA.
Mentions: To examine the effect of chemerin expression on body weight, glucose and lipid metabolism, as well as atherosclerosis in vivo, LDLRKO mice on HFD were injected with 1 × 1013 particles of AAV.chemerin or control (AAV.lacZ). Injection of AAV.chemerin resulted in specific and sustained chemerin expression over the course of the study with serum levels comparable with those seen in healthy human volunteers (Fig. 1A and B). Expression of human chemerin did not alter murine chemerin serum levels (Fig. 1C).

Bottom Line: Chemerin reduced insulin-stimulated Akt1 phosphorylation and activation of 5'AMP-activated protein kinase (AMPK) in the skeletal muscle, but had no effect on Akt phosphorylation and insulin-stimulated AMPK activation in the liver and gonadal adipose tissue.Chemerin induces insulin resistance in the skeletal muscle in vivo.Chemerin is involved in the cross talk between liver, adipose tissue, and skeletal muscle.

View Article: PubMed Central - PubMed

Affiliation: Department of Internal Medicine II, University of Munich, Munich, Germany.

ABSTRACT

Objective: Chemerin is a recently discovered hepatoadipokine that regulates adipocyte differentiation as well as chemotaxis and activation of dendritic cells and macrophages. Chemerin was reported to modulate insulin sensitivity in adipocytes and skeletal muscle cells in vitro and to exacerbate glucose intolerance in several mouse models in vivo. In humans, chemerin was shown to be associated with multiple components of the metabolic syndrome including BMI, triglycerides, HDL cholesterol, and hypertension. This study aimed to examine the effect of chemerin on weight, glucose and lipid metabolism, as well as atherosclerosis in vivo.

Research design and methods: We used recombinant adeno-associated virus to express human chemerin in LDL receptor knockout mice on high-fat diet.

Results: Expression of chemerin did not significantly alter weight, lipid levels, and extent of atherosclerosis. Chemerin, however, significantly increased glucose levels during the intraperitoneal glucose tolerance test without affecting endogenous insulin levels and the insulin tolerance test. Chemerin reduced insulin-stimulated Akt1 phosphorylation and activation of 5'AMP-activated protein kinase (AMPK) in the skeletal muscle, but had no effect on Akt phosphorylation and insulin-stimulated AMPK activation in the liver and gonadal adipose tissue.

Conclusions: Chemerin induces insulin resistance in the skeletal muscle in vivo. Chemerin is involved in the cross talk between liver, adipose tissue, and skeletal muscle.

Show MeSH
Related in: MedlinePlus