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Obesity and Metabolic Syndrome
Skeletal Muscle Thermogenesis and Its Role in Whole Body Energy Metabolism
Muthu Periasamy, Jose Luis Herrera, Felipe C. G. Reis
Diabetes Metab J. 2017;41(5):327-336.   Published online October 24, 2017
DOI: https://doi.org/10.4093/dmj.2017.41.5.327
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AbstractAbstract PDFPubReader   

Obesity and diabetes has become a major epidemic across the globe. Controlling obesity has been a challenge since this would require either increased physical activity or reduced caloric intake; both are difficult to enforce. There has been renewed interest in exploiting pathways such as uncoupling protein 1 (UCP1)-mediated uncoupling in brown adipose tissue (BAT) and white adipose tissue to increase energy expenditure to control weight gain. However, relying on UCP1-based thermogenesis alone may not be sufficient to control obesity in humans. On the other hand, skeletal muscle is the largest organ and a major contributor to basal metabolic rate and increasing energy expenditure in muscle through nonshivering thermogenic mechanisms, which can substantially affect whole body metabolism and weight gain. In this review we will describe the role of Sarcolipin-mediated uncoupling of Sarcoplasmic Reticulum Calcium ATPase (SERCA) as a potential mechanism for increased energy expenditure both during cold and diet-induced thermogenesis.

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Original Articles
Effects of Aerobic Exercise Intensity on Abdominal and Thigh Adipose Tissue and Skeletal Muscle Attenuation in Overweight Women with Type 2 Diabetes Mellitus
Ji Yeon Jung, Kyung Ah Han, Hee Jung Ahn, Hwi Ryun Kwon, Jae Hyuk Lee, Kang Seo Park, Kyung Wan Min
Diabetes Metab J. 2012;36(3):211-221.   Published online June 14, 2012
DOI: https://doi.org/10.4093/dmj.2012.36.3.211
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AbstractAbstract PDFPubReader   
Background

We investigated the effects of exercise intensity on abdominal and mid-thigh adipose tissue, attenuation of skeletal muscle, and insulin sensitivity in overweight women with type 2 diabetes mellitus (T2DM).

Methods

Twenty-eight patients were randomly assigned to control (CG, n=12), moderate intensity exercise (MEG, n=8), or vigorous intensity exercise (VEG, n=8) group. Subjects in both exercise groups completed a 12-week exercise program (MEG, 3.6 to 5.2 METs; VEG, ≥5.2 METs) that was monitored by accelerometers. We assessed body mass index (BMI), total fat area (TFA), visceral fat area (VFA), subcutaneous fat area (SFA), mid-thigh intramuscular adipose tissue (TIMAT), total skeletal muscle (TTM), low density skeletal muscle (TLDM), and normal density skeletal muscle (TNDM) using computed tomography, and measured insulin sensitivity with an insulin tolerance test (KITT), before and after the intervention.

Results

At baseline, the mean age was 53.8±7.9 years, duration of diabetes was 3.8±2.3 years, and BMI was 26.6±2.6 kg/m2. After 12 weeks, the percent change (%C) in BMI, TIMAT, and TLDM were not different among three groups. However, %C in TFA and VFA were significantly reduced in MEG compared to CG (P=0.026 and P=0.008, respectively). %C SFA was significantly reduced in VEG compared to CG (P=0.038) and %C TTM, TNDM, and KITT were significantly increased in VEG compared to the CG (P=0.044, P=0.007, and P=0.016, respectively).

Conclusion

Although there was no difference in the change in BMI among groups, TFA and VFA were more reduced in MEG, and only VEG increased TTM, TNDM, and insulin sensitivity compared to CG.

Citations

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    Byung Sam Park, Ji Sung Yoon
    Diabetes & Metabolism Journal.2013; 37(6): 458.     CrossRef
  • Effect of exercise on abdominal fat loss in men and women with and without type 2 diabetes
    Devon A Dobrosielski, Bethany Barone Gibbs, Sameer Chaudhari, Pamela Ouyang, Harry A Silber, Kerry J Stewart
    BMJ Open.2013; 3(11): e003897.     CrossRef
The Association of Unintentional Changes in Weight, Body Composition, and Homeostasis Model Assessment Index with Glycemic Progression in Non-Diabetic Healthy Subjects
Eun-Jung Rhee, Ji-Hun Choi, Seung-Hyun Yoo, Ji-Cheol Bae, Won-Jun Kim, Eun-Suk Choi, Se Eun Park, Cheol-Young Park, Seok Won Park, Ki-Won Oh, Sung-Woo Park, Sun-Woo Kim, Won-Young Lee
Diabetes Metab J. 2011;35(2):138-148.   Published online April 30, 2011
DOI: https://doi.org/10.4093/dmj.2011.35.2.138
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AbstractAbstract PDFPubReader   
Background

We performed a retrospective longitudinal study on the effects of changes in weight, body composition, and homeostasis model assessment (HOMA) indices on glycemic progression in subjects without diabetes during a four-year follow-up period in a community cohort without intentional intervention.

Methods

From 28,440 non-diabetic subjects who participated in a medical check-up program in 2004, data on anthropometric and metabolic parameters were obtained after four years in 2008. Body composition analyses were performed with a bioelectrical impedance analyzer. Skeletal muscle index (SMI, %) was calculated with lean mass/weight×100. Subjects were divided into three groups according to weight change status in four years: weight loss (≤-5.0%), stable weight (-5.0 to 5.0%), weight gain (≥5.0%). Progressors were defined as the subjects who progressed to impaired fasting glucose or diabetes.

Results

Progressors showed worse baseline metabolic profiles compared with non-progressors. In logistic regression analyses, the increase in changes of HOMA-insulin resistance (HOMA-IR) in four years presented higher odds ratios for glycemic progression compared with other changes during that period. Among the components of body composition, a change in waist-hip ratio was the strongest predictor, and SMI change in four years was a significant negative predictor for glycemic progression. Changes in HOMA β-cell function in four years was a negative predictor for glycemic progression.

Conclusion

Increased interval changes in HOMA-IR, weight gain and waist-hip ratio was associated with glycemic progression during a four-year period without intentional intervention in non-diabetic Korean subjects.

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    Endocrinology and Metabolism.2021; 36(4): 845.     CrossRef
  • Effects of nutritional supplementation on glucose metabolism and insulin function among people with HIV initiating ART
    Hiwot Amare, Mette F. Olsen, Henrik Friis, Pernille Kæstel, Åse B. Andersen, Alemseged Abdissa, Daniel Yilma, Tsinuel Girma, Daniel Faurholt-Jepsen
    BMC Nutrition.2021;[Epub]     CrossRef
  • The ratio of estimated average glucose to fasting plasma glucose level as an indicator of insulin resistance in young adult diabetes
    Jun Guo, Sisi Lei, Yu Zhou, Congqing Pan
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  • Reduced Skeletal Muscle Volume and Increased Skeletal Muscle Fat Deposition Characterize Diabetes in Individuals after Pancreatitis: A Magnetic Resonance Imaging Study
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    Diseases.2020; 8(3): 25.     CrossRef
  • Insulin resistance increases the risk of incident type 2 diabetes mellitus in patients with non‐alcoholic fatty liver disease
    Yuya Seko, Yoshio Sumida, Saiyu Tanaka, Kojiroh Mori, Hiroyoshi Taketani, Hiroshi Ishiba, Tasuku Hara, Akira Okajima, Atsushi Umemura, Taichiro Nishikawa, Kanji Yamaguchi, Michihisa Moriguchi, Kazuyuki Kanemasa, Kohichiroh Yasui, Shunsuke Imai, Keiji Shim
    Hepatology Research.2018;[Epub]     CrossRef
  • Use of Novel High-Protein Functional Food Products as Part of a Calorie-Restricted Diet to Reduce Insulin Resistance and Increase Lean Body Mass in Adults: A Randomized Controlled Trial
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    Nutrients.2017; 9(11): 1182.     CrossRef
  • Gender differences in the association between food insecurity and insulin resistance among U.S. adults: National Health and Nutrition Examination Survey, 2005–2010
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  • Serum glycated albumin as a new glycemic marker in pediatric diabetes
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    Annals of Pediatric Endocrinology & Metabolism.2013; 18(4): 208.     CrossRef
  • The Association of Maximum Body Weight on the Development of Type 2 Diabetes and Microvascular Complications: MAXWEL Study
    Soo Lim, Kyoung Min Kim, Min Joo Kim, Se Joon Woo, Sung Hee Choi, Kyong Soo Park, Hak Chul Jang, James B. Meigs, Deborah J. Wexler, Noel Christopher Barengo
    PLoS ONE.2013; 8(12): e80525.     CrossRef
  • Relative contributions of insulin resistance and β‐cell dysfunction to the development of Type 2 diabetes in Koreans
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    Diabetic Medicine.2013; 30(9): 1075.     CrossRef
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Effect of Adipose Differentiation-Related Protein (ADRP) on Glucose Uptake of Skeletal Muscle.
Yun Hyi Ku, Min Kim, Sena Kim, Ho Seon Park, Han Jong Kim, In Kyu Lee, Dong Hoon Shin, Sung Soo Chung, Sang Gyu Park, Young Min Cho, Hong Kyu Lee, Kyong Soo Park
Korean Diabetes J. 2009;33(3):206-214.   Published online June 1, 2009
DOI: https://doi.org/10.4093/kdj.2009.33.3.206
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AbstractAbstract PDF
BACKGROUND
Skeletal muscle is the most important tissue contributing to insulin resistance. Several studies have shown that accumulation of intramyocellular lipid is associated with the development of insulin resistance. Thus, proteins involved in lipid transport, storage and metabolism might also be involved in insulin action in skeletal muscle. Adipose differentiation-related protein (ADRP), which is localized at the surface of lipid droplets, is known to be regulated by peroxisome proliferator activated receptor gamma (PPARgamma). However, it is not known whether ADRP plays a role in regulating glucose uptake and insulin action in skeletal muscle. METHODS: ADRP expression in skeletal muscle was measured by RT-PCR and western blot in db/db mice with and without PPARgamma agonist. The effect of PPARgamma agonist or high lipid concentration (0.4% intralipos) on ADRP expression was also obtained in cultured human skeletal muscle cells. Glucose uptake was measured when ADRP was down-regulated with siRNA or when ADRP was overexpressed with adenovirus. RESULTS: ADRP expression increased in the skeletal muscle of db/db mice in comparison with normal controls and tended to increase with the treatment of PPARgamma agonist. In cultured human skeletal muscle cells, the treatment of PPARgamma agonist or high lipid concentration increased ADRP expression. siADRP treatment decreased both basal and insulin-stimulated glucose uptake whereas ADRP overexpression increased glucose uptake in cultured human skeletal muscle cells. CONCLUSION: ADRP expression in skeletal muscle is increased by PPARgamma agonist or exposure to high lipid concentration. In these conditions, increased ADRP contributed to increase glucose uptake. These results suggest that insulin-sensitizing effects of PPARgamma are at least partially achieved by the increase of ADRP expression, and ADRP has a protective effect against intramyocellular lipid-induced insulin resistance.
Effects of Lovastatin on Free Fatty Acid Oxidation in Cultured L6 Rat Skeletal Muscle Cells.
Dong Lim Kim, Kee Ho Song, Hae Rim Kim, Suk Kyeong Kim
Korean Diabetes J. 2007;31(3):230-235.   Published online May 1, 2007
DOI: https://doi.org/10.4093/jkda.2007.31.3.230
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AbstractAbstract PDF
BACKGROUND
Recent clinical studies suggest that statins improve insulin resistance and glucose metabolism in patients with metabolic syndrome and type 2 diabetes. To evaluate the possible mechanism of this action, we measured free fatty acid oxidation in cultured L6 rat skeletal muscle cell line. METHODS: Cultured L6 myotubes were treated with or without lovastatin (1, 5, 20 micrometer) for 24 hours or 48 hours and palmitate oxidation was measured. We also measured protein concentration of the cells. RESULTS: Lovastain increased palmitate oxidation in dose and time dependent manner in L6 myotubes (24 hr; 1 micrometer 119.2 +/- 11.9% of control, 5 micrometer 140.9 +/- 8.1%, 20 micrometer 150 +/- 5%, P = 0.05 vs control, respectively, 48 hr 1 micrometer 120.9 +/- 14.5%, 5 micrometer 176.6 +/- 28.2%, 20 micrometer 196.0 +/- 19.9%, P < 0.01 vs control, respectively). However, lovastatin decreased total cellular protein (24 hr: 1 micrometer 89.2 +/- 6.1% of control, 5 micrometer 79.3 +/- 7.6%, 20 micrometer 65.4 +/- 4.2%, P = 0.05 vs control, respectively, 48 hr: 1 micrometer 81.7 +/- 5.1%, 5 micrometer 58.6 +/- 11.9%, 20 micrometer 48.1 +/- 6.9%, P < 0.01 vs control, respectively). CONCLUSION: Lovastatin increased skeletal muscle free fatty acid oxidation in L6 rat skeletal muscle cells. This would be one of the mechanisms which lovastatin improves insulin resistance.

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  • Characterization and Mechanisms of Action of Avocado Extract Enriched in Mannoheptulose as a Candidate Calorie Restriction Mimetic
    Donald K. Ingram, Paul J. Pistell, Zhong Q. Wang, Yongmei Yu, Stefan Massimino, Gary M. Davenport, Michael Hayek, George S. Roth
    Journal of Agricultural and Food Chemistry.2021; 69(26): 7367.     CrossRef
Effects of PPAR-alpha and-gamma Agonists on Fatty Acid Metabolism of Muscle Cells in Hyperlipidemic and Hyperglycemic Conditions.
Yong jik Lee, Zheng Shan Zhao, Soo Kyung Kim, Hae Jin Kim, Wan Sub Shim, Chul Woo Ahn, Hyun Chul Lee, Bong Soo Cha
Korean Diabetes J. 2006;30(5):324-335.   Published online September 1, 2006
DOI: https://doi.org/10.4093/jkda.2006.30.5.324
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AbstractAbstract PDF
BACKGROUND
Studies for the regulation of fatty acid metabolism are deficient relatively in skeletal muscle and heart. The investigations in pathological conditions for malonyl-CoA decarboxylase (MCD) and for the relation of MCD and PPAR-alpha.-gamma agonists are insufficient in particular. METHODS: In the current study, fully differentiated H9c2 muscle cells were exposed to pathological conditions such as hyperlipidemic (0.1 mM Palmitate) and hyperglycemic (16.5 mM Glucose) condition with 5 uM PPAR-gamma agonist (rosiglitazone) and 10 uM PPAR-alpha agonist (WY14,643) and then experiments such as MCD activity assay, MCD real-time RT-PCR, MCD reporter gene assay, MCD Western blotting, PPAR-alpha Western blotting, and palmitate oxidation test were carried out. RESULTS: Only PPAR-alpha agonist increased MCD activity. In the result of real-time RT-PCR, both PPAR-alpha and PPAR-gamma agonists elevated MCD mRNA expression in hyperlipidemic condition. MCD protein expression was decreased in hyperlipidemic condition, however, increased in rosiglitazone, or WY14,643 treated conditions. Rosiglitazone, and WY14,643 treated groups showed incresed MCD protein expression in hyperglycemic condition. Hyperlipidemic control group and PPAR-alpha.-gamma agonists treated groups presented about 3.8 times more increased palmitate oxidation level than normolipidemic control group in hyperlipidemic condition. PPAR-alpha agonist treated group showed 49% more increased palmitate oxidation rate than hyperlipidemic control group in primary cultured rat skeletal muscle cells. The amount of palmitate oxidation from differentiated H9c2 muscle cells that had overexpressed PPAR-alpha structural genes was more increased than control group. CONCLUSION: This study suggests that PPAR-alpha agonist ameliorates the defects induced by hyperlipidemic condition through the regulation of MCD. In summary, a closely reciprocal relation among PPAR-alpha agonist, MCD, and fatty acid oxidation existed distinctly in hyperlipidemic condition, but not in hyperglycemic condition.

Citations

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  • Beneficial effect of Combination with Korean Red Ginseng and Morus alba in metabolic syndrome
    Yun Jung Lee, Hye Yoom Kim, Jung Joo Yoon, So Min Lee, You Mee Ahn, Joung Hyun Kho, Min Chul Kho, Ho Sub Lee, Kyung Min Choi, Dae Gill Kang
    The Korea Journal of Herbology.2012; 27(6): 99.     CrossRef
  • Effects of Mixed Extract from Lycium chinense, Cordyceps militaris, and Acanthopanax senticosus on Glucose-Regulating Enzymes of HepG2 in Hyperglycemic Conditions
    Dae-Jung Kim, Jeong-Mi Kim, Tae-Hyuk Kim, Jong-Mi Baek, Hyun-Sook Kim, Myeon Choe
    Journal of the Korean Society of Food Science and Nutrition.2010; 39(9): 1257.     CrossRef
Regulation of mFABP (fatty acid binding protein) Expression by PPAR in Cultured Human Skeletal Muscle Cell.
Hyeosn Jeong Jeon, Won Shik Shinn, Jeong Mi Kim, Hye Kyung Hong, Kyong Soo Park, Seong Yeon Kim, Hong Kyu Lee
Korean Diabetes J. 2000;24(4):413-420.   Published online January 1, 2001
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AbstractAbstract PDF
BACKGROUND
Fatty acid binding protein (FABP), putative mammalian fatty acid transporter, plays a role in fatty acid transport, the modulation of cellular signal transduction pathways and the protection against detergent like effects of fatty acids. FABP found in liver, adipose tissue, heart, skeletal muscle and FABP in skeletal muscle accounts for 2% of total protein mass. FABP expression has shown to be up-regulated by PPAR in liver and adipocyte. Adipocyte and liver FABP genes have a functional PPRE (PPAR responsive element) in their promoter region. This evidence led us to investigate for a possible the regulation of mFABP expression by PPAR in cultured human skeletal muscle cell. METHODS: Myoblast were cultured in SkGM for 4weeks and were differentiated into myocyte in MEM for 4days. The myocytes were treated with PPAR ligand (troglitazone: 5 g/mL) or transduction with adenovirus-PPAR 1 (Ad-PPAR 1). mFABP expression was identified by northern blot. RESULTS: mFABP expression was up-regulated by 4.0+/-1.2 fold in the PPAR ligand (p<0.05). There was increased in mFABP expression with transduction with adenovirus-PPAR 1 while there was no change in mFABP expression which transducted with adenovirus - -galactosidase. CONCLUSION: These results demonstrates that mFABP expression is up-regulated by both PPAR ligand and by PPAR 1 over expression in cultured human skeletal muscle cells.
Metabolic Phenotype of Glycogen Synthase Gene Inhibition in Human Skeletal Muscle Cells.
Jae Joon Koh, Kyong Soo Park, Jeong Mi Kim, Seong Yeon Kim, Hong Kyu Lee, Theodore P Ciaraldi, Robert R Henry
Korean Diabetes J. 2000;24(3):331-339.   Published online January 1, 2001
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AbstractAbstract PDF
BACKGROUND
Glycogen synthase (GS) is the rate-limiting enzyme controlling non-oxidative glucose disposal in skeletal muscle. Reduction in GS activity and impaired insulin responsiveness are characteristic features of skeletal muscle in type 2 diabetes that contribute to glucose intolerance. These properties also exist in human skeletal muscle cell cultures from type 2 diabetic subjects. The aim of study is to determine the effect of an isolated reduction in GS on glucose metabolism and if this change can generate a diabetes-like state. METHODS: Cultured skeletal muscle cells from non-diabetic subjects were treated with antisense oligodeoxynucleotides (ODN) to GS to interfere with expression of the gene for 6 days. GS activity, protein expression, glycogen synthesis and cellular glycogen content were measured. RESULTS: Treatment with antisense ODN reduced GS protein expression by 70% compared to control (scrambled) ODN (p<0.01). Both total GS activity and that measured at 0.1 mM G-6-P were reduced by antisense ODN treatment. Insulin responsiveness of GS was also halved. Basal GS FV0.1 was decreased in both antisense ODN and control ODN treated cells and antisense treated cells did not show increase in GS FV0.1 in response to insulin stimulation. Glucose incorporation into glycogen under basal conditions was unaltered after antisense ODN treatment, though no further stimulation in response to insulin was observed. Yet both cellular glycogen content and glycogen synthesis were lower in antisense ODN treated cells compared to control ODN treated cells. CONCLUSIONS: Reduction in GS expression in human skeletal muscle cell impair GS activity and insulin responsiveness but does not replicate the abnormalities of glycogen synthesis found in cultured diabetic skeletal muscle cells.

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