SUMO-specific protease 2 mediates leptin-induced fatty acid oxidation in skeletal muscle

Koo, Young Do; Lee, Ji Seon; Lee, Seung Ah; Quaresma, Paula G.F.; Bhat, Ratan V.; Haynes, William G.; Park, Young Joo; Kim, Young–Bum; Chung, Sung Soo; Park, Kyong Soo

doi:10.1016/j.metabol.2019.03.004

Cited by 24 publications

(23 citation statements)

References 35 publications

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“…STAT3-dependent upregulation of SENP2 keeps PPARβ/δ and PPARγ proteins at the unSUMOylated active state leading to the upregulation of CPT1b and ACSL1 and subsequentially fatty acid β-oxidation. Consistent with this proposed mechanism is the finding that leptin treatment does not upregulate CPT1b and ACSL1 as well as fatty acid β-oxidation in SENP2 knockout mice [71].…”

Section: Nuclear Receptorsmentioning

confidence: 61%

“…Importantly, the overexpression of SENP2 in muscles alleviates HFD-induced obesity and insulin resistance, demonstrating the biological significance and therapeutic potential of SENP2 activity in vivo [31]. SENP2 upregulation was also demonstrated following the treatment of C2C12 cells with the hormone leptin that activates a Signal Transducer and Activator of Transcription 3 (STAT3) transcription factor [71]. STAT3-dependent upregulation of SENP2 keeps PPARβ/δ and PPARγ proteins at the unSUMOylated active state leading to the upregulation of CPT1b and ACSL1 and subsequentially fatty acid β-oxidation.…”

Section: Nuclear Receptorsmentioning

confidence: 97%

“…This deconjugation leads to the transcriptional upregulation of fatty-acid oxidation-associated enzymes, such as carnitine palmitoyl transferase-1 (CPT1b) and long-chain acyl-CoA synthetase 1 (ACSL1). SENP2 upregulation was also demonstrated following the treatment of C2C12 cells with the hormone leptin that activates the STAT3 transcription factor [71]. In SENP2 knockout mice, leptin treatment does not upregulate CPT1b and ACSL1 levels as well as fatty acid β-oxidation, demonstrating the in vivo significance of the link between the SUMOylation of PPAR proteins and lipid metabolism [71].…”

Section: Nuclear Receptorsmentioning

confidence: 98%

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Not So Slim Anymore—Evidence for the Role of SUMO in the Regulation of Lipid Metabolism

Sapir

2020

Biomolecules

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One of the basic building blocks of all life forms are lipids—biomolecules that dissolve in nonpolar organic solvents but not in water. Lipids have numerous structural, metabolic, and regulative functions in health and disease; thus, complex networks of enzymes coordinate the different compositions and functions of lipids with the physiology of the organism. One type of control on the activity of those enzymes is the conjugation of the Small Ubiquitin-like Modifier (SUMO) that in recent years has been identified as a critical regulator of many biological processes. In this review, I summarize the current knowledge about the role of SUMO in the regulation of lipid metabolism. In particular, I discuss (i) the role of SUMO in lipid metabolism of fungi and invertebrates; (ii) the function of SUMO as a regulator of lipid metabolism in mammals with emphasis on the two most well-characterized cases of SUMO regulation of lipid homeostasis. These include the effect of SUMO on the activity of two groups of master regulators of lipid metabolism—the Sterol Regulatory Element Binding Protein (SERBP) proteins and the family of nuclear receptors—and (iii) the role of SUMO as a regulator of lipid metabolism in arteriosclerosis, nonalcoholic fatty liver, cholestasis, and other lipid-related human diseases.

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Section: Nuclear Receptorsmentioning

confidence: 61%

Section: Nuclear Receptorsmentioning

confidence: 97%

Section: Nuclear Receptorsmentioning

confidence: 98%

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Not So Slim Anymore—Evidence for the Role of SUMO in the Regulation of Lipid Metabolism

Sapir

2020

Biomolecules

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“…C2C12 myoblasts (American Type Culture Collection, ATCC Manassas, VA, USA) were maintained and differentiated as previously reported. 23 After 5 days of differentiation, C2C12 myoblasts were fused into myotubes and subjected to treatment with McAb-ATR, PA, insulin, or other reagents. PA (0.75 mM) was prepared by conjugation of PA with 2% fatty acid-free BSA dissolved in DMEM.…”

Section: Cell Culture and Treatmentmentioning

confidence: 99%

Immunotherapy against angiotensin II receptor ameliorated insulin resistance in a leptin receptor‐dependent manner

et al. 2020

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The angiotensin II type 1 receptor (AT1R) signaling pathway is reported to modulate glucose metabolism. Targeting AT1R, our group invented ATRQβ-001 vaccine, a novel immunotherapeutic strategy to block the activation of AT1R. Here, we evaluated the therapeutic efficacy of ATRQβ-001 vaccine in insulin resistance, and investigated the mechanism. Our results showed that ATRQβ-001 vaccine and specific monoclonal antibody against epitope ATR-001 (McAb-ATR) decreased fasting serum insulin concentration and improved glucose and insulin tolerance in ob/ob mice. These beneficial effects were verified in high-fat diet-induced obese mice. McAb-ATR activated insulin signaling in skeletal muscle and insulin-resistant C2C12 myotubes without affecting liver or white adipose tissue of ob/ob mice. Mechanistically, the favorable impact of McAb-ATR on insulin resistance was abolished in db/db mice and in C2C12 myotubes with leptin receptor knockdown. AT1R knockdown also eradicated the effects of McAb-ATR in C2C12 myotubes. Furthermore, McAb-ATR treatment was able to activate the leptin receptor-mediated JAK2/STAT3 signaling in skeletal muscle of ob/ob mice and C2C12 myotubes. Additionally, angiotensin II downregulated the leptin signaling in skeletal muscle of ob/ob and diet-induced obese mice. We demonstrated that ATRQβ-001 vaccine and McAb-ATR improved whole-body insulin resistance and regulated glucose metabolism in skeletal muscle in a leptin receptor-dependent manner. Our data suggest that immunotherapy targeting AT1R is a novel strategy for treating insulin resistance.

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“… Aydin et al (2014) reports that irisin, a kind of myokines secreted by muscle tissue, could convert white adipose tissue into brown adipose tissue, enhancing energy expenditure. Leptin directly induces fatty acid oxidation (FAO) in skeletal muscle by AMPK pathway ( Koo et al, 2019 ). A study has demonstrated adiponectin increases glucose uptake, enhances mitochondrial oxidation and modulates lipoclastic capacity via coupling fibroblast growth factor 21 ( FGF21 ) actions from adipocytes to skeletal myocytes ( Lin et al, 2013 ).…”

Section: Introductionmentioning

confidence: 99%

Comparative Analysis of MicroRNA Expression Profiles Between Skeletal Muscle- and Adipose-Derived Exosomes in Pig

Wen

et al. 2021

Front. Genet.

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Skeletal muscle and adipose tissues are both involved in regulation of metabolism. In the skeletal muscle-adipose tissue crosstalk, exosomes may play an important role but the main components of exosomes are not clear. In this study, we found skeletal muscle-derived exosomes can inhibit adipogenesis of porcine preadipocytes. We identified microRNA expression profiles of muscle exosomes and adipose exosomes by high-throughput sequencing. There were 104 (both novel and known microRNAs) microRNAs differentially expressed (DE miRNAs) between M-EXO (muscle-derived exosomes) and A-EXO (adipose–derived exosomes) groups. A total of 2,137 target genes of DE miRNAs for M-EXO and 2,004 target genes of DE miRNAs for A-EXO were detected. Bioinformatic analyses revealed that some DE miRNAs of M-EXO (especially miR-221-5p) were mainly enriched in lipid-related metabolism processes. The findings may serve as a fundamental resource for understanding the detailed functions of exosomes between the skeletal muscle-adipose crosstalk and the potential relationship between skeletal muscle atrophy and obesity.

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SUMO-specific protease 2 mediates leptin-induced fatty acid oxidation in skeletal muscle

Cited by 24 publications

References 35 publications

Not So Slim Anymore—Evidence for the Role of SUMO in the Regulation of Lipid Metabolism

Not So Slim Anymore—Evidence for the Role of SUMO in the Regulation of Lipid Metabolism

Immunotherapy against angiotensin II receptor ameliorated insulin resistance in a leptin receptor‐dependent manner

Comparative Analysis of MicroRNA Expression Profiles Between Skeletal Muscle- and Adipose-Derived Exosomes in Pig

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