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Skeletal muscle insulin resistance in type 2 diabetes

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  • 2015-11-13


[2015 Fall Life Sciences & IBB Regular Seminar]



            ▶Subject: Skeletal muscle insulin resistance in type 2 diabetes


            ▶Speaker: Prof. Kyong Soo Park (Seoul National University)


            ▶Date: 4:00PM/Nov./20(Fri.)/2015


            ▶Place: Auditorium(1F), Postech Biotech Center



                  Skeletal muscle is the predominant tissue for insulin mediated glucose uptake and has been considered as an important site for insulin resistance. However, mechanism of skeletal muscle insulin resistance are not completely understood. Skeletal muscle uses fatty acids as a major fuel source in resting state. Reduced fatty acid oxidation(FAO) capacity is associated with accumulation of intracellular lipid metabolites and inhibition of IRS activation.

Recently, we found SUMO-specific protease 2 (SENP2) a novel regulator of fatty acid metabolism in skeletal muscle. Palmitate increased the expression of SENP2 in C2C12 myotubes. This increase promoted the recruitment of peroxisome proliferator-activated receptor (PPAR)δ and PPARγ, through desumoylation of PPARs, to the promoters of the genes involved in FAO. In addition, SENP2 overexpression substantially increased FAO in C2C12 myotubes. Consistent with the cell culture system, muscle-specific SENP2 overexpression led to a marked increase in the mRNA levels of CPT1b and ACSL1 and thereby in FAO in the skeletal muscle, which ultimately alleviated high-fat diet-induced obesity and insulin resistance. Our data suggest that SENP2 is an important regulator of fatty acid metabolism in skeletal muscle and further implicate that muscle SENP2 could be a novel therapeutic target for reducing skeletal muscle insulin resistance.


           ▶Inquiry: Prof. Sung Ho Ryu (279-2292) 


              * This seminar will be given in English.

          please refrain from taking photos during seminars. *

790-784 SAN 31, HYOJA-DONG, NAM-GU, POHANG, GYUNGBUK. KOREA 생체분자기능연구사업단 TEL : 054-279-2997

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