title: Skeletal muscle perilipin 3 and coatomer proteins are increased following exercise and are associated with fat oxidation.
abstract: Lipid droplet-associated proteins such as perilipin 3 (PLIN3) and coatomer GTPase proteins (GBF1, ARF1, Sec23a, and ARFRP1) are expressed in skeletal muscle but little is known so far as to their regulation of lipolysis. We aimed here to explore the effects of lipolytic stimulation in vitro in primary human myotubes as well as in vivo following an acute exercise bout. In vitro lipolytic stimulation by epinephrine (100 μM) or by a lipolytic cocktail (30 μM palmitate, 4 μM forskolin, and 0.5 μM ionomycin, PFI) resulted in increases in PLIN3 protein content. Coatomer GTPases such as GBF1, ARF1, Sec23a, and ARFRP1 also increased in response to lipolytic stimuli. Furthermore, a long duration endurance exercise bout (20 males; age 24.0 ± 4.5 y; BMI 23.6 ± 1.8 kg/m(2)) increased PLIN3 protein in human skeletal muscle (p = 0.03) in proportion to ex vivo palmitate oxidation (r = 0.45, p = 0.04) and whole body in vivo fat oxidation (r = 0.52, p = 0.03). Protein content of ARF1 was increased (p = 0.04) while mRNA expression was increased for several other coatomers (GBF1, ARF1, and Sec23a, all p<0.05). These data provide novel observational insight into the possible relationships between lipolysis and PLIN3 along with these coatomoer GTPase proteins in human skeletal muscle.
authors.affiliation: Pennington Biomedical Research Center, Baton Rouge, Louisiana, United States of America.
authors.forename: Jeffrey D
authors.initials: JD
authors.lastname: Covington
authors.affiliation: School of Medicine, Pontificia Universidad Catolica de Chile, Santiago, Chile.
authors.forename: Jose E
authors.initials: JE
authors.lastname: Galgani
authors.affiliation: Inserm UMR 1048, Institute of Metabolic and Cardiovascular Diseases and Paul Sabatier University, Toulouse, France.
authors.forename: Cedric
authors.initials: C
authors.lastname: Moro
authors.affiliation: Pennington Biomedical Research Center, Baton Rouge, Louisiana, United States of America.
authors.forename: Jamie M
authors.initials: JM
authors.lastname: LaGrange
authors.affiliation: Pennington Biomedical Research Center, Baton Rouge, Louisiana, United States of America.
authors.forename: Zhengyu
authors.initials: Z
authors.lastname: Zhang
authors.affiliation: Department of Pharmaceutical Biosciences, University of Oslo, Oslo, Norway.
authors.forename: Arild C
authors.initials: AC
authors.lastname: Rustan
authors.affiliation: Pennington Biomedical Research Center, Baton Rouge, Louisiana, United States of America.
authors.forename: Eric
authors.initials: E
authors.lastname: Ravussin
authors.affiliation: Pennington Biomedical Research Center, Baton Rouge, Louisiana, United States of America; Department of Kinesiology, University of Texas in El Paso, El Paso, Texas, United States of America.
authors.forename: Sudip
authors.initials: S
authors.lastname: Bajpeyi
mesh_terms: D000328:Adult; D002478:Cells, Cultured; D020756:Coatomer Protein / Q000378:metabolism*; D004837:Epinephrine / Q000494:pharmacology; D015444:Exercise; D006801:Humans; D008066:Lipolysis; D008297:Male; D018485:Muscle Fibers, Skeletal / Q000187:drug effects / Q000378:metabolism; D018482:Muscle, Skeletal / Q000187:drug effects / Q000378:metabolism*; D010084:Oxidation-Reduction; D000070796:Perilipin-3; D010807:Physical Endurance; D033921:Vesicular Transport Proteins / Q000378:metabolism*; D055815:Young Adult
chemical_list: D020756:Coatomer Protein; C038196:PLIN3 protein, human; D000070796:Perilipin-3; D033921:Vesicular Transport Proteins; D004837:Epinephrine