Ractopamine induces differential gene expression in porcine skeletal muscles.
Ractopamine (RAC) improves growth by increasing lean accretion and decreasing fat deposition through repartitioning nutrients from adipose tissue to skeletal muscle. Although the process is not completely understood, RAC alters the proportion of muscle fiber type composition toward a faster-contracting phenotype. Because one of the primary determinants of contractile speed is the relative abundance of myosin heavy chain (MyHC) isoforms and because the genes encoding these isoforms are transcriptionally regulated, RAC likely alters MyHC gene expression. Using real-time PCR, the relative abundance of transcripts of individual type I, IIA, IIX, and IIB, and total MyHC, as well as glycogen synthase, citrate synthase, lactate dehydrogenase, peroxisome proliferator activated receptor alpha, beta1-adrenergic receptor (AR), and beta2-AR were determined in the LM of 44 pigs fed RAC (20 mg/kg) for 0, 1, 2, or 4 wk. In addition, MyHC isoform expression was determined in the LM and red semitendinosus and white semitendinosus muscles of 48 pigs fed RAC (20 mg/kg) for shorter periods of 12, 24, 48, or 96 h. Type I MyHC expression was unaffected (P > 0.73) by RAC administration. Type IIA MyHC expression decreased (P < 0.0001) by 96 h, was lower (P < 0.0001) by 1 wk, and returned to normal by 4 wk. Type IIX MyHC mRNA decreased (P < 0.001) by 2 wk and continued to decrease (P < 0.0001) by 4 wk. Most interesting was an increase (P < 0.0001) in type IIB MyHC by 12 h, which was maintained at an elevated level throughout the 4-wk feeding period. Abundance of glycogen synthase transcript was increased (P < 0.05) by 12 h, but was not different from controls at 2 wk, and was lower (P < 0.01) at 4 wk. Gene expression of beta1-AR was not affected by feeding RAC, whereas beta2-AR gene expression was decreased (P < 0.05) by 2 wk. These data show MyHC genes are differentially regulated by RAC and suggest that the beta adrenergic agonist-induced repartitioning effect is, in part, mediated by changing muscle fiber type-specific gene expression, perhaps through the beta2-AR.
Gunawan
A M
AM
Department of Animal Sciences, Purdue University, West Lafayette 47907, USA.
Richert
B T
BT
Schinckel
A P
AP
Grant
A L
AL
Gerrard
D E
DE
D000318:Adrenergic beta-Agonists / Q000494:pharmacology*; D000818:Animals; D002950:Citrate (si)-Synthase / Q000378:metabolism; D005260:Female; D018507:Gene Expression Regulation, Developmental / Q000187:drug effects*; D006006:Glycogen Synthase / Q000378:metabolism; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D008297:Male; D018482:Muscle, Skeletal / Q000187:drug effects* / Q000254:growth & development / Q000378:metabolism; D018995:Myosin Heavy Chains / Q000235:genetics / Q000378:metabolism*; D047493:PPAR alpha / Q000378:metabolism; D010627:Phenethylamines / Q000494:pharmacology*; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D011897:Random Allocation; D018342:Receptors, Adrenergic, beta-1 / Q000378:metabolism; D018343:Receptors, Adrenergic, beta-2 / Q000378:metabolism; D013552:Swine / Q000235:genetics / Q000254:growth & development / Q000378:metabolism; D013997:Time Factors
D000318:Adrenergic beta-Agonists; D047493:PPAR alpha; D010627:Phenethylamines; D020033:Protein Isoforms; D018342:Receptors, Adrenergic, beta-1; D018343:Receptors, Adrenergic, beta-2; C060897:ractopamine; D007770:L-Lactate Dehydrogenase; D002950:Citrate (si)-Synthase; D006006:Glycogen Synthase; D018995:Myosin Heavy Chains