Effect of somatotropin on myosin expression in pigs1

Czerwinski, S. M.; Martin, Jeffery S.

doi:10.2527/1994.7251204x

Cited by 10 publications

(12 citation statements)

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“…This is in agreement with previous findings obtained by using histochemical staining (Solomon et al, 1988 and1990;Beermann et al, 1990;Ono et al, 1995;Sorensen et al, 1996) and by directly measuring the mRNA and protein levels of MyHC isoforms (Czerwinski and Martin, 1994). However, there have been some controversial results reported by Solomon et al (1991) who found that at the body weight of 60 and 90 kg, LD muscle of pigs injected with 100 mg/kg per day pGH from 30 to 60 kg possessed of more oxidative-glycolytic fibres and fewer glycolytic fibres.…”

Section: Discussionsupporting

confidence: 92%

“…Compared with its well-defined positive effect on myofibre hypertrophy, the influence of rpGH on myofibre-type composition is still under debate. Many studies reported that exogenous GH had no effect on the skeletal muscle fibre composition (Solomon et al, 1988 and1990;Beermann et al, 1990;Czerwinski and Martin, 1994), while some experiments -E-mail: zhao.ruqian@gmail.com demonstrated divergent results (Solomon et al, 1991 and.…”

Section: Introductionmentioning

confidence: 99%

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Muscle type-specific responses of myoD and calpain 3 expression to recombinant porcine growth hormone in the pig

Yang

Chen

et al. 2007

Animal

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Sixteen castrated male Large White 3 Landrace pigs were employed to investigate the muscle type-specific changes of gene expression in response to recombinant porcine growth hormone (rpGH) administration. Pigs were injected intramuscularly with rpGH (4 mg/day, n 5 8) or saline (n 5 8) for 28 days. Semi-quantitative reverse transcription-polymerase chain reaction (RT-PCR) was used to determine the mRNA abundance of genes related to muscle growth in longissimus dorsi (LD) and semitendinosus (ST) muscles. Myofibre-type composition was characterised by the ratio of the expression of myosin heavy chain (MyHC) 1, 2a or 2b relative to 2x. The results showed that the relative myofibre-type composition of neither LD nor ST was affected by rpGH administration. rpGH administration did not induce significant changes in the abundances of myostatin and myogenin mRNA in both types of muscle. MyoD and calpain 3 mRNA were significantly increased after rpGH treatment in ST muscle, whereas the difference was not significant in LD muscle. A tendency of down-regulation was observed for PGC-1a mRNA expression in ST muscle of rpGH-treated group (P 5 0.16). These results suggest that myoD, calpain 3 and probably PGC-1a may be involved in the mechanism of exogenous GH action on skeletal muscle growth; rpGH up-regulates mRNA expression of myoD and calpain 3 in a muscle type-specific manner, being more remarkable in ST than in LD, whereas no influences of rpGH on the mRNA expression of myostatin and myogenin were detected.

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Section: Discussionsupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Muscle type-specific responses of myoD and calpain 3 expression to recombinant porcine growth hormone in the pig

Yang

Chen

et al. 2007

Animal

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“…Lys, threonine, methionine, tryptophan, and valine are currently available in crystalline form and can be supplemented in the diet to eliminate excess AA such as Leu. Because myosin is the most abundant protein in muscle (Czerwinski and Martin, 1994), its expression can be used as indicator of protein synthesis in pigs. The objective of the present study was to analyze the effect of different Leu:Lys ratios on the expression of the cationic AA transporters b 0,+ and CAT-1 in the jejunum, liver, longissimus dorsi (LD) muscle, and semitendinosus (ST) muscle, the expression of myosin in LD and ST, and the availability of AA (serum concentration, SC).…”

Section: Introductionmentioning

confidence: 99%

Gene expression, serum amino acid levels, and growth performance of pigs fed dietary leucine and lysine at different ratios

García¹,

Morales²,

Araiza³

et al. 2015

Genet. Mol. Res.

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ABSTRACT. We examined 96 pigs (28.1 ± 0.83 kg) to analyze the effect of Leu:Lys ratios on expression of the cationic amino acid transporters b 0,+ and CAT-1 in the jejunum and liver as well as myosin expression in 2 muscles to estimate the optimum standardized ileal digestible (SID) Leu:Lys ratio for growth rate and efficiency. A wheatand wheat bran-based diets were formulated to meet the requirements of SID amino acids other than Leu (0.70%) and Lys (0.80%). L-Leu was added to the basal diet in 5 SID Leu:Lys ratios (88, 100, 120, 140, and 160% in diets 1-5). Tissue samples were collected from 8 pigs with ratios of 88, 120, and 160%. Relative expression of b 0,+ , CAT-1, and myosin was analyzed. b 0,+ expression in the jejunum was higher but lower in the liver of pigs with the 120% ratio compared to those with the 88 or 160% ratio; myosin expression in longissimus dorsi was also higher in pigs with the 120% ratio (P < 0.05). CAT-1 was lower in the jejunum and longissimus dorsi of pigs with 120 or 160% ratios than in pigs with 88%. Serum concentration of nearly all amino acids decreased with excess dietary Leu (P < 0.05). The SID Leu:Lys of 104 and 109% 1590 H. García et al. ©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 14 (1): 1589-1601 (2015 optimized average daily gain and feed conversion ratio, respectively. Thus, the dietary Leu:Lys ratio affects the expression of genes coding for amino acid transporters and myosin, the availability of Lys, and the growth rate and efficiency in pigs.

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“…According to Czerwinski and Martin (1994), myosin is the most abundant protein in muscle cells, and the isoform IIB accounts for about 80% of the total fibers in some pig muscles; this isoform is extensively expressed in LM and SM (Lefaucheur et al, 2002). Furthermore, Brodsky et al (2004) found that low intake of dietary protein reduced the synthesis of myosin in human, suggesting that myosin can be a good indicator of protein synthesis and accretion in pigs.…”

Section: Discussionmentioning

confidence: 99%

“…Type IIB fibers account for about 80% of the total fibers in some pig muscles (Czerwinski and Martin, 1994) and are extensively expressed in LM and SM of pigs (Lefaucheur et al, 2002). Also, a housekeeping 18S rRNA (GenBank AY265350) was used as an endogenous control to normalize variations in mRNA.…”

Section: Reverse Transcriptionmentioning

confidence: 99%

Expression of cationic amino acid transporters, carcass traits, and performance of growing pigs fed low-protein amino acid-supplemented versus high protein diets

Morales¹,

Grageola²,

García³

et al. 2013

Genet. Mol. Res.

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ABSTRACT. Free amino acids (AA) appear to be absorbed faster than protein-bound AA (PB-AA). We conducted an experiment to assess the effect of feeding pigs with a partially free (F-AA) or totally PB-AA diet on expression of selected genes and performance of pigs. The expression of cationic AA transporters b 0,+ and CAT-1 in intestinal mucosa, liver, and longissimus (LM) and semitendinosus (SM) muscles, as well as that of myosin in LM and SM, was analyzed. Twelve pigs (31.7 ± 2.7 kg) were used. The F-AA diet was based on wheat, supplemented with 0.59% L-Lys, 0.33% L-Thr, and 0.10% DL-Met. The PB-AA diet was formulated with wheat-soybean meal. Average daily feed intake was 1.53 kg per pig. The expression of b 0,+ and CAT-1 was analyzed in jejunal and ileal mucosa, liver, LM, and SM; myosin expression was also analyzed in both muscles. Pigs fed the PB-AA diet tended to have Effect of amino acid form on mRNA expression and performance in pigs higher weight gain and feed efficiency (P < 0.10), and had thinner back fat (P = 0.02). The expression of b 0,+ was higher (P < 0.01) in jejunum but lower (P < 0.01) in the liver of pigs fed the F-AA diet; CAT-1 tended to be lower in liver but higher in LM of PB-AA pigs. Myosin expression was not affected. Intestinal AA absorption was faster in pigs fed the F-AA diet, but AA uptake by the liver seemed to be faster in pigs fed the PB-AA. Performance and expression of AA transporters and myosin suggest that the dietary content of free or protein-bound AA does not affect their availability for protein synthesis in pigs.

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Effect of somatotropin on myosin expression in pigs1

Cited by 10 publications

References 0 publications

Muscle type-specific responses of myoD and calpain 3 expression to recombinant porcine growth hormone in the pig

Muscle type-specific responses of myoD and calpain 3 expression to recombinant porcine growth hormone in the pig

Gene expression, serum amino acid levels, and growth performance of pigs fed dietary leucine and lysine at different ratios

Expression of cationic amino acid transporters, carcass traits, and performance of growing pigs fed low-protein amino acid-supplemented versus high protein diets

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