Contractile protein content reflects myosin heavy-chain isoform gene expression1

Gunawan, Andrea; Park, S K; Pleitner, Jonathan M.; Feliciano, L San; Grant, A.L.; Gerrard, D.E.

doi:10.2527/jas.2006-511

Cited by 29 publications

(22 citation statements)

References 28 publications

(27 reference statements)

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“…Hemmings et al (2009) found a high expression of myosin IIB isoform in STM of sheep, but not in LDM. In contrast, Gunawan et al (2007) reported that myosin IIB expression was higher in LDM of pigs, as compared to STM. Brodsky et al (2004) concluded that protein deprivation in humans reduces the expression of fast twitch myosin heavy chain and that dietary amino acid scarcity produces a change in myosin isoform distribution via posttranscriptional mechanisms.…”

Section: Discussionmentioning

confidence: 86%

Supplemental leucine and isoleucine affect expression of cationic amino acid transporters and myosin, serum concentration of amino acids, and growth performance of pigs

Cervantes-Ramírez

Mendez-Trujillo²,

Araiza-Piña³

et al. 2013

Genet. Mol. Res.

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ABSTRACT. Leucine (Leu) participates in the activity of cationic amino acid (aa) transporters. Also, branched-chain aa [Leu, isoleucine (Ile), and valine (Val)] share intestinal transporters for absorption. We conducted an experiment with 16 young pigs (body weight of about 16 kg) to determine whether Leu and Ile affect expression of aa transporters b 0,+ and CAT-1 in the jejunum and expression of myosin in muscle, as well as serum concentration of essential aa, and growth performance in pigs. Dietary treatments were: wheat-based diets fortified with Lys, Thr, and Met; basal diet plus 0.50% Leu; basal diet plus 0.50% Ile, and basal diet plus 0.50% Leu and 0.50% Ile. After 28 days, the pigs were sacrificed to collect blood, jejunum, and semitendinosus and longissimus muscle samples. The effects of single and combined addition of Leu and Ile were analyzed. Leu alone or combined with Ile significantly decreased daily weight gain and reduced feed conversion. Leu and Ile, alone or in combination, significantly decreased expression of b 0,+ and significantly increased CAT-1. Ile alone or combined with Leu significantly decreased myosin expression in semitendinosus and significantly decreased it in M. Cervantes-Ramírez et al. 116©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 12 (1): 115-126 (2013) longissimus muscle. Leu alone significantly decreased Lys, Ile and Thr serum concentrations; Ile significantly decreased Thr serum concentration; combined Leu and Ile significantly decreased Thr and significantly increased Val serum concentration. We conclude that dietary levels of Leu and Ile affect growth performance, expression of aa transporters and myosin, and aa serum concentrations in pigs.

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Section: Discussionmentioning

confidence: 86%

Supplemental leucine and isoleucine affect expression of cationic amino acid transporters and myosin, serum concentration of amino acids, and growth performance of pigs

Cervantes-Ramírez

Mendez-Trujillo²,

Araiza-Piña³

et al. 2013

Genet. Mol. Res.

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“…According to Lefaucheur et al (2002), type IIB fibers, which account for approximately 80% of the total fibers in some pig muscles, are extensively expressed in the ST and LD of pigs. Gunawan et al (2007) reported higher expression of myosin IIB isoform in the LD compared with the ST in pigs. In this study, myosin was expressed in both muscles, but the expression in LD was approximately 6-fold higher compared to that in ST.…”

Section: Discussionmentioning

confidence: 93%

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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“…The diaphragm is comprised mainly of oxidative type I and type IIa fibres, where the SM has 86-88% type II fibres, with the majority of these being the fast glycolytic IIb type. [26][27][28] It has previously been shown that the myogenic behaviour of satellite cells isolated from muscle with contrasting fibre type composition, exhibit differences in proliferation and fusion rates. 29 Our findings support those of Bajot et al, 29 in that satellite cells from predominantly slow muscle types appear superior at myogenic differentiation in vitro.…”

Section: Discussionmentioning

confidence: 99%

Muscle origin of porcine satellite cells affects in vitro differentiation potential

Redshaw¹,

McOrist²,

Loughna³

2010

Cell Biochemistry & Function

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Post-natal muscle regeneration relies on the activation of tissue stem cells known as satellite cells, to repair damage following exercise trauma and disease. Satellite cells from individual muscles are known to be heterogeneous with regard to proliferation, fusion and transplantation abilities, although the muscle origin has rarely been considered pertinent to their differentiation capabilities. In this study we compared the potential of two functionally distinct skeletal muscle satellite cell populations from porcine diaphragm and hind-limb semi-membranosus muscles. These two muscles were chosen primarily for differences in metabolic and contractile properties: the diaphragm is more continuously active and has a greater oxidative capacity. Cells were induced to differentiate towards myogenic and adipogenic lineages, and here we have shown that cells from diaphragm exhibit a significantly greater degree of myogenesis compared with those from semi-membranosus, while the converse was true for adipogenesis. Unexpectedly, both conditions generated small numbers of cells with neuronal characteristics for both muscle types, although more so in cells derived from the diaphragm. With increased interest in muscle adiposity with age and disease, these findings suggest that muscle origin of satellite cells does affect lineage fate, however whether differences in developmental origin or metabolic activity of the parent tissue govern this, remains to be determined.

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Contractile protein content reflects myosin heavy-chain isoform gene expression1

Cited by 29 publications

References 28 publications

Supplemental leucine and isoleucine affect expression of cationic amino acid transporters and myosin, serum concentration of amino acids, and growth performance of pigs

Supplemental leucine and isoleucine affect expression of cationic amino acid transporters and myosin, serum concentration of amino acids, and growth performance of pigs

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

Muscle origin of porcine satellite cells affects in vitro differentiation potential

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