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Studies with a reconstituted muscle glycolytic system. The rate and extent of creatine phosphorylation by anaerobic glycolysis.

ABSTRACT: A mixture of purified muscle glycolytic enzymes was reconstituted and the mixture shown to behave in a fashion analogous to that occurring in vivo. Glycolysis leads to ATP production in muscle and results in the phosphorylation of creatine. The extent of this phosphorylation by anaerobic glycolysis was shown to depend to a small extent on the relative proportions of available P(i) and creatine initially, but more importantly on the first step in glycolysis, in this case the enzyme phosphorylase. With less than 0.1% of the phosphorylase in the a form, only about one-third of the creatine was phosphorylated in 30min, whereas with 4% or more of phosphorylase a, 90% of the creatine was phosphorylated within this time. Inclusion of an adenosine triphosphatase decreased the steady-state concentration of phosphocreatine in the system. Calculations of the theoretical concentrations of ADP and AMP showed that phosphorylase b was almost inactive even in the presence of 9mum-AMP, because of ATP inhibition. With phosphorylase a present, glycolysis was able to continue at least until the calculated concentration of MgADP(-) was only 7mum, and AMP in the sub-mumolar range. The relation of these values to measured concentrations of nucleotides and to phosphorylase a percentages in intact muscle is discussed.

SUBMITTER: Scopes RK

PROVIDER: S-EPMC1177800 | biostudies-other | 1973 May

REPOSITORIES: biostudies-other

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Project description:This study aimed to evaluate the effects of dietary creatine nitrate (CrN) on growth performance, meat quality, energy status, glycolysis, and related gene expression of liver kinase B1/AMP-activated protein kinase (LKB1/AMPK) pathway in Pectoralis major (PM) muscle of broilers. A total of 240 male Arbor Acres broilers (28-day-old) were randomly allocated to one of 5 dietary treatments: the basal diet (control group), and the basal diets supplemented with 600 mg/kg guanidinoacetic acid (GAA), 300, 600, or 900 mg/kg CrN (identified as GAA600, CrN300, CrN600, or CrN900, respectively). We found that dietary GAA and CrN supplementation for 14 d from d 28 to 42 did not affect broiler growth performance, carcass traits, and textural characteristics of breast muscle. GAA600, CrN600, and CrN900 treatments increased pH24h and decreased drip loss of PM muscle compared with the control (P < 0.05). The PM muscles of CrN600 and CrN900 groups showed higher glycogen concentration and lower lactic acid concentration accompanied by lower activities of phosphofructokinase (PFK), pyruvate kinase (PK), and lactate dehydrogenase (LDH) (P < 0.05). Simultaneously, GAA600 and all CrN treatments increased concentration of muscle creatine, phosphocreatine (PCr) and ATP, and decreased AMP concentration and AMP/ATP ratio (P < 0.05). Meanwhile, the concentrations of muscle creatine, PCr, and ATP were increased linearly, while muscle AMP concentration and AMP/ATP ratio were decreased linearly and quadratic as the dose of CrN increased (P < 0.05). GAA600, CrN600, and CrN900 treatments upregulated mRNA expression of CreaT in PM muscle, and CrN600 and CrN900 treatments downregulated GAMT expression in liver and PM muscle compared with the control or GAA600 groups (P < 0.05). The mRNA expression of muscle LKB1, AMPKα1, and AMPKα2 was downregulated linearly in response to the increasing CrN level (P < 0.05). Overall, CrN showed better efficacy on strengthening muscle energy status and improve meat quality than GAA at the some dose. These results indicate that CrN may be a potential replacement for GAA as a new creatine supplement.

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Studies with a reconstituted muscle glycolytic system. The rate and extent of creatine phosphorylation by anaerobic glycolysis.

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