Correlation of muscle activity with glycogen metabolism in muscle of Ascaris suum [a parasitic roundworm, that inhabits the upper small intestine of its host, the pig]
M. J. Donahue, N. J. Yacoub and B. G. Harris Isolated muscle segments from the parasitic roundworm Ascaris suum were shown to contract when perfused with acetylcholine (ACh). The muscle responded to ACh concentrations of 1 microM and was maximally contracted at 50 microM ACh. In fed muscle segments...
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Veröffentlicht in: | American journal of physiology. Regulatory, integrative and comparative physiology integrative and comparative physiology, 1982-05, Vol.242 (5), p.514-R521 |
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Zusammenfassung: | M. J. Donahue, N. J. Yacoub and B. G. Harris
Isolated muscle segments from the parasitic roundworm Ascaris suum were
shown to contract when perfused with acetylcholine (ACh). The muscle
responded to ACh concentrations of 1 microM and was maximally contracted at
50 microM ACh. In fed muscle segments perfused with saturating levels of
ACh the glycogen synthase Ka values for glucose 6-phosphate increased from
0.5 to 0.95 mM. In starved segments stimulated by ACh, the muscle utilized
glycogen at a rate that was 1.41 micrograms.min-1.g tissue-1 greater than
the saline-perfused controls. The cyclic AMP (cAMP) levels remained
relatively constant at 0.34 +/- 0.08 nmol/g muscle during perfusion with
ACh. Contraction in the muscle could be inhibited in a dose-dependent
manner by gamma-aminobutyric acid (GABA). The presence of GABA in starved
muscle prevented the decrease in Ka values and phosphorylase activity
ratios brought about by glucose. Perfusion of GABA did not change cAMP
levels in the muscle. Starved muscle perfused with GABA utilized glycogen
at a rate that was 0.41 microgram.min-1.g-1 greater than saline-perfused
controls. The results indicated that muscle contraction could be elicited
by ACh, and that the energy for this process was derived from endogenous
glycogen stores, which were depleted during contraction. Muscle contraction
was also correlated with inactivation of glycogen synthase and activation
of phosphorylase. These processes appeared to function via a
cAMP-independent mechanisms. |
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ISSN: | 0002-9513 0363-6119 2163-5773 1522-1490 |
DOI: | 10.1152/ajpregu.1982.242.5.r514 |