AMP deaminase binding in contracting rat skeletal muscle.

@article{Rundell1992AMPDB,
  title={AMP deaminase binding in contracting rat skeletal muscle.},
  author={Kenneth William Rundell and Peter C. Tullson and R. L. Terjung},
  journal={The American journal of physiology},
  year={1992},
  volume={263 2 Pt 1},
  pages={
          C287-93
        }
}
AMP deaminase, which hydrolyses AMP to inosine 5'-monophosphate (IMP) and NH3 at high rates during excessive energy demands in skeletal muscle, is activated when bound to myosin in vitro. We evaluated AMP deaminase binding in vivo during muscle contractions to assess whether binding 1) is inherent to deamination and found only with high rates of IMP production or simply coincident with the contractile process and 2) requires cellular acidosis. AMP deaminase activity (mumol.min-1.g-1) was… Expand
Protecting the cellular energy state during contractions: role of AMP deaminase.
  • C. Hancock, J. Brault, R. Terjung
  • Biology, Medicine
  • Journal of physiology and pharmacology : an official journal of the Polish Physiological Society
  • 2006
TLDR
There was a remarkable ability of the muscle to function under these challenging energetic conditions, which helps explain why patients deficient in AMP deaminase do not always exhibit an impaired muscle function. Expand
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TLDR
The elimination of this kinetic effect by treatment of beta-GPA-treated muscle extracts with acid phosphatase in vitro suggests that phosphorylation is involved in the kinetic control of skeletal muscle AMPD in vivo. Expand
Molecular and kinetic alterations of muscle AMP deaminase during chronic creatine depletion.
TLDR
The elimination of this kinetic effect by treatment of β-GPA-treated muscle extracts with acid phosphatase in vitro suggests that phosphorylation is involved in the kinetic control of skeletal muscle AMPD in vivo. Expand
Control of AMP deaminase 1 binding to myosin heavy chain.
TLDR
Deletion analyses demonstrate that the amino-terminal 65 residues of AMPD1 play a critical role in modulating the sensitivity to ATP-induced inhibition of MHC binding, which is discussed in the context of the various roles proposed for AMPD in energy production in the myocyte. Expand
Control of AMP deaminase 1 binding to myosin heavy chain.
TLDR
Deletion analyses demonstrate that the amino-terminal 65 residues of AMPD1 play a critical role in modulating the sensitivity to ATP-induced inhibition of MHC binding, which is discussed in the context of the various roles proposed for AMPD in energy production in the myocyte. Expand
Role of troponin T and AMP deaminase in the modulation of skeletal muscle contraction
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The data reported in this review on the interactions between AMPD and TnT strongly suggest that these proteins mutually combine to fine-tune the regulation of muscle contraction in fast muscle. Expand
AMP Deaminase 3 in Skeletal Muscle Atrophy: Regulation of Protein Degradation and Contractile Performance
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The results suggest that the upregulation of AMPD3 during atrophy improved relaxation time of muscle, which is sensitive to reductions in the free energy of ATP hydrolysis, during intense contractions. Expand
Regulation of 5'-adenosine monophosphate deaminase in the freeze tolerant wood frog, Rana sylvatica
TLDR
Stable modification of AMPD properties via freeze-responsive phosphorylation may contribute both to AMPD control and to coordinating AMPD function with other enzymes of energy metabolism in cold ischemic muscle. Expand
Localization of N-terminal sequences in human AMP deaminase isoforms that influence contractile protein binding.
TLDR
Serial N-terminal deletion mutants of up to 111, 214, and 126 residues have been constructed without significant alteration of catalytic function or protein solubility and analysis of the most truncated active enzymes demonstrates that all three isoforms can associate with skeletal muscle actomyosin and suggests that a primary binding domain is located within the C-terminals of each polypeptide. Expand
Role of the HPRG Component of Striated Muscle AMP Deaminase in the Stability and Cellular Behaviour of the Enzyme
TLDR
The hypothesis that the Zn binding properties of HPRG could promote the association of AMPD1 to the thin filament is advanced, suggesting a physiological mutual dependence between the two subunit components with regard to the stability of the two isoforms of striated muscle AMPD. Expand
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