Literature DB >> 7994802

Correlation between decreased myocardial glucose phosphorylation and the DNA mutation size in myotonic dystrophy.

D Annane1, D Duboc, B Mazoyer, P Merlet, M Fiorelli, B Eymard, H Radvanyi, C Junien, M Fardeau, P Gajdos.   

Abstract

BACKGROUND: Myotonic dystrophy, the most common form of adult dystrophy, has been shown to be caused by amplification of CTG triplet repeat in the 3' untranslated region of a protein kinase gene located on chromosome 19. Impaired glucose metabolism has been suggested as a possible explanation of brain and skeletal muscle involvement in this multisystem disease. We investigated whether myocardial glucose metabolism is impaired in myotonic dystrophy and whether this impairment is related to the size of the mutation. METHODS AND
RESULTS: The myocardial metabolic rate for glucose (MMRGlu, mumol.min-1.g-1), K1 (blood-to-tissue transfer constant), k2 (tissue-to-blood transfer constant), and k3 (phosphorylation rate constant) were determined in 7 control subjects and 12 patients with myotonic dystrophy by using parametric images generated from dynamic cardiac positron emission tomography (PET) and 18F-fluoro-2-deoxy-glucose studies. The expansion of the CTG triplet repeats was analyzed in patients with the probe cDNA25 after EcoRI digestion. Nonparametric tests were used to compare quantitative variables between control subjects and patients. The correlations between the size of the mutation and PET parameters were studied by linear regression. MMRGlu and k3 were significantly decreased in patients compared with control subjects (0.39 +/- 0.20 versus 0.64 +/- 0.25, P = .03, and 0.09 +/- 0.07 versus 0.24 +/- 0.21, P = .03, respectively), whereas K1 and k2 were not statistically different between control subjects and patients. MMRGlu and k3 correlate inversely with the length of the CTG triplet repeat (r = -.65 and P = .03 for MMRGlu, and r = -.85 and P = .001 for k3, respectively).
CONCLUSIONS: In myotonic dystrophy, the observed reductions in MMRGlu and phosphorylation are inversely linked to the length of the mutation. This observation suggests that impaired modulation of a protein kinase involved in myocardial hexokinase activation may give a pathophysiological schema to relate the molecular defect and the abnormal myocardial metabolism in myotonic dystrophy.

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Year:  1994        PMID: 7994802     DOI: 10.1161/01.cir.90.6.2629

Source DB:  PubMed          Journal:  Circulation        ISSN: 0009-7322            Impact factor:   29.690


  6 in total

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2.  Proceedings of the 4th Invitational Wintergreen Conference. Wintergreen, Virginia, USA. July 12-14, 1998. Abstracts.

Authors: 
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4.  The effect of non-insulin-dependent diabetes mellitus and obesity on glucose transport and phosphorylation in skeletal muscle.

Authors:  D E Kelley; M A Mintun; S C Watkins; J A Simoneau; F Jadali; A Fredrickson; J Beattie; R Thériault
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Journal:  IEEE Trans Radiat Plasma Med Sci       Date:  2020-10-15

6.  Receptor and post-receptor abnormalities contribute to insulin resistance in myotonic dystrophy type 1 and type 2 skeletal muscle.

Authors:  Laura Valentina Renna; Francesca Bosè; Sara Iachettini; Barbara Fossati; Lorenzo Saraceno; Valentina Milani; Roberto Colombo; Giovanni Meola; Rosanna Cardani
Journal:  PLoS One       Date:  2017-09-15       Impact factor: 3.240

  6 in total

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