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Research Article| Volume 54, ISSUE 2, P173-179, May 1982

Myotonic muscular dystrophy

Calcium-dependent phosphatidate metabolism in the erythrocyte membrane
  • Larry H. Yamaoka
    Affiliations
    Duke University Medical Center, Division of Neurology, Department of Medicine, Durham, NC 27710 U.S.A.

    Duke University Medical Center, Division of Neurology, Department of Biochemistry, Durham, NC 27710 U.S.A.
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  • Jeffery M. Vance
    Affiliations
    Duke University Medical Center, Division of Neurology, Department of Medicine, Durham, NC 27710 U.S.A.

    Duke University Medical Center, Division of Neurology, Department of Biochemistry, Durham, NC 27710 U.S.A.
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  • Allen D. Roses
    Correspondence
    Address for correspondence and reprint requests: Dr. Allen D. Roses, Division of Neurology, Department of Medicine, P.O. Box M2900, Durham, NC 27710, U.S.A.
    Affiliations
    Duke University Medical Center, Division of Neurology, Department of Medicine, Durham, NC 27710 U.S.A.

    Duke University Medical Center, Division of Neurology, Department of Biochemistry, Durham, NC 27710 U.S.A.
    Search for articles by this author
DOI:https://doi.org/10.1016/0022-510X(82)90179-4
Myotonic muscular dystrophy
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      Abstract

      It has been suggested that the erythrocytes of myotonic dystrophy (MyD) patients have a decreased calcium-stimulated phosphatidic acid (PA) accumulation. This could be the result of a defect in the calcium-stimulated hydrolysis of the polyphosphoinositides (calcium-dependent phosphodiesterase) or in the subsequent formation of PA from its precursors (diacylglycerol kinase).
      In vitro assays were established for both enzymes in erythrocyte membranes. Calcium-dependent phosphodiesterase activity was assayed with both endogenous 32P-labeled erythrocyte diphosphoinositide and triphosphoinositide and with the same phospholipids isolated from rat brain. No significant differences in activity were found between MyD patients and normal controls with either method of substrate preparation. No difference in diglyceride kinase activity was found between ghosts prepared from MyD patients and normal controls. Thus, there were no differences in either of the membrane-associated enzymes of phosphatidic acid metabolism.
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      Article info

      Publication history

      Accepted: October 7, 1981
      Received in revised form: October 5, 1981
      Received: June 17, 1981

      Footnotes

      ☆Supported by clinical research grants from the Muscular Dystrophy Association, Inc., and the National Institute for Neurological and Communicative Disorders and Stroke (NS-15060).

      ☆Academic affiliations: Dr. Yamaoka, Fellow, Membrane Training Program, Duke University Medical Center, Durham, NC 27710; Dr. Vance, MDA postdoctoral research fellow, Duke University Medical Center, Durham, NC 27710; Dr. Roses, Professor and Chief, Division of Neurology, Department of Medicine, Assistant Professor, Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, U.S.A.

      Identification

      DOI: https://doi.org/10.1016/0022-510X(82)90179-4

      Copyright

      © 1982 Published by Elsevier Inc.

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