Advertisement
Research Article| Volume 78, ISSUE 1, P63-70, March 1987

Absence of biochemical heterogeneity in McArdle's disease

A high resolution SDS-polyacrylamide gel electrophoresis study
DOI:https://doi.org/10.1016/0022-510X(87)90078-5
Absence of biochemical heterogeneity in McArdle's disease
Previous ArticleMotor unit firing intervals and other parameters of electrical activity in normal and pathological muscle
Next ArticleDihydropyrimidine dehydrogenase deficiency
      This paper is only available as a PDF. To read, Please Download here.

      Abstract

      Muscle biopsy extracts from a series of 6 patients with McArdle's disease were investigated by analytical SDS-polyacrylamide gel electrophoresis, to establish the presence or absence of the myophosphorylase protein subunit. In 4 cases, the band corresponding to the myophosphorylase subunit was totally absent from the electrophoretic staining pattern, and in 2 cases was present, but with a greatly reduced staining intensity compared with control normal patients; thus in none of the cases of McArdle's disease investigated was there evidence for a myophosphorylase subunit band of comparable staining intensity to that found in control normal patients. This result contrasts with previously reported findings (Feit and Brooke 1976) which suggested that McArdle's disease exists in biochemically heterogeneous forms; in one form of the disease myophosphorylase being totally absent and in a second form present to a similar extent as normal, but in an inactive form. On the basis of the results reported in this paper, we would suggest that myophosphorylase deficiency is a single gene disorder characterized by the absence or marked reduction of the myophosphorylase protein.

      Keywords

      To read this article in full you will need to make a payment

      Purchase one-time access:

      Academic & Personal: 24 hour online accessCorporate R&D Professionals: 24 hour online access
      One-time access price info
      • For academic or personal research use, select 'Academic and Personal'
      • For corporate R&D use, select 'Corporate R&D Professionals'

      Subscribe:

      Subscribe to Journal of the Neurological Sciences
      Already a print subscriber? Claim online access
      Already an online subscriber? Sign in
      Register: Create an account
      Institutional Access: Sign in to ScienceDirect

      References

        • Bank N.J.
        • DiMauro S.
        • Rowland L.P.
        • Milestone R.
        Heterozygotes in muscle phosphorylase deficiency.
        Trans. Amer. Neurol. Ass. 1973; 97: 179-182
        • Bertorini T.
        • Palmieri G.
        • Bhattacharya S.
        Beneficial effects of dantolene sodium in exercise-induced muscle pains: calcium mediated?.
        Lancet. 1982; i: 616-617
        • Brody I.A.
        • Gerber C.J.
        • Sidbury J.B.
        Relaxing factor in McArdle's disease.
        Neurology. 1970; 20: 555-558
        • Daegelen D.
        • Gautron S.
        • Mennecier F.
        • Munnich A.
        • Dreyfus J.C.
        • Kahn A.
        Molecular heterogeneity of McArdle's disease.
        in: Abstracts of Society of Inborn Errors Meeting, Liverpool, U.K.1985
        • DiMauro S.
        • Hartlage P.L.
        Fatal infantile form of muscle phosphorylase deficiency.
        Neurology. 1977; 28: 1124-1129
        • DiMauro S.
        • Rowland L.P.
        • Mellman W.J.
        Glycogen metabolism of human diploid fibroblast cells in culture, Part 1 (Studies of cells from patients with glycogenosis types II, III and V).
        Pediat. Res. 1973; 7: 739-744
        • DiMauro S.
        • Arnold S.
        • Miranda A.
        • Rowland L.P.
        McArdle disease: the mystery of reappearing phosphorylase activity in muscle culture — a fetal isoenzyme.
        Ann. Neurol. 1978; 3: 60-66
        • Dreyfus J.C.
        • Alexandre Y.
        Immunological studies of glycogen storage diseases type III and V: demonstration of the presence of an immunoreactive protein in one case of muscle phosphorylase deficiency.
        Biochem. Biophys. Res. Commun. 1971; 44: 1364-1370
        • Engel W.K.
        • Eyerman E.L.
        • Williams H.E.
        Late-onset type of skeletal muscle phosphorylase deficiency.
        N. Engl. J. Med. 1963; 268: 135-141
        • Feit H.
        • Brooke M.H.
        Myophosphorylase deficiency: two different molecular etiologies.
        Neurology. 1976; 26: 963-967
        • Godlewsky H.G.
        Are active and inactive phosphorylases histochemically distinguishable?.
        J. Histochem. Cytochem. 1963; 11: 108
        • Grunfield J.P.
        • Ganeval D.
        • Chanard J.
        • Fordecu M.
        • Dreyfus J.C.
        Acute renal failure in McArdle's disease.
        N. Engl. J. Med. 1972; 286: 1237-1241
        • Kost G.J.
        • Verity M.A.
        A new variant of late-onset myophosphorylase deficiency.
        Muscle and Nerve. 1980; 3: 195-201
        • Laemli U.K.
        Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
        Nature (Lond.). 1970; 227: 680-685
        • Lane R.J.M.
        • Turnbull D.M.
        • Hudgson P.
        • Walton J.N.
        Trials of verapamil and dantrolene sodium in McArdle's disease.
        Muscle and Nerve. 1984; 7: 592-593
        • Lowry O.H.
        • Rosebrough N.J.
        • Farr A.L.
        • Randall R.J.
        Protein measurement with the Folin phenol reagent.
        J. Biol. Chem. 1951; 193: 265-275
        • Meienhofer M.C.
        • Askanas V.
        • Proux-Daegelen D.
        • Dreyfus J.C.
        • Engel W.K.
        Muscle-type phosphorylase activity present in muscle cells cultured from three patients with myophosphorylase deficiency.
        Arch. Neurol. (Chic.). 1977; 34: 779-781
        • Oakley B.R.
        • Kirsch D.R.
        • Morris N.R.
        A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels.
        Anal. Biochem. 1980; 105: 361-363
        • Roelofs R.I.
        • Engel W.K.
        • Chauvin P.B.
        Histochemical phosphorylase activity in regenerating muscle fibres from myophosphorylase deficient patients.
        Science. 1972; 177: 795-797
        • Sato K.
        • Imai F.
        • Hatayama I.
        • Roelofs R.I.
        Characterization of glycogen phosphorylase isoenzymes present in cultured skeletal muscle from patients with McArdle's disease.
        Biochem. Biophys. Res. Commun. 1977; 78: 663-668
        • Schmid R.
        • Mahler R.
        Chronic progressive myopathy with myoglobinuria: demonstration of a glycogenolytic defect in muscle.
        J. Clin. Invest. 1959; 38: 2044
        • Walton J.
        Diffuse exercise-induced muscle pain of undetermined cause relieved by verapamil.
        Lancet. 1981; i: 993

      Article info

      Publication history

      Accepted: September 12, 1986
      Received in revised form: September 12, 1986
      Received: July 4, 1986

      Identification

      DOI: https://doi.org/10.1016/0022-510X(87)90078-5

      Copyright

      © 1987 Published by Elsevier Inc.

      ScienceDirect

      Access this article on ScienceDirect
      We use cookies to help provide and enhance our service and tailor content. To update your cookie settings, please visit the for this site.
      Copyright © 2023 Elsevier Inc. except certain content provided by third parties. The content on this site is intended for healthcare professionals.


      RELX