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Serum Protein Electrophoretic Pattern in Experimental Myasthenia Gravis

Received: 19 September 2018     Accepted: 29 September 2018     Published: 30 October 2018
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Abstract

Myasthenia gravis (MG) is an antibody-mediated autoimmune neuromuscular disease, leading to skeletal muscle weakness. The autoantibodies are against acetylcholine receptor (AChR) of the muscle membrane localized at the neuromuscular junction. The early diagnosis of MG is a key factorfor the advanced medical practice, but, it still remains challenging. The objective of this pilot study was to examine the pattern of serum protein electrophoresis in the animal experimental model of MG. Acetylcholine receptor (AChR) was purified from rat (mail Wistar) leg muscle by affinity chromatography. Four rabbits were immunized on day 1, week 4 and week 8 with purified rat leg muscle AChR and assayed for serum anti-AChR antibody titer on blood samples taken on week 2, week 5 and week 9. Control rabbits received an emulsion of phosphate bufferded saline in the adjuant. The serum anti-AChR anybodies were tittered using quenching fluoroimmunoassay. Electrophoresis separation of the serum proteins was performed on a cellulose acetate membrane. Results showed that Immunizations of rabbits induced muscle weakness in the animals together with elevation of serum anti-AChR antibody. During the course of immunizations, percentage of beta-globulin fraction increased gradually from 15.8% to 41.2% whereas, albumin decreased from 68.3% to 43.8%. As determined by cellulose acetate electrophoresis. These results represent proof-of principle data for diagnosis of the acetylcholine receptor-MG subtypes and severity.

Published in American Journal of Chemical and Biochemical Engineering (Volume 2, Issue 2)
DOI 10.11648/j.ajcbe.20180202.11
Page(s) 22-26
Creative Commons

This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2018. Published by Science Publishing Group

Keywords

Acetylcholine, Autoimmune Disease, Electrophoresis, Fluoroimmunoassay, Myasthenia Gravis

References
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[10] Chiou-Tan FY, Gilchrist JM. (2015). Repetitive nerve stimulation and single-fiber electromyography in the evaluation of patients with suspected myasthenia gravis or Lambert-Eaton myasthenic syndrome: Review of recent literature, Muscle Nerve. 52(3):455-62.
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[19] Messripour M, Moein S. (1997) Indirect quenching fluororeceptor assay of anti-AChR antibodies. Mol. Chem. Neuropathol. 31: 43-51.
[20] Losen M, Martinez-Martinez P, Molenaar PC, et al.(2015) Standardization of the experimental autoimmune myasthenia gravis (EAMG) model by immunization of rats with Torpedo californica acetylcholine receptors — Recommendations for methods and experimental designs. Exp. neur. 270:18-28.
[21] Chopra B, Abraham R, Abraham A, (2002). Beta-1 Globulin-a potential marker in differentiating multiple sclerosis and acute disseminated encephalomyelitis: a preliminary study, Neurol India. 50(1):41-144
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Cite This Article
  • APA Style

    Manoochehr Messripour, Soheila Moein. (2018). Serum Protein Electrophoretic Pattern in Experimental Myasthenia Gravis. American Journal of Chemical and Biochemical Engineering, 2(2), 22-26. https://doi.org/10.11648/j.ajcbe.20180202.11

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    ACS Style

    Manoochehr Messripour; Soheila Moein. Serum Protein Electrophoretic Pattern in Experimental Myasthenia Gravis. Am. J. Chem. Biochem. Eng. 2018, 2(2), 22-26. doi: 10.11648/j.ajcbe.20180202.11

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    AMA Style

    Manoochehr Messripour, Soheila Moein. Serum Protein Electrophoretic Pattern in Experimental Myasthenia Gravis. Am J Chem Biochem Eng. 2018;2(2):22-26. doi: 10.11648/j.ajcbe.20180202.11

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  • @article{10.11648/j.ajcbe.20180202.11,
      author = {Manoochehr Messripour and Soheila Moein},
      title = {Serum Protein Electrophoretic Pattern in Experimental Myasthenia Gravis},
      journal = {American Journal of Chemical and Biochemical Engineering},
      volume = {2},
      number = {2},
      pages = {22-26},
      doi = {10.11648/j.ajcbe.20180202.11},
      url = {https://doi.org/10.11648/j.ajcbe.20180202.11},
      eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajcbe.20180202.11},
      abstract = {Myasthenia gravis (MG) is an antibody-mediated autoimmune neuromuscular disease, leading to skeletal muscle weakness. The autoantibodies are against acetylcholine receptor (AChR) of the muscle membrane localized at the neuromuscular junction. The early diagnosis of MG is a key factorfor the advanced medical practice, but, it still remains challenging. The objective of this pilot study was to examine the pattern of serum protein electrophoresis in the animal experimental model of MG. Acetylcholine receptor (AChR) was purified from rat (mail Wistar) leg muscle by affinity chromatography. Four rabbits were immunized on day 1, week 4 and week 8 with purified rat leg muscle AChR and assayed for serum anti-AChR antibody titer on blood samples taken on week 2, week 5 and week 9. Control rabbits received an emulsion of phosphate bufferded saline in the adjuant. The serum anti-AChR anybodies were tittered using quenching fluoroimmunoassay. Electrophoresis separation of the serum proteins was performed on a cellulose acetate membrane. Results showed that Immunizations of rabbits induced muscle weakness in the animals together with elevation of serum anti-AChR antibody. During the course of immunizations, percentage of beta-globulin fraction increased gradually from 15.8% to 41.2% whereas, albumin decreased from 68.3% to 43.8%. As determined by cellulose acetate electrophoresis. These results represent proof-of principle data for diagnosis of the acetylcholine receptor-MG subtypes and severity.},
     year = {2018}
    }
    

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  • TY  - JOUR
    T1  - Serum Protein Electrophoretic Pattern in Experimental Myasthenia Gravis
    AU  - Manoochehr Messripour
    AU  - Soheila Moein
    Y1  - 2018/10/30
    PY  - 2018
    N1  - https://doi.org/10.11648/j.ajcbe.20180202.11
    DO  - 10.11648/j.ajcbe.20180202.11
    T2  - American Journal of Chemical and Biochemical Engineering
    JF  - American Journal of Chemical and Biochemical Engineering
    JO  - American Journal of Chemical and Biochemical Engineering
    SP  - 22
    EP  - 26
    PB  - Science Publishing Group
    SN  - 2639-9989
    UR  - https://doi.org/10.11648/j.ajcbe.20180202.11
    AB  - Myasthenia gravis (MG) is an antibody-mediated autoimmune neuromuscular disease, leading to skeletal muscle weakness. The autoantibodies are against acetylcholine receptor (AChR) of the muscle membrane localized at the neuromuscular junction. The early diagnosis of MG is a key factorfor the advanced medical practice, but, it still remains challenging. The objective of this pilot study was to examine the pattern of serum protein electrophoresis in the animal experimental model of MG. Acetylcholine receptor (AChR) was purified from rat (mail Wistar) leg muscle by affinity chromatography. Four rabbits were immunized on day 1, week 4 and week 8 with purified rat leg muscle AChR and assayed for serum anti-AChR antibody titer on blood samples taken on week 2, week 5 and week 9. Control rabbits received an emulsion of phosphate bufferded saline in the adjuant. The serum anti-AChR anybodies were tittered using quenching fluoroimmunoassay. Electrophoresis separation of the serum proteins was performed on a cellulose acetate membrane. Results showed that Immunizations of rabbits induced muscle weakness in the animals together with elevation of serum anti-AChR antibody. During the course of immunizations, percentage of beta-globulin fraction increased gradually from 15.8% to 41.2% whereas, albumin decreased from 68.3% to 43.8%. As determined by cellulose acetate electrophoresis. These results represent proof-of principle data for diagnosis of the acetylcholine receptor-MG subtypes and severity.
    VL  - 2
    IS  - 2
    ER  - 

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Author Information
  • Department of Medical Biochemistry, Isfahan University of Medical Sciences, Isfahan, Iran

  • Department of Biochemistry and Histology, Bandar-Abbass College of Medicine, Bandar-Abbass, Iran

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