Inhibition of myosin ATPase activity by human myasthenia gravis antibodies reactive with the acetylcholine receptor

Sumathy Mohan, Keith A Krolick

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Antibodies, obtained from myasthenia gravis patients, with reactivity for an immunodominant region of the nieotinic acetylcholine receptor were found to also react with muscle myosin. Since amino acid sequence analyses have previously suggested possible serological relationships between AChR and a head region sequence of myosin heavy chain, cross-reactive antibodies were examined for their ability to interfere with ATPase activities associated with this region of myosin. Results indicated that AChR-specific antibodies purified from MG patient serum by binding to and elution from antigen columns were found to inhibit Ca2+-dependent, myosin-associated ATPase activity; interestingly, this inhibition appeared to be relatively selective in that neither K+(EDTA)-dependent nor Mg2+-dependent ATPase activities were sensitive to antibody-mediated interference.

Original languageEnglish (US)
Pages (from-to)50-52
Number of pages3
JournalFEBS Letters
Volume318
Issue number1
DOIs
StatePublished - Feb 22 1993

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Myasthenia Gravis
Cholinergic Receptors
Myosins
Human Activities
Antibodies
Adenosine Triphosphatases
Ca(2+) Mg(2+)-ATPase
Immunodominant Epitopes
Myosin Heavy Chains
Protein Sequence Analysis
Edetic Acid
Muscle
Head
Antigens
Amino Acids
Muscles
Serum

Keywords

  • Acetylcholine receptor antibody
  • Acetylcholine receptor/myosin cross-reactivity
  • ATPase inhibition
  • Main immunogenic region
  • Myosin ATPase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Inhibition of myosin ATPase activity by human myasthenia gravis antibodies reactive with the acetylcholine receptor. / Mohan, Sumathy; Krolick, Keith A.

In: FEBS Letters, Vol. 318, No. 1, 22.02.1993, p. 50-52.

Research output: Contribution to journalArticle

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AB - Antibodies, obtained from myasthenia gravis patients, with reactivity for an immunodominant region of the nieotinic acetylcholine receptor were found to also react with muscle myosin. Since amino acid sequence analyses have previously suggested possible serological relationships between AChR and a head region sequence of myosin heavy chain, cross-reactive antibodies were examined for their ability to interfere with ATPase activities associated with this region of myosin. Results indicated that AChR-specific antibodies purified from MG patient serum by binding to and elution from antigen columns were found to inhibit Ca2+-dependent, myosin-associated ATPase activity; interestingly, this inhibition appeared to be relatively selective in that neither K+(EDTA)-dependent nor Mg2+-dependent ATPase activities were sensitive to antibody-mediated interference.

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