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Teplov, A.Y., Grishin, S.N., Mukhamedyarov, M.A., Ziganshin, A.U., Zefirov, A.L. and Palotas, A. (2009) Ovalbumin-induced sensitization affects non-quantal acetylcholine release from motor nerve terminals and alters contractility of skeletal muscles in mice. Experimental Physiology, 94, 264-268.
http://dx.doi.org/10.1113/expphysiol.2008.045740

has been cited by the following article:

• TITLE: Mechanisms of change contraction of function of the muscles in vitro at allergic

  AUTHORS: Alexander Y. Teplov, Albert M. Farkhutdinov, Vladimir I. Torshin

  KEYWORDS: Skeletal Muscle; Contraction Characteristics; Extensor Digitorum Longus; Soleus; Diaphragm; Non-Quantum Secretion; Protein Sensitization

  JOURNAL NAME: Health, Vol.6 No.5, February 24, 2014

  ABSTRACT: In this work, mechanisms of influence of protein sensibility of an organism on contractile function of the isolated skeletal muscles of the mouse—“fast”—musculus extensor digitorum longus, “mixed”—musculus diaphragma and “slow”— musculus soleus are investigated. It is shown that at a protein sensitization all “fast”, “mixed” and “slow” skeletal muscles change the contractile properties. The vector of these changes for muscles with a various phenotypes carries opposite character. Force of the reduction caused carbacholine at a “slow” and “mixed” muscles increase, at “fast”—decreases. A vector of change of force of reduction on carbacholine at protein sensitization at these skeletal muscles correlates with changes of non-quantum secretion acetylcholine in a zone of a trailer plate. Opposite changes of functional properties of “fast” and “mixed” muscles and “slow” muscles of a shin of the mouse at protein sensitization are caused by dynamics cholinoceptive processes of excitation of membrane muscular fibers. It comes out with the assumption, that change of the contraction functions of skeletal muscles at protein sensitization is caused by changes of cholinoceptive processes of excitation of a membrane of muscular fibers, and other changes in system of electro-mechanical interface.