Literature DB >> 9450834

A new concept in laryngeal muscle: multiple myosin isoform types in single muscle fibers of the lateral cricoarytenoid.

Y Z Wu1, M J Baker, R L Crumley, R H Blanks, V J Caiozzo.   

Abstract

This report describes the first known investigation of canine laryngeal muscle in which single fibers were dissected and their myosin heavy chain (MHC) isoform content was analyzed. Both SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and western blot techniques were used. The data from single fiber SDS-PAGE indicate that the lateral cricoarytenoid (LCA) is predominantly a fast muscle composed of the following MHC isoforms: Type I, 16.3%; Type IIA, 71.3%; Type IIX, 10.4%; and Type IIB, 2.0%. The results reveal a phenomenon that, to our knowledge, has not been previously described for laryngeal muscle: the presence of two or more MHC isoforms in a single canine LCA muscle fiber. A large number (41%) of muscle fibers coexpressed two or more MHC isoforms. The three most common patterns of coexpression were Type IIA/IIX (72%), Type IIA/I (16%), and Type IIA/IIX/I (8%). Interestingly, the fast Type IIX MHC isoform was typically present with other isoforms and rarely found by itself in individual fibers. Additional experiments are underway to determine whether other laryngeal muscles exhibit such an unusually high ratio of MHC isoform polymorphism.

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Year:  1998        PMID: 9450834     DOI: 10.1016/S0194-5998(98)70380-8

Source DB:  PubMed          Journal:  Otolaryngol Head Neck Surg        ISSN: 0194-5998            Impact factor:   3.497


  8 in total

1.  Myosin heavy chain isoform transitions in canine skeletal muscles during postnatal growth.

Authors:  Malan Strbenc; Vika Smerdu; Azra Pogacnik; Gregor Fazarinc
Journal:  J Anat       Date:  2006-08       Impact factor: 2.610

2.  Dynamics of Intrinsic Laryngeal Muscle Contraction.

Authors:  Andrew M Vahabzadeh-Hagh; Pranati Pillutla; Zhaoyan Zhang; Dinesh K Chhetri
Journal:  Laryngoscope       Date:  2018-10-16       Impact factor: 3.325

Review 3.  Fundamental approaches in molecular biology for communication sciences and disorders.

Authors:  Rebecca S Bartlett; Marie E Jetté; Suzanne N King; Allison Schaser; Susan L Thibeault
Journal:  J Speech Lang Hear Res       Date:  2012-01-09       Impact factor: 2.297

4.  Unloaded shortening velocity and myosin heavy chain variations in human laryngeal muscle fibers.

Authors:  James J Sciote; Terence J Morris; Carla A Brandon; Michael J Horton; Clark Rosen
Journal:  Ann Otol Rhinol Laryngol       Date:  2002-02       Impact factor: 1.547

5.  A continuum of myofibers in adult rabbit extraocular muscle: force, shortening velocity, and patterns of myosin heavy chain colocalization.

Authors:  Linda K McLoon; Han Na Park; Jong-Hee Kim; Fatima Pedrosa-Domellöf; Ladora V Thompson
Journal:  J Appl Physiol (1985)       Date:  2011-07-21

6.  Active and passive properties of canine abduction/adduction laryngeal muscles.

Authors:  Fariborz Alipour; Ingo R Titze; Eric Hunter; Niro Tayama
Journal:  J Voice       Date:  2005-09       Impact factor: 2.009

7.  Immunohistochemical analysis of myosin heavy chain expression in laryngeal muscles of the rabbit, cat, and baboon.

Authors:  Hannah S Rhee; Joseph F Y Hoh
Journal:  J Histochem Cytochem       Date:  2008-07-07       Impact factor: 2.479

8.  Contractile properties and myosin heavy chain isoform composition in single fibre of human laryngeal muscles.

Authors:  Giuseppe D'Antona; Aram Megighian; Susan Bortolotto; Maria Antonietta Pellegrino; Rosario Marchese-Ragona; Alberto Staffieri; Roberto Bottinelli; Carlo Reggiani
Journal:  J Muscle Res Cell Motil       Date:  2002       Impact factor: 2.698

  8 in total

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