Differential expression of myosin heavy chain isoforms between abductor and adductor muscles in the human larynx

Zhao Bo Li, Mohamed Lehar, Hideki Nakagawa, Joseph Foon Yoong Hoh, Paul Flint

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

OBJECTIVE. This study examines the differential expression of myosin heavy chain (MyHC) components in human laryngeal muscle groups. STUDY DESIGN: A battery of monospecific monoclonal antibodies in Western blots was used to determine expression of IIX, extraocular-specific (EOM), and IIB MyHCs for the thyroarytenoid (TA), vocalis (VOC), lateral cricoarytenoid (LCA), cricothyroid (CT), and posterior cricoarytenoid (PCA) muscles obtained from fresh cadaver specimens. RESULTS: Fast IIX MyHC was only expressed in the TA, VOC, and LCA muscles. Fast IIA and slow MyHCs were expressed in all laryngeal muscles including the CT and PCA. The CT with mixed phonatory and respiratory function and the PCA with respiratory function did not express IIX MyHC. The 2 MyHC isoforms associated with the highest speeds of contraction in rat laryngeal muscle, namely, the EOM MyHC and IIB MyHC, were not detected in human laryngeal muscles. Novel MyHC bands were not detected in SDS-PAGE gels or Western blots using a broad specificity MyHC antibody. CONCLUSION: The profile of MyHC expression in human laryngeal muscles differs from that observed in human extraocular and masticator muscles, and other mammalian species. Our data demonstrate that IIX MyHC expression is associated primarily with muscles affecting glottic closure and is absent in CT and PCA. SIGNIFICANCE: A higher percentage of lIX MyHC is expected to impart a high speed of shortening to the TA and LCA muscles. The absence of IIX MyHC in muscles with respiratory (PCA) and mixed respiratory/phonatory function (CT) further supports the inference that the physiologic difference between laryngeal muscles is reflected in the molecular composition of contractile protein.

Original languageEnglish (US)
Pages (from-to)217-222
Number of pages6
JournalOtolaryngology - Head and Neck Surgery
Volume130
Issue number2
DOIs
StatePublished - Feb 2004
Externally publishedYes

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Myosin Heavy Chains
Larynx
Laryngeal Muscles
Protein Isoforms
Muscles
Oculomotor Muscles
Nonmuscle Myosin Type IIB
Western Blotting
Contractile Proteins
Respiratory Muscles
Cadaver
Tongue
Polyacrylamide Gel Electrophoresis
Gels
Monoclonal Antibodies

ASJC Scopus subject areas

  • Otorhinolaryngology

Cite this

Differential expression of myosin heavy chain isoforms between abductor and adductor muscles in the human larynx. / Li, Zhao Bo; Lehar, Mohamed; Nakagawa, Hideki; Hoh, Joseph Foon Yoong; Flint, Paul.

In: Otolaryngology - Head and Neck Surgery, Vol. 130, No. 2, 02.2004, p. 217-222.

Research output: Contribution to journalArticle

Li, Zhao Bo ; Lehar, Mohamed ; Nakagawa, Hideki ; Hoh, Joseph Foon Yoong ; Flint, Paul. / Differential expression of myosin heavy chain isoforms between abductor and adductor muscles in the human larynx. In: Otolaryngology - Head and Neck Surgery. 2004 ; Vol. 130, No. 2. pp. 217-222.
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abstract = "OBJECTIVE. This study examines the differential expression of myosin heavy chain (MyHC) components in human laryngeal muscle groups. STUDY DESIGN: A battery of monospecific monoclonal antibodies in Western blots was used to determine expression of IIX, extraocular-specific (EOM), and IIB MyHCs for the thyroarytenoid (TA), vocalis (VOC), lateral cricoarytenoid (LCA), cricothyroid (CT), and posterior cricoarytenoid (PCA) muscles obtained from fresh cadaver specimens. RESULTS: Fast IIX MyHC was only expressed in the TA, VOC, and LCA muscles. Fast IIA and slow MyHCs were expressed in all laryngeal muscles including the CT and PCA. The CT with mixed phonatory and respiratory function and the PCA with respiratory function did not express IIX MyHC. The 2 MyHC isoforms associated with the highest speeds of contraction in rat laryngeal muscle, namely, the EOM MyHC and IIB MyHC, were not detected in human laryngeal muscles. Novel MyHC bands were not detected in SDS-PAGE gels or Western blots using a broad specificity MyHC antibody. CONCLUSION: The profile of MyHC expression in human laryngeal muscles differs from that observed in human extraocular and masticator muscles, and other mammalian species. Our data demonstrate that IIX MyHC expression is associated primarily with muscles affecting glottic closure and is absent in CT and PCA. SIGNIFICANCE: A higher percentage of lIX MyHC is expected to impart a high speed of shortening to the TA and LCA muscles. The absence of IIX MyHC in muscles with respiratory (PCA) and mixed respiratory/phonatory function (CT) further supports the inference that the physiologic difference between laryngeal muscles is reflected in the molecular composition of contractile protein.",
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N2 - OBJECTIVE. This study examines the differential expression of myosin heavy chain (MyHC) components in human laryngeal muscle groups. STUDY DESIGN: A battery of monospecific monoclonal antibodies in Western blots was used to determine expression of IIX, extraocular-specific (EOM), and IIB MyHCs for the thyroarytenoid (TA), vocalis (VOC), lateral cricoarytenoid (LCA), cricothyroid (CT), and posterior cricoarytenoid (PCA) muscles obtained from fresh cadaver specimens. RESULTS: Fast IIX MyHC was only expressed in the TA, VOC, and LCA muscles. Fast IIA and slow MyHCs were expressed in all laryngeal muscles including the CT and PCA. The CT with mixed phonatory and respiratory function and the PCA with respiratory function did not express IIX MyHC. The 2 MyHC isoforms associated with the highest speeds of contraction in rat laryngeal muscle, namely, the EOM MyHC and IIB MyHC, were not detected in human laryngeal muscles. Novel MyHC bands were not detected in SDS-PAGE gels or Western blots using a broad specificity MyHC antibody. CONCLUSION: The profile of MyHC expression in human laryngeal muscles differs from that observed in human extraocular and masticator muscles, and other mammalian species. Our data demonstrate that IIX MyHC expression is associated primarily with muscles affecting glottic closure and is absent in CT and PCA. SIGNIFICANCE: A higher percentage of lIX MyHC is expected to impart a high speed of shortening to the TA and LCA muscles. The absence of IIX MyHC in muscles with respiratory (PCA) and mixed respiratory/phonatory function (CT) further supports the inference that the physiologic difference between laryngeal muscles is reflected in the molecular composition of contractile protein.

AB - OBJECTIVE. This study examines the differential expression of myosin heavy chain (MyHC) components in human laryngeal muscle groups. STUDY DESIGN: A battery of monospecific monoclonal antibodies in Western blots was used to determine expression of IIX, extraocular-specific (EOM), and IIB MyHCs for the thyroarytenoid (TA), vocalis (VOC), lateral cricoarytenoid (LCA), cricothyroid (CT), and posterior cricoarytenoid (PCA) muscles obtained from fresh cadaver specimens. RESULTS: Fast IIX MyHC was only expressed in the TA, VOC, and LCA muscles. Fast IIA and slow MyHCs were expressed in all laryngeal muscles including the CT and PCA. The CT with mixed phonatory and respiratory function and the PCA with respiratory function did not express IIX MyHC. The 2 MyHC isoforms associated with the highest speeds of contraction in rat laryngeal muscle, namely, the EOM MyHC and IIB MyHC, were not detected in human laryngeal muscles. Novel MyHC bands were not detected in SDS-PAGE gels or Western blots using a broad specificity MyHC antibody. CONCLUSION: The profile of MyHC expression in human laryngeal muscles differs from that observed in human extraocular and masticator muscles, and other mammalian species. Our data demonstrate that IIX MyHC expression is associated primarily with muscles affecting glottic closure and is absent in CT and PCA. SIGNIFICANCE: A higher percentage of lIX MyHC is expected to impart a high speed of shortening to the TA and LCA muscles. The absence of IIX MyHC in muscles with respiratory (PCA) and mixed respiratory/phonatory function (CT) further supports the inference that the physiologic difference between laryngeal muscles is reflected in the molecular composition of contractile protein.

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