Literature DB >> 2140978

Transition of myosin isozymes during development of human masseter muscle. Persistence of developmental isoforms during postnatal stage.

N Soussi-Yanicostas1, J P Barbet, C Laurent-Winter, P Barton, G S Butler-Browne.   

Abstract

Previous results have shown that the adult human masseter muscle contains myosin isoforms that are specific to early stages of development in trunk and limb muscles, i.e. embryonic and fetal (neonatal) myosin heavy chains (MHC) and embryonic myosin light chain (MLC1emb). We wanted to know if this specific pattern is the result of a late maturation or of a distinct evolution during development. We show here that the embryonic and the fetal MHC and the MLC1emb are expressed throughout perinatal and postnatal masseter development. Our results also demonstrate that MLC1emb accumulation increases considerably during the postnatal period. In addition, both the slow MLCs and the slow isoform of tropomyosin are expressed later in the masseter than quadriceps and the fast skeletal muscle isoform MLC3 is not detected during fetal and early postnatal development in the masseter whereas it is expressed throughout fetal development in the quadriceps. Our results thus confirm previous histochemical data and demonstrate that the masseter muscle displays a pattern of myosin and tropomyosin isoform transitions different to that previously described in trunk and limb muscles. This suggests that control of masseter muscle development involves mechanisms distinct from other body muscles, possibly as a result of either its craniofacial innervation or of a possibly different embryonic origin.

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Year:  1990        PMID: 2140978     DOI: 10.1242/dev.108.2.239

Source DB:  PubMed          Journal:  Development        ISSN: 0950-1991            Impact factor:   6.868


  15 in total

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2.  The human embryonic myosin alkali light chain gene: use of alternative promoters and 3' non-coding regions.

Authors:  M Rotter; K Zimmerman; A Poustka; N Soussi-Yanicostas; A Starzinski-Powitz
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3.  Remarkable heterogeneity in myosin heavy-chain composition of the human young masseter compared with young biceps brachii.

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4.  Opposite changes in myosin heavy chain composition of human masseter and biceps brachii muscles during aging.

Authors:  M Monemi; P O Eriksson; F Kadi; G S Butler-Browne; L E Thornell
Journal:  J Muscle Res Cell Motil       Date:  1999-05       Impact factor: 2.698

Review 5.  Developmental and functional considerations of masseter muscle partitioning.

Authors:  C G Widmer; A W English; J Morris-Wiman
Journal:  Arch Oral Biol       Date:  2006-11-15       Impact factor: 2.633

6.  Comparison of the foetal development of fibre types in four bovine muscles.

Authors:  B Picard; J Robelin; F Pons; Y Geay
Journal:  J Muscle Res Cell Motil       Date:  1994-08       Impact factor: 2.698

7.  Myosin heavy chain expression in rabbit masseter muscle during postnatal development.

Authors:  J J Bredman; W A Weijs; H A Korfage; P Brugman; A F Moorman
Journal:  J Anat       Date:  1992-04       Impact factor: 2.610

8.  Quantification of myosin heavy chain RNA in human laryngeal muscles: differential expression in the vertical and horizontal posterior cricoarytenoid and thyroarytenoid.

Authors:  Michael J Horton; Clark Rosen; John M Close; James J Sciote
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9.  Fibre type classification and myosin isoforms in the human masseter muscle.

Authors:  J J Sciote; A M Rowlerson; C Hopper; N P Hunt
Journal:  J Neurol Sci       Date:  1994-10       Impact factor: 3.181

10.  Presence of embryonic myosin in normal postural muscles of the adult rat.

Authors:  L J Wanek; M H Snow
Journal:  Cell Tissue Res       Date:  1995-06       Impact factor: 5.249

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