Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2000-3-13
pubmed:abstractText
Since the intrinsic laryngeal muscles in humans are involved in specialized functions, one may suppose that this would be associated with the expression of specific myosin heavy chain (MHC) isoforms, as has been reported for the rat, dog, and rabbit. In order to determine which MHCs are expressed in the human laryngeal muscles, biochemical analysis using sodium dodecyl sulfate-polyacrylamide gel electrophoresis was performed. Thyroarytenoid and posterior cricoarytenoid muscles were obtained from a 7-month-old infant and 4 adults. In the adult human laryngeal muscles, 3 bands were resolved identical to those previously described in the human limb muscles (I, IIA, and IIB MHCs). In contrast, muscles from the infant also expressed fetal MHC and a novel MHC not observed in other human skeletal muscles. This novel band migrated at the same level as the laryngeal MHC previously described in the rat. Since these 2 isoforms disappear in the adult, the persistence in the infant could be correlated with the immature development of laryngeal functions and, in particular, phonation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0003-4894
pubmed:author
pubmed:issnType
Print
pubmed:volume
109
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
216-20
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Myosin heavy chain expression in human laryngeal muscle fibers. A biochemical study.
pubmed:affiliation
Service d'Oto-Rhino-Laryngologie et Chirurgie de la Face et du Cou, Faculté de Médecine Saint Antoine, Université Paris VI, Hôpital Tenon, Paris, France.
pubmed:publicationType
Journal Article, Comparative Study