Myosin heavy chain composition of the human sternocleidomastoid muscle

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F12%3A00386556" target="_blank" >RIV/67985823:_____/12:00386556 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.aanat.2012.05.001" target="_blank" >http://dx.doi.org/10.1016/j.aanat.2012.05.001</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.aanat.2012.05.001" target="_blank" >10.1016/j.aanat.2012.05.001</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Myosin heavy chain composition of the human sternocleidomastoid muscle

Popis výsledku v původním jazyce

The sternocleidomastoid (SCM) muscle is one of the neck muscles responsible for head posture and control of head movement. It functions in rotation, inclination, rotraction, extension and flexion of the head, whilst chewing and in exerting ncreased respiratory efforts. This study is the first one describing the myosin heavy chain (MyHC) isoform composition of the SCM muscle of presumably healthy young males for the purpose of better understanding the contractile properties of the muscle as well as to help in evaluation of pathologically altered structure of the muscle. Autopsy samples were processed immunohistochemically to reveal the MyHC isoform composition. The muscle fibres expressed MyHC-1 (31.5%), -2a (29.7%) and -2x (4.3%) or co-expressed MyHC-2a with MyHC-2x (26.8%), MyHC-1 with MyHC-2a (4.1%) and/or MyHC-1, -2a with -2x (1.1%). In addition to the MyHC isoforms, characteristic of adult limb muscles, a very low percentage of muscle fibres (0.2?2.7%) expressed MyHC-neo, which is

Název v anglickém jazyce

Myosin heavy chain composition of the human sternocleidomastoid muscle

Popis výsledku anglicky

The sternocleidomastoid (SCM) muscle is one of the neck muscles responsible for head posture and control of head movement. It functions in rotation, inclination, rotraction, extension and flexion of the head, whilst chewing and in exerting ncreased respiratory efforts. This study is the first one describing the myosin heavy chain (MyHC) isoform composition of the SCM muscle of presumably healthy young males for the purpose of better understanding the contractile properties of the muscle as well as to help in evaluation of pathologically altered structure of the muscle. Autopsy samples were processed immunohistochemically to reveal the MyHC isoform composition. The muscle fibres expressed MyHC-1 (31.5%), -2a (29.7%) and -2x (4.3%) or co-expressed MyHC-2a with MyHC-2x (26.8%), MyHC-1 with MyHC-2a (4.1%) and/or MyHC-1, -2a with -2x (1.1%). In addition to the MyHC isoforms, characteristic of adult limb muscles, a very low percentage of muscle fibres (0.2?2.7%) expressed MyHC-neo, which is

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

FH - Neurologie, neurochirurgie, neurovědy

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2012

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Annals of Anatomy-Anatomischer Anzeiger

ISSN

0940-9602

e-ISSN

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Svazek periodika

194

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

6

Strana od-do

467-472

Kód UT WoS článku

000310099300010

EID výsledku v databázi Scopus

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