Developmental myosin heavy chain progression in avian type IIB muscle fibres

1991 ◽  
Vol 12 (3) ◽  
pp. 281-291 ◽  
Author(s):  
Julie Ivory Rushbrook ◽  
Cipora Weiss ◽  
Tsai-Tse Yao
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Fibres ◽  
Developmental Myosin Heavy Chain

scholarly journals Myosin heavy-chain composition in striated muscle after tenotomy

1992 ◽  
Vol 282 (1) ◽  
pp. 237-242 ◽  
Author(s):  
A Jakubiec-Puka ◽  
C Catani ◽  
U Carraro
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Striated Muscle ◽  
Slow Muscle ◽  
Fast Muscle ◽  
Muscle Fibres ◽  
Adult Rats ◽  
Tendon Regeneration ◽  
Adult Muscle ◽  
Gastrocnemius Muscles

The myosin heavy-chain (MHC) isoform pattern was studied by biochemical methods in the slow-twitch (soleus) and fast-twitch (gastrocnemius) muscles of adult rats during atrophy after tenotomy and recovery after tendon regeneration. The tenotomized slow muscle atrophied more than the tenotomized fast muscle. During the 12 days after tenotomy the total MHC content decreased by about 85% in the slow muscle, and only by about 35% in the fast muscle. In the slow muscle the ratio of MHC-1 to MHC-2A(2S) remained almost unchanged, showing that similar diminution of both isoforms occurs. In the fast muscle the MHC-2A/MHC-2B ratio decreased, showing the loss of MHC-2A mainly. After tendon regeneration, the slow muscle recovered earlier than the fast muscle. Full recovery of the muscles was not observed until up to 4 months later. The embryonic MHC, which seems to be expressed in denervated adult muscle fibres, was not detected by immunoblotting in the tenotomized muscles during either atrophy or recovery after tendon regeneration. The influence of tenotomy and denervation on expression of the MHC isoforms is compared. The results show that: (a) MHC-1 and MHC-2A(2S) are very sensitive to tenotomy, whereas MHC-2B is much less sensitive; (b) expression of the embryonic MHC in adult muscle seems to be inhibited by the intact neuromuscular junction.

Three myosin heavy chain isoforms in type 2 skeletal muscle fibres

1989 ◽  
Vol 10 (3) ◽  
pp. 197-205 ◽  
Author(s):  
Stefano Schiaffino ◽  
Luisa Gorza ◽  
Saverio Sartore ◽  
Leopoldo Saggin ◽  
Simonetta Ausoni ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Muscle Fibres ◽  
Skeletal Muscle Fibres

scholarly journals Small-diameter white myotomal muscle fibres associated with growth hyperplasia in the carp (Cyprinus carpio) express a distinct myosin heavy chain gene.

1995 ◽  
Vol 198 (7) ◽  
pp. 1603-1611 ◽  
Author(s):  
S Ennion ◽  
L Gauvry ◽  
P Butterworth ◽  
G Goldspink
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
White Muscle ◽  
In Situ Hybridisation ◽  
Small Diameter ◽  
Chain Gene ◽  
Muscle Fibres ◽  
Heavy Chain Gene ◽  
Myosin Heavy Chain Gene ◽  
Myosin Heavy Chain Genes

A carp myosin heavy chain gene isoform was isolated from a genomic clone, restriction mapped and partially sequenced to reveal the location of various exons. The clone contains a complete gene of approximately 12.0 kb which is half the size of the corresponding mammalian and avian myosin heavy chain genes. The mRNA transcript of this gene, however, is the same size as mammalian and avian striated muscle myosin heavy chain genes (about 6000 nucleotides), illustrating that the difference in size at the genomic level is due to shorter introns. A 169 bp NsiI restriction fragment containing only the 3' untranslated region of this gene was subcloned and used as an isoform-specific probe to study the expression of this particular isoform. Hybridisation analysis could only detect expression of this myosin heavy chain gene in the white muscle of adult carp that had been subjected to an increased environmental temperature. No expression of this gene was detected in carp under 1 year of age. In situ hybridisation demonstrated that expression of this gene is limited to small-diameter white muscle fibres of adult carp, which are thought to be responsible for muscle growth by fibre hyperplasia.

Two functionally distinct myosin heavy chain isoforms in slow skeletal muscle fibres

FEBS Letters ◽  
1997 ◽  
Vol 410 (2-3) ◽  
pp. 150-152 ◽  
Author(s):  
Stefan Galler ◽  
Karlheinz Hilber ◽  
Bärbel Gohlsch ◽  
Dirk Pette
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Muscle Fibres ◽  
Slow Skeletal Muscle ◽  
Skeletal Muscle Fibres

scholarly journals Abundant expression of myosin heavy-chain IIB RNA in a subset of human masseter muscle fibres

2001 ◽  
Vol 46 (11) ◽  
pp. 1039-1050 ◽  
Author(s):  
Michael J Horton ◽  
Carla A Brandon ◽  
Terence J Morris ◽  
Thomas W Braun ◽  
Kenneth M Yaw ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Masseter Muscle ◽  
Muscle Fibres
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