scholarly journals Myosin heavy chain composition of single fibres from normal human muscle

1988 ◽  
Vol 250 (1) ◽  
pp. 307-308 ◽  
Author(s):  
D Biral ◽  
R Betto ◽  
D Danieli-Betto ◽  
G Salviati
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Polyclonal Antibodies ◽  
Large Population ◽  
Electrophoretic Analysis ◽  
Human Muscle ◽  
Muscle Fibres ◽  
Normal Human ◽  
Single Fibres

Electrophoretic analysis in the presence of 33% glycerol of purified myosin from normal human muscle shows three distinct protein bands which are identified as type 1, 2B, and 2A myosin heavy chain (MHC) isoforms by affinity-purified polyclonal antibodies. Analysis of MHC of single human muscle fibres shows that human muscles contain a large population of fibres showing the coexistence of type 2A and 2B MHC.

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
Sign in / Sign up

Export Citation Format

Share Document