Functional Differences of Myosin Heavy-Chain Isoforms in Skeletal Muscle

1997 ◽  
Vol 84 (5) ◽  
pp. 201-204 ◽  
Author(s):  
Karlheinz Hilber ◽  
Stefan Galler ◽  
Dirk Pette
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Functional Differences

The effect of glucocorticoids on the myosin heavy chain isoforms’ turnover in skeletal muscle

2003 ◽  
Vol 86 (2) ◽  
pp. 201-206 ◽  
Author(s):  
Teet Seene ◽  
Priit Kaasik ◽  
Ando Pehme ◽  
Karin Alev ◽  
Eva-Maria Riso
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms

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 Electrophoretic separation and quantitation of cardiac myosin heavy chain isoforms in eight mammalian species

1998 ◽  
Vol 274 (3) ◽  
pp. H1048-H1053 ◽  
Author(s):  
Peter J. Reiser ◽  
William O. Kline
Keyword(s):  
Skeletal Muscle ◽  
Sample Preparation ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Mammalian Species ◽  
Myosin Heavy Chain Isoforms ◽  
Glycerol Concentration ◽  
Cardiac Myosin ◽  
Homogenization Step

A protocol for sample preparation and gel electrophoresis is described that reliably results in the separation of the α- and β-isoforms of cardiac myosin heavy chain (MHC-α and MHC-β) in eight mammalian species. The protocol is based on a simple, nongradient denaturing gel. The magnitude of separation of MHC-α and MHC-β achieved with this protocol is sufficient for quantitative determination of the relative amounts of these two isoforms in mouse, rat, guinea pig, rabbit, canine, pig, baboon, and human myocardial samples. The sensitivity of the protocol is sufficient for the detection of MHC isoforms in samples at least as small as 1 μg. The glycerol concentration in the separating gel is an important factor for successfully separating MHC-α and MHC-β in myocardial samples from different species. The effect of sample load on MHC-α and MHC-β band resolution is illustrated. The results also indicate that inclusion of a homogenization step during sample preparation increases the amount of MHC detected on the gel for cardiac samples to a much greater extent than for skeletal muscle samples. Although the protocol described in this study is excellent for analyzing cardiac samples, it should be noted that the same protocol is not optimal for separating MHC isoforms expressed in skeletal muscle, as is illustrated.

Single-fiber myosin heavy chain polymorphism: how many patterns and what proportions?

2003 ◽  
Vol 285 (3) ◽  
pp. R570-R580 ◽  
Author(s):  
Vincent J. Caiozzo ◽  
Michael J. Baker ◽  
Karen Huang ◽  
Harvey Chou ◽  
Ya Zhen Wu ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Fibers ◽  
Myosin Heavy Chain Isoforms ◽  
Single Fiber ◽  
Myosin Heavy Chain Isoform ◽  
Skeletal Muscle Fibers ◽  
Velocity Relationship ◽  
Force Velocity

Previous studies have reported the existence of skeletal muscle fibers that coexpress multiple myosin heavy chain isoforms. These surveys have usually been limited to studying the polymorphic profiles of skeletal muscle fibers from a limited number of muscles (i.e., usually <4). Additionally, few studies have considered the functional implications of polymorphism. Hence, the primary objective of this study was to survey a relatively large number of rat skeletal muscle/muscle regions and muscle fibers ( n≈ 5,000) to test the hypothesis that polymorphic fibers represent a larger fraction of the total pool of fibers than do so-called monomorphic fibers, which express only one myosin heavy chain isoform. Additionally, we used Hill's statistical model of the force-velocity relationship to differentiate the functional consequences of single-fiber myosin heavy chain isoform distributions found in these muscles. The results demonstrate that most muscles and regions of rodent skeletal muscles contain large proportions of polymorphic fibers, with the exception of muscles such as the slow soleus muscle and white regions of fast muscles. Several muscles were also found to have polymorphic profiles that are not consistent with the I↔IIA↔IIX↔IIB scheme of muscle plasticity. For instance, it was found that the diaphragm muscle normally contains I/IIX fibers. Functionally, the high degree of polymorphism may 1) represent a strategy for producing a spectrum of contractile properties that far exceeds that simply defined by the presence of four myosin heavy chain isoforms and 2) result in relatively small differences in function as defined by the force-velocity relationship.

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
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