NDLI: Kinetic properties of cardiac myosin heavy chain isoforms in rat

Content Provider	Springer Nature Link
Author	Galler, Stefan Puchert, Emma Gohlsch, Bärbel Schmid, Doris Pette, Dirk
Copyright Year	2002
Abstract	The head portion of the myosin heavy chain (MHC) is essential in force generation. As previously shown, Ca2+-activated fibres of mammalian skeletal muscle display a strong correlation between their MHC isoform complement and the kinetics of stretch activation, suggesting isoform-specific differences in kinetic properties of myosin heads. Using the same methodology on muscle strips of atria and ventricles of hyper- and hypothyroid rats, this study showed that the kinetics of cardiac αMHC are 3 times faster than those of cardiac βMHC under isometric conditions and maximal Ca2+ activation. Comparison of rat heart and skeletal muscle fibres revealed that 100% αMHC heart muscle strips exhibited faster stretch activation kinetics (time parameter t 3: 108±18 ms, mean±SD) than rat type-IIA fibres (t 3: 157±19 ms), but slower than type-IID fibres (t 3: 55±10 ms). The kinetics of 100% βMHC heart muscle strips (t 3: 351±44 ms) were faster than that of type-I fibres in rat skeletal muscle (t 3: 901±348 ms). This difference between the two muscle types calls in question the generally accepted identity of βMHC and MHCIβ.
Starting Page	218
Ending Page	223
Page Count	6
File Format	PDF
ISSN	00316768
Journal	Pflügers Archiv
Volume Number	445
Issue Number	2
e-ISSN	14322013
Language	English
Publisher	Springer-Verlag
Publisher Date	2002-10-18
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Physiology Physiology (medical) Clinical Biochemistry

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