Expression of myosin heavy and light chains and phosphorylation of the 
phosphorylatable myosin light chain in the heart ventricle of the European 
hamster during hibernation and in summer

Morano, I.; Adler, K.; Agostini, Bruno; Hasselbach, Wilhelm

doi:10.1007/BF01738429

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Expression of myosin heavy and light chains and phosphorylation of the phosphorylatable myosin light chain in the heart ventricle of the European hamster during hibernation and in summer

MPS-Authors

/persons/resource/persons86998

Agostini, Bruno
Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons93324

Hasselbach, Wilhelm
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

http://link.springer.com/content/pdf/10.1007%2FBF01738429.pdf
(Any fulltext)

https://dx.doi.org/10.1007/BF01738429
(Any fulltext)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Morano, I., Adler, K., Agostini, B., & Hasselbach, W. (1992). Expression of myosin heavy and light chains and phosphorylation of the phosphorylatable myosin light chain in the heart ventricle of the European hamster during hibernation and in summer. Journal of Muscle Research and Cell Motility, 13(1), 64-70. doi:10.1007/BF01738429.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002B-16C1-7

Abstract

We investigated the expression of myosin subunits (myosin heavy chains) as well as light chains and the in vivo phosphorylation of the phosphorylatable myosin light chain in the heart ventricle of the adult male European hamster (Cricetus cricetus L.). Two myosin heavy chain isoenzymes could be detected under native and denaturing electrophoretic conditions having high (alpha-myosin heavy chain) and low (beta-myosin heavy chain) enzymatic activity. Enzymatic activity of alpha- and beta-myosin heavy chain revealed a different temperature dependency. When temperature increased ATPase activity of the alpha-myosin heavy chain isoenzyme increased relatively more than ATPase activity of the beta-myosin heavy chain isoenzyme. Summer animals expressed predominantly the beta-myosin heavy chain (79% of total myosin) while during hibernation the alpha-myosin heavy chain expression increased to 53% of total myosin. Winter-active hamsters kept at 22 degrees C and 12 h day/night rhythm showed the same myosin heavy chain isoenzyme pattern as summer-active animals. Two myosin light chain forms were expressed in the ventricle of all animal groups. The in vivo phosphorylation level of the phosphorylatable myosin light chain decreased from 45% in summer-active hamster to 23% during hibernation.