Functional equivalence of creatine kinase isoforms in mouse skeletal muscle
| Autor: | Brian B. Roman, Alan P. Koretsky, Bé Wieringa |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Gene isoform
Genetically modified mouse Muscle Fibers Skeletal Biochemistry adaptatie en celdood [Cellulaire herprogrammering in neuromusculaire weefsels in respons op genetische defecten in het cellulaire netwerk voor energie-homeostase] Mice medicine Animals Muscle Skeletal Molecular Biology Creatine Kinase Adaptation and Cell Death [Cellular reprogramming in tissues of neuro-muscular origin as a response on genetic defects in the network for energy-homeostasis] biology Endoplasmic reticulum Skeletal muscle Cell Biology Isoenzymes medicine.anatomical_structure Knockout mouse biology.protein Creatine kinase medicine.symptom Myofibril Energy Metabolism Muscle contraction Muscle Contraction |
| Zdroj: | Journal of Biological Chemistry, 272, 28, pp. 17790-17794 Journal of Biological Chemistry, 272, 17790-17794 |
| ISSN: | 1083-351X 0021-9258 |
| Popis: | Creatine kinase (CK) is a highly conserved enzyme abundant in skeletal muscle that has a key role in high energy phosphate metabolism. The localization of the muscle isoenzyme of CK (MM-CK) to the M line and the sarcoplasmic reticulum of myofibrils has been suggested to be important for proper force development in skeletal muscle. The importance of this subcellular compartmentation has not been directly tested in vivo. To test the role of myofibrilar localization of CK, the consequences of a complete CK isoform switch from MM-CK to the brain (BB-CK) isoform, which does not localize to the M line, was studied in transgenic mouse skeletal muscle. In MM-CK knockout mice there are large contractile defects. When MM-CK was replaced by BB-CK, the aberrant contractile phenotypes seen in MM-CK knockout mice were returned to normal despite the lack of myofibrillar localization. These results indicate that CK compartmentation to the myofibril of skeletal muscle is not essential for contractile function and that there is functional equivalence of creatine kinase isoforms in supporting cellular energy metabolism. |
| Databáze: | OpenAIRE |
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