| First Author | Jockusch H | Year | 1988 |
| Journal | Eur J Biochem | Volume | 171 |
| Issue | 1-2 | Pages | 101-5 |
| PubMed ID | 3123225 | Mgi Jnum | J:25831 |
| Mgi Id | MGI:73617 | Doi | 10.1111/j.1432-1033.1988.tb13764.x |
| Citation | Jockusch H, et al. (1988) Reduction of myosin-light-chain phosphorylation and of parvalbumin content in myotonic mouse muscle and its reversal by tocainide. Eur J Biochem 171(1-2):101-5 |
| abstractText | In muscle of the myotonic mouse mutant, 'arrested development of righting response', ADR, a reduced level of fast-myosin-light-chain-2 (LC2f) phosphorylation was observed in addition to a lowered parvalbumin content. In fast muscles, average phosphorylation levels of LC2f (LC2-P/LC2 total) were 0.76 mol/mol for wild type and 0.59 mol/mol for the myotonic mutant. The difference was not due to short-term activity prior to freezing because it was also found in curare-paralyzed muscles. Long-term treatment of genetically myotonic animals with the membrane-stabilizing drug, tocainide, led to an increase of parvalbumin content and LC2-P level. In wild-type mice, tocainide had a similar effect, leading to supranormal parvalbumin concentrations. It is concluded that both the basal level of LC2-P and parvalbumin concentration are regulated by a common factor, related to long-term muscle activity. |
