Abstract
The expression of isoforms of myosin heavy chain (MHC) during postnatal development was studied in the masseter muscle of the rabbit. Evidence is presented that in addition to adult fast and slow myosin, the rabbit masseter contains neonatal and 'cardiac' α-MHC. During postnatal growth myosin transitions take place from neonatal and fast (IIA, IIA/IIB-referring to a fibre containing both IIA and IIB MHCs) MHC to adult 'cardiac' α-MHC and I/α-MHC. Since there is a temporary population of fibres containing IIA/α-MHC during the first 4 wk of development with a peak in the 3rd to 4th wk, the transition from IIA-MHC to α-MHC may occur in these IIA/α-MHC-containing fibres. The appearance of cardiac' α-MHC coincides with the timing of weaning, suggesting that the changes in MHC content, that probably result in a transition to a lower speed of contraction, have functional significance related to weaning. The finding of neonatal MHC in adult rabbits indicates that the masseter develops at a rate and in a way that is distinct from most other skeletal muscles. A spatiotemporal variation in expression of myosin isozymes within the masseter was observed, with many fibres containing more than one myosin type, indicating developmentally regulated spatial differences in function.
| Original language | English |
|---|---|
| Pages (from-to) | 263-274 |
| Journal | Journal of anatomy |
| Volume | 180 |
| Issue number | 2 |
| Publication status | Published - 1992 |