CONTRACTION CHARACTERISTICS AND MYOSIN HEAVY-CHAIN COMPOSITION OF RABBIT MASSETER MOTOR UNITS

Citation
Shs. Kwa et al., CONTRACTION CHARACTERISTICS AND MYOSIN HEAVY-CHAIN COMPOSITION OF RABBIT MASSETER MOTOR UNITS, Journal of neurophysiology, 73(2), 1995, pp. 538-549
Citations number
74
Categorie Soggetti
Neurosciences,Physiology,Neurosciences,Physiology
Journal title
ISSN journal
00223077
Volume
73
Issue
2
Year of publication
1995
Pages
538 - 549
Database
ISI
SICI code
0022-3077(1995)73:2<538:CCAMHC>2.0.ZU;2-2
Abstract
1. We studied isometric twitch peak force (TPF) and twitch contraction time (TCT) of 249 motor units of the masseter muscle in 41 rabbits af ter extracellular electrical stimulation of single trigeminal motoneur ons in the brain stem. In 41 of these units we determined the amount o f tension decrease during a partially fused tetanus (sag) and the rati o between peak tetanic force after 2 min of intermittent tetanic stimu lation and initial tension (fatigue index). Muscle fibers of 24 motor units were identified by the glycogen depletion method and characteriz ed in serial sections with monoclonal antibodies against type IID, IIA , ''cardiac'' alpha, and I isoforms of myosin heavy chain (MHC). 2. Th e motor units had TCTs ranging from 13 to 32 ms. The majority of the u nits showed forces < 35 mN. The TPFs were larger and varied more for m otor units with short and intermediate TCTs than for units with long T CTs. There is a small but statistically significant negative correlati on between the motor unit TPF and the TCT. 3. All units exhibited ''sa g'' and, with the exeption of one, had fatigue indexes > 0.75. The stu died rabbit masseter motor units can therefore be classified as fast, fatigue-resistant, except for one that belonged to the FF (fast, fatig able) category. No slow units were represented in the sample pool. Sig nificant correlations were not found either between TCT and the amount of sag or between TCT and the fatigue index. 4. Immunohistochemical a nalysis showed that the EF unit had fibers containing only IID-MHC. Fi ve other units were found with a single MHC-three with IIA-MHC and two with alpha-MHC. In three other units all fibers showed one combinatio n of two MHCs (1 IIA/IID, 1 IIA/alpha, and 1 alpha/I). The remaining 1 5 units contained two MHCs spread unevenly over the constituting fiber s. Large variations in myosin composition of fibers within one motor u nit cast doubts on the presumed dominant neuronal influence on myosin expression in the adult animal. 5. We found a close, statistically sig nificant correlation between the TCT and the estimated MHC content of the units: the TCT was 13 ms for the IID unit, 18 ms for the pure IIA units, and 28 ms for the pure alpha units. Units with two MHCs had int ermediate TCTs; units with alpha/I-MHC mixtures had TCTs of 29-30 ms. No pure MHC-I units were identified. 6. We conclude that the almost ho mogeneous population of masseter motor units, as judged from classical physiological criteria, in reality shows a continuous spectrum of con traction speeds, accurately matching a continuous spectrum of MHC mixt ures. Contraction speed of fibers decreases dependent on their MHC con tent in the order IID-IIA-alpha-I. Our results show that only combinat ions of neighboring MHCs on this list occur in fibers and motor units.