G. Beckersbleukx

The Force-velocity Relation of the Rabbit Inferior Oblique Muscle Influence of Temperature

The contractile properties of the rabbit inferior oblique muscle (IO) were studied in vitro with direct stimulation at temperatures between 20 and 35°C. Isovelocity releases were used to determine the force/ velocity relation. Cooling the muscle from 35°C to 20°C increased contraction and half-relaxation times of single twitches with a temperature coefficient (Q10) of 0.4, but did not affect significantly the twitch tension. The tetanic tension increases with increasing temperature (Q10=1.32). Cooling decreased the maximum shortening velocity of the IO with a Q10 of 1.6 and the maximum mechanical power with a Q10 of 2.3. At 35°C, the maximum speed of shortening of the muscle (19±2 muscle lengths/s, mean ± SEM) corresponded to a maximum shortening velocity of the sarcomeres of 57±6 μm/s. This value is similar to data obtained for extraocular muscles (EOM) of smaller rodents (mice and rats). In comparison with mammalian limb muscles the isometric and force-velocity properties of mammalian EOM appear to be virtually independent of the size of the animal. Thus, IO is a fast-twitch muscle endowed with a maximum velocity of shortening higher than that of fast-twitch skeletal muscle, but using a tetanic mechanical power lower than that produced by slow-twitch muscle: the combination of these properties makes it ideally suited to move an ocular globe of low mass at high velocity.

EFFECT OF NITRIC OXIDE ON THE MAXIMAL VELOCITY OF SHORTENING OF A MOUSE SKELETAL MUSCLE

Abstract Maximum velocity of shortening, Vo, was measured by the method of Edman [J Physiol (Lond) 291:143–159, 1979] on extensor digitorum longus muscles of a mouse in vitro at 20°C. Blockers of nitric oxide synthase, 10 mM nitro-l-arginine or 1 mM 7-nitroindazole, reduced Vo by 18% and 22%, respectively. On removal of the inhibitor, Vo returned to the control value. It was found that 10 mM nitro-d-arginine, an enantiomer of nitro-l-arginine inactive against nitric oxide synthase, did not affect Vo. A donor of nitric oxide, 0.1 mM nitroprusside, increased Vo by 15%. It removed the inhibition caused by nitro-l-arginine. Another donor of nitric oxide, 1 µM (±)-S-nitroso-N-acetylpenicillamine (SNAP), increased Vo by 8%. An inhibitor of cGMP synthase, 0.01 mM Ly-83583, decreased Vo by 18%. An analogue of cGMP, 0.1 mM 8-bromo-cGMP, increased Vo by 17%. A general inhibitor of phosphodiesterases, 0.02 mM 3-isobutyl-1-methylxanthine (IBMX), increased Vo by 17%. An inhibitor specific of cGMP phosphodiesterase, 0.01 mM dipyridamole, increased Vo by 8%. The maximal isometric force (F0) was not modified by the drugs, except by 7-nitroindazole and Ly-83583, which depressed F0 by 12%. The cGMP level in tetanized muscles decreased by 12–27% in the presence of blockers of nitric oxide synthase. We conclude that the level of intracellular nitric oxide modulates Vo through thecGMP pathway.

Force-velocity relation and isomyosins in soleus muscles from two strains of mice (C57 and NMRI)

We compared soleus muscles from two strains of mice, NMRI and C57. Soleus muscles from NMRI mice produced slower twitches and lower maximum tetanic force (Fo) but higher maximum tetanic stress (So), (owing to their smaller weight). Their Hills velocity constant (b) was lower, but their force constant (a/So), their maximum velocity of unloaded shortening (Vu) and their maximal mechanical power (Pmax) were similar. All soleus muscles contained two isomyosins (SM2 and IM) and the two myosin heavy chains (MHC1 and MHC2A) corresponding to type I fibres and type IIA fibres; however, soleus muscles from NMRI strain had higher proportions of isomyosin SM2 and of myosin heavy chain 2A. Regression equations were computed between the mechanical variables and the myosin heavy chain content. Using a simple hypothesis, the results were used to estimate the mechanical properties of type I and type IIA fibres. We conclude that type IIA fibres from soleus muscle are mechanically more similar to slow-twitch type I fibres than to fast-twitch type II fibres. The results also suggest a hypothesis to account for the diversity of isomyosins, by a matching diversity of mechanical properties based on a separate physiological control of the three factors that control Pmax.

The Isomyosins of Rabbit Middle-ear Muscles

Isomyosins of the two middle ear muscles of rabbit have been separated by electrophoresis in non-dissociating conditions. Tensor tympani has four isomyosins called MM1 to MM4 by order of decreasing mobility. Stapedius has two isomyosins, similar to MM1 and MM4. MM1 and MM2 have the same mobility than FM2 and FM3, fast isomyosins observed in psoas. MM4 has the same mobility than IM, a slow isomyosin observed in extensor digitorum longus. MM3 is absent in soleus, psoas or extensor digitorum longus. Slow myosin (SM) of soleus and fast myosin (FM1) of psoas are not observed in middle ear muscles.