• The Korean Journal of Physiology and Pharmacology
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• v.15 no.3
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• pp.171-177
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• 2011

Tonic smooth muscle exhibit the latch phenomenon: high force at low myosin regulatory light chains (MRLC) phosphorylation, shortening velocity (Vo), and energy consumption. However, the kinetics of MRLC phosphorylation and cellular activation in phasic smooth muscle are unknown. The present study was to determine whether $Ca^{2+}$-stimulated MRLC phosphorylation could suffice to explain the agonist- or high $K^+$-induced contraction in a fast, phasic smooth muscle. We measured myoplasmic [$Ca^{2+}$], MRLC phosphorylation, half-time after step-shortening (a measure of Vo) and contractile stress in rabbit urinary bladder strips. High $K^+$-induced contractions were phasic at both $22^{\circ}C$ and $37^{\circ}C$: myoplasmic [$Ca^{2+}$], MRLC phosphorylation, 1/half-time, and contractile stress increased transiently and then all decreased to intermediate values. Carbachol (CCh)-induced contractions exhibited latch at $37^{\circ}C$: stress was maintained at high levels despite decreasing myoplasmic [$Ca^{2+}$], MRLC phosphorylation, and 1/half-time. At $22^{\circ}C$ CCh induced sustained elevations in all parameters. 1/half-time depended on both myoplasmic [$Ca^{2+}$] and MRLC phosphorylation. The steady-state dependence of stress on MRLC phosphorylation was very steep at $37^{\circ}C$ in the CCh- or $K^+$-depolarized tissue and reduced temperature flattend the dependence of stress on MRLC phosphorylation compared to $37^{\circ}C$. These data suggest that phasic smooth muscle also exhibits latch behavior and latch is less prominent at lower temperature.

• The Korean Journal of Physiology
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• v.20 no.1
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• pp.31-41
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• 1986

The sufficient myoplasmic $Ca^{++}$ to react with the contractile proteins is necessary to induce contraction of a cardiac muscle. These $Ca^{++}$ for the production of muscle contraction are supplied from the three recognized $Ca^{++}$ sources; internal $Ca^{++}$ release via the sarcoplasmic reticulum(SR), $Ca^{++}$ influx through a gated Ca-channel in the membrane as a Isi, and $Ca^{++}$ transport by the mechanism of Na/ca exchange. However, it is still controversial which $Ca^{++}$ sources act as a main contributor for myoplasmic $Ca^{++}$, Therefore, this study was undertaken in order to examine the $Ca^{++}$ sources for the contraction of frog ventricle. There is evidence that the SR is sparse in frog ventricular fibers, and that T-tubules are absent. Isolated ventricular strips of frog, Rana nigromaculata, were used in this experiment. Isometric tension was recorded by force transducer, and membrane potentials of ventricular muscles were measured through the intracellular glass microelectrodes, which were filled with 3M KCI and had resistance of $30{\pm}50M{\Omega}$. All experiments were performed at room temperature in a tris·buffered Ringer solution which was aerated with 100% $O_2$. Isotonic high K, low Na solution was used to induce K-contracture, K-contracture appeared at the concentration of 20 to 30mM-KCI and was potentiated in parallel with the increase in KCI concentration. The contracture had two components: an initial rapid phasic and a subsequent slow tonic contractile responses. Membrane Potentials measured at normal Ringer solution(2.5mM KCI) was -90 to -100 mV, and decreased linearly as the KCI concentration increased; -55mV at 20mM.KCI, -45mV at 30 mM.KCI, -30 mY at 50 mM.KCI, and -12 mV at 100 mM.KCI. K-contracture was evoked firstly at the membrane potential of -45 mV. The contracture was potentiated by the increase of bathing extracellular $Ca^{++}$ concentration. However, in the absence of $Ca^{++}$ the contracture was almost not induced by 50 mM.KCI solution. Caffeine(20mM) in normal Ringer solution, which is known to release $Ca^{++}$ from SR without substantial effects on the $Ca^{++}$ fluxes across the surface membrane, did not affect membrane potential and also not initiate contracture, but the caffeine in 20 mM-KCI Ringer solution produced a contracture. Above results suggest that the main $Ca^{++}$ source for the K·contracture of frog ventricle is $Ca^{++}$ influx through the voltage-dependent Ca-channel, and that in the K-contracture at the concentration of 100 mM-KCI, the mechanism of Na/ca exchange also partly contributs, in addition to the $Ca^{++}$ influx.

• The Journal of Korean Physical Therapy
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• v.13 no.1
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• pp.237-243
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• 2001

Skeletal muscle cells are activated by ${\alpha}$-motorneurons which release acetylcholine at the neuromuscular junction. This results in a local depolarization of surface membrane which triggers an action potential. The action potential propagates along the surface membrane and also into the T-tubule system. In the triads T-tubules are in close connection with the terminal cisternae of the sarcoplasmic reticulum(SR). The action potential activaies T-tubule voltage sensors(DHP receptors). which activates SR Ca$^{2+}$ release channels(ryanodinc receptors). Ca$^{2+}$ have a key role in skeletal muscle in that an increase of free myoplasmic Ca$^{2+}$ concentration. The process of coupling chemical and electrical signals at the cell surface to the intracellular release of Ca$^{2+}$and ultimate contraction of muscle fibers is termed excitation-contraction coupling(ECC). Coupling of cel1 surface signals to intracellular Ca$^{2+}$ release proceeds by several mechanisms in skeletal muscle cells. This review focus on sarcopiasmic reticulum(SR) Ca$^{2+}$ releasing mechanisms from sarcoplasmic reticulum in the skeletal muscle. The mechanisms include DCCR, CICR, and HCR.

• The Korean Journal of Pharmacology
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• v.31 no.3
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• pp.291-297
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• 1995

The objectives of this study is to compare the inhibitory mechanism of sodium nitroprusside and forskolin on the phorbol ester, activator of protein kinase C (PKC), -induced contractions in rat aorta. $0.1\;{\mu}M$ phorbol dibutyrate (PDBu) induced sustained contractions and increased phosphorylations of myosin light chain (MLC) time-dependently. At 30 min, the contractions and phosphorylations of MLC by PDBu were augmented maximally and remained constant. Moreover, $^{45}Ca^{2+}$ uptake was increased 30 min after PDBu stimulation from resting values. Sodium nitroprusside which activates guanylyl cyclase followed by increasing cGMP, inhibited the PDBu-induced contractions concentration-dependently. On the other hand, forskolin which activates adenylyl cyclase followed by increasing cAMP, also inhibited the PDBu-induced contractions concentration-dependently. However, sodium nitroprusside was more potent to inhibition of the PDBu-induced contractions than forskolin. Sodium nitroprusside inhibited $^{45}Ca^{2+}$ uptake by PDBu stimulation. Forskolin also inhibited $^{45}Ca^{2+}$ uptake by PDBu stimulation. Sodium nitroprusside and forskolin inhibited the phosphorylations of MLC by PDBu, respectively. However, sodium nitroprusside was more potent to inhibition of phosphorylations of MLC by PDBu than forskolin. From these results, Sodium nitroprusside via cGMP or forskilin via cAMP may reduce myoplasmic $Ca^{2+}$ followed by suppression of phosphorylations of MLC of PKC-mediated contractions, which results in vasodilation. However, cGMP may play a role more importantly than cAMP on the regulation of protein kinase C-mediated contraction in vascular smooth muscle.