Smooth muscle structure

Somlyo AV, Franzini-Armstrong C 1985 New views of smooth muscle structure using freezing, deep-etching and rotary shadowing. Experientia 41 841-856 Somlyo AP, Somlyo AV 1994 Signal transduction and regulation in smooth muscle. Nature 372 231-236... 

Succinylcholine acts primarily at the skeletal neuromuscular junction and has little effect at autonomic ganglia or at postganglionic cholinergic (muscarinic) junctions. Actions at these sites attributed to succinylcholine may arise from the effects of choline. Succinylcholine has no direct action on the uterus or other smooth muscle structures. It does not enter the CNS and does not cross the placental barrier. It may, however, release histamine from mast cells. Because succinylcholine works by stimulating rather than blocking end plate receptors, anti-AChEs will not reverse muscle paralysis and may actually prolong the block. 

Duarte J, Vizcaino FP, Utrilla P, Jimenez J, Tamargo J, Zarzuelo A. VasodUatory effects of flavonoids in rat aortic smooth muscle. Structure activity relationships. Biochem Pharmacol 1993 24 857-862. 

Nasal vasculature may offer some insight into this question, though research to date has been equivocal. Nasal turbinate vessels can be classified as either capacitance vessels or resistive vessels. Capacitance vessels appear to vasodilate in response to infection while resistance vessels appear to respond to cold stimuli by vasoconstriction. Buccal vascular structures also respond to thermal stimuli but appear to respond principally to cutaneous stimuli. How pharyngeal and tracheobronchial submucosal vessels react to thermal stimuli is not known, though cold-induced asthma is believed to result from broncho-spasms caused by susceptible bronchial smooth muscle responding to exposure to cold dry air.- This asthmatic response suggests an inadequate vascular response to surface cooling. 

Reseaich in physiology caiiied out in the 1930s established that the lipid fraction of semen contains small fflnounts of substances that exert powerful effects on smooth muscle. Sheep prostate glands proved to be a convenient source of this material and yielded a mixture of structurally related substances refened to collectively as prostaglandins. We now know that prostaglandins are present in almost all animal tissues, where they cany out a variety of regulatory functions. 

Nonmuscle/smooth muscle myosins-Il are structurally similar to striated muscle myosin-II, but they have slower rates of ATP hydrolysis than do their striated muscle counterparts. Nonmuscle/smooth muscle myosin-II is also regulated differently than striated muscle myosin-II. Nonmuscle myosin-II is divided into the invertebrate and vertebrate branches (Cheney et al., 1993). This group is ubiquitous because it is present in most lower organisms, such as slime molds, amoeba, sea urchins, etc., and in virtually all mammalian nonmuscle cells. Smooth muscle myosin-II is also somewhat heterogeneous in that at least three separate forms of smooth muscle heavy chains, with molecular weights of 196,000, 200,000, and 204,000 have been identified (Kawamoto and Adelstein, 1987). The physiological properties of these separate myosin heavy chains are not yet known. 

Smooth muscles, as the name implies, do not contain sarcomeres. In fact, it was initially difficult to demonstrate the presence of thick filaments in smooth muscle, although their presence is now well-established. On the other hand, it is very difficult to demonstrate thick filaments in highly motile cells, such as macrophages and neutrophils, and this may reflect the necessity to rapidly form and redistribute cytoskeletal elements during migration. Thick filaments in smooth muscles appear to be considerably longer than those in striated muscles. They run diagonally in smooth muscle cells and attach to the membrane at structures known as dense bodies. Thus, there is a cork-screw effect when smooth muscles contract (Warshaw etal., 1987). 

Inside the typical smooth muscle cell, the cytoplasmic filaments course around the nuclei filling most of the cytoplasm between the nuclei and the plasma membrane. There are two filamentous systems in the smooth muscle cell which run lengthwise through the cell. The first is the more intensively studied actin-myosin sliding filament system. This is the system to which a consensus of investigators attribute most of the active mechanical properties of smooth muscle. It will be discussed in detail below. The second system is the intermediate filament system which to an unknown degree runs in parallel to the actin-myosin system and whose functional role has not yet been completely agreed upon. The intermediate filaments are so named because their diameters are intermediate between those of myosin and actin. These very stable filaments are functionally associated with various protein cytoarchitectural structures, microtubular systems, and desmosomes. Various proteins may participate in the formation of intermediate filaments, e.g., vimentin. 

The structure of the contractile apparatus of smooth muscle at the next higher level is also characteristically different from other muscles. The concentrations of actin and myosin in smooth muscle are about three times higher for actin and four times lower for myosin than in skeletal muscle. Correspondingly, in smooth muscle the ratio of the numbers of moles of actin to moles of myosin, and the ratio of the number of actin filaments to those of myosin filaments, are about 12 times larger than for other muscles. Thus, the arrangements of the two sets of filaments are bound to be quite different just on the basis of numbers of actin and myosin... 

The compliance in series with the active force. Force exerted by the activated elements must be transmitted or borne by whatever structural elements are in series with them. In skeletal muscle there is clearly a tendon in series but not so with smooth muscle. In smooth muscle, the total length of contractile apparatus is broken up into individual cells with intercalating extracellular connective structures. In addition, the portions of the crossbridges in series with the pulling site must also be stretched before force can rise to isometric levels. Taken together, the... 

In order to exert a force from one end of a muscle to the other, a structure must be continuous from one end to the other. In smooth muscle tissue, this structure is a system of alternating myosin and actin filaments within a cell, firm attachments first to the cell membrane, and beyond that extracellular attachments to the... 

Organization into macromolecular structures. There are no apparent templates necessary for the assembly of muscle filaments. The association of the component proteins in vitro is spontaneous, stable, and relatively quick. Filaments will form in vitro from the myosins or actins from all three kinds of muscle. Yet in vitro smooth muscle myosin filaments are found to be stable only in solutions somewhat different from in vivo conditions. The organizing principles which govern the assembly of myosin filaments in smooth muscle are not well understood. It is clear, however, a filament is a sturdy structure and that individual myosin molecules go in and out of filaments whose structure remains in a functional steady-state. As described above, the crossbridges sticking out of one side of a smooth muscle myosin filament are all oriented and presumably all pull on the actin filament in one direction along the filament axis, while on the other side the crossbridges all point and pull in the opposite direction. The complement of minor proteins involved in the structure of the smooth muscle myosin filament is unknown, albeit not the same as that of skeletal muscle since C-protein and M-protein are absent. 

The superstructure of smooth muscle actin filaments is differentiated from those of striated muscle by the absence of the troponins and the lateral organization by association of the filaments with dense bodies instead of with the Z-line. How these differences are encoded is again not at all clear. However, the myofibrillar structure and the alignment of the alternating actin and myosin filaments is apparently due primarily to dense bodies and the actin-actinin macrostructures. As the bent dumbbell shaped actins assemble into filaments they are all oriented in the same direction. The S-1 fragments of myosin will bind to actin filaments in vitro and in... 

In addition to its effects on enzymes and ion transport, Ca /calmodulin regulates the activity of many structural elements in cells. These include the actin-myosin complex of smooth muscle, which is under (3-adrenergic control, and various microfilament-medi-ated processes in noncontractile cells, including cell motility, cell conformation changes, mitosis, granule release, and endocytosis. 

Smooth muscles have molecular structures similar to those in striated muscle, but the sarcomeres are not aligned so as to generate the striated appearance. Smooth muscles contain a-actinin and tropomyosin molecules, as do skeletal muscles. They do not have the troponin system, and the fight chains of smooth muscle myosin molecules differ from those of striated muscle myosin. Regulation of smooth muscle contraction is myosin-based, unlike striated muscle, which is actin-based. However, like striated muscle, smooth muscle contraction is regulated by Ca. ... 

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