The length-tension relationship of the dorsal longitudinal muscle of a leech

1975 ◽  
Vol 62 (1) ◽  
pp. 43-53
Author(s):  
JB Miller
Keyword(s):  
Body Wall ◽  
Longitudinal Muscle ◽  
Muscle Fibres ◽  
Passive Tension ◽  
Active Tension ◽  
Thin Filaments ◽  
Thick Filaments ◽  
Tension Curve ◽  
Cross Bridges ◽  
Relationship Of

The length-tension relationship of a preparation of the dorsal body wall of the leech Haemopis sanguisuga was determined. Passive tension is low except at very long lengths of the preparation, when it rises steeply. It is due mainly to the epidermis present in the preparation. The active tension curve is very flat, with tension being reduced only at very short and very long lengths. This shape is explained in the context of the myofilament arrangement of the muscle fibres. It may be that thin filaments can form cross-bridges with different thick filaments at different lengths of the preparation.

scholarly journals Structure and paramyosin content of tarantula thick filaments.

1983 ◽  
Vol 97 (1) ◽  
pp. 186-195 ◽  
Author(s):  
R J Levine ◽  
R W Kensler ◽  
M C Reedy ◽  
W Hofmann ◽  
H A King
Keyword(s):  
Evolutionary Relationship ◽  
Radial Distance ◽  
Thick Filament ◽  
Optical Diffraction ◽  
Thin Filaments ◽  
Biochemical Characteristics ◽  
Thick Filaments ◽  
Cross Bridges ◽  
Centers Of Mass ◽  
Relationship Of

Muscle fibers of the tarantula femur exhibit structural and biochemical characteristics similar to those of other long-sarcomere invertebrate muscles, having long A-bands and long thick filaments. 9-12 thin filaments surround each thick filament. Tarantula muscle has a paramyosin:myosin heavy chain molecular ratio of 0.31 +/- 0.079 SD. We studied the myosin cross-bridge arrangement on the surface of tarantula thick filaments on isolated, negatively stained, and unidirectionally metal-shadowed specimens by electron microscopy and optical diffraction and filtering and found it to be similar to that previously described for the thick filaments of muscle of the closely related chelicerate arthropod, Limulus. Cross-bridges are disposed in a four-stranded right-handed helical arrangement, with 14.5-nm axial spacing between successive levels of four bridges, and a helical repeat period every 43.5 nm. The orientation of cross-bridges on the surface of tarantula filaments is also likely to be very similar to that on Limulus filaments as suggested by the similarity between filtered images of the two types of filaments and the radial distance of the centers of mass of the cross-bridges from the surfaces of both types of filaments. Tarantula filaments, however, have smaller diameters than Limulus filaments, contain less paramyosin, and display structure that probably reflects the organization of the filament backbone which is not as apparent in images of Limulus filaments. We suggest that the similarities between Limulus and tarantula thick filaments may be governed, in part, by the close evolutionary relationship of the two species.

Mechanical properties of porcine intralobar pulmonary arteries

1988 ◽  
Vol 64 (4) ◽  
pp. 1537-1545 ◽  
Author(s):  
H. Ohtaka ◽  
J. C. Hogg ◽  
R. H. Moreno ◽  
P. D. Pare ◽  
R. R. Schellenberg
Keyword(s):  
Pulmonary Arteries ◽  
Pressure Change ◽  
Passive Tension ◽  
Active Tension ◽  
Balloon Inflation ◽  
Optimal Length ◽  
Active Volume ◽  
Calculated Length ◽  
Passive Pressure ◽  
Tension Curve

The isobaric and isovolumetric properties of intrapulmonary arteries were evaluated by placing a highly compliant balloon inside arterial segments. The passive pressure-volume (P-V) curve was obtained by changing volume (0.004 ml/s) and measuring pressure. The isobaric active volume change (delta V) or isovolumetric active pressure change (delta P) generated by submaximal histamine was measured at four different transmural pressures (Ptm's) reached by balloon inflation. The maximal delta P = 11.2 +/- 0.6 cmH2O (mean +/- SE) was achieved at 30.8 +/- 1.2 cmH2O Ptm and maximal delta V = 0.20 +/- 0.02 ml at 16.7 +/- 1.7 cmH2O Ptm. The P-V relationships were similar when volume was increased after either isobaric or isovolumetric contraction. The calculated length-tension (L-T) relationship showed that the active tension curve was relatively flat and that the passive tension at the optimal length was 149 +/- 11% of maximal active tension. These data show that 1) a large elastic component operates in parallel with the smooth muscle in intralobar pulmonary arteries, and 2) the change in resistance associated with vascular expansion of the proximal arteries is independent of the type of contraction that occurs in the more distal arterial segments.

Increased responsiveness of jejunal longitudinal muscle in Trichinella-infected rats

1988 ◽  
Vol 254 (1) ◽  
pp. G124-G129 ◽  
Author(s):  
D. L. Vermillion ◽  
S. M. Collins
Keyword(s):  
Smooth Muscle ◽  
Muscle Function ◽  
Longitudinal Muscle ◽  
Trichinella Spiralis ◽  
Passive Tension ◽  
Active Tension ◽  
Maximum Tension ◽  
Longitudinal Smooth Muscle ◽  
Smooth Muscle Function

We examined in vitro changes in contractility of jejunal longitudinal muscle strips in rats infected with the nematode parasite Trichinella spiralis. Length-passive tension relationships were unchanged. However, muscle from infected rats on days 5 and 6 postinfection (PI) generated maximal active tension induced by carbachol at significantly less stretch (39.9 +/- 1.0 and 34.3 +/- 6.3%, respectively) than control tissues (66.0 +/- 2.3%). In infected rats on day 5 PI, the maximum tension generated by carbachol (1.6 +/- 0.4 g/mm2) and by 5-hydroxytryptamine (5-HTP) (2.6 +/- 0.1 g/mm2) was significantly greater than in control tissue (0.5 +/- 0.2 g/mm2). On removal of calcium from the medium, responses of muscle from control and infected rats were reduced in a proportionate manner. The increased responsiveness to carbachol and 5-HTP was maximal by day 5 PI and was associated with a decrease in the ED50 value for 5-HTP but not for carbachol. All changes were reversed by 23 days PI. These results indicate that T. spiralis infection in the rat is associated with alterations in jejunal longitudinal smooth muscle function.

The Z band in skeletal muscle in rigor exhibits the activated lattice form

1989 ◽  
Vol 47 ◽  
pp. 252-253
Author(s):  
R. J. Edwards
Keyword(s):  
Skeletal Muscle ◽  
Cross Sections ◽  
Active Tension ◽  
Thin Filaments ◽  
Cross Bridge ◽  
The Cross ◽  
Cross Bridges ◽  
Glycerinated Muscle

The Z band of skeletal muscle is a tetragonal array of interdigitating thin filaments from adjacent sarcomeres held together by cross connecting filaments. Two visually unique forms of the Z band (small square, ss, and basketweave, bw) can be observed by TEM of cross sections. The ss form is found in relaxed muscle and the bw is found in maximally activated muscle. The average Z spacing in the bw form is 20% largerthan in the ss form. There is a correlation between active tension and the form of the Z band. This correlation suggests that cross bridge binding in the A band is directly related to the form of the Z band. In rigor, the cross bridges are completely bound; therefore, we predicted that the Z band would exhibit the bw form. To test this hypothesis we compared unstimulated muscle to glycerinated muscle in rigor.

scholarly journals Evidence that actomyosin cross bridges contribute to “passive” tension in detrusor smooth muscle

2010 ◽  
Vol 298 (6) ◽  
pp. F1424-F1435 ◽  
Author(s):  
Paul H. Ratz ◽  
John E. Speich
Keyword(s):  
Smooth Muscle ◽  
Actin Polymerization ◽  
Contractile Function ◽  
Cyclooxygenase Inhibitors ◽  
Passive Tension ◽  
Detrusor Smooth Muscle ◽  
Free Solution ◽  
Active Tension ◽  
Working Length ◽  
Cross Bridges

Contraction of detrusor smooth muscle (DSM) at short muscle lengths generates a stiffness component we termed adjustable passive stiffness (APS) that is retained in tissues incubated in a Ca2+-free solution, shifts the DSM length-passive tension curve up and to the left, and is softened by muscle strain and release (strain softened). In the present study, we tested the hypothesis that APS is due to slowly cycling actomyosin cross bridges. APS and active tension produced by the stimulus, KCl, displayed similar length dependencies with identical optimum length values. The myosin II inhibitor blebbistatin relaxed active tension maintained during a KCl-induced contraction and the passive tension maintained during stress-relaxation induced by muscle stretch in a Ca2+-free solution. Passive tension was attributed to tension maintaining rather than tension developing cross bridges because tension did not recover after a rapid 10% stretch and release as it did during a KCl-induced contraction. APS generated by a KCl-induced contraction in intact tissues was preserved in tissues permeabilized with Triton X-100. Blebbistatin and the actin polymerization inhibitor latrunculin-B reduced the degree of APS generated by a KCl-induced contraction. The degree of APS generated by KCl was inhibited to a greater degree than was the peak KCl-induced tension by rhoA kinase and cyclooxygenase inhibitors. These data support the hypothesis that APS is due to slowly cycling actomyosin cross bridges and suggest that cross bridges may play a novel role in DSM that uniquely serves to ensure proper contractile function over an extreme working length range.

The musculature of Peripatus and its innervation

1980 ◽  
Vol 288 (1031) ◽  
pp. 481-510 ◽  
Keyword(s):  
Body Wall ◽  
Fibre Length ◽  
Gross Anatomy ◽  
Small Degree ◽  
The Body ◽  
Muscle Fibres ◽  
Neuromuscular Synapses ◽  
Thick Filaments ◽  
Small Muscle ◽  
Tubule Diameter

The musculature of the Onychophoran Peripatus dominicae , its ultrastructure and details of innervation are described. Significant differences were noted between its gross anatomy and that reported in previous accounts, notably in the presence of inner circular body wall muscle and a prominent, functionally significant, levator of the leg. The former is important in regard to the evolutionary position of the Onychophora while the latter helps us to understand the control of walking in a lobopodial leg, and therefore the evolution of arthropod locomotion, which was the focus of our interest. Individual muscle fibres are either directly or indirectly attached to the body wall by collagen. There is a small degree of branching of fibres, with or without anastomosis, near their insertions, but most are as long as the muscle of which they are part, and are unbranched except for an occasional thin arm, emerging at an angle, that becomes invaded by collagen fibres and inserts in the skin. Diameters of muscle fibres vary from 1 to 45 pm. They are invaginated by two separate systems of unique wide (0.3 pm) tubules, longitudinal and radial. These are lined with similar material to that forming the basement material of the sarcolemma, and also contain fine strands with collagen-type cross-banding that connect to collagen bundles outside the fibres. In addition there are narrow tubules of ordinary T-tubule diameter. Both wide and narrow tubules make contacts with sarcoplasmic reticulum cysternae. Dense Z bodies are attached to both kinds of wide tubule, to the inside of the sarcolemma, and are scattered, without any obvious array, in the sarcoplasm. Thin myofilaments emerge from the Z bodies parallel to the fibre axis. Thick filaments occur in clusters with a loosely hexagonal array, but without any regular relation to thin ones: relatively few orbits of thin around thick filaments were seen in many muscle fibres regardless of fibre length and conditions during fixation. A unique innervation pattern was found, consisting of a combination of muscle arm to nerve contacts, which appear to be the commonest, and nerve on muscle fibre synapses. At least 13 motor axons were found to supply each small muscle or cluster of muscle fibres in a large muscle. Each muscle arm simultaneously makes synaptic contact with 3 to 7 axons. Nerve on muscle junctions contain from 1 to 8 axons, each making synaptic contacts. The details of the postsynaptic endplate-specializations resemble those seen in mammalian endplates and are markedly different from both arthropod and annelidan neuromuscular synapses.

scholarly journals THE STRUCTURE OF THE SMOOTH MUSCLE FIBRES IN THE BODY WALL OF THE EARTHWORM

1957 ◽  
Vol 3 (1) ◽  
pp. 111-122 ◽  
Author(s):  
Jean Hanson
Keyword(s):  
Smooth Muscle ◽  
Phase Contrast ◽  
Body Wall ◽  
Longitudinal Muscle ◽  
Lumbricus Terrestris ◽  
Mirror Image ◽  
The Body ◽  
The Other ◽  
Muscle Fibres ◽  
Muscle Coat

1. The structure of the smooth muscle fibres in the longitudinal muscle coat of the body wall of Lumbricus terrestris has been investigated by phase contrast light microscopy and electron microscopy. 2. The muscle fibre is ribbon-shaped, and attached to each of its two surfaces is a set of myofibrils. These are also ribbon-shaped, and they lie with their surfaces perpendicular to the surfaces of the fibre, and their inner edges nearly meeting in the middle of the fibre. These fibrils are oriented at an angle to the fibre axis, and diminish greatly in width as they approach the edge of the fibre. The orientation of the set of fibrils belonging to one surface of the fibre is the mirror image of that of the set belonging to the other surface; thus, when both sets are in view in a fibre lying flat on one face, the fibre exhibits double oblique striation. A comparison of extended and contracted fibres indicates that as the fibre contracts, the angle made between fibre and fibril axes increases (e.g. from 5 to 30°) and so does the angle made between the two sets of fibrils (e.g. from 10 to 60°). 3. The myofibril, throughout its length, contains irregularly packed filaments, commonly 250 A in diameter, which are parallel to its long axis and remain straight in contracted muscles. Between them is material which probably consists of much finer filaments. Thus A and I bands are absent. 4. Bound to one face of each fibril, but not penetrating inside it, is a regularly spaced series of transverse stripes. They are of two kinds, alternating along the length of the fibril, and it is suggested that they are comparable to the Z and M lines of a cross-striated fibril. The spacing of these stripes is about 0.5 µ ("Z" to "Z") in extended muscles, and 0.25 µ in contracted muscles. A bridge extends from each stripe across to the stripeless surface of the next fibril.

Plasticity in smooth muscle, a hypothesis

1994 ◽  
Vol 72 (11) ◽  
pp. 1320-1324 ◽  
Author(s):  
Lincoln E. Ford ◽  
Chun Y. Seow ◽  
Victor R. Pratusevich
Keyword(s):  
Smooth Muscle ◽  
Preliminary Finding ◽  
Muscle Length ◽  
Shortening Velocity ◽  
Thin Filaments ◽  
Thick Filaments ◽  
Initial Hypothesis ◽  
In Series ◽  
Cross Bridges ◽  
Muscle Myosin

The controversial finding that the thick filaments of smooth muscle can be evanescent leads to the hypothesis that the large functional range of this muscle is accommodated by plastic rearrangements that place more thick filaments in series at longer lengths. Our preliminary finding that the shortening velocity and compliance of dog tracheal muscle were strongly dependent on adapted muscle length, while force was much less length dependent, supports this hypothesis (V.R. Pratusevich, C.Y. Seow, and L.E. Ford. Biophys. J. 66: A139, 1994). The hypothesis leads to two further corollaries. The first is that the lengthening of the thick filaments that must accompany their reformation will cause a series to parallel transition: fewer long filaments span the muscle length, but the longer filaments have more cross bridges acting in parallel. The second is that there is more than one activating mechanism in smooth muscle. It is known that myosin light chain phosphorylation activates the actomyosin ATPase, but this same phosphorylation also causes a structural change that facilitates filament formation. The consideration that the unaggregated, phosphorylated myosin must be prevented from competing with myosin in thick filaments and hydrolyzing ATP suggests that there must be a second mechanism that must allow the thin filaments to interact selectively with filamentous myosin. This need for a second activating mechanism may explain the presence of tropomyosin, calponin, and caldesmon on thin filaments. Although the two corollaries follow from the initial hypothesis, it should be emphasized that the three are not mutually dependent, and that the proof or disproof of any one of them would not prove or disprove the others.Key words: smooth muscle, myosin, thick filaments, contraction.

scholarly journals Bridgelike interconnections between thick filaments in stretched skeletal muscle fibers observed by the freeze-fracture method.

1986 ◽  
Vol 102 (3) ◽  
pp. 1093-1098 ◽  
Author(s):  
S Suzuki ◽  
G H Pollack
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibers ◽  
Freeze Fracture ◽  
Thick Filament ◽  
Rapid Freezing ◽  
Semitendinosus Muscle ◽  
Thin Filaments ◽  
Thick Filaments ◽  
Cross Bridges ◽  
Half Length

The ultrastructure of frog semitendinosus muscle was explored using the freeze-fracture, deep-etch, rotary-shadowing technique. Mechanically skinned fibers were stretched to decrease or eliminate the overlap of thick and thin filaments before rapid freezing with liquid propane. In relaxed, contracting, and rigor fibers, a significant number of bridgelike interconnections, distinct from those observed in the M-region, were observed between adjacent thick filaments in the non-overlap region. Their half-length and diameter corresponded approximately to the known dimensions of the cross-bridge (or myosin S-1). The interconnection may thus be formed by the binding of two apposed cross-bridges projecting from adjacent thick filaments. Fixation with 0.5% glutaraldehyde for 5-10 min before freezing effectively preserved these structures. The results indicate that the interconnections are genuine structures that appear commonly in stretched muscle fibers. They may play a role in stabilizing the thick filament lattice, and possibly in the contractile process.

scholarly journals Series Elasticity in Frog Muscle as Revealed by Optical Diffraction

1982 ◽  
Vol 35 (6) ◽  
pp. 617
Author(s):  
Julian A Barden ◽  
Peter Mason
Keyword(s):  
Sarcomere Length ◽  
Striated Muscle ◽  
Small Population ◽  
Frog Muscle ◽  
Optical Diffraction ◽  
Muscle Fibres ◽  
Series Elasticity ◽  
Thick Filaments ◽  
Cross Bridges ◽  
Made In

Using an optical diffraction technique, the series elasticity of frog striated muscle fibres was investigated. One source of series elasticity was located in the cross-bridges during the application of either quick stretches or releases of muscle fibres. Evidence is presented here for a second component attributable to a small population of slowly activated sarcomeres. The size of the second component was progressively reduced until it virtually disappeared at a sarcomere length of 3 pm. A third component appears to reside in the thick filaments. Calculation of the elastic energy in the muscle fibres enabled an identification of the source of the energy to be made in terms of the components of the series elasticity. Evidence is presented of a short-range elastic component present in resting fibres.

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