scholarly journals Quantitative studies on the polarization optical properties of striated muscle. I. Birefringence changes of rabbit psoas muscle in the transition from rigor to relaxed state.

1976 ◽  
Vol 68 (3) ◽  
pp. 497-511 ◽  
Author(s):  
D L Toylor
Keyword(s):  
Striated Muscle ◽  
Polarized Light ◽  
Psoas Muscle ◽  
Maximum Increase ◽  
Rabbit Psoas ◽  
Form Birefringence ◽  
Quantitative Studies ◽  
Relaxation Solution ◽  
Myosin Filaments ◽  
Rigor Solution

The changes in birefringence in the rigor to relax transition of single triton-extracted rabbit psoas muscle fibers have been investigated with quantitative polarized light techniques. The total birefringence of rest lenght fibers in rigor was (1.46 +/- 0.08) x 10(-3) and increased to (1.67 +/- 0.05) x 10(-3) after Mg-ATP relaxation. Pyrophosphate relaxation increased the total birefringence only slightly, whereas subsequent Mg-ATP relaxation elicited the maximum increase in birefringence. Changes in lattice spacing did not account for the total increase in birefrigence during relaxation. Moreover, the increase in total birefringence was attributable to increases in intrinsic birefringence as well as form birefringence. No change in birefringence was exhibited upon exposure to a relaxation solution after myosin extraction. Synthetic myosin filaments were prepared and treated with relaxation and rigor solutions. The negatively stained filaments treated with a rigor solution had gross irregular projections at either end, while the filaments treated with a relaxing solution were more spindle shaped. The results are compatible with the view that the subfragment-2 moieties of myosin angle away from the myosin aggregates (light meromyosin) to permit the attachment of the subfragment-1 moieties to actin.

scholarly journals Differences in the Charge Distribution of Glycerol-Extracted Muscle Fibers in Rigor, Relaxation, and Contraction

1974 ◽  
Vol 64 (5) ◽  
pp. 551-567 ◽  
Author(s):  
Suzanne M. Pemrick ◽  
Charles Edwards
Keyword(s):  
Charge Distribution ◽  
Sarcomere Length ◽  
Muscle Fibers ◽  
Psoas Muscle ◽  
Nonlinear Relationship ◽  
Thin Filaments ◽  
Rabbit Psoas ◽  
Relaxation Solution ◽  
The Difference ◽  
Rest Length

Glycerol-extracted rabbit psoas muscle fibers were impaled with KCl-filled glass microelectrodes. For fibers at rest-length, the potentials were significantly more negative in solutions producing relaxation than in solutions producing either rigor or contraction; further the potentials in the latter two cases were not significantly different. For stretched fibers, with no overlap between thick and thin filaments, the potentials did not differ in the rigor, the relaxation, or the contraction solutions. The potentials measured from fibers in rigor did not vary significantly with the sarcomere length. For relaxed fibers, however, the potential magnitude decreased with increasing sarcomere length. The difference between the potentials measured for rigor and relaxed fibers exhibited a nonlinear relationship with sarcomere length. The potentials from calcium-insensitive fibers were less negative in both the rigor and the relaxation solutions than those from normal fibers. When calcium-insensitive fibers had been incubated in Hasselbach and Schneider's solution plus MgCl2 or Guba-Straub's solution plus MgATP the potentials recorded upon impalement were similar in the rigor and the relaxation solution to those obtained from normal fibers in the relaxed state. It is concluded that the increase in the negative potential as the glycerinated fiber goes from rigor to relaxation may be due to an alteration in the conformation of the contractile proteins in the relaxed state.

scholarly journals ANOMALOUS CONTRACTION OF INVERTEBRATE STRIATED MUSCLE

1965 ◽  
Vol 27 (3) ◽  
pp. 639-649 ◽  
Author(s):  
R. E. Stephens
Keyword(s):  
Mass Distribution ◽  
Striated Muscle ◽  
Psoas Muscle ◽  
Homarus Americanus ◽  
Limulus Polyphemus ◽  
Polarization Microscopy ◽  
Trypsin Treatment ◽  
Rabbit Psoas ◽  
Ultraviolet Microbeam ◽  
Intrinsic Birefringence

The phenomenon of A band shortening or contraction has been investigated in glycerinated myofibrils of Pecten irradians, Homarus americanus, Cambarus virilis, and Limulus polyphemus through the techniques of ultraviolet microbeam inactivation and polarization microscopy. With the former method, it has been shown that these muscles, even though exhibiting the shortening effect, contract in a manner consistent with only the sliding filament model. Intrinsic birefringence studies have indicated no significant changes in mass distribution or orientation within the shortened A bands. Except in the case of Limulus muscle, the shortening effect was seen only in contraction under tension. The magnitude of this anomalous phenomenon was dependent upon glycerination time and has been duplicated in rabbit psoas muscle through brief trypsin treatment. A band shortening could not be observed in glutaraldehyde-fixed muscle or in myofibrils glycerinated for only short periods. It has been concluded that the phenomenon of A band contraction is an artifact induced by the glycerination procedure, possibly through weakening of the sarcomere structure. However, the fact that the A band shortens under tension rather than lengthens poses an interesting paradox.

scholarly journals Variations of the Contractile Apparatus in Smooth and Striated Muscles

1967 ◽  
Vol 50 (6) ◽  
pp. 171-184 ◽  
Author(s):  
G. F. Elliott
Keyword(s):  
Smooth Muscle ◽  
Sarcomere Length ◽  
Striated Muscle ◽  
Structural Information ◽  
Psoas Muscle ◽  
Colloidal System ◽  
Active Living ◽  
Striated Muscles ◽  
Contractile Apparatus ◽  
Myosin Filaments

Structural information is presented for three muscle systems—mammalian smooth muscle at rest and partially active, living toad striated muscle at rest and contracting, and glycerinated rabbit psoas muscle under various conditions of pH and ionic environment. In the smooth muscle no evidence of organized myosin filaments has been found. In the striated muscle the myosin-to-actin distance can vary widely, according to sarcomere length and to muscle treatment, both at rest and during contraction. In the discussion it is suggested that muscle should be considered as a colloidal system and that there need not necessarily be any chemical bonding (cross-linking) involved in the contractile process.

scholarly journals QUANTITATIVE AND HISTOCHEMICAL STUDIES ON THE DESORPTION AND READSORPTION OF ALDOLASE IN CROSS-STRIATED MUSCLE

1969 ◽  
Vol 17 (5) ◽  
pp. 314-320 ◽  
Author(s):  
H. ARNOLD ◽  
J. NOLTE ◽  
D. PETTE
Keyword(s):  
Enzyme Activity ◽  
Actin Filaments ◽  
Phosphate Buffer ◽  
Striated Muscle ◽  
Psoas Muscle ◽  
Histochemical Staining ◽  
Intracellular Location ◽  
Successive Extraction ◽  
Complete Extraction

Complete extraction of aldolase from minced rabbit psoas muscle was achieved by successive extraction steps in 0.1 M phosphate buffer. Aldolase was then readsorbed quantitatively to the depleted myofibrils. Extraction, readsorption and a final redsorption of the enzyme were followed quantitatively by enzyme activity determinations and qualitatively by histochemical staining of aldolase. The intracellular location of the readsorbed enzyme was found to be identical with that of aldolase in native muscle. In both cases, aldolase was localized within the isotropic bands. These results as well as the previously demonstrated binding of the enzyme to F-actin suggest that aldolase is located within the interfilamentary sarcoplasm of the isotropic bands and is probably also bound in vivo to the actin filaments.

scholarly journals Phosphate has dual roles in cross-bridge kinetics in rabbit psoas single myofibrils

2021 ◽  
Vol 153 (3) ◽  
Author(s):  
Masataka Kawai ◽  
Robert Stehle ◽  
Gabriele Pfitzer ◽  
Bogdan Iorga
Keyword(s):  
Rate Constants ◽  
Striated Muscle ◽  
Intrinsic Rate ◽  
Isometric Tension ◽  
Force Generation ◽  
Skinned Fibers ◽  
Sinusoidal Analysis ◽  
Rabbit Psoas ◽  
Cross Bridge

In this study, we aimed to study the role of inorganic phosphate (Pi) in the production of oscillatory work and cross-bridge (CB) kinetics of striated muscle. We applied small-amplitude sinusoidal length oscillations to rabbit psoas single myofibrils and muscle fibers, and the resulting force responses were analyzed during maximal Ca2+ activation (pCa 4.65) at 15°C. Three exponential processes, A, B, and C, were identified from the tension transients, which were studied as functions of Pi concentration ([Pi]). In myofibrils, we found that process C, corresponding to phase 2 of step analysis during isometric contraction, is almost a perfect single exponential function compared with skinned fibers, which exhibit distributed rate constants, as described previously. The [Pi] dependence of the apparent rate constants 2πb and 2πc, and that of isometric tension, was studied to characterize the force generation and Pi release steps in the CB cycle, as well as the inhibitory effect of Pi. In contrast to skinned fibers, Pi does not accumulate in the core of myofibrils, allowing sinusoidal analysis to be performed nearly at [Pi] = 0. Process B disappeared as [Pi] approached 0 mM in myofibrils, indicating the significance of the role of Pi rebinding to CBs in the production of oscillatory work (process B). Our results also suggest that Pi competitively inhibits ATP binding to CBs, with an inhibitory dissociation constant of ∼2.6 mM. Finally, we found that the sinusoidal waveform of tension is mostly distorted by second harmonics and that this distortion is closely correlated with production of oscillatory work, indicating that the mechanism of generating force is intrinsically nonlinear. A nonlinear force generation mechanism suggests that the length-dependent intrinsic rate constant is asymmetric upon stretch and release and that there may be a ratchet mechanism involved in the CB cycle.

Calcium regulation of the contractile state of isolated mammalian fibroblast cytoplasm

1975 ◽  
Vol 18 (2) ◽  
pp. 241-256
Author(s):  
C.S. Izzard ◽  
S.L. Izzard
Keyword(s):  
Plasma Membrane ◽  
Striated Muscle ◽  
Calcium Regulation ◽  
Threshold Concentration ◽  
Free Access ◽  
Contractile State ◽  
Relaxing Solution ◽  
Calcium Dependent ◽  
Rigor Solution

Calcium-dependent contractions have been induced in fresh, naked cytoplasm of L-929 fibroblasts using physiological solutions (rigor, relaxing and contracting) similar to those designed to control the contractile state of vertebrate striated muscle. Free access of solutions to the cytoplasm was achieved by popping and stripping the plasma membrane from cells using 7–10 strokes of a Dounce homogenizer. Contracting solution (free Ca2+ 7 X 10(−5) M; with added MgATP) applied locally from a micropipette to cells popped in rigor (free Ca2+ less than 10(−8) M) or relaxing (free Ca2+ less than 10(−8) M; with added MgATP) solutions induced symmetrical contractions of unstretched cytoplasm and directional shortening of stretched cytoplasm. The contractions produced 12–18% shortenings and were complete in 1–3 s. The cytoplasm could be cycled repeatedly through the contracted state from the relaxed state. Exogenous MgATP was required for the Ca2+-dependent contractions. At low free Ca2+ concentrations (less than 10(−8) M), MgATP had a marked plasticizing effect on the cytoplasm. Thus cytoplasm prepared in relaxing solution was less cohesive and more easily deformed than cytoplasm prepared in rigor solution. When induced to contract, relaxed cytoplasm showed a loss of plasticity. Using this criterion, the threshold concentration of free Ca2+ for contraction was determined to lie between 7 X 10(−8) M and 5 X 10(−7) M.

Sign in / Sign up

Export Citation Format

Share Document