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At least 595 records · Page 33Linked to original sources

PubMed1989

Observation of Brillouin scattering from single muscle fibres.

The propagation of sound waves along relaxed single fibres of glycerinated rabbit psoas muscle has been observed using Brillouin scattering at frequencies up to 1.6 GHz. Two types of waves were observed: one with a velocity of 1508 +/- 7 m s-1, which is attributed to sound waves in intra-cellular saline, the other with a velocity of 912 +/- 25 m s-1, which is attributed to waves propagating along the protein filaments within individual sarcomeres. The latter sound velocity is much higher than that which has been reported by Stienen and Blangé (1985) for 50 microseconds tension transients, and the difference is attributed to the much higher stiffness of the protein filaments compared to the cross-bridges which determine the low-frequency elasticity of muscle fibres.

Acoustics↗

PubMed1986

Phosphate burst in permeable muscle fibers of the rabbit.

The transient kinetics of ATP hydrolysis in chemically skinned psoas muscle fibers of the rabbit have been measured. Muscles fibers in the rigor state (absence of nucleotide) were relaxed rapidly by the photochemical release of [2-3H]ATP from caged-ATP (P3-1-(2-nitro)phenylethyl[2-3H]adenosine 5'-triphosphate) in the absence of calcium ions. Rapid freezing of the fiber to stop hydrolysis, followed by analysis of the tritiated nucleotide content allowed the course of the hydrolysis to be determined. The timecourse of ATP hydrolysis was biphasic, with an initial rapid phase occurring at a rate of approximately 60 s-1 at 12 degrees C for fibers exposed to greater than 0.7 mM ATP. The amplitude of the rapid phase was as previously reported (Ferenczi, M. A., E. Homsher, and D. R. Trentham, 1984, J. Physiol. (Lond.)., 352:575-599).

Adenosine Diphosphate↗

PubMed1977

Purification and characterization of human muscle pyruvate kinase.

The M1 isozyme of pyruvate kinase has been purified from human psoas muscle in a seven-step procedure. Fractionation by ammonium sulfate precipitation, heat treatment, acetone precipitation, diethylaminoethyl cellulose batchwise treatment followed by chromatography on carboxymethyl cellulose and Sephadex G-200 gave a product with a specific activity of 383 U/mg representing a 294-fold purification with a yield of 11%. The product formed orthorhombic crystals and was homogeneous on polyacrylamide gel electrophoresis with and without sodium dodecyl sulfate, sedimentation velocity, sedimentation equilibrium, and immunodiffusion. The purified enzyme has a molecular weight of 240700 and has a sedimentation coefficient (S20,W) of 10.04S. It contains four subunits with identical molecular weights of 61000. No free N-terminal amino acids could be detected. Antibody prepared against the purified human M1 isozyme does not cross-react by immunodiffusion or enzyme inactivation with the human erythrocyte isozyme and in the reverse experiment antibody prepared against human erythrocyte pyruvate kinase does not cross-react with the purified M1 isozyme. The amino acid composition of the M1 isozyme is presented.

Amino Acids↗

PubMed1986

Oxygen exchange between Pi in the medium and water during ATP hydrolysis mediated by skinned fibers from rabbit skeletal muscle. Evidence for Pi binding to a force-generating state.

Oxygen exchange between (18O4)Pi in the medium and water accompanies ATP hydrolysis catalyzed by the calcium-regulated MgATPase of vertebrate skeletal muscle. Exchange was observed in chemically skinned fibers from rabbit psoas muscle held isometrically and activated by 30 microM free Ca2+. The rate of exchange was approximately proportional to Pi concentration (up to 10 mM) and was characterized by an apparent second order rate constant greater than or equal to 475 M-1 S-1 (pH 7.1, ionic strength 0.2 M, 22 degrees C). Much less exchange occurred in the absence of Ca2+ or when ATP was replaced by ADP. It has been inferred from mechanical experiments that Pi can bind to a force-generating ADP-bound state of actomyosin with resultant suppression of force (Hibberd, M. G., Dantzig, J. A., Trentham, D. R., and Goldman, Y. E. (1985) Science 228, 1317-1319). The oxygen exchange results support this inference by providing direct evidence that Pi in the medium binds at the ATPase catalytic site in activated isometric fibers. The inter-relationship of these two effects involving Pi on mechanochemical coupling in muscle is discussed.

Adenosine Diphosphate↗

PubMed1987

[An unusual clinical variant of pubic pain in females: the case of an athlete].

Gynaecological types of pain in high-powered sportswomen can be of traumatic origin (bony, muscular or cartilaginous) in the region around the pubis. A case of vaginal pain which proved to be due to adductor tendinitis in the hip in a long distance walker is described. A review of the differential diagnosis of gynaecological pain that can occur in sportswomen is carried out. These consist of instability in the symphysis of the pubis as well as muscular lesions of the abdominal muscles of the hip adductors and of the ilio-psoas muscles. In addition, stress fractures of the pubic rami as well as inflammation of the symphysis due to stress, and pubic osteomyelitis are described.

Female↗

PubMed1994

Non-spinal psoas abscess due to Mycobacterium tuberculosis in a patient with acquired immunodeficiency syndrome: report of a case.

Of the 36 patients with human immunodeficiency virus (HIV) infection admitted to our institution since 1985, one had a non-spinal psoas abscess due to Mycobacterium tuberculosis without pulmonary involvement. A 32-year-old male homosexual had prolonged fever and weight loss for two months. Serologic tests for antibodies against HIV were positive. A characteristic hypodense lesion within the right psoas muscle was noted by computerized tomographic (CT) scanning. Diagnosis of psoas abscess was confirmed by ultrasound-guided needle aspiration. The smear of the aspirated pus showed numerous acid-fast bacilli and cultures grew M. tuberculosis. The lesion responded rapidly to antituberculous therapy and a follow-up CT scan 10 months later showed improvement.

AIDS-Related Opportunistic Infections↗

PubMed2001

Nucleotide binding induces global and local structural changes of myosin head in muscle fibres.

Thermal stability and internal dynamics of myosin heads in fiber bundles from rabbit psoas muscle has been studied by electron paramagnetic resonance (EPR) spectroscopy and differential scanning calorimetry (DSC). Using ADP, ATP and orthovanadate (V(i)), three intermediate states of the ATP hydrolysis cycle were simulated in glycerinated muscle fibers. DSC transitions contained three overlapping endotherms in each state. Deconvolution showed that the transition temperature of 58.4 degrees C was almost independent of the intermediate state of myosin, while nucleotide binding shifted the melting temperatures of 54.0 and 62.3 degrees C, and changed the enthalpies. These changes suggest global rearrangements of the internal structure in myosin head. In the presence of ADP and ADP plus V(i), the conventional EPR spectra showed changes in the ordering of the probe molecules, suggesting local conformational and motional changes in the internal structure of myosin heads. Saturation transfer EPR measurements reported increased rotational mobility of spin labels in the presence of ATP plus orthovanadate corresponding to a weakly binding state of myosin to actin.

Adenosine Diphosphate↗

PubMed1991

Force, length, and Ca(2+)-troponin C affinity in skeletal muscle.

On the basis of isotopic methods it has been found that force generation promotes increased Ca2+ binding to troponin C in cardiac muscle [P. Hofmann and F. Fuchs. Am. J. Physiol. 253 (Cell Physiol. 22): C541-C546, 1987] but not in skeletal muscle (J. Muscle Res. Cell Motil. 6: 477, 1985). However, studies with skinned rabbit psoas muscle fibers containing substituted fluorescent troponin C analogues indicate that force-generating cross bridges do promote increased Ca2+ binding in skeletal muscle (K. Güth and J. D. Potter. J. Biol. Chem. 262: 13627-13635, 1987). We have reexamined this question using a modified contraction-relaxation protocol in which Ca2+ binding to detergent-treated rabbit psoas fibers was measured either during steady-state force development or after relaxation was induced by one of two myosin ATPase inhibitors, vanadate or 2,3-butanedione monoxime. A standard double-isotope technique was used to measure Ca2+ binding. Another set of experiments was done in which force was reduced by releasing muscle fibers from sarcomere lengths of 2.4-2.6 microns to 1.5-1.7 microns, and bound Ca2+ was determined either before or after the release. No statistically significant effect of force generation or sarcomere length on Ca(2+)-troponin C affinity was observed. Thus the discrepancy remains between results obtained with isotopic and fluorescence methods. It is possible that in skinned fibers emission from fluorescence probes is more closely related to protein-protein interactions than to the amount of Ca2+ bound to troponin C.

Animals↗

PubMed1995

The role of the psoas and iliacus muscles for stability and movement of the lumbar spine, pelvis and hip.

The activation patterns of the psoas and iliacus muscles were investigated in 7 healthy adult subjects (4 men and 3 women) during a variety of motor tasks in standing, sitting and lying. Myoelectric activity was recorded simultaneously from the 2 muscles using thin wire electrodes inserted under guidance of high-resolution ultrasound. In general, both muscles were coactivated, albeit to different relative levels, particularly when hip flexor torque was required. Selective activation of the iliacus could, however, be seen to stabilize the pelvis in contralateral hip extension during standing. Psoas was found to be selectively involved in sitting with a straight back and in contralateral loading situations requiring stabilization of the spine in the frontal plane. During training exercises from a supine position, such as sit-ups, the contribution of the psoas and iliacus muscles could be varied by changing the range of motion as well as the position and support for the legs. Thus, the 2 anatomically different muscles of the iliopsoas complex were shown to have individual and task-specific activation patterns depending on the particular demands for stability and movement at the lumbar spine, pelvis and hip.

Adult↗

PubMed1993

Effects of pressure on equatorial x-ray fiber diffraction from skeletal muscle fibers.

When skeletal muscle fibers are subjected to a hydrostatic pressure of 10 MPa (100 atmospheres), reversible changes in tension occur. Passive tension from relaxed muscle is unaffected, rigor tension rises, and active tension falls. The effects of pressure on muscle structure are unknown: therefore a pressure-resistant cell for x-ray diffraction has been built, and this paper reports the first study of the low-angle equatorial patterns of pressurized relaxed, rigor, and active muscle fibers, with direct comparisons from the same chemically skinned rabbit psoas muscle fibers at 0.1 and 10 MPa. Relaxed and rigor fibers show little change in the intensity of the equatorial reflections when pressurized to 10 MPa, but there is a small, reversible expansion of the lattice of 0.7 and 0.4%, respectively. This shows that the order and stability of the myofilament lattice is undisturbed by this pressure. The rise in rigor tension under pressure is thus probably due to axial shortening of one or more components of the sarcomere. Initial results from active fibers at 0.1 MPa show that when phosphate is added the lattice spacing and equatorial intensities change toward their relaxed values. This indicates cross-bridge detachment, as expected from the reduction in tension that phosphate induces. 10 MPa in the presence of phosphate at 11 degrees C causes tension to fall by a further 12%, but not change is detected in the relative intensity of the reflections, only a small increase in lattice spacing. Thus pressure appears to increase the proportion of attached cross-bridges in a low-force state.

Animals↗

PubMed1993

Calcium-independent activation of skeletal muscle fibers by a modified form of cardiac troponin C.

A conformational change accompanying Ca2+ binding to troponin C (TnC) constitutes the initial event in contractile regulation of vertebrate striated muscle. We replaced endogenous TnC in single skinned fibers from rabbit psoas muscle with a modified form of cardiac TnC (cTnC) which, unlike native cTnC, probably contains an intramolecular disulfide bond. We found that such activating TnC (aTnC) enables force generation and shortening in the absence of calcium. With aTnC, both force and shortening velocity were the same at pCa 9.2 and pCa 4.0. aTnc could not be extracted under conditions which resulted in extraction of endogenous TnC. Thus, aTnC provides a stable model for structural studies of a calcium binding protein in the active conformation as well as a useful tool for physiological studies on the primary and secondary effects of Ca2+ on the molecular kinetics of muscle contraction.

Animals↗

PubMed1996

Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts.

Recent studies have suggested that activation of the ubiquitin-proteasome pathway is primarily responsible for the rapid loss of muscle proteins in various types of atrophy. The present studies were undertaken to test if different classes of muscle proteins are degraded by this pathway. In extracts of rabbit psoas muscle, the complete degradation of soluble proteins to amino acids was stimulated up to 6-fold by ATP. Peptide aldehyde inhibitors of the proteasome or the removal of proteasomes markedly inhibited only the ATP-dependent process. Addition of purified myosin, actin, troponin, or tropomyosin to these extracts showed that these proteins served as substrates for the ubiquitin-proteasome pathway. By contrast, degradation of myoglobin did not require ATP, proteasomes, or any known proteases in muscles. When myosin, actin, and troponin were added as actomyosin complexes or as intact myofibrils to these extracts, they were not hydrolyzed at a significant rate, probably because in these multicomponent complexes, these proteins are protected from degradation. Accordingly, actin (but not albumin or troponin) inhibited the degradation of 125I-myosin, and actin was found to selectively inhibit ubiquitin conjugation to 125I-myosin. Also, the presence of tropomyosin inhibited the degradation of 125I-troponin. However, neither actin nor tropomyosin inhibited the degradation of 125I-lysozyme or soluble muscle proteins. Thus, specific interactions between the myofibrillar proteins appear to protect them from ubiquitin-dependent degradation, and the rate-limiting step in their degradation is probably their dissociation from the myofibril.

Adenosine Triphosphate↗

PubMed1981

Surgical technique of hemipelvectomy in the lateral position.

Hemipelvectomy is most frequently indicated for sarcoma of the upper thigh, hip, or pelvis. With the patient in the lateral position the incision is made through the anterior abdominal wall, and the iliac vessels are dissected free and divided just distal to the aortic bifurcation. The multiple visceral branches of the internal iliac vessels are divided and ligated to expose the sacral nerve roots deep within the pelvis. The posterior skin flap is dissected free and the gluteus maximus muscle severed from its origin on the sacrum. Back muscles are detached from the wing of the ilium and the psoas muscle with accompanying obturator and femoral nerves is divided. The pelvis begins to open as the symphysis pubis is divided. Next the sacral nerve roots are divided and anterior capsule of the sacroiliac joint. The muscles and ligaments of the pelvic floor are severed including the urogenital diaphragm, levator ani muscle, sacrotuberous ligament, and sacrospinalis ligament. The specimen is released by severing the sacroiliac joint posteriorly. The operative defect is closed by suturing gluteal fascia to inguinal ligament over suction drains.

Amputation, Surgical↗

PubMed1978

On the relation between filament overlap and the number of calcium-binding sites on glycerinated muscle fibers.

The formation of rigor complexes between the thick and thin filaments of glycerinated rabbit psoas muscle fibers causes the fibers to bind more calcium at any given level of free calcium. I studied the maximum amount of calcium bound as a function of filament overlap under rigor conditions. Fibers stretched to zero filament overlap (sarcomere length greater than 3.8 micron) bound exactly 75% as much calcium as fibers with maximum overlap. Between these extremes a linear relationship was found between maximum bound calcium and the length of the overlap zone. The results support the hypothesis that in the intact filament lattice one of the four calcium-binding sites of troponin depends for its existence on attachment between myosin and actin. In addition, the linear relation between maximum bound calcium and filament overlap is consistent with the assumption that the cooperative effect of rigor complex formation on calcium binding is limited to the binding site in the immediate vicinity of the rigor complex.

Animals↗

PubMed1975

Birefringence changes in vertebrate striated muscle.

The changes in birefringence in the rigor to relax transition of single Triton-extracted rabbit psoas muscle fibers have been investigated. The total birefringence of rigor muscle fibers was dependent on sarcomere length and ranged from (1.46 +/- 0.08) X 10(-3) to (1.60 +/- 0.06) X 10(-3) at sarcomere lengths from 2.70 mum to 3.40 mum. An increase in total birefringence was measured dependent on sarcomere length when 55 single fibers were relaxed from the rigor state with Mg-ATP. Pyrophosphate relaxation produced a smaller increase in retardation when compared to Mg-ATP. The expected change in intrinsic birefringence during the rigor to relax transition was calculated assuming a hinge function of the subfragment 2 moiety of myosin. The changes in birefringence during isometric contraction and relaxation have been discussed in relation to possible structural changes.

Adenosine Triphosphate↗

PubMed1998

Fluorescence of NBD-labelled troponin-I as a probe for the kinetics of thin filament activation in skeletal muscle fibers.

Using fluorescence of NBD-labelled troponin I incorporated into skinned fibers of the rabbit psoas muscle by chasing native troponin by troponin with the NBD-labelled TnI subunit we attempted to study kinetics of thin filament activation at different Ca(++)-concentrations. Since fluorescence of NBD-labelled TnI is sensitive to both, changes in Ca++, and strong cross-bridge attachment, we were able to induce changes thin filament activation by rapidly dropping the fraction of strongly attached cross-bridges to very low levels, e.g. by switching from isometric to isotonic contraction conditions. At any [Ca++], the time course of the resulting changes in fluorescence of NBD-labelled TnI was found at least an order of magnitude faster than the time course of force redevelopment subsequent to the period of isotonic contraction. Modelling shows that with the kinetics of thin filament activation derived from these studies, common kinetic schemes of the actomyosin ATPase predict regulation to act via changes in cross-bridge cycling kinetics, as we had previously proposed.

Animals↗

PubMed1997

Strain-dependent modulation of phosphate transients in rabbit skeletal muscle fibers.

When inorganic phosphate (Pi) is photogenerated from caged Pi during isometric contractions of glycerinated rabbit psoas muscle fibers, the released Pi binds to cross-bridges and reverses the working stroke of cross-bridges. The consequent force decline, the Pi-transient, is exponential and probes the kinetics of the power-stroke and Pi release. During muscle shortening, the fraction of attached cross-bridges and the average strain on them decreases (Ford, L. E., A.F. Huxley, and R.M. Simmons, 1977. Tension responses to sudden length change in stimulated frog muscle fibers near slack length. J. Physiol. (Lond.). 269:441-515; Ford, L. E., A. F. Huxley, and R.M. Simmons, 1985. Tension transients during steady state shortening of frog muscle fibers. J. Physiol. (Lond.). 361:131-150. To learn to what extent the Pi transient is strain dependent, muscle fibers were activated and shortened or lengthened at a fixed velocity during the photogeneration of Pi. The Pi transients observed during changes in muscle length showed three primary characteristics: 1) during shortening the Pi transient rate, Kpi, increased and its amplitude decreased with shortening velocity; Kpi increased linearly with velocity to > 110 s-1 at 0.3 muscle lengths per second (ML/s). 2) At a specific shortening velocity, increases in [Pi] produce increases in Kpi that are nonlinear with [Pi] and approach an asymptote. 3) During forced lengthening Kpi and the amplitude of the Pi transient are little different from the isometric contractions. These data can be approximated by a strain-dependent three-state cross-bridge model. The results show that the power stroke's rate is strain-dependent, and are consistent with biochemical studies indicating that the rate-limiting step at low strains is a transition from a weakly to a strongly bound cross-bridge state.

Animals↗

PubMed1998

ATP analogs and muscle contraction: mechanics and kinetics of nucleoside triphosphate binding and hydrolysis.

The mechanical behavior of skinned rabbit psoas muscle fiber contractions and in vitro motility of F-actin (Vf) have been examined using ATP, CTP, UTP, or their 2-deoxy forms (collectively designated as nucleotide triphosphates or NTPs) as contractile substrates. Measurements of actin-activated heavy meromyosin (HMM) NTPase, the rates of NTP binding to myosin and actomyosin, NTP-mediated acto-HMM dissociation, and NTP hydrolysis by acto-HMM were made for comparison to the mechanical results. The data suggest a very similar mechanism of acto-HMM NTP hydrolysis. Whereas all NTPs studied support force production and stiffness that vary by a factor 2 or less, the unloaded shortening velocity (Vu) of muscle fibers varies by almost 10-fold. 2-Deoxy ATP (dATP) was unique in that Vu was 30% greater than with ATP. Parallel behavior was observed between Vf and the steady-state maximum actin-activated HMM ATPase rate. Further comparisons suggest that the variation in force correlates with the rate and equilibrium constant for NTP cleavage; the variations in Vu or Vf are related to the rate of cross-bridge dissociation caused by NTP binding or to the rate(s) of product release.

Acid Anhydride Hydrolases↗