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PubMed1996

Variant slips of psoas and iliacus muscles, with splitting of the femoral nerve.

In bilateral dissections of 68 cadavers, four examples were found unilaterally of variant slips of iliacus and psoas major muscles. In three of them the femoral nerve was pierced by the variant slip. One of these variants was a previously undocumented accessory slip of iliacus, originating from the iliolumbar ligament, passing inferiorly anterior to iliacus, and traversing the femoral nerve; its tendon split to be attached proximally to the lesser trochanter of the femur and distally to an unknown insertion. Such anomalies might cause tension on the femoral nerve resulting in referred pain to the hip and knee joints and to the lumbar dermatomes L2,3 and 4.

Femoral Nerve↗
PubMed1993

Immunologic evidence for three isoforms of AMP deaminase (AMPD) in mature skeletal muscle.

Four rabbit polyclonal antisera to purified AMP deaminase (AMPD) isozymes were used to precipitate homogenate AMPD activity from dissected gracilis, soleus and gastrocnemius muscles of the cat, rabbit, rat, mouse, Rhesus monkey, human and toad. The antisera were also tested against other unusual muscles: autonomically innervated striated muscle of the upper esophagus (UEM), skeletal muscle of patients with myo-AMPD deficiency and extraocular muscles (EOM) of humans and Rhesus monkeys. The reference antiserum, M, prepared against human psoas muscle AMPD, precipitated > 90% AMPD from all primate skeletal muscles tested, and from type-2 muscles of all mammals tested, but < 75% from cat and rodent soleus, toad gastrocnemius and primate UEM, EOM and myo-AMPD deficient muscles. Thus, a second isozyme was clearly indicated. Antibody B, against rat liver and kidney AMPD, had no effect with any muscle specimen. Antibody C, against rat heart AMPD, produced additive precipitation of AMPD from soleus of rat and mouse, while antibody E1, against human red cell (and heart) AMPD, produced additive AMPD precipitation from toad gastrocnemius, cat soleus and muscles of several AMPD-deficient humans. A second AMPD isozyme thus accounted for as much as 25% of total activity in some animal red muscles, but no more than 5% in human mixed muscles. At least one more isozyme is needed to account for muscle AMPD unreactive with all antibodies tested in rabbit soleus, toad gastrocnemius and primate UEM and EOM. A list is appended of the approximate AMPD activity in various human cells and tissues.

AMP Deaminase↗
PubMed1993

A single order-disorder transition generates tension during the Huxley-Simmons phase 2 in muscle.

Increasing temperature was used to progressively interconvert non-force-generating into force-generating states in skinned rabbit psoas muscle fibers contracting isometrically. Laser temperature-jump and length-jump experiments were used to characterize tension generation in the time domain of the Huxley-Simmons phase 2. In our experiments, phase 2 is subdivisible into two kinetic steps each with quite different physical properties. The fast kinetic component has rate constant of 950 s-1 at 1 degrees C and a Q10 of approximately 1.2. Its rate is tension insensitive and its normalized amplitude declines with rising temperature--behavior that closely parallels the instantaneous stiffness of the cross-bridge. It is likely that this kinetic step is a manifestation of a damped elastic element/s in the fiber. The slow component of phase 2 is temperature-dependent with a Q10 of approximately 3.0. Its rate is sensitive to tension. Unlike the fast component, its amplitude remains in fixed proportion to isometric tension at different temperatures indicating direct participation in tension generation. Similar T-jump studies on frog fibers are also included. The combined results (frog and rabbit) suggest that tension generation occurs in a single endothermic (entropy driven) step in phase 2.

Animals↗
PubMed1994

X-ray equatorial diffraction during ATP-induced Ca(2+)-free muscle contraction and the effect of ADP.

We examined the equatorial X-ray diffraction of skinned fibers from rat psoas muscle in isometric contraction induced by photorelease of 1.1 mM ATP at 24 degrees C in the absence of Ca2+. At 15-20 ms after release of ATP, tension peaked at 21% of the maximum active tension. From the equatorial intensity ratio (I1,0/I1,1), we estimated the amount of myosin heads associated with actin filaments (A.M) at the tension peak. It was 32% of that in rigor and about half of that in the maximum contraction. ADP (0.7 mM) enhanced the contraction: tension peaked at 47% of the maximum at 25-30 ms. The estimated A.M at this peak was 50% of that in rigor, which was close to that in the maximum contraction. These results indicate that the association of myosin heads with the actin filaments in the Ca(2+)-free contraction is more than expected from the tension size, both in the absence and presence of ADP.

Actins↗
PubMed1988

Muscle cross-bridge attachment: effects on calcium binding and calcium activation.

Data from intact and skinned muscle fibers support the hypothesis that cross-bridge interaction modifies TnC structure and calcium activation. Barnacle single muscle fibers microinjected with the calcium bioluminescent photoprotein, aequorin, show extra light (calcium) when shortened during the declining phase of the calcium transient. The extra calcium is increased by increases in muscle force, and its decline is delayed at higher forces. This extra calcium occurs probably because calcium binding to the activating sites is increased by cross-bridge interaction. In rabbit muscle, TnC structure is modified by cross-bridge interaction, since in skinned rabbit psoas muscle fibers TnC extraction is slower at shorter sarcomere lengths, where cross-bridge attachment is increased. Thus the rigor bridges formed in the extraction solution strengthen the attachment of TnC to the thin filament. Reintroduction of TnC, labeled with fluorescent probes near the Ca specific binding sites (Danzylaziridine-DANZ) and Ca-Mg sites (Rhodamine), into the partially TnC extracted fibers allows us to assess the structural changes (total fluorescence for the DANZ probes, linear dichroism for the RHOD probe) in response to calcium binding and cross-bridge attachment. At sarcomere lengths beyond overlap, calcium binding increases the DANZ-TnC fluorescence and disorders the RHOD-TnC label. At full overlap of filaments, rigor cross-bridges also increase the DANZ-TnC fluorescence and RHOD-TnC disorder. The addition of calcium in rigor increases the DANZ-TnC fluorescence little but causes additional RHOD-TnC disorder, although both fluorescence and disorder are increased further in the presence of calcium plus MgATP. In fibers containing DANZ-TnC, decreasing MgATP in the absence of calcium increases both the force and the fluorescence as rigor cross-bridges activate the muscle. In the presence of calcium, an increase in MgATP to 0.75 microM produces a small fluorescent enhancement, but an increase in MgATP to 10 microM and to 3 mM produces a substantial enhancement. The data imply that calcium activates the thin filament, but that the filament is activated further by rigor cross-bridges. Active cross-bridges activate the thin filament still further. Thus, cross-bridges modify TnC structure and calcium activation, with active cross-bridges being more effective than rigor cross-bridges.

Adenosine Triphosphate↗
PubMedDate not supplied

Identification of the anterior psoas sheath as a landmark for lumbar sympathetic block.

This clinical report demonstrates that identification of the psoas muscle via contrast media injection under fluoroscopy and the subsequent tenting and puncture of the psoas fascia with a 6-inch 22-gauge needle is a definite aid in the correct placement of the needle for lumbar sympathetic block. In ten patients in whom this technique was used, the needle position was subsequently proven to be correctly placed in all cases. The authors conclude that this method is a valuable adjunct in fluoroscopy-guided lumbar sympathetic block.

Autonomic Nerve Block↗
PubMed1986

Relationship of psoas width to osteoporosis.

We have related the radiographic width of the psoas muscle to age, degree of osteoporosis, height, and weight, and to constitution in 234 subjects. The psoas width correlated well with age. When the subjects were grouped according to age, an association was observed between narrowing psoas width and increasing osteoporosis. Narrowing of the psoas was evident some years prior to radiographic evidence of osteoporosis.

Age Factors↗
PubMed2004

Bifunctional rhodamine probes of Myosin regulatory light chain orientation in relaxed skeletal muscle fibers.

The orientation of the regulatory light chain (RLC) region of the myosin heads in relaxed skinned fibers from rabbit psoas muscle was investigated by polarized fluorescence from bifunctional rhodamine (BR) probes cross-linking pairs of cysteine residues introduced into the RLC. Pure 1:1 BR-RLC complexes were exchanged into single muscle fibers in EDTA rigor solution for 30 min at 30 degrees C; approximately 60% of the native RLC was removed and stoichiometrically replaced by BR-RLC, and >85% of the BR-RLC was located in the sarcomeric A-bands. The second- and fourth-rank order parameters of the orientation distributions of BR dipoles linking RLC cysteine pairs 100-108, 100-113, 108-113, and 104-115 were calculated from polarized fluorescence intensities, and used to determine the smoothest RLC orientation distribution-the maximum entropy distribution-consistent with the polarized fluorescence data. Maximum entropy distributions in relaxed muscle were relatively broad. At the peak of the distribution, the "lever" axis, linking Cys707 and Lys843 of the myosin heavy chain, was at 70-80 degrees to the fiber axis, and the "hook" helix (Pro830-Lys843) was almost coplanar with the fiber and lever axes. The temperature and ionic strength of the relaxing solution had small but reproducible effects on the orientation of the RLC region.

Animals↗
PubMed1965

Contractility and ultrastructure in glycerol--extracted muscle fibers. I. The relationship of contractility to sarcomere length.

This study was undertaken to determine whether glycerol-extracted rabbit psoas muscle fibers can develop tension and shorten after being stretched to such a length that the primary and secondary filaments no longer overlap. A method was devised to measure the initial sarcomere length and the ATP-induced isotonic shortening in prestretched isolated fibers subjected to a small preload (0.02 to 0.15 P(0)). At all degrees of stretch, the fiber was able to shorten (60 to 75 per cent): to a sarcomere length of 0.7 micro when the initial length was 3.7 micro or less, and to an increasing length of 0.9 to 1.8 micro with increasing initial sarcomere length (3.8 to 4.4 micro). At sarcomere lengths of 3.8 to 4.5 micro, overlap of filaments was lost, as verified by electron microscopy. The variation in sarcomere length within individual fibers has been assessed by both light and electron microscopic measurements. In fibers up to 10 mm in length the stretch was evenly distributed along the fiber, and with sarcomere spacings greater than 4 micro there was only a slight chance of finding sarcomeres with filament overlap. These observations are in apparent contradiction to the assumption that an overlap of A and I filaments is necessary for tension generation and shortening.

Adenosine Triphosphate↗
PubMed1988

Effect of paratropomyosin on the increase in sarcomere length of rigor-shortened skeletal muscles.

Paratropomyosin is a myofibrillar protein believed to weaken rigor linkages formed between actin and myosin. Using glycerinated fibers of rabbit psoas muscles, we studied the effect of paratropomyosin on the weakening of rigor linkages, which was followed in terms of the increase in sarcomere length of rigor-shortened muscles. The rigor tension developed was reduced to about 65% of the initial value within 10 min after the addition of purified paratropomyosin, whereas it remained constant for at least 3.5 h in control fibers. Paratropomyosin showed a stronger effect on the increase in sarcomere length of passively stretched fibers, which developed weaker rigor-tensions. The purpose of our research was to establish a rigor solution which would best permit the observation of the workings of paratropomyosin. The most successful rigor solution contained 0.2-0.25 M KCl, pH 5.5, at 5-10 degrees C. Under these conditions, the sarcomere length was easily increased from 2.4 to 3.6 micron, if rigor-contracted fibers were passively stretched after the addition of purified paratropomyosin. Because the experimental conditions coincide well with those of postmortem muscles, it is very probable that paratropomyosin plays an important role in restoration of the sarcomere length of rigor-shortened muscles, resulting in tenderization of meat during postrigor ageing.

Animals↗
PubMed1979

In vitro effect of branched chain amino acids on the ribosomal cycle in muscles of fasted rats.

1) The effect of a single i.p injection of branched chain amino acids on ribosomal profiles of psoas muscles was studied in rats after a 48--96 hour fast. Experimental and control animals received glucose and insulin 1--2 hours before killing. 2) The ratio of polysomes to subunits and monomers decreased progressively during the fast. 3) The administration of the three branched chain amino acids together or leucine alone significantly increased the proportion of polysomes. 4) This effect was not observed in rats fed ad libitum. 5) It is suggested that the branched chain amino acids and specifically leucine may be required for the full protein anabolic response of muscles to insulin during a prolonged fast.

Amino Acids↗
PubMed1980

Computed tomography of psoas abscesses.

Nine surgically proven cases of pyogenic psoas abscesses are presented. The most common finding on computed tomography was diffuse enlargement of the psoas with a central low density area corresponding to an abcess cavity. This was noted in seven patients. The anatomy of the psoas muscle and retrofascial area is discussed, as well as the changing etiology and bacteriology of psoas abscesses.

Abscess↗
PubMed2005

Psoas abscess: report of a series and review of the literature.

We describe a series of twelve patients with a psoas abscess seen in a three-year period in a university hospital and a large teaching hospital in the Netherlands. In our series, five of the 12 patients had a primary psoas abscess. The predisposing conditions were intravenous drug use, diabetes mellitus, prostate carcinoma and haematoma in the psoas muscle in a patient with haemophilia A. Seven of the 12 patients had a secondary psoas abscess. Five cases were due to vertebral osteomyelitis including two cases of tuberculosis. In the other two cases it was due to colitis and urinary tract infection. It is remarkable that in our series there was only one patient with a psoas abscess secondary to a disease of the digestive tract, while this is the most common cause of a secondary psoas abscess in the literature. There were two cases of tuberculosis which is an emerging disease again.

Adult↗
PubMed1983

Polymorphism of alpha-actinin. Electrophoretic and immunological studies of rabbit skeletal muscle alpha-actinins.

Heterogeneity of alpha-actinins from rabbit skeletal muscles was studied. Polyacrylamide gel electrophoresis in the presence and absence of sodium dodecyl sulfate has made it possible to distinguish two closely related alpha-actinins from rabbit fast, white muscle. One isoprotein (designated type I alpha-actinin) appears to be preferentially located in the psoas muscle, while the other (designated type II alpha-actinin) appears to be preferentially located in the longissimus dorsi muscle. Electrophoretic analyses have further shown that the two isoproteins are present as mixtures in most rabbit white, fast-twitch muscles. A standard polyacrylamide gel--sodium dodecyl sulfate/polyacrylamide gel sequential electrophoretic procedure was developed to resolve the different alpha-actinin dimers and to determine their subunit compositions. By this technique, both type I and type II alpha-actinins appeared to be homodimers. No heterodimeric species of alpha-actinin were detected. alpha-Actinin of red, slow-twitch muscles was similar to type II alpha-actinin of fast, white muscle on one-dimensional and two dimensional gels. However, slow, red muscle alpha-actinin was significantly different from fast, white muscle alpha-actinins in terms of one-dimensional peptide mapping and immunological cross-reactivity.

Actinin↗
PubMed1989

[Postural examination in daily occlusodontology].

According to the osteopathic and chiropractic concepts, facing a TMJ problem, the practitioner has to determine if the trouble observed in the stomatognatic apparatus is the cause or the effect of the structural problems present anywhere else in the body. The postural examination allows to answer this question. Tow techniques can be used. First a static and dynamic posture test proposed by Bricot. The level of the cranium, the eyes, the shoulders, the wrists, the pelvis and the ankles is analysed, from a front view; from the side, the gravity line is inspected: vertex, auditory meatus, shoulder, hip joint, anterior side of the tibia, ankle joint. The vertical posture can be studied from the front: the arms are held straight and the antero-posterior length between the fingers is measured. From the back, one notes the recoil of the buttocks on one side. An ocular convergence test is performed. Then one uses a Romberg test (oscillation of the body when the eyes are closed), and a Fukuda stepping test. The patient is then asked to bite on a compress, and the same exams are redone. If no change occurs, we are dealing with an ascending problem: the origin of the problem is not the stomatognathic system. The second technique is the Meerssemann test that needs the practice of Applied Kinesiology muscle testing. The patient is lying supine and one tests: the dental occlusion, the two TMJs, the temporal muscles, masseters, pterygoids, sterno-cleido-mastoids, upper tapezius, left and right sacro-iliac joints, psoas muscles bilaterally.(ABSTRACT TRUNCATED AT 250 WORDS)

Dental Occlusion↗
PubMed1979

Muscle protein analysis. I. High-resolution two-dimensional electrophoresis of skeletal muscle proteins for analysis of small biopsy samples.

We have been developing a clinically useful method for high-resolution two-dimensional electrophoretic analysis of small (5--10 mg) human muscle biopsy samples with sufficient resolution to resolve the major contractile proteins and enzymes. Using rabbit psoas muscle as a model, we describe methods for sample preparation and two-dimensional electrophoresis. Basic proteins, which appear as streaks when conventional isoelectric focusing is used in the first dimension, are resolved through a modification of the nonequilibrium pH gradient electrophoresis method [Cell 12, 1133 (1977)]. In the two-dimensional patterns obtained from rabbit muscle, we identify the components of 10 enzymes and of myosin, actin, tropomyosin, and troponin. These patterns indicate charge heterogeneity in a large fraction of the proteins. Comparison of rabbit and normal human muscle patterns shows many similarities, but much additional work is required to confirm identifications. We conclude that analysis of small biopsy samples is feasible, but that all aspects of human sample acquisition, storage (when necessary), and preparation require thorough study before the method becomes routine in human muscle research and, ultimately, in the diagnosis of some muscle diseases.

Animals↗