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At least 649 records · Page 36Linked to original sources
PubMed2005

Revisiting vascularized muscle flaps for complicated sternal wounds in children.

Surgeons at our center previously reported a case of a 2-month-old infant who underwent closure of an infected sternal wound following open cardiac surgery with debridement followed by closure with bilateral pectoralis muscle flaps and a unilateral rectus abdominis muscle flap. The success of the procedure has spawned refinements in the technique, such as the one described herein. A 2-week-old neonate was evaluated for postoperative sternal dehiscence and instability following open cardiac surgery for severe congenital cardiac anomalies. Management included initial debridement and application of a vacuum-assisted closure (V.A.C.) system (KCI, Oxfordshire, UK). In conjunction with the final V.A.C. dressing change, the patient underwent delay of the left rectus muscle by division of the inferior epigastric pedicle. She subsequently underwent transposition of the left rectus muscle and application of a full-thickness skin graft for coverage of the sternal defect. She has since done well and still requires further invasive cardiac procedures.

Cardiac Surgical Procedures↗
PubMed1983

Louis Ombredanne and the origin of muscle flap use for immediate breast mound reconstruction.

The myocutaneous flaps that are being used for breast reconstruction have a long history, although the techniques of today are more sophisticated than those of the past. Louis Ombredanne was the first to describe the pectoralis muscle flap for immediate breast mound reconstruction in 1906. Mastectomy, as performed by Halstead, is described with some insight into the reasons why breast reconstruction was not encouraged in this country in the early part of this century. Lately, the advances in the myocutaneous flap have made breast reconstruction without a prosthesis possible. The tissue that was transferred to reconstruct a breast using a tubed pedicle flap in multiple stages can now be transferred in a single stage with a better result.

Breast↗
PubMed2001

Aggressive primary treatment for poststernotomy acute mediastinitis: our experience with omental- and muscle flaps surgery.

OBJECTIVE: The surgical treatment of poststernotomy acute mediastinitis remains challenging. After disappointing results with a conservative management of post coronary artery bypass grafting (CABG) mediastinitis, we shifted towards a more aggressive surgical management. METHODS: From March 1993 until December 1999, 32 patients (6 female/26 male), 0.5% of the total sternotomy population, were operated for mediastinitis, defined as wound and sternal dehiscence with medistinal pus and positive culture. Mean age was 66 years (32-79 years). Twenty-two patients (75%) underwent CABG and 16 patients were in New York Heart Association (NYHA) class III/IV. RESULTS: We performed an omentoplasty in 11 patients, a pectoralis muscle flap associated with an omentoplasty in 20 patients. One patient had a bilateral pectoralis myoplasty. The reconstruction surgery occurred at an average of 11 days (6-26) after primary surgery. Twelve patients had a previous surgical drainage (1-3 surgical procedures) of the mediastinum. Hospital mortality was nine patients (28%). Seven of these patients (77%) were in NYHA IV with inotropic support. Five patients had to be reoperated on: four patients had a bilateral myoplasty after omentoplasty, one patient had an omentoplasty after a unilateral myoplasty. Late epigastric hernia was seen in three patients, two patients had wound revision and one had a retroperitoneal drainage for pancreatitis. There were no early or late flap failures. CONCLUSION: In our experience, omental and pectoralis flaps for poststernotomy acute mediastinitis provides good outcome of our stable patients. We would be reluctant to use it as standard therapy in our unstable patients.

Aged↗
PubMed1987

Transient appearance of a fast myosin heavy chain epitope in slow-type muscle fibres during stretch hypertrophy of the anterior latissimus dorsi muscle in the adult chicken.

Myosin expression during hypertrophy of the chicken anterior latissimus dorsi (ALD) muscle was investigated by immunocytochemical procedures using monoclonal antibodies to the fast and slow isoforms of the myosin heavy chain (myosin HC). Antifast antibody 1F9 bound to the adult fast HC of pectoralis muscle and cross-reacted with the HC found in early developing muscle. Antislow antibody 3D1 bound exclusively to the HC of slow myosin 2 (SM2). Stretch hypertrophy of the ALD was produced by attaching a weight to the wing; there was no evidence for a change in fibre number in the muscle. Between 4 and 6 days of stretch there appeared a dramatic increase in the number of fibres staining with the antifast antibody which reached a peak between 12 and 19 days. By this time between 28 and 52% of the fibres in the stretched ALD stained to varying degrees with the antifast antibody compared with much less than 1% in the unstretched control ALD. Most antifast-stained fibres in the stretched muscle also stained with the antislow antibody; the contralateral control muscle showed mostly antislow staining except for the very small number of strongly antifast-stained fibres. By 50 days in some birds and by 80 days in all birds antifast staining had returned to normal. Analysis of the isomyosin composition of the ALD by native gel electrophoresis did not reveal a significant increase in fast myosin content of the hypertrophied muscle even though immunocytochemical staining may have suggested otherwise.

Animals↗
PubMed1995

Antisense suppression of skeletal muscle myosin light chain-1 biosynthesis impairs myofibrillogenesis in cultured myotubes.

Although the alkali or essential light chains of skeletal muscle myosin are not required for actin-activated myosin ATPase activity, these myosin subunits are necessary for force transmission with in vitro actin motility assays and are believed to stabilize the alpha-helical neck region of myosin subfragment-1. To probe the functions of the essential light chains during myofibril assembly, we used recombinant DNA procedures to deplete this light chain in cultured muscle. Retroviral expression vectors were constructed which encoded the exon-1 sequence of the myosin light chain-1 gene in antisense orientation. These vectors were applied to myogenic cells from embryonic chick and quail pectoralis muscle. Colonies expressing antisense RNA were selected in growth medium containing the neomycin analogue G-418, plus 5-bromo-2'-deoxyuridine (BrdU) and triggered to differentiate by removal of the latter. Expression of antisense myosin light chain-1 mRNA impaired muscle development. In the antisense cultures there were more mononucleated cells, fewer and smaller myotubes which had poorly developed myofibrils and high levels of diffusely staining myosin heavy chain, not apparent in control myotubes. Protein synthesis in the myotube cultures was analyzed by 35S-methionine labelling and two-dimensional gel electrophoresis. Except for a suppression of approximately 80% of myosin light chain-1f synthesis, the overall pattern of protein synthesis was not altered significantly. These studies suggest that retardation of myosin light chain-1f accumulation inhibits or delays myofibrillogenesis.

Animals↗
PubMed2002

IGF-I, IGF-II, and IGF-receptor-1 transcript and IGF-II protein expression in myostatin knockout mice tissues.

Semiquantitative reverse transcriptase-polymerase chain reaction (RT-PCR) and immunohistochemistry were performed to demonstrate whether a correlation exists between insulin-like growth factors (IGFs)-positive regulators of growth-and myostatin, a negative regulator of muscle growth. IGF-I, -II, and IGF-receptor-1 (IGF-R1) mRNA and IGF-II protein expressions were determined in control and myostatin knockout mice tissues. IGF-I gene expressions were similar between control and knockout mice tissues, whereas IGF-II mRNA levels were significantly higher in myostatin knockout mice kidney and soleus muscles than those of control mice (P <.01). IGF-R1 mRNA levels from control mice heart (P <.05) and kidney (P <.01) were significantly higher than in myostatin knockout mice, whereas levels were lower in pectoralis muscle of control mice than knockout mice (P <.01). The strongly IGF-II-positive cells in soleus muscle were more common in myostatin knockout mice and were seen in a few foci in control mice. IGF-II immunoreactivity in both control and myostatin knockout mice kidneys was localized to the epithelium of renal tubules and collecting ducts. Reciprocal changes in the expression of myostatin and IGF-II and IGF-R1 may underlie normal growth of skeletal muscle and other organs in mammals, and the changes in these tissues associated with disease.

Actins↗
PubMed1988

Regional distribution of blood flow during swimming in the tufted duck (Aythya fuligula).

The distribution of blood flow to a number of organs and tissues of the tufted duck was determined (by the microsphere technique) before and while the birds were swimming at close to their maximum sustainable velocity (i.e. at 0.69 +/- 0.01 ms-1). During swimming, oxygen uptake was twice the pre-exercise value. Cardiac output increased by 70%, there was no significant change in arterial blood pressure and total systemic conductance increased by 44%. There were no significant changes in blood flow to the brain, liver, adrenal glands, spleen and respiratory muscles. Not surprisingly, there were increases in blood flow to the heart (30% increase) and to the muscles of the hindlimbs (to 3.1 times the pre-exercise value). Significant reductions in flow occurred to various parts of the gastrointestinal tract (although not to the gastrointestinal tract as a whole), to the pancreas and to the pectoralis muscles. In the case of the flight musculature as a whole, the reduction was to approximately 40% of the values in the ducks before exercise. Thus, despite the fact that cardiac output was some three times lower than it would have been during flight, there was a clear redistribution of blood away from some visceral organs and inactive muscles during surface swimming in the tufted duck. This lends support to the suggestion that blood is selectively directed to the legs, as well as to the brain and central nervous system (CNS) and away from the visceral organs and inactive muscles during voluntary diving in these birds.

Animals↗
PubMed1998

Extensive pectoral muscle necrosis after defibrillation: nonthermal skeletal muscle damage caused by electroporation.

A 37-year-old Italian male developed a myocardial infarct with subsequent ventricular fibrillation. He was defibrillated seven times with up to 360 Joules. Thirteen days later the patient died of recurrent myocardial infarct due to thrombotic occlusion of the left circumflex coronary artery. At autopsy, necrosis of the right pectoralis muscle was observed. Electroporation is the pathogenetic mechanism of skeletal muscle damage due to multiple defibrillations with high energy levels.

Adult↗
PubMed1991

The primary structure of skeletal muscle myosin heavy chain: IV. Sequence of the rod, and the complete 1,938-residue sequence of the heavy chain.

In the preceding paper [Maita, T., Miyanishi, T., Matsuzono, K., Tanioka, Y., & Matsuda, G. (1991) J. Biochem. 110, 68-74], we reported the amino-terminal 837-residue sequence of the heavy chain of adult chicken pectoralis muscle myosin. This paper describes the carboxyl terminal 1,097-residue sequence and the linkage of the two sequences. Rod obtained by digesting myosin filaments with alpha-chymotrypsin was redigested with the protease at high KCl concentration, and two fragments, subfragment-2 and light meromyosin, were isolated and sequenced by conventional methods. The linkage of the two fragments was deduced from the sequence of an overlapping peptide obtained by cleaving the rod with cyanogen bromide. The rod contained 1,039 amino acid residues, but lacked the carboxyl-terminal 58 residues of the heavy chain. A carboxyl-terminal 63-residue peptide obtained by cleaving the whole heavy chain with cyanogen bromide was sequenced. Thus, the carboxyl terminal 1,097-residue sequence of the heavy chain was completed. The linkage of subfragment-1 and the rod was deduced from the sequence of an overlapping peptide between the two which was obtained by cleaving heavy meromyosin with cyanogen bromide. Comparing the sequence of the adult myosin thus determined with that of chicken embryonic myosin reported by Molina et al. [Molina, M.I., Kropp, K.E., Gulick, J., & Robbins, J. (1987) J. Biol. Chem. 262, 6478-6488], we found that the sequence homology is 94%.

Amino Acid Sequence↗
PubMed1995

Effect of stunning amperage on broiler breast muscle rigor development and meat quality.

Two experiments were conducted to determine the effects of constant amperage (as opposed to constant voltage) electrical stunning on broiler blood loss, post-mortem breast muscle (Pectoralis major) rigor development, and breast meat quality. Broilers were individually stunned for 5 s at 0 (unstunned control group), 50, 100, 150, and 200 mA in Experiment 1 and at 0, 50, and 125 mA in Experiment 2. Breast muscle pH and R-value (ratio of adenosine to inosine nucleotides) were determined at 15 min and 24 h post-mortem; breast meat shear value and color were determined at 48 h post-mortem. Stunning amperage had no effect on percentage blood loss in either experiment. The most rapid post-mortem reactions were observed for the unstunned control group as determined by pH and R-value at 15 min post-mortem. Birds stunned with 50 mA were intermediate with regard to rate of rigor development. The slowest post-mortem reactions occurred in broilers stunned from 100 to 200 mA. There were no differences in pH, R-value, or color between stunning treatments after carcasses were aged for 24 h. Stunning amperage did not affect Allo-Kramer shear value for breast muscles deboned at 15 min post-mortem. In Experiment 2, 24 h aged breast meat from broilers stunned with 125 mA required significantly higher shear value (4.5 kg/g) than breast meat from broilers stunned at 0 or 50 mA (3.8 and 3.6 kg/g, respectively). Results indicate that stunning amperages between 0 and 200 mA had effects on the rate of early rigor development but there were no consistent effects on final breast meat quality.

Animals↗
PubMed1977

Myosin types during the development of embryonic chicken fast and slow muscles.

We have studied the myosin types present in developing fast and slow muscles of the chicken embryo. Myosin light chains were characterized by their mobility on sodium dodecyl sulfate/polyacrylamide gels; myosin heavy chains were identified by their reaction with antibodies specific for adult fast or adult slow myosin heavy chains. During development, the pectoralis muscle, a fast muscle in the adult, contains heavy chains and two of the three light chains characteristic of adult fast muscle myosin. However, the anterior latissimus dorsi muscle, a slow muscle in the adult, also contains fast myosin light and heavy chains during early development. Only after the time of innervation does this muscle begin synthesizing predominantly the slow myosin heavy and light chains. We hypothesize that the synthesis of fast myosin in both early fast and slow muscles is the result of the endogenous program for muscle development; initiation of the synthesis of slow myosin, however, is dependent upon exogenous factors.

Aging↗
PubMed1996

[Myoneuropathy in patients with chronic renal failure treated with hemodialysis (HD) and intermittent peritoneal dialysis (IPD). I. Evaluation of myoelectric activity of selected skeletal muscles in patients with chronic renal failure treated with hemodialysis and intermittent peritoneal dialysis].

The aim of the study was the analysis of the sequence of electrophysiological changes occurring in the skeletal muscles in patients with chronic renal failure treated with hemodialysis (HD) and intermittent peritoneal dialysis (IPD). In 30 patients (10 treated with IPD-group I, 20 with HD-group II) the global electromyography (EMG) was determined in the muscles: pectoralis, obliqus and rectus abd., biceps brachii, thenar and hypothenar. The fatigue test was determined in the m. biceps brachii. The examinations were done twice during the 12 months of observations. The analysis of the material showed that myoelectrical activity of the examined muscles was significantly lower compared to a control group and did not changed during the 12 months of observations. The results of the fatigue test showed that in uremic patients the fatiguability of m. biceps brachii was significantly greater and was deeper after 12 months of observations. The analysis of the maximal inspiratory and expiratory pressure showed that respiratory muscles in uremic patients were weak. The results of the measurements the hand grip pressure showed that hand muscles were weak also.

Adult↗
PubMed1979

Peripheral neuropathy after administration of tetanus toxoid.

A reversible paresis of several muscles of the right arm was observed in a 20-year-old female, 3 weeks after the intragluteal injection of tetanus toxoid and 6--7 weeks after multiple injuries. The EMG findings indicated a transitory conduction block of nerve fibers to the deltoid and pectoralis muscles and a more severe axonal-demyelinating lesion of fibers to the biceps muscle. The cause of the palsy was probably a reaction to the administration of tetanus toxoid; other possible causes are discussed.

Accidents, Traffic↗
PubMed1998

Isolation and characterization of a calpain activator in chicken skeletal muscle.

The calpains (E.C. 3.4.22.17) and calpastatin constitute an ubiquitous, intracellular, Ca2+-dependent protease/inhibitor system. This system has been implicated as a principal regulator of myofibrillar protein degradation in both ante-mortem and postmortem muscle. Although proteolytic activity of the calpains is primarily controlled through interaction of calpain and calpastatin, evidence for an activator(s) has been limited and the reported characteristics varied. The function of the activator has not been elucidated. A putative calpain activator has been isolated from the Pectoralis muscle of broiler breeders (Cobb x Cobb). The activator elutes from an ion-exchange column at approximately 200 mM NaCl. Addition of activator increased apparent m-calpain activity to a level demonstrating a fourfold increase in proteolysis. The activator/calpain complex maintains a requirement for Ca2+ for proteolytic activity. Under physiological conditions, presence of the activator negates the ability of calpastatin to inhibit m-calpain. Additionally, the activator alone does not demonstrate proteolytic activity. Effect of the activator is pH-dependent; in a physiological pH range, the activator enhances m-calpain proteolytic activity but at pH less than 6.75 the effect is to inhibit m-calpain. The activator's ability to modulate m-calpain activity and eliminate calpastatin's effect provides a further means of regulating this important enzyme system.

Animals↗
PubMed1992

Heterogeneity and distribution of fast myosin heavy chains in some adult vertebrate skeletal muscles.

Three monoclonal antibodies, LM5, F2 and F39 raised to chicken fast skeletal muscle myosin, specific for myosin heavy chain (MHC) subunit, were used to study the composition and distribution of this protein in some vertebrate skeletal muscles. These antibodies in immunohistochemical investigations did not react with the majority of the type I fibres in most muscles. Antibodies LM5 and F39 stained all the type II fibres in all the adult chicken skeletal muscles studied. Antibody F2 also stained all the type II fibres in most chicken skeletal muscles tested except in gastrocnemius in which a proportion of both the type IIA and IIB fibres either did not stain or stained only weakly. Antibody F2 unlike LM5 and F39 stained most of the type IIIB fibres in anterior latissimus dorsi (ALD) and IB fibres in red strip of chicken Pectoralis muscle. Antibodies LM5 and F2 in the rat diaphragm reacted with all the type IIA and IIB fibres, while antibody F39 stained only the type IIB fibres darkly with most IIA fibres being either not stained or only weakly stained. In the rat extensor digitorum longus (EDL) and tibialis anterior (TA) muscles, antibody LM5 stained all the IIA and IIB fibres. Antibody F2 in these muscles stained all the type IIA fibres but only a proportion of the IIB fibres. The remaining IIB fibres were either unstained or only weakly positive. Antibody F39 in rat EDL and TA muscles did not only distinguish subgroups of IIB fibres (dark, intermediate and negative or very weak) but also of the IIA fibres. These three antibodies used together therefore detected a great deal of heterogeneity in the myosin heavy chain composition and muscle fibre types of several skeletal muscles.

Animals↗
PubMed1989

Altered contents of tocopherols in chickens with inherited muscular dystrophy.

Oxidative damage has been hypothesized as the basis for some of the changes in enzymatic functions and physical properties of membranes in inherited muscular dystrophy. The contents of alpha- and gamma-tocopherol (vitamin E) and their oxidation products, the tocopheryl quinones, were measured at 1 to 4 weeks after hatching in the muscle and other tissues of chickens with inherited muscular dystrophy. Analyses at these early ages minimized the potential influence of pathological changes on the measured parameters. The affected muscle (pectoralis major) of dystrophic birds contained significantly higher levels of alpha-tocopheryl quinone and a decreased ratio of alpha- to gamma-tocopherol. Consistent changes in these parameters were not observed in other tissues. Although their basis remains unclear, these changes in the tocopherols are suggestive of oxidative stress in dystrophic muscle membranes. Lipid extracts of tissues of normal and dystrophic birds exhibited no significant differences in the content of conjugated dienes or lipofuscins, two other indices of oxidative stress. These data do not consistently support the hypothesis that oxidative stress plays a causal role in damage to dystrophic muscle, although it remains possible that free-radical damage is involved in the secondary alterations associated with muscular dystrophy.

Aging↗
PubMed2006

Muscles within muscles: Coordination of 19 muscle segments within three shoulder muscles during isometric motor tasks.

The aim of the present study was to determine how the intra-muscular segments of three shoulder muscles were coordinated to produce isometric force impulses around the shoulder joint and how muscle segment coordination was influenced by changes in movement direction, mechanical line of action and moment arm (ma). Twenty male subjects (mean age 22 years; range 18-30 years) with no known history of shoulder pathologies, volunteered to participate in this experiment. Utilising an electromyographic technique, the timing and intensity of contraction within 19 muscle segments of three superficial shoulder muscles (Pectoralis Major, Deltoid and Latissimus Dorsi) were studied and compared during the production of rapid (e.g. approximately 400ms time to peak) isometric force impulses in four different movement directions of the shoulder joint (flexion, extension, abduction and adduction). The results of this investigation have suggested that the timing and intensity of each muscle segment's activation was coordinated across muscles and influenced by the muscle segment's moment arm and its mechanical line of action in relation to the intended direction of shoulder movement (e.g. flexion, extension, abduction or adduction). There was also evidence that motor unit task groups were formed for individual motor tasks which comprise motor units from both adjacent and distant muscles. It was also confirmed that for any particular motor task, individual muscle segments can be functionally classified as prime mover, synergist or antagonist - classifications which are flexible from one movement to the next.

Adaptation, Physiological↗
PubMed1995

The chicken muscle thick filament: temperature and the relaxed cross-bridge arrangement.

Although chicken myosin S1 has recently been crystallized and its structure analysed, the relaxed periodic arrangement of myosin heads on the chicken thick filament has not been determined. We report here that the cross-bridge array of chicken filaments is temperature sensitive, and the myosin heads become disordered at temperatures near 4 degrees C. At 25 degrees C, however, thick filaments from chicken pectoralis muscle can be isolated with a well ordered, near-helical, arrangement of cross-bridges as seen in negatively stained preparations. This periodicity is confirmed by optical diffraction and computed transforms of images of the filaments. These show a strong series of layer lines near the orders of a 43 nm near-helical periodicity as expected from X-ray diffraction. Both analysis of phases on the first layer line, and computer filtered images of the filaments, are consistent with a three-stranded arrangement of the myosin heads on the filament.

Actin Cytoskeleton↗