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Background

The developmental profile of chicken carbonic anhydrase-III (CA-III) blood levels has not been previously determined or reported. We isolated CA-III from chicken muscle and investigated age-related changes in the levels of CA-III in blood.

Methods

CA-III was purified from chicken muscle. The levels of CA-III in plasma and erythrocytes from 278 female chickens (aged 1-93 weeks) and 68 male chickens (aged 3-59 weeks) were determined by ELISA.

Results

The mean level of CA-III in female chicken erythrocytes (1 week old) was 4.6 μg/g of Hb, and the CA-III level did not change until 16 weeks of age. The level then increased until 63 weeks of age (11.8 μg/g of Hb), decreased to 4.7 μg/g of Hb at 73 weeks of age, and increased again until 93 weeks of age (8.6 μg/g of Hb). The mean level of CA-III in erythrocytes from male chickens (3 weeks old) was 2.4 μg/g of Hb, and this level remained steady until 59 weeks of age. The mean plasma level of CA-III in 1-week-old female chickens was 60 ng/mL, and this level was increased at 3 weeks of age (141 ng/mL) and then remained steady until 80 weeks of age (122 ng/mL). The mean plasma level of CA-III in 3-week-old male chickens was 58 ng/mL, and this level remained steady until 59 weeks of age.

Conclusion

We observed both developmental changes and sex differences in CA-III concentrations in White Leghorn (WL) chicken erythrocytes and plasma. Simple linear regression analysis showed a significant association between the erythrocyte CA-III level and egg-laying rate in WL-chickens 16-63 weeks of age (p < 0.01).

Seven patients with dystrophia myotonica were investigated using neurophysiological combined with histochemical techniques to elucidate motor unit properties in foot extensor muscles, which are often involved in the early stages of this disorder. For the 25 extensor digitorum brevis motor units studied the axonal conduction velocity, the axonal refractory period and the voluntary firing properties were within normal limits. However, high threshold motor units were not observed and the mean value of the axonal conduction velocities was lower (p less than 0.02) for the dystrophia myotonica motor units when compared with corresponding data from healthy subjects. There were also signs of impaired impulse propagation in the terminal part of the motor unit. In muscle biopsy specimens from the anterior tibial muscle, fibre type composition and structure were demonstrated using enzyme histochemical techniques for adenosine-triphosphate and immunohistochemical techniques for identification of the types of myosin isoform present. The histochemical findings indicated a type I fibre dominance, which was most obvious in the more seriously affected muscles. Neonatal myosin was observed preferentially in small but also in some normal sized fibres. Furthermore, some ring fibres were present and these showed staining with antineonatal myosin in their superficial portion. This indicates that an abnormal regeneration is one cause of the myopathic appearance of the muscle fibres in dystrophia myotonica. These investigations show that there is a reduced proportion of type II motor units in foot extensor muscles involved in the myopathy in dystrophia myotonica although it cannot definitely be established whether this is due to a loss of high threshold type II motor units or type II to type I transformation.

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Background

Carbonic anhydrase (CA) of the chicken has attracted attention for a long time because it has an important role in the eggshell formation. The developmental profile of CA-II isozyme levels in chicken erythrocytes has not been determined or reported. Furthermore, the relations with CA-II in erythrocyte and egg production are not discussed. In the present study, we isolated CA-II from erythrocytes of chickens and determined age-related changes of CA-II levels in erythrocytes.

Methods

Chicken CA-II was purified by a combination of column chromatography. The levels of CA-II in the hemolysate of the chicken were determined using the ELISA system in blood samples from 279 female chickens, ages 1 to 93 weeks, 69 male chickens, ages 3 to 59 weeks and 52 weeks female Araucana-chickens.

Results

The mean concentration of CA-II in hemolysate from 1-week-old female was 50.8 ± 11.9 mg/g of Hb. The mean levels of CA-II in 25-week-old (188.1 ± 82.6 mg/g of Hb), 31-week-old (193.6 ± 69.7 mg/g of Hb) and 49-week-old (203.8 ± 123.5 mg/g of Hb) female-chickens showed the highest level of CA-II. The levels of CA-II in female WL-chickens significantly decreased at 63 week (139.0 ± 19.3 mg/g of Hb). The levels of CA-II in female WL-chicken did not change from week 63 until week 93.The mean level of CA-II in hemolysate of 3-week-old male WL-chickens was 78.3 ± 20.7 mg/g of Hb. The levels of CA-II in male WL-chickens did not show changes in the week 3 to week 59 timeframe. The mean level of CA-II in 53-week-old female Araucana-chickens was 23.4 ± 1.78 mg/g of Hb. These levels of CA-II were about 11% of those of 49-week-old female WL-chickens. Simple linear regression analysis showed significant associations between the level of CA-II and egg laying rate from 16 week-old at 63 week-old WL-chicken (p < 0.01).

Conclusions

Developmental changes and sexual differences of CA-II concentration in WL-chicken erythrocytes were observed. The concentration of CA-II in the erythrocyte of WL-chicken was much higher than that in Araucana-chicken (p < 0.01).

Serum insulin, blood sugar, and growth hormone levels were measured in response to a 50g oral glucose tolerance test in 10 patients with proven dystrophia myotonica. Three patients belonged to one family; seven patients had no known family history of the disease. One patient, a chronic invalid aged 56 years, produced a mild diabetic glucose tolerance curve and a delayed prolonged rise in serum insulin. Six of the group, including the three affected members from one family, exhibited normal glucose tolerance and fasting serum insulin values, but a markedly exaggerated rise in peripheral insulin levels maximal at 30 and 60 min. This abnormality showed no correlation with age of onset of the disease nor with severity of the muscle weakness. Growth hormone levels were normal in all of the patients studied. It is concluded that an excessive rise in circulating immunoreactive insulin in response to glucose is a common abnormality in dystrophia myotonica and reflects genetic heterogeneity in this condition. Futhermore, if the index patient in a family demostrates this abnormality, it is suggested that the 30- or 60-min blood insulin level during a glucose tolerance test is a useful methold of intra-family screen-ing for asymptomatic heterozygotes at an early stage before the development of physical defects.

Myotonic Dystrophy type 1 (DM1) is a multi-system disorder characterized by muscle wasting, myotonia, cardiac conduction defects, cataracts, and neuropsychological dysfunction. DM1 is caused by expansion of a CTG repeat in the 3´untranslated region (UTR) of the Dystrophia Myotonica Protein Kinase (DMPK) gene. A body of work demonstrates that DMPK mRNAs containing abnormally expanded CUG repeats are toxic to several cell types. A core mechanism underlying symptoms of DM1 is that mutant DMPK RNA interferes with the developmentally regulated alternative splicing of defined pre-mRNAs. Expanded CUG repeats fold into ds(CUG) hairpins that sequester nuclear proteins including human Muscleblind-like (MBNL) and hnRNP H alternative splicing factors. DM1 cells activate CELF family member CUG-BP1 protein through hyperphosphorylation and stabilization in the cell nucleus. CUG-BP1 and MBNL1 proteins act antagonistically in exon selection in several pre-mRNA transcripts, thus MBNL1 sequestration and increase in nuclear activity of CUG-BP1 both act synergistically to missplice defined transcripts. Mutant DMPK-mediated effect on subcellular localization, and defective phosphorylation of cytoplasmic CUG-BP1, have additionally been linked to defective translation of p21 and MEF2A in DM1, possibly explaining delayed differentiation of DM1 muscle cells. Mutant DMPK transcripts bind and sequester transcription factors such as Specificity protein 1 leading to reduced transcription of selected genes. Recently, transcripts containing long hairpin structures of CUG repeats have been shown to be a Dicer ribonuclease target and Dicer-induced downregulation of the mutant DMPK transcripts triggers silencing effects on RNAs containing long complementary repeats. In summary, mutant DMPK transcripts alter gene transcription, alternative splicing, and translation of specific gene transcripts, and have the ability to trigger gene-specific silencing effects in DM1 cells. Therapies aimed at reversing these gene expression alterations should prove effective ways to treat DM1.

Levels of immunoglobulins IgG, IgA, and IgM were measured in 38 patients with myotonic dystrophy, in normal members of their families, and in matched controls. Log IgG was significantly reduced in the patients. IgG investigation provides a further parameter to appraise the status of apparently unaffected members of myotonic dystrophy families.

Myotilin cDNA has been cloned for the first time from chicken muscles and sequenced. Ectopically expressed chicken and human YFP-myotilin fusion proteins localized in avian muscle cells in the Z-bodies of premyofibrils and the Z-bands of mature myofibrils. Fluorescence Recovery After Photobleaching (FRAP) experiments demonstrated that chicken and human myotilin were equally dynamic with 100% mobile fraction in premyofibrils and Z-bands of mature myofibrils. Seven myotilin mutants cDNAs (S55F, S55I, T57I, S60C, S60F, S95I, R405K) with known muscular dystrophy association localized in mature myofibrils in the same way as normal myotilin without affecting the formation and maintenance of myofibrils. N- and C-terminal halves of human myotilin were cloned and expressed as YFP fusions in myotubes and cardiomyocytes. N-terminal myotilin (aa 1–250) localized weakly in Z-bands with a high level of unincorporated protein and no adverse effect on myofibril structure. C-terminal myotilin (aa 251–498) localized in Z-bands and in aggregates. Formation of aggregated C-terminal myotilin was accompanied by the loss of Z-band localization of C-terminal myotilin and partial or complete loss of alpha-actinin from the Z-bands. In regions of myotubes with high concentrations of myotilin aggregates there were no alpha-actinin positive Z-bands or organized F-actin. The dynamics of the C-terminal-myotilin and N-terminal myotilin fragments differed significantly from each other and from full-length myotilin. In contrast, no significant changes in dynamics were detected after expression in myotubes of myotilin mutants with single amino acid changes known to be associated with myopathies.

X-linked muscular dystrophy is a highly progressive disease of childhood and characterized by primary genetic abnormalities in the dystrophin gene. Senescent mdx specimens were used for a large-scale survey of potential age-related alterations in the dystrophic phenotype, because the established mdx animal model of dystrophinopathy exhibits progressive deterioration of muscle tissue with age. Since the mdx tibialis anterior muscle is a frequently used model system in muscular dystrophy research, we employed this particular muscle to determine global changes in the dystrophic skeletal muscle proteome. The comparison of mdx mice aged 8 weeks versus 22 months by mass-spectrometry-based proteomics revealed altered expression levels in 8 distinct protein species. Increased levels were shown for carbonic anhydrase, aldolase, and electron transferring flavoprotein, while the expressions of pyruvate kinase, myosin, tropomyosin, and the small heat shock protein Hsp27 were found to be reduced in aged muscle. Immunoblotting confirmed age-dependent changes in the density of key muscle proteins in mdx muscle. Thus, segmental necrosis in mdx tibialis anterior muscle appears to trigger age-related protein perturbations due to dystrophin deficiency. The identification of novel indicators of progressive muscular dystrophy might be useful for the establishment of a muscle subtype-specific biomarker signature of dystrophinopathy.

The expression of the myofibrillar M-band proteins myomesin and M- protein was studied in chicken pectoral muscle and heart during differentiation using monoclonal antibodies in a double-antibody sandwich enzyme-linked immunosorbent assay, immunoblotting, and immunocytochemistry. In presumptive pectoral muscle, myomesin accumulated first, increasing from 2% of the adult concentration at day 7 to 70% by day 16 in ovo. M-protein accumulation lagged 6-7 d behind that of myomesin attaining only 40% of the adult concentration in ovo. The molecular masses of myomesin (185 kD) and M-protein (165 kD) remained constant during embryogenesis. In cultured myogenic cells the accumulation and M-band localization of myomesin preceded that of M- protein by 1.5 d. Chicken heart was shown, in addition to M-protein, to contain unique isoforms of myomesin. In hearts of 6 d embryos, a 195-kD myomesin isoform was the major species; throughout development, however, a transition to a mixture of 195 and 190 kD was observed, the latter being the major species in the adult tissue. During heart differentiation the initial accumulation of myomesin again preceded that of M-protein, albeit on an earlier time scale than in pectoral muscle with M-protein reaching adult proportions first.

Carbonic anhydrase III is a cytosolic protein which is particularly abundant in skeletal muscle, adipocytes, and liver. The specific activity of this isozyme is quite low, suggesting that its physiological function is not that of hydrating carbon dioxide. To understand the cellular roles of carbonic anhydrase III, we inactivated the Car3 gene. Mice lacking carbonic anhydrase III were viable and fertile and had normal life spans. Carbonic anhydrase III has also been implicated in the response to oxidative stress. We found that mice lacking the protein had the same response to a hyperoxic challenge as did their wild-type siblings. No anatomic alterations were noted in the mice lacking carbonic anhydrase III. They had normal amounts and distribution of fat, despite the fact that carbonic anhydrase III constitutes about 30% of the soluble protein in adipocytes. We conclude that carbonic anhydrase III is dispensable for mice living under standard laboratory husbandry conditions.

Introduction

Pyomyositis is a disease in which an abscess is formed deep within large striated muscles.

Case presentation

We report the case of a 10-year-old boy who presented with fever and a painful hip and was subsequently diagnosed with pyomyositis of the tensor fascia lata. In children with clinical and laboratory findings of inflammation in the vicinity of the hip joint, the differential diagnosis includes transient synovitis, an early stage of Legg-Calvé-Perthes disease, infectious arthritis of the hip, rheumatologic diseases and extracapsular infection such as osteomyelitis.

Conclusion

To the best of the authors' knowledge, this is the first report of pyomyositis of the tensor fascia lata. Although pyomyositis is a rare disease and the differential diagnosis includes a variety of other commonly observed diseases, pyomyositis should be considered in cases where children present with fever, leukocytosis and localized pain.

The purpose of this study was to estimate mean concentrations of total arsenic in chicken liver tissue and then estimate total and inorganic arsenic ingested by humans through chicken consumption. We used national monitoring data from the Food Safety and Inspection Service National Residue Program to estimate mean arsenic concentrations for 1994-2000. Incorporating assumptions about the concentrations of arsenic in liver and muscle tissues as well as the proportions of inorganic and organic arsenic, we then applied the estimates to national chicken consumption data to calculate inorganic, organic, and total arsenic ingested by eating chicken. The mean concentration of total arsenic in young chickens was 0.39 ppm, 3- to 4-fold higher than in other poultry and meat. At mean levels of chicken consumption (60 g/person/day), people may ingest 1.38-5.24 microg/day of inorganic arsenic from chicken alone. At the 99th percentile of chicken consumption (350 g chicken/day), people may ingest 21.13-30.59 microg inorganic arsenic/day and 32.50-47.07 microg total arsenic/day from chicken. These concentrations are higher than previously recognized in chicken, which may necessitate adjustments to estimates of arsenic ingested through diet and may need to be considered when estimating overall exposure to arsenic.

Background

Minimally invasive techniques in THA are intended to minimize periarticular muscle trauma. The lateral approach has a risk of partial gluteal insufficiency, while the anterolateral approach carries the risk of damaging the tensor fasciae latae through intermuscular nerve and compression injury.

Questions/purposes

We assessed the surgical influence of the anterolateral minimally invasive approach and the modified direct lateral approach on the tensor fasciae latae and gluteus medius.

Methods

We prospectively randomized 44 patients with primary coxarthrosis to receive a cementless THA via the anterolateral minimally invasive approach or the modified direct lateral approach. We performed clinical and MRI examinations preoperatively and 3 and 12 months postoperatively, including Harris hip and pain scores. MRI analysis included assessment of the tensor fasciae latae and gluteus medius with regard to fatty atrophy and changes in the muscle cross-sectional area.

Results

Clinical scores were similar in the two groups but a low-grade Trendelenburg sign was observed more frequently in the lateral group. MRI showed a pronounced, postoperative fatty atrophy of the anterior part of the gluteus medius more often; and a compensatory hypertrophy of the tensor fasciae latae occurred. Higher-grade atrophy of the tensor fasciae latae and gluteus medius did not occur with the anterolateral approach.

Conclusions

We found no increased damage to the tensor fasciae latae with the anterolateral approach. The lateral approach was associated with increased partial gluteus atrophy and a compensatory hypertrophy of the tensor fasciae latae. Based on fewer structural changes in the musculature, we recommend the anterolateral minimally invasive approach.

A comprehensive electrophysiological study has been made of the extensor digitorum brevis muscle and its motor innervation in 17 patients with dystrophia myotonica. The mean contraction and half-relaxation times were prolonged in the isometric twitches of dystrophic muscles. Decremental responses to repetitive motor nerve stimulation were found in two patients. All the terminal latency measurements were normal and only one patient had a reduced nerve conduction velocity. As the patients aged their muscles became weaker, due to a progressive loss of motor units. This finding, and the normal sizes of many surviving motor units, suggested that the muscle changes resulted from a primary defect of motor innervation.

BACKGROUND--Breathlessness appears to be closely related to the perception of the outgoing motor command to breathe and should be increased in the presence of muscle weakness. However, breathlessness is not a common symptom in patients with chronic muscle disease who have weak respiratory muscles. The factors that determine the perception of respiratory effort in such patients have not been examined. METHODS--The inspiratory effort sensation during resting breathing and progressive hypercapnia was investigated in 12 patients with dystrophia myotonica with weak respiratory muscles (nine men and three women of mean (SD) age 41.1 (10.5) years; maximum inspiratory pressure 43.1 (17.2) cm H2O) and an age and sex matched control group of normal subjects of mean age 39.6 (10.6) years and a maximum inspiratory pressure of 123 (15.2) cm H2O. RESULTS--During resting breathing with a mouthpiece no differences were seen in inspiratory effort sensation, mouth occlusion pressure, or tidal volume, but inspiratory time and cycle duration were significantly shorter in the patients with dystrophia. Minute ventilation (VE) was significantly higher in the patients (15.8 (4.0) l/min v 12.5 (2.6) l/min), while resting breathing was no more variable in the patients than in controls. The ventilatory response to carbon dioxide (VE/PCO2) was not significantly lower in the patients (14.9 (6.9) l/min/kPa) than in the controls (17.4 (4.3) l/min/kPa). Effort sensation responses to carbon dioxide driven breathing were similar in the control subjects and the patients. With regression analysis of pooled data neither maximum inspiratory pressure nor disease state contributed to perceived inspiratory effort during hypercapnia. CONCLUSIONS--Moderately severe global respiratory muscle weakness does not appear to influence the ventilatory response to rising carbon dioxide tension or the perception of inspiratory effort in patients with dystrophia myotonica.

A gene (designated ecaA) encoding a vertebrate-like (alpha-type) carbonic anhydrase (CA) has been isolated from two disparate cyanobacteria, Anabaena sp. strain PCC 7120 and Synechococcus sp. strain PCC 7942. The deduced amino acid sequences correspond to proteins of 29 and 26 kDa, respectively, and revealed significant sequence similarity to human CAI and CAII, as well as Chlamydomonas CAHI, including conservation of most active-site residues identified in the animal enzymes. Structural similarities between the animal and cyanobacterial enzymes extend to the levels of antigenicity, as the Anabaena protein cross-reacts with antisera derived against chicken CAII. Expression of the cyanobacterial ecaA is regulated by CO2 concentration and is highest in cells grown at elevated levels of CO2. Immunogold localization using an antibody derived against the ecaA protein indicated an extracellular location. Preliminary analysis of Synechococcus mutants in which ecaA has been inactivated by insertion of a drug resistance cassette suggests that extracellular carbonic anhydrase plays a role in inorganic-carbon accumulation by maintaining equilibrium levels of CO2 and HCO3- in the periplasm.

Background

Development of hip adductor, tensor fascia lata, and rectus femoris muscle contractures following total hip arthroplasties are quite common, with some patients failing to improve despite treatment with a variety of non-operative modalities. The purpose of the present study was to describe the use of and patient outcomes of botulinum toxin injections as an adjunctive treatment for muscle tightness following total hip arthroplasty.

Methods

Ten patients (14 hips) who had hip adductor, abductor, and/or flexor muscle contractures following total arthroplasty and had been refractory to physical therapeutic efforts were treated with injection of botulinum toxin A. Eight limbs received injections into the adductor muscle, 8 limbs received injections into the tensor fascia lata muscle, and 2 limbs received injection into the rectus femoris muscle, followed by intensive physical therapy for 6 weeks.

Results

At a mean final follow-up of 20 months, all 14 hips had increased range in the affected arc of motion, with a mean improvement of 23 degrees (range, 10 to 45 degrees). Additionally all hips had an improvement in hip scores, with a significant increase in mean score from 74 points (range, 57 to 91 points) prior to injection to a mean of 96 points (range, 93 to 98) at final follow-up. There were no serious treatment-related adverse events.

Conclusion

Botulinum toxin A injections combined with intensive physical therapy may be considered as a potential treatment modality, especially in difficult cases of muscle tightness that are refractory to standard therapy.

Soft tissue artifacts during motion capture can lead to errors in kinematics and incorrect estimation of joint angles and segment motion. The aim of this study was to evaluate the effect of shank segment axial rotation and knee rotator muscle bounds on predicted muscle and joint forces in a musculoskeletal model of the lower limb. A maximal height jump for ten subjects was analysed using the original motion data and then modified for different levels of internal and external rotation, and with the upper force bound doubled for five muscles. Both externally rotating the shank and doubling the muscle bounds increased the ability of the model to find a solution in regions of high loading. Muscle force levels in popliteus and tensor fascia latae showed statistically significant differences, but less so in plantaris, sartorius or gracilis. The shear and patellofemoral joint forces were found to be significantly affected by axial rotation during specific phases of the motion and were dependent on the amount of rotation. Fewer differences were observed when doubling the muscle bounds, except for the patellofemoral force and plantaris and sartorius muscle force, which were significantly increased in many of the jump phases. These results give an insight into the behaviour of the model and give an indication of the importance of accurate kinematics and subject-specific geometry.

The intact chicken transferrin gene was microinjected into fertilized mouse eggs, and the resulting transgenic animals were used to produce lines of mice containing integrated copies of the chicken gene. The levels of expression of the chicken gene were quantitated in various tissues, and the response of the gene to estrogen stimulation was measured after chronic or acute estrogen exposure. Two of the three mouse lines studied maintained stable levels of expression in successive generations of offspring, and the third line had two- to threefold-higher levels in offspring than in the original parent. In the third line, the original transgenic parent was found to be a mosaic. The chicken transferrin gene was expressed at 10- to 20-fold-higher levels in liver than in any other tissue; however, the levels of chicken transferrin mRNA in kidney were higher than expected, indicating that the tissue specificity was only partial. In all three lines, the foreign gene was induced by estrogen administration. After 10 days of estrogen administration, there was a twofold increase in both transferrin mRNA and transcription of the chicken transferrin gene. A single injection of estradiol led to a fourfold increase in transferrin mRNA synthesis at 4h. As a control the levels of mouse albumin were measured, and both the level of albumin mRNA and its rate of transcription declined about twofold after estrogen administration. Our results indicate that the intact chicken gene with 2.2 kilobases of 5' flanking sequence contains signals for both tissue specificity and steroid regulation that can be recognized in mice.

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We have generated transgenic mouse lines that carry the promoter region of the chicken skeletal muscle alpha (alpha sk) actin gene linked to the bacterial chloramphenicol acetyltransferase (CAT) gene. In adult mice, the pattern of transgene expression resembled that of the endogenous alpha sk actin gene. In most of the transgenic lines, high levels of CAT activity were detected in striated muscle (skeletal and cardiac) but not in the other tissues tested. In striated muscle, transcription of the transgene was initiated at the normal transcriptional start site of the chicken alpha sk actin gene. The region from nucleotides -191 to +27 of the chicken alpha sk actin gene was sufficient to direct the expression of CAT in striated muscle of transgenic mice. These observations suggest that the mechanism of tissue-specific actin gene expression is well conserved in higher vertebrate species.

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Humoral and cellular immunity have been investigated in 15 patients with dystrophia myotonica. No abnormalities in total serum levels of the five major immunoglobulin classes were found but there was a rise in the mean serum level of β1A complement. Altogether, 54% of patients failed to make antibody to tetanus toxoid as compared with 1% of controls: 13% of patients failed to make antibody to Salmonella typhi H antigen as compared with no failure of this function in control subjects. There was a reduced uptake of tritiated thymidine by whole blood lymphocyte cultures spontaneously, while in the presence of phytohaemagglutinin (PHA) and both autologous and fetal calf serum the uptake was normal. It is suggested that there may be a wider derangement of immunological function in dystrophia myotonica than previously thought.

We quantified chicken calpain 2 (CAPN2) expression in two Chinese chicken breeds (mountainous black-bone chicken breed [MB] and a commercial meat type chicken breed [S01]) to discern the tissue and ontogenic expression pattern and its effect on muscle metabolism. Real-time quantitative PCR assay was developed for accurate measurement of the CAPN2 mRNA expression in various tissues from chickens of different ages (0, 2, 4, 6, 8, 10, and 12 weeks). Results showed that the breast muscle and leg muscle tissues had the highest expression of CAPN2 compared to the other tissues from the same individual (P < .05). Overall, the CAPN2 mRNA level exhibited a “rise” developmental change in all tissues. The S01 chicken had a higher expression of the CAPN2 mRNA in all tissues than the MB chicken. Our results suggest that chicken CAPN2 expression may be related to chicken breeds and tissues.

Murine epidermal growth factor (EGF) binds with approximately 250-fold higher binding affinity to the human EGF receptor (EGFR) than to the chicken EGFR. This difference in binding affinity enabled the identification of a major ligand-binding domain for EGF by studying the binding properties of various chicken/human EGFR chimera expressed in transfected cells lacking endogenous EGFR. It was shown that domain III of EGFR is a major ligand-binding region. Here, we analyze the binding properties of novel chicken/human chimera to further delineate the contact sequences in domain III and to assess the role of other regions of EGFR for their contribution to the display of high-affinity EGF binding. The chimeric receptors include chicken EGFR containing domain I of the human EGFR, chicken receptor containing domain I and III of the human EGFR, and two chimeric chicken EGFR containing either the amino terminal or the carboxy terminal halves of domain III of human EGFR, respectively. In addition, the binding of various human-specific anti-EGFR monoclonal antibodies that interfere with EGF binding is also compared. It is concluded that noncontiguous regions of the EGFR contribute additively to the binding of EGF. Each of the two halves of domain III has a similar contribution to the binding energy, and the sum of both is close to that of the entire domain III. This suggests that the folding of domain III juxtaposes sequences that together constitute the ligand-binding site. Domain I also provides a contribution to the binding energy, and the added contributions of both domain I and III to the binding energy generate the high-affinity binding site typical of human EGFR.

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In this paper, 152 patients with 187 osteonecrotic femoral heads (83 idiopathic, 56 corticosteroid induced, 40 post-traumatic, seven alcohol abuse and one associated with gout) were classified according to the staging by Ficat and Arlet (Ischemia and necroses of bone, Williams and Wilkins, Baltimore, Maryland, pp 171–182, 1980); four were in Stage I, 82 in Stage II and 101 in Stage III. The majority of the patients were young (average age 35.5 years). Multiple drilling, curettage of the necrotic bone and muscle-pedicle bone grafting using tensor fascia lata was carried out in all patients except in six adolescents, where sartorius grafting was performed. Cheilectomy of the femoral head and subcutaneous adductor tenotomy were also performed in the advanced stages. During the follow up of 10 to 21.5 years (average 16.5 years), radiological improvement was noted in 81.3% of patients in Stage II and 70.1% of patients in Stage III cases. Excellent and good results according to the Hospital for Special Surgery (HSS) score were obtained in 100% of cases in Stage I, 92% in Stage II and 80.4% in stage III, with a survivorship of 91% in Stage II and 82% in Stage III cases. The patients having an HSS score below 20 (non-survival) were recommended for total hip replacement (THR) therapy.

Erythrocyte labeling by random and cohort techniques was used to study erythrocyte survival in normal chickens and in chickens infected with Plasmodium gallinaceum. White Leghorn chickens, eight weeks of age, were used in this series of experiments.

In chickens given P. gallinaceum on the day following erythrocyte labeling there was destruction of labeled erythrocytes at a much more rapid rate than would result from normal ageing processes. Chickens given P. gallinaceum 12, 18 and 21 days after the labeling of the erythrocytes failed to show any greater destruction of the labeled red cells beyond that resulting from normal senescence. This result indicates that erythrocytes over 12 days of age are not destroyed by P. gallinaceum.