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Biomedical subjects

F J Wilson

Publications and source records attributed to F J Wilson.

36 records · Page 2Linked to original sources
PubMed1983

Type II collagen-induced arthritis. Studies with purified anticollagen immunoglobulin.

Immunization of rats with native bovine type II collagen results in a polyarthritis by day 21 in approximately 40% of the rats. Sera of these rats contained anticollagen IgG, principally IgG2a. Small amounts of IgG2b were also detected, but IgG1 and IgG2c were absent. By enzyme-linked immunosorbent assay, the paw tissue of these polyarthritic rats was shown to contain anticollagen IgG, the principal subclass being IgG2a, with minor amounts of IgG2b. Immunofluorescence examination of the paws from polyarthritic rats demonstrated deposition of both IgG and C3 on the articular surface. Passive transfer of disease was accomplished by injection of affinity-purified anticollagen immunoglobulin into naive recipients; paw swelling and histopathologic changes were detected 24 hours after transfer, and by immunofluorescence techniques IgG and C3 deposits were demonstrable on the articular cartilage. On passive transfer, neutrophils invaded the joint space and became juxtaposed to the surface of the articular cartilage. Passive transfer of the disease with anticollagen immunoglobulin was unsuccessful after rats were decomplemented with cobra venom factor; immunofluorescence demonstrated IgG but not C3 on the articular cartilage of these decomplemented rats. In rats decomplemented with cobra venom factor, neutrophils did not accumulate in the joint and erosion of articular cartilage was not detected.

Animals↗
PubMed1983

A covalently cross-linked matrix in skeletal muscle fibers.

When skeletal, cardiac, and smooth muscle is exhaustively extracted with a protein-unfolding reagent such as 6 M guanidine HCl and a disulfide-reducing reagent such as 5% beta-mercaptoethanol, a tissue ghost remains intact and retains the characteristic shape and dimensions of the tissue before extraction. In the case of chicken pectoral muscle, the tissue ghost contains 1% of the original muscle proteins. Guanidine HCl extraction followed by collagenase treatment of glycerol-extracted chicken pectoral muscle releases a clean preparation of elongated structures containing 0.2% of the original protein and representing the covalently cross-linked remnants of the muscle fibers. The material of these muscle fiber ghosts extends throughout the interior of the cell. Antibodies raised against the tissue ghosts of smooth muscle cross-react with glycerol extracted skeletal myofibrils, forming a banding pattern which coincides with the banding pattern observed when myofibrils are reacted with antibodies against titin. Titin, a large and soluble protein found in skeletal muscle, cross-reacts with our antigizzard antibody. However, amino acid analysis of the muscle fiber ghosts indicates that titin cannot be the only subunit of the insoluble polymer, but that one or more proteins with a very high glycine and alanine content and a very low basic and acidic amino acid content must also form part of the covalently cross-linked matrix. The possibility is presented that this matrix may be the basis of the superthin 2-3-nm filaments which have been observed in a variety of cell types.

Amino Acids↗
PubMed1983

Immunohistochemical localization of troponin-C in cultured neurons.

Our previous immunofluorescence studies on neurons have demonstrated the presence of myosin in regions of neurons which contained actin. To determine if a system similar to the troponin complex of striated muscle is present in neurons, antibody shown to be specific for the calcium-binding component of troponin (troponin-C) was applied to cultures of embryonic chick and rat dorsal root ganglia. Neurites treated with anti-troponin-C exhibited a bright fluorescence. Accompanying non-neuronal cells were less reactive than the neuronal elements. Immunodiffusion and immunofluorescence showed that the anti-troponin-C did not react with calmodulin, whereas homogenates of the ganglia elicited a positive immunochemical reaction with the anti-troponin-C in Ouchterlony tests. Our results suggest that some intra-axonal movements may be generated by the interaction of actin and myosin and controlled in part by a calcium-troponin-C-dependent mechanism.

Animals↗
PubMed1983

Evaluation and management of acute asthma.

Successful management of asthma requires an expectant, aggressive approach to asthma attacks as well as a careful management program to maintain remissions. The patient must recognize when he or she needs help, and the physician must be able to assess the severity of deterioration and provide rapid aggressive care. Failures are usually due to patient or physician error, or both. These relate to failures both outside and inside the hospital. Once inside the hospital, failure is mainly the responsibility of the physician. It is clear that deaths in the hospital have been associated with inadequate patient observation and monitoring, and treatment that is less aggressive than required. With appropriate patient and physician education and aggressive management, deaths during acute asthma attacks should be rare.

Acute Disease↗
PubMed1982

Oculopharyngeal dystrophy: ultrastructure of muscles distinct from the primary myopathy.

The pectoral and psoas muscles from a 72-year-old man afflicted with oculopharyngeal muscular dystrophy were processed at autopsy for electron microscopy. The ultrastructural analyses of the pectoral muscle showed myofibrils which exhibited Z line streaming and a general breakdown in the organization of the sarcomere. In addition, some of the myofibrils displayed sites of degeneration at the center of the A band. The changes in the psoas muscles which are distant from the primary myopathic loci of oculopharyngeal muscular dystrophy were more extensive than that seen in the pectoral muscle. Control tissues showed intact myofibrils ad little postmortem alteration.

Aged↗
PubMed1982

Haemophilus influenzae infection of an existing lung cyst.

Although Haemophilus influenzae is becoming recognized as a cause of serious pulmonary infections in adults, it has not been previously reported to infect lung cysts. We describe a 25-year-old man who had a lung cyst in which a serious infection developed. Both needle aspiration of the cyst and blood culture confirmed that the infection was caused by H influenzae.

Adult↗
PubMed1982

Ibuprofen in canine endotoxin shock.

The participation of prostaglandins in the physiologic alterations of endotoxin shock has been well established with the aid of prostaglandin synthetase inhibitors. Our study was designed to investigate the potential of ibuprofen, a highly specific cyclooxygenase inhibitor, to reverse the hemodynamic and acid base abnormalities of canine endotoxin shock. Mean blood pressure fell to 49.8 +/- 6.6 mm Hg in dogs given endotoxin by 5 min after injection, and remained below 83 mm Hg for the duration of the 120-min observation period. In animals given endotoxin followed by ibuprofen, a similar initial drop of systemic blood pressure was seen, but it subsequently recovered to 150.2 +/- 4.1 mm Hg by 120 min (P less than 0.001). Cardiac index increased in animals given ibuprofen (2.3 +/- 0.28 liter/m2 per min) compared with animals given endotoxin alone (1.0 +/- 0.09 liter/m2 per min) by termination of the experiment. The arterial pH dropped in endotoxin treated animals to 7.18 +/- 0.03 by 120 min. Ibuprofen prevented the acidosis, the final pH in ibuprofen and endotoxin treated animals measuring 7.36 +/- 0.01. We conclude that ibuprofen protects against the hypotension, acidosis, and depression of cardiac index of canine endotoxin shock.

Animals↗
PubMed1980

The structure of segments of the anisotropic band of muscle. II. Preparation and properties of A segments from vertebrate skeletal muscle.

The anisotropic band of skeletal muscle is a complex structural assembly of the protein myosin and associated nonmyosin components. To study the relationships among these proteins, aggregates of thick myofilaments held together at the M line (A segments) have been prepared from fresh and glycerol extracted chicken pectoralis and rabbit psoas muscles and from fresh frog sartorius muscle. The structure of the A segments included several thick filaments, an M line, and a bare zone or pseudo-H zone, lateral to the M line. Most of the A segments exhibited a pattern of eleven periodic stripes in each half lateral to the bare zone. The A segments from fresh muscle displayed these stripes more consistently than did the A segments from glycerinated muscle. Some of the major stripes appeared to be double, and there were two subdivisions between the stripes nearest the bare zone. The more lateral of the major A band stripes, however, had one subdivision between them. The M line consisted of three prominent medial stripes and two fainter lateral stripes. In the M lines of rabbit A segments the lateral stripes were located well into the bare zone whereas the lateral stripes of M lines in chicken A segments were closer to the three medial M line stripes. Our results on the preparation and properties of A segments are compared with those of of the investigators.

Animals↗
PubMed1979

The structure of A segments from glycerinated skeletal muscle.

The A band of skeletal muscle consists of an array of thick myosin-containing filaments along with non-myosin proteins such as C protein and M line protein. In order to study the arrangement of the myosin and non-myosin components, A segments which are aggregations of thick filaments held together at the M line were prepared from glycerinated chicken pectoral and rabbit psoas muscles and examined by electron microscopy. Details of the preparative technique and comparison of the morphologies of A segments and I segments are provided. The A segments from chicken pectoral muscle exhibited 11 to 12 stripes in each half lateral to the bare zone. Several less distinct bands as well as subdivisions of the individual stripes were also observed. The periodicity of the major stripes in the A segments was 424 +/- 10 A. The A segments prepared from rabbit psoas muscle had a periodicity of 432 +/- 13 A, but in contrast with chicken A segments, fewer rabbit A segments showed this periodicity. We conclude that A segments can be separated from glycerinated chicken and rabbit skeletal muscles and compare our results with those of others who prepared A segments from frog and rabbit skeletal muscles in the absence of glycerol.

Animals↗
PubMed1979

Method for sampling airway gas.

We have devised an improved technique for sampling gas from endotracheal airways for mass spectrometer analysis. It is reliable and unobtrusive and is particularly resistant to occlusion of the sampling line by secrections. It has performed well during continuous monitoring of patients in a respiratory ICU.

Gases↗
PubMed1978

Immunohistochemical and ultrastructural distribution of antibodies to troponin-C and troponin-I in normal and dystrophic chicken skeletal muscle.

The pectoral muscles from normal and dystrophic chickens were reacted with rabbit antisera to troponin-C and to troponin-I, and the distribution of antibodies was determined by fluorescence microscopy of antibody-stained myofibrils and immuno-electron microscopy of separated I band segments. Chickens of dystrophic strain 308 and control New Hampshire hens were used in this work. Myofibrils which were prepared from both normal and dystrophic muscles and reacted with anti-troponin-I were fluorescent in the I band and A band regions. The Z lines and H zones were unstained. Myofibrils prepared from normal pectoral muscle and treated with anti-troponin-C yielded a pattern of fluorescence similar to that for anti-troponin-I treated myofibrils. However, those myofibrils isolated from dystrophic muscle and reacted with anti-tropinin-C had a weak fluorescence over their entire lengths, and discrete A- and I-band staining was not visible. These results were confirmed by ultrastructural studies of separated I segments reacted with the antisera. It is concluded that in the dystrophic muscle either the antigenic sites of troponin-C are changed which results in a loss of antibody-combining ability or these sites are masked in some way which prevents the reaction with the antibody.

Animals↗
PubMed1977

An effect of avian hereditary muscular dystrophy on the reaction of troponin-C with its antibody.

Antibody prepared against troponin-C, the calcium binding component of the troponin complex, was reacted with I band segments, and the distribution of antibody binding was assessed by immuno-electron microscopy. The I segments were isolated from glycerinated pectoral muscle which was prepared from normal adult chickens and from dystrophic chickens of strain 308. The antibody was deposited at 384 A +/- 7 A intervals along the thin filaments of the normal muscle. In contrast to the normal controls the dystrophic muscle did not exhibit a distinct periodicity when reacted with anti-troponin-C. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate revealed that although protein bands corresponding to troponin-C could be observed in the gels of the dystrophic preparations, the troponin-C band had migrated slower than that from normal thin filaments. It is concluded that avian muscular dystrophy produces an alteration of the structure of troponin-C resulting in (1) an inability of the protein to combine with its specific antibody and (2) a change in its electrophoretic behavior.

Animals↗
PubMed1977

Distribution of antibodies to the troponin complex, troponin-C and troponin-I in chicken skeletal muscle as determined by a simplified method for immuno-electron microscopy.

Antisera against the troponin complex, troponin-C and troponin-I have been utilized to locate these proteins in normal, adult chicken skeletal muscle and in filaments prepared from chicken acetone dried powder. The antisera had been previously characterized by immunochemical methods and were employed to ascertain the distribution of the proteins by a simple method for immuno-electron microscopy. Glycerinated chicken breast muscle was treated with the antisera, unreacted antibody was washed from the muscle, and a goat anti-rabbit gamma-globulin was added to enhance the electron density of the antigen-antibody complexes. A periodic distribution of anti-troponin-C at a mean interval of 389 A was observed along the thin filaments in the sectioned tissue. Anti-troponin-I was deposited every 399 A (P less than 0-01). Thin filaments were prepared from acetone dried powder and reacted with the antisera. The anti-troponin-C was located every 389 A; anti-troponin-I, every 399 A (P less than 0-01). Our technique for immuno-electron microscopy is compared with that used by others, and the significance of the findings is discussed.

Analysis of Variance↗