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Biomedical subjects

B W Wilson

Publications and source records attributed to B W Wilson.

At least 127 records · Page 7Linked to original sources
PubMed1976

Measurement of prostaglandin F2alpha in human cerebrospinal fluid by single ion monitoring.

An imporved method is described for measuring low levels of prostaglandin F2alpha in small volumes of cerebrospinal fluid. Single ion monitoring of the ion at m/e 423, derived from the methyl ester tri-TMS ether derivatives of prostaglandin F2alpha and the internal standard, w-trinor-16-cyclohexyl prostaglandin F2alpha, is employed. Injection of 2 pg of prostaglandin F2 alpha derivative gave a standard deviation of +/- 9%. The majority of patients had cerebrospinal fluid levels of up to 2 ng ml-1 of prostaglandin F2 alpha, whereas in certain neurological conditions with progressive disease, elevated levels were encountered, some of which were higher than 10 ng ml-1.

Chromatography, Gas↗
PubMed1976

A method for the measurement of ultra-low amounts of prostaglandins in inflammatory exudates using gas chromatography and mass spectrometry.

A GC-MS assay for PGE2 and PGF2alpha has been described. The method is highly specific and sensitive down to the sub-picogram level. The assay has been used to measure the time dependence of PG concentration in carrageenan-induced inflammatory exudates and the results compared with a bioassay. Estimates of the extraction and purification yield of PGs from exudates have also been obtained.

Animals↗
PubMed1976

Regulation of acetylcholinesterase in cultured muscle by chemical agents and electrical stimulation.

Cultures of 11 day old chick embryo pectoral muscle were used to study the effects of direct electrical stimulation and neurochemicals such as acetylcholine, acetyl-beta-methylcholine, tetrodotoxin, and d-tubocurarine on the acetylcholinesterase levels of muscle. The results suggest that excitation-contraction is an important factor in regulation of muscle acetylcholinesterase. Tetrodotoxin, acetylcholine and its analog acetyl-beta-methylcholine increased acetylcholinesterase levels and reduced spontaneous contractions. D-tubocurarine blocked the increase in acetylcholinesterase and the decrease in spontaneous contractions caused by acetyl-beta-methylcholine. Electrical stimulation decreased acetylcholinesterase and increased muscle contractions in normal and in diisopropylfluorophosphate treated cultures. Tetrodotoxin also affected the morphology of the muscle cells, as if it adversely affected normal growth and differentiation. Electrical stimulation did not increase muscle creatine kinase.

Acetylcholine↗
PubMed1976

Regulation of acetylcholinesterase in chick muscle cultures after treatment with diisopropylphosphorofluoridate: ribonucleic acid and protein synthesis.

Previous studies have established that short treatments with diisoprophylphosphorofluoridate of chick embryo muscle cultures irreversibly inhibit the enzyme acetylcholinesterase and that the enzyme's levels in the cells rapidly recover due to synthesis of new protein. In addition, it has been shown that acetylcholine, acetyl-beta-methylcholine and choline increase the acetylcholinesterase content of the cultures. In the experiments presented here, actinomycin D and cycloheximide were used to study the relationships between the synthesis of ribonucleic acid and of protein, the recovery of acetylcholinesterase levels after diisopropylphosphorofluoridate treatment and the increase of acetylcholinesterase levels evoked by choline and its esters. Both recovery of acetylcholinesterase and the increase in its activity with acetyl-beta-methylcholine occurred in the absence of ribonucleic acid synthesis but required protein synthesis. The results suggest that transcription of desoxyribonucleic acid and a change in the degradation rate of acetylcholinesterase are not involved. An additional finding was that the level of newly synthesized acetylcholinesterase activity continued to increase for a short period of time after synthesis of protein had ceased, as if some previously synthesized protein was being transformed into active enzyme.

Acetylcholinesterase↗
PubMed1976

Ultrastructural localization of acetylcholinesterase in cultured cells. I. Embryo muscle.

Several techniques were employed to examine the localization of acetylcholinesterase (EC 3.1.1.7, AChE) in cultured chick embryonic skeletal muscle. Glutaraldehyde produced the best cellular preservation but less enzyme activity was lost when the cells were fixed in paraformaldehyde. Two staining methods were examined: in one (Karnovsky MJ, Roots L: J Histochem Cytochem 12:219, 1964) potassium ferricyanide was added with the primary reactants, and in the other (Tsuji S: Histochemistry 42:99, 1974) the potassium ferricyanide was added at the end of the staining procedure. Localizations of AChE were similar with both stains; activity was present in the nuclear envelope, the perinuclear sarcoplasm, the sarcoplasmic reticulum, subsurface vesicles and bound outside the cells. /owever, a granular artifact was found with the method of Karnovsky and Roots that did not appear with the method of Tsuji. The localization of AChE are consistent with kinetic data that AchE binds, moves and is released from cultured muscle fibers.

Acetylcholinesterase↗
PubMed1976

Absorption of 125I-labelled sheep growth hormone in single proximal tubules of the rat kidney.

Techniques of kidney micropuncture and electron microscope autoradiography have been used to study the uptake of 125I-labelled sheep growth hormone (GH) in rat renal proximal tubules. After microperfusion of a proximal tubule with 125I-labelled GH, the transport of label by the tubular epithelium was studied autoradiographically at selected times up to 1 h. The sequential transfer of labelled material from tubule to microvilli, then to small and large apical vacuoles and finally to lysosomes followed the pattern of absorption that has been described for other proteins. Evidence of lysosomal degradation of the transported protein was obtained from studies in vitro; lysosomes isolated from the renal cortex rapidly converted 125I-labelled GH to products of lower molecular weight. In addition to the absorptive pathway through the intracellular vacuolar apparatus is appeared that there was also an alternative pathway, less well defined, whereby GH could be absorbed without being degraded.

Animals↗
PubMed1976

Acetylcholinesterase in abnormal human muscle.

Fifty human muscle biopsies were examined for histochemical localization of acetylcholinesterase (AChE) activity. Six normal muscle samples had AChE at the myoneural junctions and around the periphery of many fibers. The AChE within the sarcoplasm itself was found in only a few atrophied fibers. However, 21 of 44 biopsies of abnormal muscles had sarcoplasmic AChE in more than 10% of their fibers. Such cases included Duchenne, limb-girdle and facio-scapulo-humeral dystrophy, neurogenic and spinal muscle atrophy, spinal cord injury, peripheral nerve injury, Schwartz-Jampel syndrome and myasthenic syndrome. Sarcoplasmic AChE is found in embryo muscle and usually declines after birth. It appears after denervation in the chicken but not the rat and remains in muscles of chickens with an inherited muscular dystrophy. The results of the human muscle study support the idea that in the human, as in the chicken, interruption of a neurally-mediated regulation of AChE results in the reappearance of high AChE activity in the sarcoplasm of the muscle fibers.

Acetylcholinesterase↗
PubMed1975

Myogenic defect in acetylcholinesterase regulation in muscular dystrophy of the chicken.

To determine whether inherited muscular dystrophy of the chicken is neurogenic or myogenic in origin, limb buds from homozygous normal and dystrophic chick embryos were exchanged prior to muscle differentiation and innervation. Biceps muscles of hatched chicks, in which muscle of the donor was innervated by nerves of the host, were analyzed for embryonic properties of muscle acetylcholinesterase and for fiber diameter, two distinctive markers for expression of the dystrophic gene. The results indicate that muscular dystrophy of the chicken is caused by an initial biochemical lesion in the limb and its muscle rather than in its innervating nerve.

Acetylcholinesterase↗
PubMed1975

Acetylcholinesterase in singly and multiply innervated muscles of normal and dystrophic chickens. II. Effects of denervation.

Neural regulation of mature normal fast twitch muscle of the chicken suppresses high activity, extrajunctional localization, and isozyme forms of acetylcholinesterase (AChE) characteristic of embryonic, denervated and dystrophic muscle. Normal adult slow tonic muscle ofthe chicken retains intermediate levels of activity and embryonic isozyme forms but not extrajunctional activity; it is not affected by muscular dystrophy. The hypothesis that neural regulation of the AChE system is lacking in slow tonic muscle and thus not affected by dystrophy was tested by denervating the fast twitch posterior latissimus dorsi and slow tonic anterior latissimus dorsi muscles of normal and dystrophic chickens. Extrajunctional AChE activity and embryonic isozyme forms increased, then declined, in both muscles. The results suggest that ocntrol of AChE is qualitatively similar in slow tonic and fast twitch muscle of the chicken.

Acetylcholinesterase↗
PubMed1975

Incidence of acetylcholinesterase in the sarcoplasm of human and chicken muscles.

Fifty-nine biopsies of human muscle, 53 of them abnormal, 6 normal, were studied for the histochemical localization of acetylcholinesterase (AChE) using frozen sections and light microscopy. In addition to AChE which was found at the myoneural and myotendon junction, specific staining was found around the periphery of many fibers from normal and abnormal muscles. Moreover, AChE activity was found to be high in the sarcoplasm of more than 10% of the fibers from 28 biopsies of abnormal muscle including cases of hemiplegia, spinal cord injury, denervation and neuropathy, infantile spinal muscle atrophy, Duchenne, limb-girdle and facioscapulohumeral dystrophies, Schwartz-Jampel syndrome and a myasthenic syndrome. Of the muscles from experimental animals examined, only the Rhesus monkey exhibited AChE around the periphery of the fibers, and only the dystrophic chicken and not the dystrophic mouse or hamster, showed extensive sarcoplasmic AChE. Histograms of muscle fiber diameters indicated that AChE in the sarcoplasm was associated with fibers of all sizes, depending on the nature of the disorder examined. Fibers containing AChE were smaller than unstained fibers in dystrophic chicken muscle. The results suggest that in the human, sarcoplasmic AChE is reversibly repressed during muscle maturation and that its mode of regulation by motor neurons is similar to that found in the chicken.

Acetylcholinesterase↗
PubMed1975

Appearance of acetylcholinesterase and creatine kinase in plasma of normal chickens after denervation.

Evidence that acetylcholinesterase (AChE) activity is released from normal chick embryonic muscle fibers and from muscles of chickens with inherited muscular dystrophy suggested that denervated chick muscles, which have AChE properties similar to dystrophic muscles, would also release AChE. Bilateral denervation of the breast and wing muscles of normal chickens was followed by the appearance of AChE activity, distinguished from plasma cholinesterase by differential substrate hydrolysis, inhibitor sensitivity, and electrophoretic migration. Plasma creatine kinase (CK) activity was also elevated after denervation.

Acetylcholinesterase↗