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Biomedical subjects

D L Simpson

Publications and source records attributed to D L Simpson.

36 records · Page 2Linked to original sources
PubMed1978

Age related alterations in the chromosomal proteins from human diploid fibroblasts.

Histone and non-histone chromosomal proteins from human diploid fibroblasts of different in vitro ages were extracted and subjected to SDS--polycrylamide gel electrophoresis. The proteins were taken from cells maintained in three distinct culture states: preconfluent (log phase of growth), confluent (stationary phase of growth), and arrested (presumptive G0 phase). Age associated alterations in the incorporation of radioactive amino acids were detected in the fractionated proteins in every culture state but were less pronounced during the arrested state. Age related difference detected under growth conditions may reflect variations in the proliferative nature of the populations. Differences seen during the arrested state may be indicative of basic changes in the chromosomal protein complement of different age populations.

Amino Acids↗
PubMed1978

Long-term follow-up and bronchial reactivity testing in survivors of the adult respiratory distress syndrome.

Long-term follow-up of 9 survivors of the adult respiratory distress syndrome at 39 to 83 months demonstrated 2 patients with continued improvement of their restrictive pattern, 3 patients with stable mild obstructive disease, one patient who had had chronic obstructive pulmonary disease before the adult respiratory distress syndrome with continued pulmonary deterioration, and 4 patients without symptoms and with normal pulmonary function tests. Attention is drawn to bronchial reactivity as defined by a bronchodilator response of more than 60 per cent increase in maximal mid-expiratory flow, positive methacholine challenge, or development of bronchospasm after exercise in 3 patients having clinical symptoms of wheezing on recovery.

Adolescent↗
PubMed1976

Sulfated glycoproteins, glycolipids, and glycosaminoglycans from synaptic plasma and myelin membranes: isolation and characterization of sulfated glycopeptides.

In this report we provide biochemical evidence that a highly purified synaptic plasma membrane fraction derived from rat brain, after intraventricular injection of 35S-labeled sodium sulfate, is enriched in a number of large sulfated glycoproteins compared with a purified myelin fraction studied concurrently. A fraction of the detergent-solubilized sulfated glycoprotein bound specifically to concanavalin A-Sepharose. In addition, we have identified the 35S-labeled lipid-soluble material in these membrane fractions as cerebroside sulfate. The sulfated protein in the lipid-extracted membranes was shown to consist predominantly of a class of glycoproteins containing sulfate in ester linkage to oligosaccharide chains, which are differentiated structurally from the sulfated glycosaminoglycans of brain. These two classes of sulfated macromolecules were distinguished from one another by several chemical and physical parameters. We present the chemical characterization of the sulfated glycopeptides derived from synaptic plasma and myelin membranes by extensive proteolytic digestion after quantitative removal of cerebroside sulfate. Membrane-associated glycosaminoglycans, either specifically or adventitously associated with these neuronal membranes, were quantitatively precipitated and identified.

Amino Acids↗
PubMed1975

Pallidin. Purification and characterization of a carbohydrate-binding protein from Polysphondylium pallidum implicated in intercellular adhesion.

A carbohydrate-binding protein from Polysphondylium pallidum, a species of cellular slime mold, was purified to homogeneity by adsorption to formalinized erythrocytes and elution with D-galactose. The protein, for which we propose the name PALLIDIN, is assayed by its activity as an agglutinin of erythrocytes. It was previously shown to have different carbohydrate-binding specificities than discoidin, a carbohydrate-binding protein from Dictyostelium discoideum, another species of slime mold. Evidence has been presented previously that each of these proteins is detectable on the cell surface. In the present report we show that the physico-chemical properties of pallidin are different from discoidin. Pallidin has a subunit molecular weight of 24 800 +/- 1100 determined by polyacrylamide electrophoresis in the presence of dodecyl sulfate and 2-mercaptoethanol, compared to 26 100 +/- 1000 for discoidin. The weight-average molecular weight of pallidin is 250 000 +/- 50 000 determined by equilibrium sedimentation in the presence of D-galactose compared to 100 000 +/- 2000 for discoidin. In equilibrium sedimentation studies, pallidin exhibited some heterogeneity at equilibrium while discoidin was homogeneous. The amino acid composition of pallidin is generally similar but clearly different from the composition of discoidin. The isoelectric point of pallidin is 7.0 compared to 6.1 for discoidin. Like discoidin, pallidin contains no detectable hexosamine or neutral sugar. These results establish that agglutinins from two species of cellular slime molds are distinct. The different properties of the cell-surface agglutinins, pallidin and discoidin, are consistent with their suggested role in species-specific cellular recognition and adhesion in the species of slime mold from which they are derived.

Amino Acids↗
PubMed1973

Developmentally regulated, carbohydrate-binding protein in Dictyostelium discoideum.

A carbohydrate-binding protein assayed by its ability to agglutinate formalinized sheep erythrocytes is synthesized between 3 and 9 hr after Dictyostelium discoideum cells are deprived of food, as the cells become cohesive. Agglutination of erythrocytes by this protein was inhibited by N-acetyl-D-galactosamine, D-galactose, and L-fucose, but other monosaccharides had little or no effect. The protein bound completely to Sepharose 4B, and was isolated in highly purified form by elution with D-galactose. It appears to be present on the surface of cohesive but not vegetative slime-mold cells. The possibility that this protein may mediate intercellular adhesion in Dictyostelium is considered.

Agglutination↗
PubMedDate not supplied

Gracilis or semitendinosus myopathy in 18 dogs.

The clinical findings in 18 dogs with gracilis (n = 17) or semitendinosus (n = 1) myopathy are described. Each dog had a similar hind-limb gait abnormality characterized by a shortened stride with a rapid, elastic medial rotation of the paw, internal rotation of the hock and external rotation of the calcaneus [corrected] and internal rotation of the stifle during the mid-to-late swing phase of the stride. Medical management prior to or in lieu of surgery was attempted (n = 8) with no apparent response. Fifteen dogs had one or multiple surgical procedures. Although transection, partial excision, or complete resection of the affected muscle resulted in resolution of lameness following surgery, lameness recurred six weeks to five months (mean, 2.5 months; median, two months) following surgery. Adjunctive medical treatment did not prevent recurrence. Variable replacement of the affected muscle with fibrous connective tissue (predominantly along the caudolateral border of the muscle) was evident grossly, and replacement of myofibers with fibrous connective tissue was confirmed histologically. A definitive etiology could not be established.

Animals↗