Uptake by central nervous tissues as a mechanism for the regulation of extracellular adenosine concentrations

The various facets of the uptake of adenosine by central nervous tissues are described. The uptake process includes the transport of nucleoside across neuronal and glial plasma membranes and its metabolism within the cell. Much of the transported adenosine is phosphorylated into adenosine nucleotides. Inhibitors of adenosine uptake increase extracellular levels of adenosine and can thus potentiate its pharmacological actions. This may be an important component in the actions of various groups of psychoactive drugs.     

Effects of prostaglandin E2, 16,16-dimethyl prostaglandin E2 and a prostaglandin endoperoxide analogue (U-46619) on gastric secretory volume, [H] and mucus synthesis and secretion in the rat

The effects of orally administered prostaglandin E₂, 16,16-dimethyl prostaglandin E₂ and U-46619, an analogue of the prostaglandin endoperoxide PGH₂, on gastric secretory volume, acid and mucus were studied in the rat. All of the compounds significantly increased the volume of gastric secretion, mucus secretion, measured as N-acetylneuraminic acid and mucus synthesis measured as the incorporation of [³H]-glucosamine into mucosal glycoprotein; however, only PGE₂ and 16,16-dimethyl PGE₂ inhibited acid secretion. U-46619, 1.5 mg/kg provided significant protection against ethanol-induced gastric ulcers, an effect that has been previously shown for the other two compounds. These studies provide additional evidence that prostaglandin induced mucosal protection may by related to an effect on mucus and on stimulation of nonparietal cell gastric secretion. Further study of these parameters may be important in the development of antiulcer drugs for long term clinical use.     

The shape of myosin subfragment-1. A equivalent oblate ellipsoid model based on hydrodynamic properties

The molecular weights of the two heads of myosin subfragment-1, S-1(A1) and S-1(A2), based on sedimentation equilibrium are 120 000 and 110 000. Hydrodynamically, the two heads are indistinguishable, with intrinsic viscosity, [eta], of 0.064-0.065 dL/g and sedimentation coefficient, s(0)20,w, of 5.8 S.Together with the rotational correlation time taken from the literature (235 ns), all three hydrodynamic properties can be better fitted with an equivalent oblate ellipsoid of revolution than a prolate model. The width of the equatorial axis of the ellipsoid is about 135 A (the axial ratio is about 6). Probably, the S-1(A1) and S-1(A2) molecules have a half-doughnutlike or a flattened pearlike shape rather than an elongated one.     

Hyphal anastomosis inPyricularia oryzae cav.

Summary Hyphal anastomosis inPyricularia oryzae occurs naturally in the lower epidermal cells and in the vascular bundles of young lesions on rice. In those cells the invading blast fungus are active. Two hyphal cells lying side by side start an anastomosis by forming two, one from each, very short penetration pegs which are opposite to each other. The cell wall of the pegs and the wall in the vicinity of them are then gradually eliminated and thus form a fusion aperture of 0.2–0.6 m in diameter that is big enough for the migration or exchange of nucleus and cytoplasm between two hyphal cells. The explanation of genetical variation inP. oryzae may be sought on the basis of the ultrastructural evidence of hyphal anastomoses presented in this paper.     

Glutamine synthetase. IX. Purification and characterization of the enzyme from sheep spleen.

Glutamine synthetase (L-glutamate: ammonia ligase (ADP-forming), EC 6.3.1.2) has been purified about 550-fold from sheep spleen. The subunit weight of the enzyme is estimated to be 48 000. Sedimentation coefficient determination by density gradient centrifugation gives a value of 15.0 S. The approximate molecular weight calculated from the S value is 378500. In addition, electron micrographs of the enzyme show an "H" shape. Hence, the protein appears to have eight subunits. In sheep spleen, the enzyme resides chiefly in the soluble fraction of the cell. The amino acid composition of the enzyme from spleen shows similarity to that from other sources. The enzyme activity is nearly five times as high in Mg2+ as in Mn2+. ATP inhibits the enzyme; the inhibition is competitive with respect to Mg2+ATP. A number of compounds, such as D-alanine, AMP, creatine phosphate, arsenite in combination with 2,3-dimercaptopropanol, and 2-amino-4-phosphonobutyrate, also inhibit the enzyme. The inhibition by the last compound is competitive with respect to glutamate. D-Glutamate and alpha-methyl-DL-glutamate can serve as substrates in the synthesis reaction, but N-methyl-DL-glutamate cannot. On the other hand, neither D-glutamine nor N-acetyl-L-glutamine can replace L-glutamine as a substrate in the gamma-glutamyl transfer reaction of the enzyme. Inhibition of Mn2+ and ATP and its reversal by Mg2+ have been discussed as a means of regulating the enzyme activity in mammalian tissues.