Parthenogenetic activation decreases the polyphosphoinositide content of frog eggs

Polyphosphoinositides were quantified in metaphase II-arrested eggs of the amphibian Xenopus laevis and 8-10 min later in eggs activated by pricking. The content of phosphatidylinositol 4,5-biphosphate (PIP2) was remarkably high in metaphase II-arrested eggs with respect to that of phosphatidylinositol 4-phosphate (PIP). It was found to drop dramatically at activation. In contrast PIP content did not change significantly.     

Cellular receptors for type beta transforming growth factor. Ligand binding and affinity labeling in human and rodent cell lines

Type beta transforming growth factor (beta TGF) purified from human platelets to homogeneity as judged by NH2-terminal amino acid sequence analysis has been labeled with 125I to characterize its interaction with cellular receptors. Binding of 125I-beta TGF to target cells is temperature- and time-dependent, specific, saturable, and reversible. About 1.6-1.9 X 10(4) binding sites/cell with high affinity for beta TGF (Kd = 5.6-7.8 X 10(-11) M and 9.1-14 X 10(-11) M, respectively) are found in NRK-49F and BALB/c 3T3 cells. beta TGF receptors do not appear to undergo acute down-regulation by the ligand. Specific binding of 125I-beta TGF has been observed in several human, rat, and mouse fibroblast lines and in some, but not all, tumor-derived cell lines examined. 125I-beta TGF has been cross-linked to intact cells and isolated membrane preparations using disuccinimidyl suberate. Cells and isolated membranes from human, rat, and mouse origin affinity labeled with 125I-beta TGF exhibit a major labeled species of approximately 280 kilodaltons that has the properties of high affinity and specificity expected from a physiologically relevant beta TGF receptor. Minor labeled species of 70-90 kilodaltons are also labeled by 125I-beta TGF, but they correspond to molecular species with low apparent affinity (Kd approximately 10(-8) M) for 125I-beta TGF.     

Changes in the electrophoretic pattern of the venom of the bushmaster (Lachesis muta stenophrys) stored under various conditions

Liquid and lyophilized samples of Lachesis muta venom were stored at different temperatures and for different periods of time, and analyzed by polyacrylamide gel electrophoresis (PAGE) and immunoelectrophoresis. Only slight variations were evident when three pools of freeze-dried venom, that had been kept at -30 degrees C for several months were compared with fresh venom. These results suggest that L. muta venom is not altered drastically when stored under these conditions.     

Respiratory effects of naloxone

The respiratory effects of naloxone (200 micrograms X kg-1) on dogs, was studied measuring the parameters breath rate, inspiratory volume, breath minute volume, inspiratory time, total time of cycle, inspiratory volume/inspiratory time ratio, and inspiratory time/total time of cycle ratio. The statistical study was made by using the analysis of variance. Naloxone increases all the parameters studied as well as the response to CO2 while it decreases inspiratory time. The results suggest that there are opioid neurons in the respiratory centre. The blockade of the opioid receptors by naloxone almost explains the respiratory effects observed.     

Effect of naloxone on coughing

Naloxone at doses of 200 micrograms X kg-1 increases cough, in experiments carried out on dogs. With stimuli of the same intensity, after naloxone, a significant increase in the number of coughs in each fit, is observed. Changes in the first cough burst, compared with spontaneous respiration at rest, are statistically significant and they contribute to define the characteristics of the cough burst. The increase of cough by naloxone blockade of endorphinic neurons of the respiratory center shows that usually the activity of these inhibitory neurons, tonically depresses the tussive response. The antitussive opiates would seem to operate by activating these inhibitory synapses.     

Stimulation of intestinal adenylate cyclase by cholera toxin in malnourished rats

The stimulation of intestinal adenylate cyclase by cholera toxin (CT) was studied in normal and malnourished rats 4 to 24 hr after a 30-min incubation of intestinal loops with the toxin. Whereas in control rats the enzyme activity returned to basal levels after 12 hr of incubation, in malnourished rats the activity of the enzyme remained significantly elevated even after 24 hr of the initial incubation. Malnourished animals had a reduced turnover rate of intestinal cells as determined by thymidine kinase activity. The delayed turnover of intoxicated cells may account for continuous activation of mucosal adenylate cyclase and possibly for prolongation of diarrhea in malnutrition.     

Synthesis and molecular structure of prolame, N-(3-hydroxy-1,3,5(10)-estratrien-17 beta-yl)-3-hydroxypropylamine; an amino-estrogen with prolonged anticoagulant and brief estrogenic effects

The synthesis and molecular structure of prolame, N-(3-hydroxy-1,3,5(10)-estratrien-17 beta-yl)-3-hydroxypropylamine, is described. It was characterized by ir, nmr, mass spectrometry and chemical analysis. The crystal structure of this compound was determined by single-crystal x-ray diffraction. Prolame belongs to space group P212121. Cell dimensions are: a = 8.356(2), b = 13.343(4) and c = 16.119(4) A. Z = 4; R = 4.1%.     

Isoproterenol induces a ribosomal modification in the heart and the skeletal muscle of hamsters

The protein synthesis activity of heart, skeletal muscle and liver polysomes from isoprotenerol-treated and control hamsters has been compared in an in vitro non-inititating translation system. Heart and skeletal muscle polysomes from treated hamsters were less active than controls and required a higher magnesium concentration for optimal protein synthesis. These results suggest that there is a conformational modification in heart and skeletal muscle ribosomes from isoprotenerol-treated hamsters. No such change was observed with ribosomes from the liver of isoproterenol-treated hamsters.