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Biomedical subjects

A Cogoli

Publications and source records attributed to A Cogoli.

84 records · Page 5Linked to original sources
PubMed1980

Effect of hypogravity on human lymphocyte activation.

Cultures of human lymphocytes were exposed to the mitogen concanavalin A in a low-G environment generated by a fast rotating clinostat. DNA-synthesis was determined by incorporation of 3H-thymidine as the parameter for activation, cell ultrastructure was analyzed by electron microscopy, and cell movements were recorded by a cinecamera. The results were compared with 1-G controls. The cells cultured at low G show: (i) depression of activation by 50%, (ii) appearance of "mitochondria-rich" cells, and (iii) enhanced formation of pseudovilli and uropods. Our investigations in vitro at low and high G and reports on the effect of spaceflights on lymphocytes from cosmonauts and astronauts suggest that hypogravity depresses, whereas hypergravity enhances, lymphocyte activation by mitogens. This study is complementary to an experiment which will study the in vitro activation of lymphocytes in weightlessness during the first Spacelab mission.

Cell Movement↗
PubMed1979

Effect of gravity on lymphocyte proliferation.

Reports on postflight examination of lymphocytes from crew members of soviet and american spaceships show a depression of reactivity towards mitogens in vitro. The purpose of this communication is to present experimental evidence that gravity can interfere with lymphocyte activation. Lymphocytes were incubated in the presence of concanavalin A in a centrifuge at 2 and 4 g for four days. This environment causes a significant acceleration of the response to the mitogen. In addition, remarkable differences in the ultrastructure of cells grown at 1 g and 4 g are observed by electron microscopy. This investigation is related to the experiment "Effect of weightlessness on lymphocyte proliferation" experiment which will be performed during the first Spacelab mission.

Animals↗
PubMed1977

Carboxyl groups at the two active centers of sucrase-isomaltase from rabbit small intestine.

1. Seveal selective reagents were employed to identify the amino acid residues essential for the catalytic activity of sucrase-isomaltase. 2. Modification of histidine, lysine and carboxyl residues resulted in a partial inactivation of the enzyme. Substrates or competitive inhibitors provided protection against inactivation only in the reaction of carboxyl groups with carbodiimide (+lycine ethyl ester) or with diazoacetic ethyl ester. This indicated the occurrence of carboxyl groups at the two active centers of the enzyme complex. 3. Protection against inactivation of the enzyme by carbodiimide was provided also by the presence of alkali and alkaline earth metal ions, which are non-essential activators of sucrase-isomaltase. The presence of Na+ and Ba2+ protected approximately one carboxyl group per active center from reacting with carbodiimide plus glycine ethyl ester. 4. The carbodiimide-reactive groups were not identical with the two carboxylate groups recently found to react with conduritol-B-epoxide, an active-site-directed inhibitor of sucrase-isomaltase (Quaroni, A. and Semenza, G., 1976, J. Biol. Chem 251,3250--3253). A possible role for the carbodiimide-reactive carboxyl groups at the active centers of sucrase-isomaltase is discussed.

Animals↗
PubMed1976

A spectroscopic technique for measuring slow rotational diffusion of macromolecules. 1: Preparation and properties of a triplet probe.

Slow rotational diffusion may be investigated by measuring the decay of dichroism of flash-induced transient absorption changes of suitable probes. The preparation of the covalent ""triplets" probe eosin isothiocyanate is described together with investigations of spectroscopic properties of eosin-protein conjugates. Triplet state lifetimes of air-equilibrated solutions of eosin-protein conjugates are in the order of 10 mus, demonstrating that the probe is protected from oxygen quenching by the protein. Experiments with the sucrase-isomaltase complex from small intestine show that its enzymatic activity is little affected by binding up to 2 mol of eosin/mol of protein.

Animals↗
PubMed1975

A probable oxocarbonium ion in the reaction mechanism of small intestinal sucrase and isomaltase.

1-5-D-Gluconolactone is a competitive inhibitor of both sucrase and isomaltase. Substitution of the 1H and 2H at C1 of the glucosyl moiety in p-CL-phenyl-alpha-D-glucopyranoside leads to a decrease in kcat of both sucrase and isomaltase, the k1H/k2H ranging between 1.14 and 1.20. Treatment of the association constants and of the kcat values for a number of p-substituted phenyl-alpha-D-glucopyranosides on the basis of the Hammet-Hansch equation has allowed the estimation of the importance of hydrophilicity-hydrophobicity as well as of the magnitude of the p values for both substrate-enzyme interaction and catalysis in both sucrase and isomaltase. The magnitude of the secondary deuterium effect as well as the low values of p in both sucrase and isomlatase are strongly indicative of the rate-limiting step going through the formation of an oxocarbonium ion. In conjunction with other observations reported previously, the data presented here led to the suggestion of the main lines of a reaction mechanism for the two glucosidases: prptonation of the glycosidic oxygen is followed by the liberation of the "aglycone" with formation of an oxocarbonium ion, which is temporarily stabilized by a carboxylate group.

Animals↗
PubMed1975

Dissociation of small-intestinal sucrase - isomaltase complex into enzymatically active subunits.

1. The sucrase - isomaltase complex from rabbit small intestine dissociated into its subunits upon reaction with citraconic anhydride. They can recombine after deacylation under mild acidic conditions. 2. When citraconylated, the subunits could be separated and isolated in a catalytically active form. 3. The previously reported procedure for separation of the subunits by alkaline treatment at pH 9.6 is apparently not due to contaminating degradative enzymes (possibly still present at undetectable levels in the isolated sucrase - isomaltase complex) but to the action of alkali.

Animals↗
PubMedDate not supplied

Hematological and immunological changes during space flight.

This paper gives a summary of the principal hematological and immunological changes observed in crews after space flight. Reduction of red blood cell mass (2-21%) and of hemoglobin mass (12-33%) is generally observed after the US and Soviet space missions. The changes are accompanied with a loss of plasma volume (4-16%). Erythrocyte and hemoglobin concentrations in the blood remain constant, suggesting that the changes are driven by a feed-back mechanism. Immunological changes consist mainly of reduced T-lymphocyte reactivity. The results of the 96-day and 140-day Salyut-6 missions suggest that the adaptation of the immune system to spaceflight occurs in two stages: the first takes place during the first 2-3 months in space, the second follows and consists of further weakening of the immune response. Our experiments with human lymphocytes in vitro indicate that high-g enhance, whereas low-g depress lymphocyte activity. Finally, our investigations to be performed on Spacelab are described.

Adaptation, Physiological↗