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A Santos Ruiz

Publications and source records attributed to A Santos Ruiz.

7 recordsLinked to original sources

[Physiopathologic implications of telomerase].

Telomerase is a specialized RNA-directed DNA polymerase that extends telomeres of eukaryotic chromosomes. Telomerase gene expression is active in germinal, stem and tumoral cells and repressed in normal human somatic cells. Activation of telomerase involves immortalization, while repression of this enzyme involves the shortening of telomeres in each round of chromosomal replication. Telomere shortening constitutes a mechanism for cells to control cell division and the entrance in the replicative senescence state. If the expression of this enzyme is forced, senescent human cells will extend their life span reaching the immortalization and malignization of the cells. Activation or depression of telomerase activity has important implications in aging and cancer therapy. Telomerase regulation is a multifactorial process in which telomerase expression, post-translational protein-protein interactions and protein phosphorylation are involved.

Apoptosis↗

[Changes in lipid metabolism which accompany thioacetamide-induced cirrhosis].

Intraperitoneally-administered thioacetamide to rats produces the incorporation of 3H2O into the liver lipids during eight days, diminishing thereafter together with a decrease in 32P incorporation to phosphatidyl choline. Contrarily, the sphingomyelin incorporated 32P increases by the effect of the toxic action of the drug, while the 3H binding decreases. The cirrhosis-inducing agent possibly produces a shunt of the common CDP-choline precursor to the biosynthesis of sphingomyelin with detriment to the synthesis of phosphatidyl choline. The role of the unsaturation of fatty acids by thioacetamide is considered.

Acetamides↗

[Kinetic properties of membrane dopamine-beta-hydroxylase. ].

We studied membrane bound dopamine-beta-hydroxylase (DBH) from chromaffin granules, in order to determine whether a biological form of immobilization of the enzyme altered its kinetic properties. The results obtained suggested that DBH either in soluble or solubilized form showed a ping-pong mechanism whereas the membrane bound DBH did not. Affinity for the substrate and the pH stability were lower in soluble or solubilized form than in membrane bound DBH.

Animals↗