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La adenosin deaminasa representa un punto de control en la regulación de los niveles extracelulares de adenosina, desempeñando así un papel fundamental en la modulación de las respuestas purinérgicas a ciertos eventos patofisiológicos. Diversos estudios señalan que los niveles séricos y plasmáticos de la enzima se elevan en algunas enfermedades causadas por microorganismos, lo cual podría representar un mecanismo compensatorio como consecuencia de la elevación de las concentraciones de adenosina y la liberación de mediadores inflamatorios. Recientes investigaciones indican que la actividad de la adenosin deaminasa disminuye e influye en los parámetros hematológicos de animales infectados con Trypanosoma evansi, de manera que tales alteraciones podrían tener implicaciones en la patogénesis de la enfermedad. Adicionalmente, la enzima ha sido detectada en este parásito; lo que permite inferir que podría estar asociada a las funciones vitales del mismo, de manera similar a lo que ocurre en los mamíferos. Este conocimiento puede ser útil al asociar la quimioterapia con inhibidores específicos de la enzima en futuros estudios. The adenosine deaminase represents a control point in the regulation of extracellular adenosine levels, thus playing a critical role in the modulation of purinergic responses to certain pathophysiological events. Several studies have shown that serum and plasma enzyme levels are elevated in some diseases caused by microorganisms, which may represent a compensatory mechanism due to the elevated levels of adenosine and the release of inflammatory mediators. Recent research indicates that adenosine deaminase activity decreases and affects hematological parameters of infected animals with Trypanosoma evansi, so that such alterations could have implications in the pathogenesis of the disease. In addition, the enzyme has been detected in this parasite; allowing the inference that it could be associated with the vital functions of the same, similar to what occurs in mammals. This knowledge may be useful in the association of chemotherapy with specific inhibitors of the enzyme in future studies.

The addition of long chain fatty acids to the incubation medium of isolated rat lung cells produced a dose-dependent inhibition of protein labelling from L-[3H]valine. Maximal rate changes were observed at fatty acids levels within the range of their physiological concentration. (2) The effect of fatty acids on protein labelling does not seem to be mediated by their oxidation. The following observations seem to support this conclusion: (a) the rate of fatty acid oxidation by lung cells was remarkably low, so that no significant variations in the state of reduction of the NAD system were detected; (b) there was no correspondence in the dose-response patterns of fatty acid oxidation and inhibition of protein labelling; (c) octanoate was much more actively oxidized than oleate, however the latter was more effective in decreasing protein labelling. (3) An apparent relationship between the length of the fatty chain and its ability to inhibit protein labelling seems to exist. The longer the chain the stronger the inhibitory effect observed. (4) The effect of fatty acid on protein labelling seems to be mediated by a cellular energy depletion secondary to an inhibition of the respiratory chain. Their ability to decrease oxygen uptake and adenine nucleotide content was also proportional to the chain length. (5) Glucose, which apparently acted by increasing energy production at substrate level phosphorylation, partially prevented the inhibitory effect of fatty acid on protein labelling. This observation supports the point of view that fatty acids do not act in decreasing protein labelling by perturbing directly the protein synthesis machinery but decreasing the phosphorylation potential., This work has been supported in part by grants from the Spanish Comisión Asesora de Investigación Científica y Técnica, Essex Laboratories of Spain and from Fondo de Investigaciones Sanitarias del Ministerio de Sanidad.