Changes in digestive enzymes activities during the initial ontogeny of wolf cichlid, Parachromis dovii (Perciformes: Cichlidae)

Wolf cichlid, Parachromis dovii, is a species with a high potential for aquaculture in Central America; however, the knowledge of the digestive physiology in larvae period is limited. For these reason, this study evaluated the changes on digestive enzymes (alkaline and acid proteases, trypsin, chymotrypsin, aminopeptidase, carboxypeptidase, lipases, amylases, and phosphatases) during early ontogeny by biochemical analysis. All digestive enzymes were detected at first feeding (6 days after hatching, DAH, 9.49 mm, 168 degree-days DD). Afterwards all enzymes reached two main peaks in activity at 14 or 22 DAH (15.10 mm, 364 DD and 20.83 mm, 550 DD, respectively). Later, there was a gradual decrease in activity for trypsin and acid and alkaline phosphatases until reach the lowest values at 41 DAH. In the case of acid proteases, chymotrypsin, aminopeptidase, carboxypeptidase, lipase and amylase, all activities reached their maximum values at the end of the larval period, except for alkaline proteases, which showed the maximum value at 14 DAH (15.10 mm, 364 DD). Parachromis dovii larvae have an early capability to hydrolyze exogenous food, agreeing with other carnivorous neotropical cichlid species, for this reason we proposed that the weaning process could begin at 14 DAH.(AU)

El guapote lagunero (Parachromis dovii) es una especie con un alto potencial para la acuicultura en la región de América Central; sin embargo, existe un conocimiento limitado sobre la capacidad digestiva en el periodo larval. Por este motivo, este estudio evaluó los cambios de las enzimas digestivas (proteasas alcalinas y ácidas, tripsina, quimotripsina, aminopeptidasa, carboxipeptidasa, lipasas, amilasas y fosfatasas) durante la ontogenia temprana mediante análisis bioquímico. Todas las enzimas digestivas analizadas se detectaron en la primera alimentación (6 días después de la eclosión, DAH, 9.49 mm, 168 día-grados DD). Después, todas las enzimas alcanzaron dos picos máximos a los 14 o 22 DAH (15.10 mm, 364 DD and 20.83 mm, 550 DD, respectivamente). Después las actividades tripsina, fosfatasas ácidas y alcalina disminuyeron a sus valores más bajos a los 41 DAH. En el caso de las proteasas ácidas y alcalinas, quimotripsina, aminopeptidasa, carboxipeptidasa, lipasa y amilasa, los niveles de actividad aumentaron y alcanzaron su máximo valor al final del período larvario, excepto las proteasas alcalinas, que mostraron su máximo valor a los 14 DAH (15.10 mm, 364 DD). Las larvas de P. dovii tienen una capacidad temprana para hidrolizar alimentos exógenos, lo que concuerda con otras especies de cíclidos neotropicales carnívoros, por lo que proponemos que el proceso de destete inicie a los 14 DAH.(AU)

Target-directed catalytic metallodrugs

Most drugs function by binding reversibly to specific biological targets, and therapeutic effects generally require saturation of these targets. One means of decreasing required drug concentrations is incorporation of reactive metal centers that elicit irreversible modification of targets. A common approach has been the design of artificial proteases/nucleases containing metal centers capable of hydrolyzing targeted proteins or nucleic acids. However, these hydrolytic catalysts typically provide relatively low rate constants for target inactivation. Recently, various catalysts were synthesized that use oxidative mechanisms to selectively cleave/inactivate therapeutic targets, including HIV RRE RNA or angiotensin converting enzyme (ACE). These oxidative mechanisms, which typically involve reactive oxygen species (ROS), provide access to comparatively high rate constants for target inactivation. Target-binding affinity, co-reactant selectivity, reduction potential, coordination unsaturation, ROS products (metal-associated vs metal-dissociated; hydroxyl vs superoxide), and multiple-turnover redox chemistry were studied for each catalyst, and these parameters were related to the efficiency, selectivity, and mechanism(s) of inactivation/cleavage of the corresponding target for each catalyst. Important factors for future oxidative catalyst development are 1) positioning of catalyst reduction potential and redox reactivity to match the physiological environment of use, 2) maintenance of catalyst stability by use of chelates with either high denticity or other means of stabilization, such as the square planar geometric stabilization of Ni- and Cu-ATCUN complexes, 3) optimal rate of inactivation of targets relative to the rate of generation of diffusible ROS, 4) targeting and linker domains that afford better control of catalyst orientation, and 5) general bio-availability and drug delivery requirements.