Food resources influencing the asexual reproductive cycle of coronate Scyphozoa

The study of the strobilation process, a feature unique in the class Scyphozoa, is an issue that helps understanding the patterns of asexual reproduction in sessile invertebrates. Many inducers of asexual reproduction are known for scyphozoans. However, the influence of food resources on the strobilation of Coronate Scyphozoa has never been tested. WO observed strobilation of a large number of polyps of Nausithoe aurea, from a wide sampling area along the South Atlantic coast of Brazil, through the administration of controlled number of hatched nauplii of Artemia franciscana under a previous tested starvation and feeding protocol. The number of strobilations between and within groups varied and the fate and shape of strobilation deviated from the biology reported in the original description. Artificial seawater was used to reduce the influence of dissolved organic matter as likely important alternative nourishment.

Biological effects of anionic meso-tetrakis (para-sulfonatophenyl) porphyrins modulated by the metal center. Studies in rat liver mitochondria

In this paper, we present a study about the influence of the porphyrin metal center and mesa ligands on the biological effects of meso-tetrakis porphyrins. Different from the cationic meso-tetrakis 4-N-methyl pyridinium (Mn(III)TMPyP), the anionic Mn(III) meso-tetrakis (para-sulfonatophenyl) porphyrin (Mn(III)TPPS4) exhibited no protector effect against Fe(citrate)-induced lipid oxidation. Mn(III)TPPS4 did not protect mitochondria against endogenous hydrogen peroxide and only delayed the swelling caused by tert-BuOOH and Ca(2+). Fe(III)TPPS4 exacerbated the effect of the tert-BuOOH, and both porphyrins did not significantly affect Fe(II)citrate-induced swelling. Consistently, Fe(III)TPPS4 predominantly promotes the homolytic cleavage of peroxides and exhibits catalytic efficiency ten-fold higher than Mn(III)TPPS4. For Mn(III)TPPS4, the microenvironment of rat liver mitochondria favors the heterolytic cleavage of peroxides and increases the catalytic efficiency of the manganese porphyrin due to the availability of axial ligands for the metal center and reducing agents such as glutathione (GSH) and proteins necessary for Compound II (oxomanganese IV) recycling to the initial Mn(III) form. The use of thiol reducing agents for the recycling of Mn(III)TPPS4 leads to GSH depletion and protein oxidation and consequent damages in the organelle. (C) 2009 Elsevier Ireland Ltd. All rights reserved.