Mechanisms of seawater acclimation in a primitive, anadromous fish, the green sturgeon

Relatively little is known about salinity acclimation in the primitive groups of fishes. To test whether physiological preparative changes occur and to investigate the mechanisms of salinity acclimation, anadromous green sturgeon, Acipenser medirostris (Chondrostei) of three different ages (100, 170, and 533 dph) were acclimated for 7 weeks to three different salinities (<3, 10, and 33 ppt). Gill, kidney, pyloric caeca, and spiral intestine tissues were assayed for Na+, K+-ATPase activity; and gills were analyzed for mitochondria-rich cell (MRC) size, abundance, localization and Na+, K+-ATPase content. Kidneys were analyzed for Na+, K+-ATPase localization and the gastro-intestinal tract (GIT) was assessed for changes in ion and base content. Na+, K+-ATPase activities increased in the gills and decreased in the kidneys with increasing salinity. Gill MRCs increased in size and decreased in relative abundance with fish size/age. Gill MRC Na+, K+-ATPase content (e.g., ion-pumping capacity) was proportional to MRC size, indicating greater abilities to regulate ions with size/age. Developmental/ontogenetic changes were seen in the rapid increases in gill MRC size and lamellar length between 100 and 170 dph. Na+, K+-ATPase activities increased fourfold in the pyloric caeca in 33 ppt, presumably due to increased salt and water absorption as indicated by GIT fluids, solids, and ion concentrations. In contrast to teleosts, a greater proportion of base (HCO3− and 2CO32−) was found in intestinal precipitates than fluids. Green sturgeon osmo- and ionoregulate with similar mechanisms to more-derived teleosts, indicating the importance of these mechanisms during the evolution of fishes, although salinity acclimation may be more dependent on body size

Intestinal glucose transport in carnivorous and herbivorous marine fishes

The influx and transepithelial movements of glucose and their effects on the electrophysiology and Na transport in upper and lower intestines of the herbivorous surgeonfish, Acanthurus mata , and carnivorous eel, Gymnothorax undulatus , were measured. The K t G and J max G of glucose influx into the tissues were higher in the surgeonfish upper intestine than in the surgeonfish lower intestine or in both segments of the eel intestine. A prominent diffusion-like transport component was also measured in all four segments during influx experiments. Net transepithelial glucose fluxes (0.05 mM) were greater in eel intestine than in those of the surgeonfish largely due to an apparent lower apical membrane permeability of the former coincident with reduced backflux of glucose from epithelium to lumen. All four stripped intestinal segments exhibited non-significant (from zero; P &gt;0.05) or small, serosa-negative transepithelial potential differences (-0.1 to -2.2 mV), and low transepithelial resistances (40–88 O cm -2 ). Each tissue displayed significant ( P P &gt;0.05) change the transepithelial resistance, but did induce a significant ( P J net Na with added luminal glucose, these increased net cation fluxes were not quite significant ( P &gt;0.05). It is concluded that coupled Na-glucose transport occurs in these tissues, but that metabolic enhancement of unrelated current-generating mechanisms also takes place and may modify depolarizing effects of organic solute transfer

Mutant huntingtin can paradoxically protect neurons from death

Huntington's disease (HD) is a progressive neurodegenerative disorder caused by a mutation in the gene huntingtin and characterized by motor, cognitive and psychiatric symptoms. Huntingtin contains a CAG repeat in exon 1. An expansion of this CAG repeat above 35 results in misfolding of Huntingtin, giving rise to protein aggregates and neuronal cell death. There are several transgenic HD mouse models that reproduce most of the features of the human disorder, for example protein inclusions, some neurodegeneration as well as motor and cognitive symptoms. At the same time, a subgroup of the HD transgenic mouse models exhibit dramatically reduced susceptibility to excitotoxicity. The mechanism behind this is unknown. Here, we review the literature regarding this phenomenon, attempt to explain what protein domains are crucial for this phenomenon and point toward a putative mechanism. We suggest, that the C-terminal domain of exon 1 Huntingtin, namely the proline rich domain, is responsible for mediating a neuroprotective effect against excitotoxicity. Furthermore, we point out the possible importance of this mechanism for future therapies in neurological disorders that have been suggested to be associated with excitotoxicity, for example Alzheimer's disease, Parkinson's disease and amyotrophic lateral sclerosis