Endogenous lactate transport in Xenopus laevis oocyte: dependence on cytoskeleton and regulation by protein kinases.

Carbon flux in Xenopus laevis oocyte is glycogenic and an endogenous monocarboxylate transporter is responsible for intracellular lactate uptake. The aim of the present study was to determine if direct activation of protein kinases C and A modulates the activity of lactate transporter, as well as to investigate the possible role of cytoskeleton in these regulatory phenomena. The modulation was studied in isolated Xenopus oocytes of stage V-VI by measuring (14)C-lactate uptake, both in the absence and in the presence of cytoskeletal-perturbing toxins.

Oxidative stress reduces transintestinal transports and (Na+, K+) -ATPase activity in rat jejunum.

Because oxidative stress is a component of gastrointestinal injury, we investigated the effect of H(2)O(2) on transintestinal transport using isolated rat jejunum incubated in vitro. Millimolar concentrations of H(2)O(2) inhibited all the tested parameters without inducing any cytotoxic effect. Electrophysiological experiments indicated that H(2)O(2) decreases significantly both short circuit current and transepithelial electrical potential difference without affecting transepithelial resistance.

Expression and immunolocalization of aquaporin-7 in rat gastrointestinal tract.

Background Information: In the gastrointestinal tract of mammals, water can either be secreted with digestive juices or absorbed by the small and large intestine. Transcellular water movement can be mediated by the transmembrane protein family of AQPs (aquaporins), as has also been recently identified in the gastrointestinal tract. However, the localization, expression and functioning of AQPs in the gastrointestinal tract have not been completely characterized.

PKA regulation of bicarbonate and lactate movements across rat jejunal plasma membranes.

Background/aims: Evidence was previously given that the mechanisms involved in bicarbonate and lactate movements across rat jejunal enterocyte are modulated by PKC and Ca2+/CaM. Aim of this study was to investigate the possible role of PKA on bicarbonate and lactate transports.

Methods: Enzymatic assays in isolated plasma membranes were performed.

Protein kinase C regulation of rat jejunal transport system: mechanisms involved in lactate movement.

We examined whether protein kinase C (PKC) modulates the transport systems involved in lactate movements across the plasma membranes of rat jejunum. In vitro phosphorylated membrane vesicles were used to perform uptake studies, the results of which suggested that PKC activation exerts an inhibitory effect on basolateral H+-lactate symport, as well as on apical N-+glucose cotransport. The specificity of the response to PKC was confirmed by using staurosporine, chelerythrine or 4-alpha-PMA.

Guanidine transport across the apical and basolateral membranes of human intestinal Caco-2 cells is mediated by two different mechanisms.

The functional characteristics of the intestinal absorption and secretion of guanidine as a model of a nutritionally and metabolically essential organic cation were examined in the Caco-2 human intestinal cell line. Both apical and basolateral transport of [14C]-guanidine were studied using Caco-2 cells grown on polycarbonate permeable membranes. The basolateral-to-apical flux of [14C]-guanidine (i.

Protein kinase C regulation of rat jejunal transport systems: mechanisms involved in bicarbonate absorption.

We examined whether protein kinase C (PKC) modulates the transport systems involved in bicarbonate movements across the plasma membranes of rat jejunum. Results of enzymatic assays provide evidence that under basal conditions conventional PKC (cPKC) is present in both basolateral membranes (BLMs) and apical (brush border) membranes (BBMs) of the enterocyte. In BLMs the basal expression of the kinase is low compared to expression in BBMs; however, treatment with Ca(2+) and phorbol 12-myristate 13-acetate (PMA) causes a significant increase, thus suggesting an asymmetrical kinase translocation.

Calmodulin-mediated regulation of bicarbonate and lactate transports in rat jejunum.

Background/aims: Ca(2+)/CaM is known to modulate the activity of several transport systems and its regulation can be accomplished either directly or via the involvement of specific protein kinases. Aim of this study was to investigate the possible role of Ca(2+)/CaM on bicarbonate and lactate transports in rat jejunal enterocyte.

Methods: Enzymatic assays in isolated plasma membranes were performed.