phenylalanylalanine and calmidazolium

phenylalanylalanine has been researched along with calmidazolium* in 1 studies

Other Studies

1 other study(ies) available for phenylalanylalanine and calmidazolium

ArticleYear
Regulation of the high-affinity H+/peptide cotransporter in renal LLC-PK1 cells.
    Journal of cellular physiology, 1999, Volume: 178, Issue:3

    Di- and tripeptides and peptide mimetics such as beta-lactam antibiotics are efficiently reabsorbed from the tubular lumen by a high-affinity peptide transporter. We have recently identified and characterized this H+-coupled high-affinity peptide transport system in the porcine proximal tubular cell line LLC-PK1. Here we describe for the first time the regulation of the renal high-affinity peptide cotransporter at the cellular level. Uptake of 5 microM 3H-D-Phe-L-Ala into LLC-PK1 cells was significantly increased by lowering [Ca2+]in and decreased by increasing [Ca2+] in. Moreover, it was shown that the [Ca2+]in effects on peptide transport activity were dependent on Ca2+ entry from the extracellular site (e.g., via a store-regulated capacitative Ca2+ influx). Protein kinase C (PKC) was found to transmit the effects of [Ca2+]in on peptide transport. Although we demonstrate by pHin measurements that the PKC inhibitor staurosporine did decrease the transmembrane H+ gradient and consequently should have reduced the driving force for peptide uptake, the only effect on transport kinetics of 3H-D-Phe-L-Ala observed was a significant decrease in Km from 22.7+/-2.5 microM to 10.2+/-1.9 microM with no change in maximal velocity.

    Topics: Animals; Biological Transport; Calcium; Carrier Proteins; Cell Survival; Dipeptides; Enzyme Inhibitors; Hydrogen-Ion Concentration; Imidazoles; Kidney Tubules, Proximal; Kinetics; LLC-PK1 Cells; Protein Kinase C; Signal Transduction; Staurosporine; Stereoisomerism; Sulfonamides; Swine; Symporters; Tetradecanoylphorbol Acetate; Trifluoperazine

1999