Search results for "Cationic Amino Acid Transporters"

showing 3 items of 3 documents

Activation of classical protein kinase C decreases transport via systems y+and y+L

2007

Activation of protein kinase C (PKC) downregulates the human cationic amino acid transporters hCAT-1 (SLC7A1) and hCAT-3 (SLC7A3) (Rotmann A, Strand D, Martiné U, Closs EI. J Biol Chem 279: 54185–54192, 2004; Rotmann A, Vekony N, Gassner D, Niegisch G, Strand D, Martine U, Closs EI. Biochem J 395: 117–123, 2006). However, others found that PKC increased arginine transport in various mammalian cell types, suggesting that the expression of different arginine transporters might be responsible for the opposite PKC effects. We thus investigated the consequence of PKC activation by phorbol-12-myristate-13-acetate (PMA) in various human cell lines expressing leucine-insensitive system y+[hCAT-1, h…

Amino Acid Transport System y+ArgininePhysiologyBiological Transport ActiveBiologyArginineEnzyme activatorLeucineCell Line TumorHumansRNA MessengerCationic Amino Acid TransportersProtein Kinase CProtein kinase CRegulation of gene expressionchemistry.chemical_classificationBase SequenceAmino Acid Transport System y+LCell BiologyMolecular biologyEnzyme ActivationEnzymeGene Expression RegulationchemistryTetradecanoylphorbol AcetateTetradecanoylphorbol AcetateLeucineAmerican Journal of Physiology-Cell Physiology
researchProduct

Human cationic amino acid transporter hCAT-3 is preferentially expressed in peripheral tissues.

2001

At least five distinct carrier proteins form the family of mammalian cationic amino acid transporters (CATs). We have cloned a cDNA containing the complete coding region of human CAT-3. hCAT-3 is glycosylated and localized to the plasma membrane. Transport studies in Xenopus laevis oocytes revealed that hCAT-3 is selective for cationic L-amino acids and exhibits a maximal transport activity similar to other CAT proteins. The apparent substrate affinity and sensitivity to trans-stimulation of hCAT-3 resembles most closely hCAT-2B. This is in contrast to rat and murine CAT-3 proteins that have been reported to display a very low activity and to be inhibited by neutral and anionic L-amino acid…

MaleDNA ComplementaryGene ExpressionThymus GlandIn Vitro TechniquesBiochemistryCell LineMiceXenopus laevisComplementary DNACoding regionAnimalsHumansTissue DistributionAmino acid transporterAmino Acid SequenceCationic Amino Acid Transporterschemistry.chemical_classificationCATSBase SequenceChemistryCationic polymerizationBrainMembrane ProteinsAmino acidRatsBiochemistryCarrier proteinOocytesAmino Acid Transport Systems BasicFemaleCarrier ProteinsBiochemistry
researchProduct

Cationic Amino Acid Transporters (CATs)

2002

When the transport properties of mCAT-1 were described in 1991, the y+ carrier and major transporter for cationic amino acids seemed to be discovered. Today, we know that there are at least three different CAT isoforms that mediate y+ activity and the family might be growing. In addition, transport systems for cationic amino acids other than y + have been described and proteins that induce the respective transport activities have been identified. Consequently, the transport of cationic amino acids appears to be a complex process involving many proteins— carriers and possibly also regulatory proteins—whose expression is cell-specific and dependent on a variety of external stimuli. The multit…

chemistry.chemical_classificationGene isoformCATSmedicine.anatomical_structureBiochemistryChemistryCellmedicineCationic polymerizationTransporterCationic Amino Acid TransportersFunction (biology)Amino acid
researchProduct