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Valacyclovir: a substrate for the intestinal and renal peptide transporters PEPT1 and PEPT2.
Valacyclovir is a prodrug of the antiviral agent acyclovir and it does not contain a peptide bond in its structure. We studied the interaction of valacyclovir with the peptide transporters in theExpand
Cloning of an Amino Acid Transporter with Functional Characteristics and Tissue Expression Pattern Identical to That of System A*
We report here on the cloning and functional characterization of the protein responsible for the system A amino acid transport activity that is known to be expressed in most mammalian tissues. ThisExpand
β-Lactam Antibiotics as Substrates for OCTN2, an Organic Cation/Carnitine Transporter*
Therapeutic use of cephaloridine, a β-lactam antibiotic, in humans is associated with carnitine deficiency. A potential mechanism for the development of carnitine deficiency is competition betweenExpand
Structure, function, and regional distribution of the organic cation transporter OCT3 in the kidney.
We examined in this study the expression of the potential-sensitive organic cation transporter OCT3 in the kidney. A functionally active OCT3 was cloned from a mouse kidney cDNA library. The clonedExpand
cDNA structure, genomic organization, and promoter analysis of the mouse intestinal peptide transporter PEPT1.
We describe in this report the cDNA structure, functional characteristics, genomic organization, and promoter analysis of the mouse H(+)-coupled low-affinity peptide transporter PEPT1. The mouseExpand
Transport of valganciclovir, a ganciclovir prodrug, via peptide transporters PEPT1 and PEPT2.
In clinical trials, valganciclovir, the valyl ester of ganciclovir, has been shown to enhance the bioavailability of ganciclovir when taken orally by patients with cytomegalovirus infection. WeExpand
Na+- and Cl--coupled active transport of carnitine by the amino acid transporter ATB(0,+) from mouse colon expressed in HRPE cells and Xenopus oocytes.
1. ATB(0,+) is an amino acid transporter energized by transmembrane gradients of Na+ and Cl(-) and membrane potential. We cloned this transporter from mouse colon and expressed the clone functionallyExpand
Structure and function of ATA3, a new subtype of amino acid transport system A, primarily expressed in the liver and skeletal muscle.
To date, two different transporters that are capable of transporting alpha-(methylamino)isobutyric acid, the specific substrate for amino acid transport system A, have been cloned. These twoExpand
Molecular cloning of PEPT 2, a new member of the H+/peptide cotransporter family, from human kidney.
Mammalian kidney is known to express a transport system specific for small peptides and pharmacologically active aminocephalosporins. This system is energized by a transmembrane electrochemical H+Expand
Differential Recognition of β-Lactam Antibiotics by Intestinal and Renal Peptide Transporters, PEPT 1 and PEPT 2 (*)
This study was initiated to determine if there are differences in the recognition of β-lactam antibiotics as substrates between intestinal and renal peptide transporters, PEPT 1 and PEPT 2. ReverseExpand