title: Peptide transport in rabbit kidney. Studies with L-carnosine.
abstract: L-Carnosine was shown to be transported into rabbit renal brush-border membrane vesicles by an Na+ -independent mechanism. The transport was competitively inhibited by glycyl-L-proline. Various di- and tripeptides inhibited L-carnosine transport, whereas free amino acids did not. Inhibition studies showed that blocking the free amino and carboxyl groups of the peptide reduced its affinity for the transport carrier. Under the conditions in which there was no detectable hydrolysis of L-carnosine in the medium, intravesicular contents showed a 30% hydrolysis of the peptide within the vesicles. Disruption of membrane vesicles with deoxycholate resulted in a 3-fold increase in L-carnosine hydrolyzing activity over untreated intact vesicles. Based on these observations, a model for peptide transport is proposed in which transport of the intact peptide across the membrane is followed by its partial or complete hydrolysis by a membrane peptidase whose active site is on the cytoplasmic side of the membrane.
mesh_terms: D000818:Animals; D001692:Biological Transport / Q000187:drug effects; D002336:Carnosine / Q000378:metabolism*; D004151:Dipeptides / Q000378:metabolism*; D007672:Kidney Cortex / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D008871:Microvilli / Q000378:metabolism; D009994:Osmolar Concentration; D010447:Peptide Hydrolases / Q000378:metabolism; D010455:Peptides / Q000494:pharmacology; D011817:Rabbits; D013654:Taurine / Q000378:metabolism; D015091:beta-Alanine / Q000378:metabolism
chemical_list: D004151:Dipeptides; D008565:Membrane Proteins; D010455:Peptides; D015091:beta-Alanine; D013654:Taurine; D002336:Carnosine; D010447:Peptide Hydrolases