{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T10:58:42Z","timestamp":1758279522268},"reference-count":0,"publisher":"American Physiological Society","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Cell Physiology"],"published-print":{"date-parts":[[1988,12,1]]},"abstract":"<jats:p> These studies were performed to determine if a transmembrane carrier for pyroglutamyl-histidine (pGlu-His) is present in the luminal membrane of renal proximal tubular cells. Previous studies have suggested the intact transepithelial transport of pGlu-His, a dipeptide formed by the hydrolysis of luteinizing hormone-releasing hormone by enzymes associated with the brush border in the proximal nephron. With the use of a renal brush border membrane vesicle preparation, pGlu-His showed H+-stimulated, Na-independent, saturable transport into an osmotically active space. High-pressure liquid chromatographic analysis of both the intravesicular and extravesicular fluids indicated intact uptake of the dipeptide. The transport constant (Kt) and Vmax for pGlu-His transport were 9.3 X 10(-8) M and 6.1 X 10(-12) mol.mg-1.min-1, respectively. Transport of pGlu-His was not inhibited by the dipeptides glycyl-proline, glycyl-sarcosine, and N-beta-alanyl-L-histidine, which have been previously shown to be transported into renal brush border vesicles via a single, low-affinity, high-capacity, Na-independent, and H+-stimulated peptide carrier. In addition, the gamma-glutamyl-containing peptides gamma-glutamyl-histidine and N(N-L-gamma-glutamyl-L-cysteinyl)glycine and the tripeptide pyroglutamyl-histidyl-prolinamide were without an inhibitory effect. In contrast, transport of pGlu-His was inhibited by the dipeptide pyroglutamyl-alanine. This study demonstrates the existence of a high-affinity, low-capacity H+ cotransport system for pGlu-His in the proximal tubular luminal plasmalemma, which appears to be specific for pyroglutamyl-containing dipeptides. The data indicate that multiple dipeptide carriers are present in the proximal nephron. <\/jats:p>","DOI":"10.1152\/ajpcell.1988.255.6.c822","type":"journal-article","created":{"date-parts":[[2017,12,24]],"date-time":"2017-12-24T15:17:54Z","timestamp":1514128674000},"page":"C822-C827","source":"Crossref","is-referenced-by-count":15,"title":["Carrier-mediated transport of pyroglutamyl-histidine in renal brush border membrane vesicles"],"prefix":"10.1152","volume":"255","author":[{"given":"H. A.","family":"Skopicki","sequence":"first","affiliation":[{"name":"Department of Physiology, University of Health Sciences, ChicagoMedical School, Illinois."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"K.","family":"Fisher","sequence":"additional","affiliation":[{"name":"Department of Physiology, University of Health Sciences, ChicagoMedical School, Illinois."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D.","family":"Zikos","sequence":"additional","affiliation":[{"name":"Department of Physiology, University of Health Sciences, ChicagoMedical School, Illinois."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G.","family":"Flouret","sequence":"additional","affiliation":[{"name":"Department of Physiology, University of Health Sciences, ChicagoMedical School, Illinois."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R.","family":"Bloch","sequence":"additional","affiliation":[{"name":"Department of Physiology, University of Health Sciences, ChicagoMedical School, Illinois."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S.","family":"Kubillus","sequence":"additional","affiliation":[{"name":"Department of Physiology, University of Health Sciences, ChicagoMedical School, Illinois."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D. R.","family":"Peterson","sequence":"additional","affiliation":[{"name":"Department of Physiology, University of Health Sciences, ChicagoMedical School, Illinois."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"24","container-title":["American Journal of Physiology-Cell Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.physiology.org\/doi\/pdf\/10.1152\/ajpcell.1988.255.6.C822","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,17]],"date-time":"2024-06-17T19:50:46Z","timestamp":1718653846000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.physiology.org\/doi\/10.1152\/ajpcell.1988.255.6.C822"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1988,12,1]]},"references-count":0,"journal-issue":{"issue":"6","published-print":{"date-parts":[[1988,12,1]]}},"alternative-id":["10.1152\/ajpcell.1988.255.6.C822"],"URL":"https:\/\/doi.org\/10.1152\/ajpcell.1988.255.6.c822","relation":{},"ISSN":["0363-6143","1522-1563"],"issn-type":[{"value":"0363-6143","type":"print"},{"value":"1522-1563","type":"electronic"}],"subject":[],"published":{"date-parts":[[1988,12,1]]}}}