Abstract:
: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.
journal_name
J Cell Physioljournal_title
Journal of cellular physiologyauthors
Wenzel U,Diehl D,Herget M,Kuntz S,Daniel Hdoi
10.1002/(SICI)1097-4652(199903)178:3<341::AID-JCP8subject
Has Abstractpub_date
1999-03-01 00:00:00pages
341-8issue
3eissn
0021-9541issn
1097-4652pii
10.1002/(SICI)1097-4652(199903)178:3<341::AID-JCP8journal_volume
178pub_type
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