Home LiteratureArticle Details
PMID: 9092716 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Interaction of anionic cephalosporins with the intestinal and renal peptide transporters PEPT 1 and PEPT 2.

Biochimica et biophysica acta ·Vol. 1324 ·No. 2 ·1997-03-13 ·Pages 296-308

Ganapathy ME, Prasad PD, Mackenzie B, Ganapathy V, Leibach FH

Abstract

The present study was undertaken to investigate the interaction of anionic cephalosporins (cefixime, ceftibuten, and cefdinir) with the renal peptide transporter (PEPT 2) and the intestinal peptide transporter (PEPT 1) using four different experimental model systems. In the first approach, the human colon carcinoma cell line Caco-2 which expresses PEPT 1 and the SHR rat kidney cell line SKPT which expresses PEPT 2 were used. The uptake of the dipeptide Gly-Sar mediated by PEPT 1 or PEPT 2 in these cells was inhibited significantly by the anionic cephalosporins, with the following order of potency: ceftibuten > cefixime > cefdinir. The inhibition was competitive in nature. Even though the order of potency was the same for PEPT 1 and PEPT 2, PEPT 1 exhibited much lesser sensitivity to inhibition than PEPT 2. In the second approach, the cloned human PEPT 1 and PEPT 2 were functionally expressed in HeLa cells following which the cells were used to study the interaction of anionic cephalosporins with PEPT 1 and PEPT 2. Again, Gly-Sar uptake mediated by the human PEPT 1 and PEPT 2 in HeLa cells was found to be inhibited by the anionic cephalosporins with the same order potency as in Caco-2 and SKPT cells. In the third approach, brush border membrane vesicles isolated from rat kidneys were employed. In this approach also it was found that PEPT 2-mediated Gly-Sar uptake was inhibited by cefixime and ceftibuten. In the fourth approach, the human PEPT 1 was expressed in Xenopus laevis oocytes and PEPT 1-mediated transport of ceftibuten was investigated directly by electrophysiological methods. Ceftibuten evoked inward currents in PEPT 1-expressing oocytes but not in water-injected oocytes, showing that the transport of the anionic cephalosporin via PEPT 1 is associated with transfer of positive charge. The ceftibuten-evoked currents were saturable with respect to ceftibuten concentration and were markedly dependent on membrane potential. It is concluded that anionic cephalosporins interact with the peptide transporters expressed in the intestine (PEPT 1) as well as in the kidney (PEPT 2).

MeSH Terms
Animals Biological Transport/drug effects Caco-2 Cells/metabolism Carrier Proteins/genetics,metabolism Cell Line Cephalosporins/pharmacology Colon/metabolism Dipeptides/metabolism Evoked Potentials HeLa Cells Humans Kidney/metabolism Microvilli/metabolism Oocytes/physiology Peptide Transporter 1 Rats Rats, Inbred SHR Rats, Sprague-Dawley Symporters Transfection Xenopus laevis
Chemicals
Carrier Proteins Cephalosporins Dipeptides Peptide Transporter 1 SLC15A1 protein, human Slc15a1 protein, rat Symporters hydrogen-coupled oligopeptide transporter PepT2 glycylsarcosine
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Ganapathy M E
Department of Medicine, Medical College of Georgia, Augusta 30912, USA.
Prasad P D
Mackenzie B
Ganapathy V
Leibach F H
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1997-03-13
Pages
296-308
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
Grants
NIGMS NIH HHS · GM 54122 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]