Expression of multidrug resistance-associated protein (MRP) in human retinal pigment epithelial cells and its interaction with BAPSG, a novel aldose reductase inhibitor

J. V. Aukunuru, G. Sunkara, N. Bandi, Wallace B Thoreson, U. B. Kompella

Research output: Contribution to journalArticle

69 Citations (Scopus)

Abstract

Purpose. The objective of this study was to determine the expression and activity of multidrug resistance-associated protein (MRP) in the retinal pigment epithelial (RPE) cells and to further assess whether BAPSG, a novel anionic aldose reductase inhibitor, interacts with MRP. Methods. Functional and biochemical evidence for MRP was obtained in a human retinal pigment epithelial (ARPE-19) cell line and primary cultures of human retinal pigment epithelial (HRPE) cells. Fluorescein accumulation and efflux in the presence and absence of MRP inhibitors was used to obtain functional evidence for MRP. Western blots and RT-PCR were used to obtain biochemical evidence for MRP1. The influence of MRP inhibitors on BAPSG accumulation and effiux in ARPE-19 cells was determined to understand its interaction with MRP. Results. MRP inhibitors increased fluorescein accumulation and reduced efflux in RPE cells. Both cell types exhibited a 190-kDa western blot band corresponding to MRP1 protein and a 287 bp RT-PCR band corresponding to MRP1 mRNA. MRP inhibitors reduced BAPSG efflux and increased its accumulation in ARPE-19 cells. Conclusions. MRP is functionally and biochemically active in human RPE cells. Anionic BAPSG is a likely substrate for MRP.

Original languageEnglish (US)
Pages (from-to)565-572
Number of pages8
JournalPharmaceutical Research
Volume18
Issue number5
DOIs
StatePublished - Jul 11 2001

Fingerprint

Multidrug Resistance-Associated Proteins
Aldehyde Reductase
Retinal Pigments
Cell Communication
Epithelial Cells
Fluorescein
N-(((4-benzoylamino)phenyl)sulfonyl)glycine
Western Blotting
Polymerase Chain Reaction
Cell culture

Keywords

  • Aldose reductase inhibitor
  • Fluorescein
  • MRP
  • RPE cells

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Medicine
  • Pharmacology
  • Pharmaceutical Science
  • Organic Chemistry
  • Pharmacology (medical)

Cite this

Expression of multidrug resistance-associated protein (MRP) in human retinal pigment epithelial cells and its interaction with BAPSG, a novel aldose reductase inhibitor. / Aukunuru, J. V.; Sunkara, G.; Bandi, N.; Thoreson, Wallace B; Kompella, U. B.

In: Pharmaceutical Research, Vol. 18, No. 5, 11.07.2001, p. 565-572.

Research output: Contribution to journalArticle

@article{346b2d269a2e4ba5a560f1b40bb9d245,
title = "Expression of multidrug resistance-associated protein (MRP) in human retinal pigment epithelial cells and its interaction with BAPSG, a novel aldose reductase inhibitor",
abstract = "Purpose. The objective of this study was to determine the expression and activity of multidrug resistance-associated protein (MRP) in the retinal pigment epithelial (RPE) cells and to further assess whether BAPSG, a novel anionic aldose reductase inhibitor, interacts with MRP. Methods. Functional and biochemical evidence for MRP was obtained in a human retinal pigment epithelial (ARPE-19) cell line and primary cultures of human retinal pigment epithelial (HRPE) cells. Fluorescein accumulation and efflux in the presence and absence of MRP inhibitors was used to obtain functional evidence for MRP. Western blots and RT-PCR were used to obtain biochemical evidence for MRP1. The influence of MRP inhibitors on BAPSG accumulation and effiux in ARPE-19 cells was determined to understand its interaction with MRP. Results. MRP inhibitors increased fluorescein accumulation and reduced efflux in RPE cells. Both cell types exhibited a 190-kDa western blot band corresponding to MRP1 protein and a 287 bp RT-PCR band corresponding to MRP1 mRNA. MRP inhibitors reduced BAPSG efflux and increased its accumulation in ARPE-19 cells. Conclusions. MRP is functionally and biochemically active in human RPE cells. Anionic BAPSG is a likely substrate for MRP.",
keywords = "Aldose reductase inhibitor, Fluorescein, MRP, RPE cells",
author = "Aukunuru, {J. V.} and G. Sunkara and N. Bandi and Thoreson, {Wallace B} and Kompella, {U. B.}",
year = "2001",
month = "7",
day = "11",
doi = "10.1023/A:1011060705599",
language = "English (US)",
volume = "18",
pages = "565--572",
journal = "Pharmaceutical Research",
issn = "0724-8741",
publisher = "Springer New York",
number = "5",

}

TY - JOUR

T1 - Expression of multidrug resistance-associated protein (MRP) in human retinal pigment epithelial cells and its interaction with BAPSG, a novel aldose reductase inhibitor

AU - Aukunuru, J. V.

AU - Sunkara, G.

AU - Bandi, N.

AU - Thoreson, Wallace B

AU - Kompella, U. B.

PY - 2001/7/11

Y1 - 2001/7/11

N2 - Purpose. The objective of this study was to determine the expression and activity of multidrug resistance-associated protein (MRP) in the retinal pigment epithelial (RPE) cells and to further assess whether BAPSG, a novel anionic aldose reductase inhibitor, interacts with MRP. Methods. Functional and biochemical evidence for MRP was obtained in a human retinal pigment epithelial (ARPE-19) cell line and primary cultures of human retinal pigment epithelial (HRPE) cells. Fluorescein accumulation and efflux in the presence and absence of MRP inhibitors was used to obtain functional evidence for MRP. Western blots and RT-PCR were used to obtain biochemical evidence for MRP1. The influence of MRP inhibitors on BAPSG accumulation and effiux in ARPE-19 cells was determined to understand its interaction with MRP. Results. MRP inhibitors increased fluorescein accumulation and reduced efflux in RPE cells. Both cell types exhibited a 190-kDa western blot band corresponding to MRP1 protein and a 287 bp RT-PCR band corresponding to MRP1 mRNA. MRP inhibitors reduced BAPSG efflux and increased its accumulation in ARPE-19 cells. Conclusions. MRP is functionally and biochemically active in human RPE cells. Anionic BAPSG is a likely substrate for MRP.

AB - Purpose. The objective of this study was to determine the expression and activity of multidrug resistance-associated protein (MRP) in the retinal pigment epithelial (RPE) cells and to further assess whether BAPSG, a novel anionic aldose reductase inhibitor, interacts with MRP. Methods. Functional and biochemical evidence for MRP was obtained in a human retinal pigment epithelial (ARPE-19) cell line and primary cultures of human retinal pigment epithelial (HRPE) cells. Fluorescein accumulation and efflux in the presence and absence of MRP inhibitors was used to obtain functional evidence for MRP. Western blots and RT-PCR were used to obtain biochemical evidence for MRP1. The influence of MRP inhibitors on BAPSG accumulation and effiux in ARPE-19 cells was determined to understand its interaction with MRP. Results. MRP inhibitors increased fluorescein accumulation and reduced efflux in RPE cells. Both cell types exhibited a 190-kDa western blot band corresponding to MRP1 protein and a 287 bp RT-PCR band corresponding to MRP1 mRNA. MRP inhibitors reduced BAPSG efflux and increased its accumulation in ARPE-19 cells. Conclusions. MRP is functionally and biochemically active in human RPE cells. Anionic BAPSG is a likely substrate for MRP.

KW - Aldose reductase inhibitor

KW - Fluorescein

KW - MRP

KW - RPE cells

UR - http://www.scopus.com/inward/record.url?scp=0034950241&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034950241&partnerID=8YFLogxK

U2 - 10.1023/A:1011060705599

DO - 10.1023/A:1011060705599

M3 - Article

C2 - 11465409

AN - SCOPUS:0034950241

VL - 18

SP - 565

EP - 572

JO - Pharmaceutical Research

JF - Pharmaceutical Research

SN - 0724-8741

IS - 5

ER -