Characterization of monocarboxylate transport in human kidney HK-2 cells.

Characterization of monocarboxylate transport in human kidney HK-2 cells. Research Abstract Details 

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Characterization of monocarboxylate transport in human kidney HK-2 cells. Abstract Text:

Qi Wang,Ye Lu,Min Yuan,Inger M Darling,Elizabeth A Repasky,Marilyn E Morris,

The objectives of this study were to characterize the expression and function of monocarboxylate transporters (MCTs) in human kidney HK-2 cells and to compare the expression of MCTs in HK-2 cells to that found in human kidney. mRNA and protein expression of MCTs were determined by RT-PCR and Western analyses, respectively, while immunofluorescence staining was used to determine the membrane localization of MCT1. The driving force, transport kinetics, and inhibition of two MCT substrates, D-lactate and butyrate, were characterized in HK-2 cells. mRNA of MCT1, -2, -3, -4 isoforms were present in HK-2 cells and in human kidney cortex. MCT1 was present predominantly on the basal membranes of HK-2 cells. The cellular uptake of D-lactate and butyrate exhibited pH- and concentration-dependence (D-lactate, Km of 26.5 +/- 2.2 mM and Vmax of 72.0 +/- 14.5 nmol mg-1 min-1; butyrate, Km of 0.8 +/- 0.3 mM, Vmax of 29.3 +/- 2.5 nmol mg-1 min-1, and a diffusional clearance of 2.1 microL mg-1 min-1). The uptake of D-lactate and butyrate by HK-2 cells was inhibited by MCT analogues and the classical MCT inhibitors alpha-cyano-4-hydroxycinnamate, pCMB, and phloretin. The uptake of D-lactate and butyrate by HK-2 cells significantly decreased after transfection with small-interference RNA for MCT1. In summary, MCTs were present in both HK-2 cells and human kidney cortex, and HK-2 cells exhibited polarized MCT expression and pH-dependent transport of D-lactate and butyrate. Our results also support the usefulness of HK-2 cells as an in vitro model for studying monocarboxylate transport in renal proximal tubule cells.

Characterization of monocarboxylate transport in human kidney HK-2 cells. Publishing Authors By Initials

Q Wang,Y Lu,M Yuan,IM Darling,EA Repasky,ME Morris,

For similar proteins: carrier proteins: membrane transport proteins: ion pumps: symporters research abstracts see: proteins: carrier proteins: membrane transport proteins: ion pumps: symporters research

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MEDLINE DATE:

Characterization of monocarboxylate transport in human kidney HK-2 cells. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Molecular pharmaceutics

VOLUME: 3

Page Numbers: 675-85

Journal Abbreviation: Mol. Pharm.

ISSN: 1543-8384

DAY: 3

MONTH: 12

YEAR: 2007

Characterization of monocarboxylate transport in human kidney HK-2 cells. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101197791

Characterization of monocarboxylate transport in human kidney HK-2 cells. Keywords Mesh Terms:

KEYWORDS: Symporters

MESH TERMS: metabolism

Chemical & Substance for Abstract: Characterization of monocarboxylate transport in human kidney HK-2 cells. Information

Substance Name: Sodium

Registry Number: 7440-23-5

Grant and Affiliation Information for Characterization of monocarboxylate transport in human kidney HK-2 cells.

AFFILIATION: Department of Pharmaceutical Sciences, School of Pharmacy and Pharmaceutical Sciences, University at Buffalo, State University of New York, Amherst, New York 14260, USA.

Country: United States

AGENCY: United States NIDA

GRANT: DA14988

ACRONYM: DA

MEDLINETA: Mol Pharm

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