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Submitted on May 15, 2006
Accepted on August 9, 2006

Proteomic analysis of apical and basolateral plasma membranes of rat renal collecting duct cells

Ming-Jiun Yu, Trairak Pisitkun, Guanghui Wang, Rong-Fong Shen, and Mark A Knepper

Laboratory of Kidney and Electrolyte Metabolism, National Heart, Lung, and Blood Institute, Bethesda, MD 20892-1603

Corresponding Author: knepperm{at}nhlbi.nih.gov

We employed biotinylation and streptavidin affinity chromatography to label and enrich proteins from apical and basolateral membranes of rat kidney inner medullary collecting ducts (IMCDs) prior to LC-MS/MS protein identification. To enrich apical membrane proteins and bound peripheral membrane proteins, IMCDs were perfusion-labeled with primary amine-reactive biotinylation reagents at 2 C using a double-barreled pipette. The perfusion-biotinylated proteins, and proteins bound to them were isolated with CaptAvidin-agarose beads, separated with SDS-PAGE, and sliced into continuous gel pieces for LC-MS/MS protein identification (LTQ, Thermo Electron Corp.). 17 integral and GPI-linked membrane proteins and 44 non-integral membrane proteins were identified. Immunofluorescence confocal microscopy confirmed ACVRL1, H/K ATPase 1, NHE2, and TauT expression in the IMCDs. Basement membrane and basolateral membrane proteins were biotinylated via incubation of IMCD suspensions with biotinylation reagents on ice. 23 integral and GPI-linked membrane proteins and 134 non-integral membrane proteins were identified. Analyses of non-integral membrane proteins preferentially identified in the perfusion-biotinylated and not in the incubation-biotinylated IMCDs reveals protein kinases, scaffold proteins, SNARE proteins, motor proteins, small GTP-binding proteins and related proteins that may be involved in vasopressin-stimulated AQP2, UT-A1, and ENaC regulation. A WWW-accessible database was constructed of 222 membrane proteins (integral and GPI-linked) from this study and prior studies.


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