Am J Physiol Cell Physiol AJP: Heart and Circulatory Physiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 296: C414-C421, 2009. First published December 10, 2008; doi:10.1152/ajpcell.00430.2008
0363-6143/09 $8.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Tables
Right arrow All Versions of this Article:
296/3/C414    most recent
00430.2008v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via Web of Science (2)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gallagher, S. M.
Right arrow Articles by Philp, N. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gallagher, S. M.
Right arrow Articles by Philp, N. J.

MEMBRANE TRANSPORTERS, ION CHANNELS, AND PUMPS

Interaction of monocarboxylate transporter 4 with β1-integrin and its role in cell migration

Shannon M. Gallagher, John J. Castorino, and Nancy J. Philp

Department of Anatomy, Pathology and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania

Submitted 20 August 2008 ; accepted in final form 9 December 2008

Monocarboxylate transporter (MCT) 4 is a heteromeric proton-coupled lactate transporter that is noncovalently linked to the extracellular matrix metalloproteinase inducer CD147 and is typically expressed in glycolytic tissues. There is increasing evidence to suggest that ion transporters are part of macromolecular complexes involved in regulating β1-integrin adhesion and cell movement. In the present study we examined whether MCTs play a role in cell migration through their interaction with β1-integrin. Using reciprocal coimmunoprecipitation assays, we found that β1-integrin selectively associated with MCT4 in ARPE-19 and MDCK cells, two epithelial cell lines that express both MCT1 and MCT4. In polarized monolayers of ARPE-19 cells, MCT4 and β1-integrin colocalized to the basolateral membrane, while both proteins were found in the leading edge lamellapodia of migrating cells. In scratch-wound assays, MCT4 knockdown slowed migration and increased focal adhesion size. In contrast, silencing MCT1 did not alter the rate of cell migration or focal adhesion size. Taken together, our findings suggest that the specific interaction of MCT4 with β1-integrin may regulate cell migration through modulation of focal adhesions.

MCT4; CD147


Address for reprint requests and other correspondence: N. J. Philp, Dept. of Pathology, Anatomy and Cell Biology, Jefferson Medical College, Thomas Jefferson Univ., 1020 Locust St., Philadelphia, PA 19107 (e-mail: nancy.philp{at}jefferson.edu)






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online
Copyright © 2009 by the American Physiological Society.