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Volume 272, Number 50, Issue of December 12, 1997
pp. 31213-31216
(Received for publication, August 27, 1997, and in revised form, October 8, 1997)
From the Immunohistochemistry of porcine pulmonary artery
endothelial cells (PAEC) with antibodies specific for caveolin,
endothelial nitric-oxide synthase (eNOS), and the arginine transporter
(CAT1) demonstrates that all of these proteins co-localize in plasma membrane caveolae. When incubated with solubilized PAEC plasma membrane
proteins, eNOS-specific antibody immunoprecipitates CAT1-mediated arginine transport. These results document the existence of a caveolar
complex between CAT1 and eNOS in PAEC that provides a mechanism for the
directed delivery of substrate arginine to eNOS. Direct transfer of
extracellular arginine to membrane-bound eNOS accounts for the
"arginine paradox" and explains why caveolar localization of eNOS
is required for optimal nitric oxide production by endothelial
cells.
COMMUNICATION:
A Caveolar Complex between the Cationic Amino Acid
Transporter 1 and Endothelial Nitric-oxide Synthase May Explain the
"Arginine Paradox"
,
Department of Biochemistry and Molecular
Biology and the Center for Structural Biology and the ¶ Department
of Medicine and the Gainesville VA Medical Center, University of
Florida College of Medicine, Gainesville, Florida 32610-0245
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