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Research Service, Malcom Randall Department of Veterans Affairs Medical Center, and Department of Medicine, University of Florida, Gainesville, Florida 32608-1197
In this study, we
investigated the possible interaction between the cationic amino acid
transporter (CAT)-1 arginine transporter and ankyrin or
fodrin. Because ankyrin and fodrin are substrates for
calpain and because hypoxia increases calpain expression and activity
in pulmonary artery endothelial cells (PAEC), we also studied the
effect of hypoxia on ankyrin, fodrin, and CAT-1 contents in PAEC.
Exposure to long-term hypoxia (24 h) inhibited L-arginine uptake by PAEC, and this inhibition was prevented by calpain inhibitor 1. The effects of hypoxia and calpain inhibitor 1 were not associated with changes in CAT-1 transporter content in PAEC plasma membranes. However, hypoxia stimulated the hydrolysis of ankyrin and fodrin in
PAEC, and this could be prevented by calpain inhibitor 1. Incubation of
solubilized plasma membrane proteins with anti-fodrin antibodies resulted in a 70% depletion of CAT-1 immunoreactivity and in a 60%
decrease in L-arginine transport activity in reconstituted proteoliposomes (3,291 ± 117 vs. 8,101 ± 481 pmol · mg
protein
1 · 3 min1 in
control). Incubation with anti-ankyrin antibodies had
no effect on CAT-1 content or L-arginine transport in
reconstituted proteoliposomes. These results demonstrate that CAT-1
arginine transporters in PAEC are associated with fodrin, but not with
ankyrin, and that long-term hypoxia decreases L-arginine
transport by a calpain-mediated mechanism that may involve fodrin proteolysis.
ankyrin; calpain; hypoxia; pulmonary artery endothelial cells; cationic amino acid transporter-1
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