Basolateral distribution of caveolin-1 in the kidney. Absence from H+-atpase-coated endocytic vesicles in intercalated cells.
In kidney epithelial cells, a variety of physiological processes are dependent on the active recycling of membrane proteins between intracellular vesicles and the cell surface. Although clathrin-mediated endocytosis occurs in several renal cell types, endocytosis can also occur by non-clathrin-coated vesicles, including pinocytotic structures known as caveolae that contain a novel coat protein, caveolin. Exo- and endocytosis of a vacuolar H+-ATPase in intercalated cells also occurs via specialized "coated" vesicles that do not contain clathrin. The aim of this study was to localize caveolin in the kidney and, in addition, to determine whether it could be a component of the H+-ATPase recycling process. Using an antibody against the alpha- and beta-isoforms of caveolin-1, our immunocytochemical data show a marked heterogeneity in the cellular expression of this isoform of caveolin in kidney. In contrast, caveolin-3 was not detectable in renal epithelial cells. Caveolin-1 was abundant in endothelial cells and smooth muscle cells and was present in the parietal cells of Bowman's capsule. Distal tubule cells, connecting tubule cells, and collecting duct principal cells exhibited marked punctate basolateral staining, corresponding to the presence of caveolae detected by electron microscopy, whereas all intercalated cells were negative in both cortex and medulla. These data indicate that although caveolin-1 may participate in basolateral events in some kidney epithelial cell types, it does not appear to be involved in the regulated recycling of H+-ATPase in intercalated cells. Therefore, these cells recycle H+-ATPase by a mechanism that involves neither clathrin nor caveolin-1.
Breton
S
S
Renal Unit and Department of Pathology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts, USA.
Lisanti
M P
MP
Tyszkowski
R
R
McLaughlin
M
M
Brown
D
D
D000818:Animals; D015153:Blotting, Western; D051242:Caveolin 1; D022461:Caveolins; D002462:Cell Membrane / Q000737:chemistry / Q000648:ultrastructure; D018699:Coated Vesicles / Q000737:chemistry* / Q000201:enzymology / Q000648:ultrastructure; D003911:Dextrans / Q000378:metabolism; D004705:Endocytosis; D004847:Epithelial Cells / Q000737:chemistry / Q000648:ultrastructure; D016650:Fluorescein-5-isothiocyanate / Q000031:analogs & derivatives / Q000378:metabolism; D007668:Kidney / Q000737:chemistry* / Q000648:ultrastructure; D007672:Kidney Cortex / Q000737:chemistry / Q000648:ultrastructure; D007679:Kidney Medulla / Q000737:chemistry / Q000648:ultrastructure; D007684:Kidney Tubules / Q000737:chemistry / Q000648:ultrastructure; D008297:Male; D008565:Membrane Proteins / Q000032:analysis*; D008854:Microscopy, Electron; D008856:Microscopy, Fluorescence; D015388:Organelles / Q000737:chemistry* / Q000648:ultrastructure; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley
C495537:Cav1 protein, rat; D051242:Caveolin 1; D022461:Caveolins; D003911:Dextrans; D008565:Membrane Proteins; C015219:fluorescein isothiocyanate dextran; D006180:Proton-Translocating ATPases; D016650:Fluorescein-5-isothiocyanate