Presence of an extensive clathrin coat on the apical plasmalemma of the rat kidney proximal tubule cell.

Rodman, Jane Somsel; Kerjaschki, Dontscho; Merisko, Elaine M.; Farquhar, M G

doi:10.1083/jcb.98.5.1630

Cited by 73 publications

(40 citation statements)

References 25 publications

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“…Studies on isolated, microdissected nephron segments have also described N-ethyl maleimide (NEM)-sensitive ATPase activity in regions where we find immunoreactive sites (10). The location of the antigenic sites in the proximal tubule appears distinct from the known distribution of clathrin in these cells (25,26). Coated pits are found in all cell types in the kidney, and no specific labeling of these structures was detectable with our antibodies.…”

Section: Immunocytochemistrymentioning

confidence: 52%

See 1 more Smart Citation

Localization of a proton-pumping ATPase in rat kidney.

Brown¹,

Hirsch²,

Gluck³

1988

J. Clin. Invest.

319

192

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The distribution of vacuolar H'ATPase in rat kidney was examined by immunocytochemistry using affinity-purified antibodies against the 31-, 56-, and 70-kD subunits of the bovine kidney proton pump. Proximal convoluted tubules were labeled over apical plasma membrane invaginations, and in the initial part of the thin descending limb, apical and basolateral plasma membranes were moderately stained. Thick ascending limbs and distal convoluted tubules were apically stained although the intensity was greater in the distal convoluted tubule. Collecting duct principal cells were virtually unlabeled, but intercalated cells had intense staining with an apical, basolateral or diffuse pattern in the cortex, and exclusively apical staining in the medulla. These results (a) show the presence of an H'ATPase in the apical plasma membrane of the proximal tubule that may contribute to H+ transport in this segment; (b) provide direct evidence that the intercalated cell contains most of the H'ATPase detectable in the collecting duct, supporting its proposed role in H+ transport; (c) demonstrate that subpopulations of cortical intercalated cells have opposite polarities of an H'ATPase, consistent with the presence of both proton-and bicarbonate-secreting cells; and (d) suggest a role for the H+ATPase in acid/base regulation or H+ transport in segments other than the collecting duct and the proximal tubule.

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Section: Immunocytochemistrymentioning

confidence: 52%

“…5). The labeled invaginations appeared distinct from the coated pits previously shown to be labeled with anti-clathrin antibodies (25,26). The clathrin-coated membranes were apparent in K4M-embedded tissues even in the absence of specific immunolabeling, because they have a distinct, clear halo on their cytoplasmic side (see Fig.…”

Section: Immunocytochemistrymentioning

confidence: 72%

Localization of a proton-pumping ATPase in rat kidney.

Brown¹,

Hirsch²,

Gluck³

1988

J. Clin. Invest.

319

192

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“…There is now very good evidence that all of these compartments are acidified by a proton-translocating ATPase (30)(31)(32)(33)(34)(35). Recently, it has been shown that the endocytic vesicles budding off the apical plasma membranes of proximal tubules are coated with clathrin (36). Such vesicles in other tissues are acidified by H+ translocating ATPases (32)(33)(34).…”

Section: Discussionmentioning

confidence: 99%

Carbon dioxide causes exocytosis of vesicles containing H+ pumps in isolated perfused proximal and collecting tubules.

Schwartz¹,

Al‐Awqati²

1985

J. Clin. Invest.

233

105

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In the turtle bladder it has recently been shown that CO2 stimulates H' secretion, at least in part, by causing fusion of vesicles enriched in H' pumps with the luminal plasma membrane. To test for the presence of this mechanism in the kidney we perfused collecting ducts and proximal straight tubules on the stage of an inverted epifluorescence microscope with fluorescein isothiocyanate dextran (70,000 mol wt) in CO2-free medium. After washout we noted punctate fluorescence in endocytic vesicles in some collecting ducts and in all proximal straight tubule cells. More cells took up fluorescent dextran in outer medullary than in cortical collecting ducts. Using the pH dependence of the excitation spectrum of fluorescein we found the pH of the vesicles to be acid (-pH 6). Addition of proton ionophores increased vesicular pH by 0.6±0.1 U, suggesting that the acidity of the vesicles was caused by H' pumps. CO2 added to the medium (25 mmHg, pH 7.6 at 370C) reduced fluorescence intensity by 24±5% in cortical collecting ducts, 27±5% in medullary collecting ducts, and 25±5% in proximal straight tubules. Since this effect was prevented by the prior addition of colchicine to the bath, we believe that CO2 caused a decrease in cytoplasmic fluorescence by stimulating exocytotic fusion of the vesicles and thereby secretion of fluorescent dextran. This exocytotic fusion also occurred when tubules that were loaded with fluorescent dextran at a pCO2 of 37 mmHg were exposed isohydrically to a pCO2 of 114 mmHg; the mean decrease was 53±4%.We conclude that some cells in the collecting ducts and all cells in the proximal straight tubule incorporate fluorescent dextran into the apical cytoplasmic vesicles and acidify them with H+ pumps. CO2 causes fusion of these vesicles with the luminal membrane, but whether CO2 stimulates H+ secretion by increasing the number of functioning H+ pumps remains to be determined.

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“…At the light microscope level, the proximal tubule vacuolar H ϩ -ATPase localizes at the base of the brush border, which is the membrane domain showing a high level of clathrin-mediated endocytotic activity (430). The brush-border microvilli are also labeled to a variable extent, depending on the precise tubule segment examined and on the antibodies used for immunostaining (79, 232).…”

Section: A Proximal Tubulementioning

confidence: 99%

Renal Vacuolar H⁺-ATPase

Wagner¹,

Finberg²,

Breton³

et al. 2004

Physiological Reviews

413

476

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Vacuolar H+-ATPases are ubiquitous multisubunit complexes mediating the ATP-dependent transport of protons. In addition to their role in acidifying the lumen of various intracellular organelles, vacuolar H+-ATPases fulfill special tasks in the kidney. Vacuolar H+-ATPases are expressed in the plasma membrane in the kidney almost along the entire length of the nephron with apical and/or basolateral localization patterns. In the proximal tubule, a high number of vacuolar H+-ATPases are also found in endosomes, which are acidified by the pump. In addition, vacuolar H+-ATPases contribute to proximal tubular bicarbonate reabsorption. The importance in final urinary acidification along the collecting system is highlighted by monogenic defects in two subunits (ATP6V0A4, ATP6V1B1) of the vacuolar H+-ATPase in patients with distal renal tubular acidosis. The activity of vacuolar H+-ATPases is tightly regulated by a variety of factors such as the acid-base or electrolyte status. This regulation is at least in part mediated by various hormones and protein-protein interactions between regulatory proteins and multiple subunits of the pump.

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Presence of an extensive clathrin coat on the apical plasmalemma of the rat kidney proximal tubule cell.

Cited by 73 publications

References 25 publications

Localization of a proton-pumping ATPase in rat kidney.

Localization of a proton-pumping ATPase in rat kidney.

Carbon dioxide causes exocytosis of vesicles containing H+ pumps in isolated perfused proximal and collecting tubules.

Renal Vacuolar H⁺-ATPase

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Presence of an extensive clathrin coat on the apical plasmalemma of the rat kidney proximal tubule cell.

Cited by 73 publications

References 25 publications

Localization of a proton-pumping ATPase in rat kidney.

Localization of a proton-pumping ATPase in rat kidney.

Carbon dioxide causes exocytosis of vesicles containing H+ pumps in isolated perfused proximal and collecting tubules.

Renal Vacuolar H+-ATPase

Contact Info

Product

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Renal Vacuolar H⁺-ATPase