Localization of a calcium-stimulated ATPase in the basal-lateral plasma membranes of the proximal tubule of rat kidney cortex

Kinne-Saffran, Evamaria; Kinne, Rolf

doi:10.1007/bf01870187

Cited by 103 publications

(25 citation statements)

References 24 publications

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“…2A. The basal-lateral membrane fractions (10)(11)(12)(13)(14)(15)(16)(17) were pooled and re-electrophorized, to eliminate contaminating brush border membranes (Fig. 2 B).…”

Section: Enzymatic Characteristics Of'tlw Azide-insensitive Ca2 '-Atpmentioning

confidence: 99%

An azide‐insensitive low‐affinity ATPase stimulated by Ca²⁺ or Mg²⁺ in basal‐lateral and brush border membranes of kidney cortex

Ilsbroux¹,

Vanduffel²,

Teuchy³

et al. 1985

European Journal of Biochemistry

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Basal‐lateral and brush border membranes from pig kidney cortex were prepared by differential centrifugation followed by free‐flow electrophoresis. In each type of membrane, azide‐insensitive, low‐affinity Ca2+‐ATPase and Mg2+‐ATPase activities are demonstrated. A comparative study for both membranes further reveals the following analogies between these ATPase: (a) they show maximal activity between pH 8 and 8.5; (b) they exhibit Km values for Ca‐ATP or Mg‐ATP in the millimolar range and have a comparable low substrate specificity; (c) they are insensitive to 10 μM of vanadate, N,N′‐dicyclohexylcarbodiimide, diethylstillbestrol, quercetin, harmaline and amiloride. The partial inhibition by 1 mM of the various compounds is rather aspecific. In view of these similarities it is concluded that only one enzyme entity is responsible for the activity which is measured in both membrane types. The HCO3−‐stimulated Mg2+‐ATPase activity in pig kidney cortex was also studied. This enzyme, however, is clearly of mitochondrial origin since the HCO3−‐stimulation coincides with the distribution profile of succinate dehydrogenase, a mitochondrial marker; and since it is inhibited by azide.

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“…2A. The basal-lateral membrane fractions (10)(11)(12)(13)(14)(15)(16)(17) were pooled and re-electrophorized, to eliminate contaminating brush border membranes (Fig. 2 B).…”

Section: Enzymatic Characteristics Of'tlw Azide-insensitive Ca2 '-Atpmentioning

confidence: 99%

An azide‐insensitive low‐affinity ATPase stimulated by Ca²⁺ or Mg²⁺ in basal‐lateral and brush border membranes of kidney cortex

Ilsbroux¹,

Vanduffel²,

Teuchy³

et al. 1985

European Journal of Biochemistry

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“…In fact, assuming reflection coefficient of zero for calcium in this segment, the amount of calcium calculated to be removed with sodium and water is only a fraction of the measured calcium efflux. Consequently, the ratio of the concentration of calcium (17) have localized a calcium-stimulated ATPase in the basolateral plasma membrane ofrat cortical proximal tubule. This enzyme, therefore, may play an important role in calcium transport out of the superficial proximal straight tubule of the rabbit.…”

mentioning

confidence: 99%

“…This enzyme, therefore, may play an important role in calcium transport out of the superficial proximal straight tubule of the rabbit. Because it was resistant to known inhibitors (17), the precise role of this enzyme will have to await the identification of specific inhibitors of its activity.…”

mentioning

confidence: 99%

Calcium transport in the pars recta and thin descending limb of Henle of the rabbit, perfused in vitro.

Rouse¹,

Ng²,

Suki³

1980

J. Clin. Invest.

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“…HC03-ATPase was selected as a marker for the luminal membranes of the collecting duct epithelial cell because this enzyme has been shown to be contained exclusively in the brush border fraction of the proximal tubular epithelial cell membrane (25), where it is probably implicated in the process by which proximal tubular urine is acidified; it is reasonable to assume a similar luminal localization in the collecting duct, which is also a site of urinary acidification (35).…”

Section: Discussionmentioning

confidence: 99%

“…1). In analogy to the proximal tubule, Ca-ATPase (24) and HCO3-ATPase (25) were used as marker enzymes for the contraluminal and luminal plasma membranes, respectively. As shown in Table 1, the enrichment of Ca-ATPase activity in fraction I and the enrichment of HCO3-ATPase activity in fraction II identified these membrane fractions as contraluminal and luminal, respectively.…”

mentioning

confidence: 99%

Target Cell Polarity and Membrane Phosphorylation in Relation to the Mechanism of Action of Antidiuretic Hormone

Schwartz

Shlatz

Kinne-Saffran

et al. 1974

Proc. Natl. Acad. Sci. U.S.A.

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The plasma membrane of the bovine renal collecting duct epithelial cell has been resolved into its apical (luminal) and basal-lateral (contraluminal) components by free flow electr4iphoresis. The contraluminal, but not the luminal, membrane was found to contain antidiuretic hormone-sensitive adenylate cyclase. The luminal membrane was found to contain a cyclic 3': 5'-adenosine monophosphate-sensitive self-phosphorylating system consisting of a membrane-bound protein kinase and its membrane-bound substrate(s); this intrinsic protein kinase was not present in the contraluminal membrane.These Recently we have shown that parathyroid hormone (PT hormone)-sensitive adenylate cyclase is localized in the contraluminal (basal-lateral) but not in the luminal (apical) plasma membranes of rat renal cortical epithelial cells, whereas cAMP-dependent phosphorylation occurs in the luminal but not the contraluminal membranes (9, 10). To determine whether a similar enzymatic distribution occurs in other segments of the nephron, we have investigated the localization of antidiuretic hormone (AD hormone)-sensitive adenylate cyclase and of cAMP-dependent protein kinase in the papillary collecting duct epithelium. The results of these studies indicate that AD hormone-stimulated cAMP generation is localized in the contraluminal plasma membrane, whereas cAMP-mediated membrane phosphorylation is localized in the luminal plasma membrane. The latter localization-in conjunction with the well-established luminal site 10 mM triethanolamine-HCl, pH 7.6); all subsequent procedures were carried out at 0-4'. The kidneys were freed from adherent connective tissues and the papillae were removed by careful dissection of the renal pelvis. Six grams of tissue were minced in a small volume of ST-buffer and then diluted to a final volume of 30 ml. Aliquots (10 ml) of the suspension were homogenized in a Dounce homogenizer by five strokes with a loose-fitting pestle. The homogenates were combined and filtered through two layers of cheese cloth and further homogenized by 15 strokes with a tight-fitting pestle. This homogenate was centrifuged at 700 X g for 10 min; the supernatant was centrifuged at 10,000 X g for 10 mmi. The second supernatant was saved and the pellet resuspended in 5 ml of STbuffer. Then 10 ml of ST-buffer was added and the suspension centrifuged for 10 min at 10,000 X g. The resulting supernatant was combined with the "saved" supernatant and the solution was centrifuged at 100,000 X g for 1 hr. The pellet was suspended in 4 ml of electrophoresis buffer (8.5 mM acetic acid, 8.5 mM triethanolamine, and 280 mM sucrose adjusted to pH 7.4 with 2 M NaOH), homogenized with 10 strokes in the tight-fitting Dounce honiogenizer, and diluted to a final volume of 10 ml with the electrophoresis buffer. The resulting preparation, observed by electron microscopy to consist of membrane fragments and vesicles, was used to study the properties of papillary plasma membranes prior to electrophoretic separation.To prepare for electrophoresis, we cent...

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Localization of a calcium-stimulated ATPase in the basal-lateral plasma membranes of the proximal tubule of rat kidney cortex

Cited by 103 publications

References 24 publications

An azide‐insensitive low‐affinity ATPase stimulated by Ca²⁺ or Mg²⁺ in basal‐lateral and brush border membranes of kidney cortex

An azide‐insensitive low‐affinity ATPase stimulated by Ca²⁺ or Mg²⁺ in basal‐lateral and brush border membranes of kidney cortex

Calcium transport in the pars recta and thin descending limb of Henle of the rabbit, perfused in vitro.

Target Cell Polarity and Membrane Phosphorylation in Relation to the Mechanism of Action of Antidiuretic Hormone

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Localization of a calcium-stimulated ATPase in the basal-lateral plasma membranes of the proximal tubule of rat kidney cortex

Cited by 103 publications

References 24 publications

An azide‐insensitive low‐affinity ATPase stimulated by Ca2+ or Mg2+ in basal‐lateral and brush border membranes of kidney cortex

An azide‐insensitive low‐affinity ATPase stimulated by Ca2+ or Mg2+ in basal‐lateral and brush border membranes of kidney cortex

Calcium transport in the pars recta and thin descending limb of Henle of the rabbit, perfused in vitro.

Target Cell Polarity and Membrane Phosphorylation in Relation to the Mechanism of Action of Antidiuretic Hormone

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An azide‐insensitive low‐affinity ATPase stimulated by Ca²⁺ or Mg²⁺ in basal‐lateral and brush border membranes of kidney cortex

An azide‐insensitive low‐affinity ATPase stimulated by Ca²⁺ or Mg²⁺ in basal‐lateral and brush border membranes of kidney cortex