Is there a plasma membrane-located anion-sensitive ATPase? IV. Distribution of the enzyme in rat pancreas

Amelsvoort, J.M.M. van; Jansen, J.W.C.M.; Pont, J.J.H.H.M. de; Bonting, S.L.

doi:10.1016/0005-2736(78)90254-7

Cited by 31 publications

(9 citation statements)

References 26 publications

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“…Various kinds of anion-stimulated ATPase activity have been reported in a number of tissues and organs [12,14,45,48], including the kidney [8,22,26,31]. In epithelial ceils, these ATPases are thought to be involved in transepithelial transport of chloride and/or bicarbonate.…”

Section: Introductionmentioning

confidence: 99%

Presence of an extramitochondrial anion-stimulated ATPase in the rabbit kidney: Localization along the nephron and effect of corticosteroids

1986

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To determine whether kidney membrane fractions contain an extramitochondrial anion-stimulated ATPase, we compared the pharmacological and kinetic properties of HCO3-ATPase activities in mitochondrial and microsomal fractions prepared from rabbit kidney cortex and outer medulla. The results indicated that this activity differed markedly in each type of fraction. Microsomal HCO3-ATPase was less sensitive than mitochondrial ATPase to azide, oligomycin, DCCD and thiocyanate, but was more sensitive to filipin and displayed different dependency towards ATP, magnesium and pH. Microsomal ATPase activity was stimulated by sulfite much more strongly than by bicarbonate, whereas mitochondrial activity was stimulated by both these anions to a similar extent. These results demonstrate the presence of an extramitochondrial HCO3-ATPase in kidney membrane fractions. HCO3-ATPase was also measured in single microdissected segments of the rabbit nephron using a radiochemical microassay previously developed for tubular Na, K-ATPase activity. An enzyme with the pharmacological and kinetic properties of the microsomal enzyme was detected in both proximal tubule, distal convoluted tubule and collecting duct, but the thick ascending limb was devoid of any detectable activity. Long-term DOCA administration markedly increased HCO3-ATPase activity in the distal convoluted and collecting tubule. The insensitivity of microsomal HCO3-ATPase to vanadate indicates that it belongs to the F0-F1 class of ATPases, and might therefore be involved in proton transport. This hypothesis is also supported by the localization of tubular HCO3-ATPase activity at the sites of urinary acidification.

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Section: Introductionmentioning

confidence: 99%

Presence of an extramitochondrial anion-stimulated ATPase in the rabbit kidney: Localization along the nephron and effect of corticosteroids

1986

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“…ATP is the preferred substrate for the anionstimulated ATPase, with an optimal Mg 2+ /ATP ratio ranging from 0.5 to 2.0 (Simon & Thomas, 1972;Van Amelsvoort et al, 1977 a, b;Vara & Serrano, 1982). GTP and ITP are less preferred substrates than ATP for the anion-stimulated ATPase, whereas UTP and CTP are slightly hydrolysed or not hydrolysed at all by the enzyme Simon & Thomas, 1972).…”

Section: General Properties Of Anion ( CL X )-Atpasesmentioning

confidence: 99%

“…The divalent cation Mg 2+ is absolutely required for anion-stimulated ATPase activity, but inhibits at high concentrations Gerencser & Lee, 1985 b;Gerencser & Zelezna, 1993) as are also the cases for the cation-stimulated enzymes: (Na + +K + )-ATPase and (Ca 2+ +Mg 2+ )-ATPase. Rat Iritani & Wells ( 1976) Mn 2+ can substitute for Mg 2+ in the gastric mucosal enzyme (Sachs, Mitch & Hirschowitz, 1965), but does so to a lesser extent in the pancreatic enzyme (Simon, Kinne & Sachs, 1972 b;Van Amelsvoort et al, 1978;Vara & Serrano, 1982). Generally, Na + or K + has little or no effect on the anion-ATPase activity Simon & Thomas, 1972); however, K + was shown to have a stimulatory effect on the enzyme in rat salivary glands (Wais & Knauf, 1975) while NH 4 + appears to inhibit anion-stimulated ATPase activity (Sachs et al, 1965) in frog gastric mucosa.…”

Section: General Properties Of Anion ( CL X )-Atpasesmentioning

confidence: 99%

Chloride ATPase pumps in nature: do they exist?

Gerencser

Zhang

2003

Biological Reviews

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Five widely documented mechanisms for chloride transport across biological membranes are known: anion-coupled antiport, Na+ and H(+)-coupled symport, Cl- channels and an electrochemical coupling process. These transport processes for chloride are either secondarily active or are driven by the electrochemical gradient for chloride. Until recently, the evidence in favour of a primary active transport mechanism for chloride has been inconclusive despite numerous reports of cellular Cl(-)-stimulated ATPases coexisting, in the same tissue, with uphill ATP-dependent chloride transport. Cl(-)-stimulated ATPase activity is a ubiquitous property of practically all cells with the major location being of mitochondrial origin. It also appears that plasma membranes are sites of Cl(-)-stimulated ATPase pump activity. Recent studies of Cl(-) -stimulated ATPase activity and ATP-dependent chloride transport in the same plasma membrane system, including liposomes, strongly suggest a mediation by the ATPase in the net movement of chloride up its electrochemical gradient across the plasma membrane structure. Contemporary evidence points to the existence of Cl(-)-ATPase pumps; however, these primary active transporters exist as either P-, F- or V-type ATPase pumps depending upon the tissue under study.

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“…The ATPase activity in the mitochondrial flactions as well as in the brush border membrane fractions was determined according to Bornancin et al 1 The incubation medium contained 2 x 10-3 M ouabain, 1 x 10 3 M MgSO4, 1 x 10-3 N Na2-ATP, 5 x 10-2 N gtycineTris, pH 8.0, and HCO~ in a final concentration of 2.5 x 10-2 M.…”

Section: Determination Of the Bicarbonate-stimulated Mg 2 +-A Tpase Amentioning

confidence: 99%

“…One of the difficulties in studies on the distribution of this enzyme in the cells of the proximal tubule is the presence of a high bicarbonate stimulated Mg 2 § activity in the mitochondria. So the existence of a plasma membrane bound anion sensitive Mg 2 § -ATPase in the kidney and also in various other tissues has been recently questioned and has been attributed to the mitochondrial contamination of the membrane fractions [1][2][3]. …”

mentioning

confidence: 99%

Further evidence for the existence of an intrinsic bicarbonate-stimulated Mg2+-ATPase in brush border membranes isolated from rat kidney cortex

Kinne-Saffran

Kinne

1979

J. Membrain Biol.

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The aim of this study was to provide further evidence for the existence of a nonmitochondrial becarbonate-stimulated Mg2+-ATPase in brush border membranes derived from rat kidney cortex. A plasma membrane fraction rich in brush border microvilli and a mitochondrial fraction were isolated by differential centrifugation. Both fractions contain a Mg2+-ATPase activity which can be stimulated by bicarbonate. The two Mg2+-ATPases are stimulated likewise by chloride, bicarbonate, and sulfite or inhibited by oligomycin and aurovertin, though to different degrees. In contrast to these similarities, only the Mg2+-ATPase activity of the mitochondrial fraction is inhibited by atractyloside, a substance which blocks an adenine nucleotide translocator in the inner mitochondrial membrane. On the other hand, filipin, an antibiotic that complexes with cholesterol in the membranes inhibits exclusively the Mg2+-ATPase of the cholesterol-rich brush border membranes. Furthermore it could be demonstrated by the use of bromotetramisole, an inhibitor of alkaline phosphatase activity, that the Mg2+-ATPase activity in the membrane fraction is not due to the presence of the highly active alkaline phosphatase in these membranes. These results support the assumption that an intrinsic bicarbonate-stimulated Mg2+-ATPase is present in rat kidney brush border membranes.

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Is there a plasma membrane-located anion-sensitive ATPase? IV. Distribution of the enzyme in rat pancreas

Cited by 31 publications

References 26 publications

Presence of an extramitochondrial anion-stimulated ATPase in the rabbit kidney: Localization along the nephron and effect of corticosteroids

Presence of an extramitochondrial anion-stimulated ATPase in the rabbit kidney: Localization along the nephron and effect of corticosteroids

Chloride ATPase pumps in nature: do they exist?

Further evidence for the existence of an intrinsic bicarbonate-stimulated Mg2+-ATPase in brush border membranes isolated from rat kidney cortex

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