A high yield preparation for rat kidney brush border membranes Different behaviour of lysosomal markers

Biber, J; Stieger, Bruno; Haase, Winfried; Murer, Heini

doi:10.1016/0005-2736(81)90243-1

Cited by 429 publications

(193 citation statements)

References 18 publications

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“…However, a relation of the divalent cationstimulated ATPase activities in our membrane preparation with lysosomal Mg2+-ATPase is improbable since the lysosoinal enzyme shows a totally different substrate specificity: ITP, CTP and UTP are hydrolyzed at respectively 66%, 24% and 34% of the rate of ATP hydrolysis [29]. Furthermore, the different lysosomal markers are unreliable because they show non-parallel distribution patterns during subcellular fractionation of kidney cortex [30].…”

Section: I'o-~mentioning

confidence: 95%

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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Section: I'o-~mentioning

confidence: 95%

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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“…Brush-border membranes were prepared from rat kidney [29] and stored as previously described [14]. The glutamine/amino acid transporter was solubilized by treating the membrane preparation (50 µl, about 0.15 mg protein) with 1.3 % C 12 E 8 in a final volume of 150 µl and centrifuged at 13000 g for 4 min at 4° C. The supernatant (extract) was used for the reconstitution.…”

Section: Solubilization Of the Glutamine/amino Acid Transportermentioning

confidence: 99%

Inactivation by Hg2+ and methylmercury of the glutamine/amino acid transporter (ASCT2) reconstituted in liposomes: Prediction of the involvement of a CXXC motif by homology modelling

Oppedisano

Galluccio

Indiveri

2010

Biochemical Pharmacology

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A c c e p t e d M a n u s c r i p t 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64

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“…Rat kidney brush border membrane vesicles were prepared by an EGTA/magnesium precipitation method as described previously in detail (Biber et al, 1981;Stieger et al, 1995). After the final centrifugation step, membrane vesicles were taken up in 400 mM Hepes/Tris, pH 7.4, dispersed using a syringe with a fine needle and used immediately for transport experiments.…”

Section: Isolation Of Proximal Tubular Brush Border Membrane Vesiclesmentioning

confidence: 99%

The plasma carnitine concentration regulates renal OCTN2 expression and carnitine transport in rats

Schürch

Todesco

Nováková

et al. 2010

European Journal of Pharmacology

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Previous findings in rats and in human vegetarians suggest that the plasma carnitine concentration and/or carnitine ingestion may influence the renal reabsorption of carnitine. We tested this hypothesis in rats with secondary carnitine deficiency following treatment with N-trimethyl-hydrazine-3-propionate (THP) for 2 weeks and rats treated with excess L-carnitine for 2 weeks. Compared to untreated control rats, treatment with THP was associated with an approximately 70% decrease in plasma carnitine and with a 74% decrease in the skeletal muscle carnitine content. In contrast, treatment with Lcarnitine increased plasma carnitine levels by 80% and the skeletal muscle carnitine content by 50%. Treatment with L-carnitine affected neither the activity of carnitine transport into isolated renal brush border membrane vesicles, nor renal mRNA expression of the carnitine transporter OCTN2. In contrast, in carnitine deficient rats, carnitine transport into isolated brush border membrane vesicles was increased 1.9-fold compared to untreated control rats. Similarly, renal mRNA expression of OCTN2 increased by a factor of 1.7 in carnitine deficient rats, whereas OCTN2 mRNA expression remained unchanged in gut, liver or skeletal muscle. Our study supports the hypothesis that a decrease in the carnitine plasma and/or glomerular filtrate concentration increases renal expression and activity of OCTN2.

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A high yield preparation for rat kidney brush border membranes Different behaviour of lysosomal markers

Cited by 429 publications

References 18 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

Inactivation by Hg2+ and methylmercury of the glutamine/amino acid transporter (ASCT2) reconstituted in liposomes: Prediction of the involvement of a CXXC motif by homology modelling

The plasma carnitine concentration regulates renal OCTN2 expression and carnitine transport in rats

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A high yield preparation for rat kidney brush border membranes Different behaviour of lysosomal markers

Cited by 429 publications

References 18 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

Inactivation by Hg2+ and methylmercury of the glutamine/amino acid transporter (ASCT2) reconstituted in liposomes: Prediction of the involvement of a CXXC motif by homology modelling

The plasma carnitine concentration regulates renal OCTN2 expression and carnitine transport in rats

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Product

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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