Reversible inhibition by 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid of the plasma membrane calcium-magnesium ATPase from kidney proximal tubules

Biochemistry ◽  
1991 ◽  
Vol 30 (23) ◽  
pp. 5700-5706 ◽  
Author(s):  
Adilson Guilherme ◽  
Jose Roberto Meyer-Fernandes ◽  
Adalberto Vieyra
Keyword(s):  
Plasma Membrane ◽  
Proximal Tubules ◽  
Disulfonic Acid ◽  
Reversible Inhibition ◽  
Magnesium Atpase ◽  
Calcium Magnesium ◽  
Kidney Proximal Tubules

Lysophosphatidic acid (LPA) as a modulator of plasma membrane Ca2+-ATPase from basolateral membranes of kidney proximal tubules

2021 ◽  
Author(s):  
Julliana F. Sant’Anna ◽  
Vanessa S. Baldez ◽  
Natalie A. Razuck-Garrão ◽  
Thiago Lemos ◽  
Bruno L. Diaz ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Lysophosphatidic Acid ◽  
Proximal Tubules ◽  
Basolateral Membranes ◽  
Kidney Proximal Tubules

scholarly journals Structural requirements for protection by small amino acids against hypoxic injury in kidney proximal tubules 1

1990 ◽  
Vol 4 (15) ◽  
pp. 3347-3354 ◽  
Author(s):  
Joel M. Weinberg ◽  
Manjeri A. Venkatachalam ◽  
Ricardo Garzo‐Quintero ◽  
Nancy F. Roeser ◽  
Julie A. Davis
Keyword(s):  
Amino Acids ◽  
Proximal Tubules ◽  
Structural Requirements ◽  
Hypoxic Injury ◽  
Kidney Proximal Tubules

Calcium pump, high-affinity Ca2+-ATPase, and other ATPases in dog antrum smooth muscle plasma membrane

1985 ◽  
Vol 248 (5) ◽  
pp. C449-C456 ◽  
Author(s):  
A. K. Grover ◽  
C. Y. Kwan ◽  
P. J. Oakes
Keyword(s):  
Smooth Muscle ◽  
Plasma Membrane ◽  
Maximal Activity ◽  
Calcium Pump ◽  
Disulfonic Acid ◽  
Calmodulin Antagonists ◽  
High Affinity ◽  
Chelex 100 ◽  
Muscle Plasma Membrane ◽  
Absolute Requirement

The plasma membrane-enriched fraction from dog antrum smooth muscle is enriched in ATP-dependent azide-insensitive Ca2+ uptake (0.3-0.4 microM Ca2+ required for half-maximal activity), a high-affinity Ca2+-ATPase (Km of 0.3-0.8 microM for Ca2+), a low-affinity Ca2+-ATPase (Km for 250-400 microM for Ca2+), and a Mg2+-ATPase. Studies using membranes washed with EDTA and assay media treated with Chelex 100 showed that the high-affinity Ca2+-ATPase did not depend on contaminating Mg2+. Thus, whereas the ATP-dependent Ca2+ uptake had an absolute requirement for Mg2+, the Ca2+-ATPases did not. Studies using gamma-irradiation showed that the protein responsible for the ATP-dependent Ca2+ uptake was inactivated at significantly lower doses of radiation than the three ATPases. The Ca2+ uptake and the high-affinity Ca2+-ATPase also differed in their inhibition by calmodulin antagonists and 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid. Thus it is unlikely that the high-affinity Ca2+-ATPase by itself is responsible for the ATP-dependent Ca2+ uptake.

Ouabain-insensitive, Na-ATPase activity in pure suspensions of rat kidney proximal tubules

FEBS Letters ◽  
1990 ◽  
Vol 269 (1) ◽  
pp. 77-78 ◽  
Author(s):  
Reinaldo Marín ◽  
Daniela C. Gómez ◽  
Gloria A. Rodríguez ◽  
Teresa Proverbio ◽  
Fulgencio Proverbio
Keyword(s):  
Atpase Activity ◽  
Rat Kidney ◽  
Proximal Tubules ◽  
Kidney Proximal Tubules

scholarly journals Immunoelectron Microscopic Localization of the Electrogenic Na/HCO3 Cotransporter in Rat and Ambystoma Kidney

2000 ◽  
Vol 11 (12) ◽  
pp. 2179-2189
Author(s):  
ARVID B. MAUNSBACH ◽  
HENRIK VORUM ◽  
TAE-HWAN KWON ◽  
SØREN NIELSEN ◽  
BRIAN SIMONSEN ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Proximal Tubule ◽  
Rat Kidney ◽  
Proximal Tubules ◽  
Kidney Cortex ◽  
Apical Plasma Membrane ◽  
Rat Kidney Cortex ◽  
C Terminus ◽  
Basolateral Plasma Membrane ◽  
Intracellular Vesicles

Abstract. Immunofluorescence analysis has revealed that electrogenic Na+/HCO3- (NBC1) is expressed in the proximal tubule of rat kidney and in the proximal and distal tubules of the salamander Ambystoma tigrinum kidney. The present study was undertaken to define the detailed subcellular localization of the NBC1 in rat and Ambystoma kidney using high-resolution immunoelectron microscopy. For this purpose, two rabbit polyclonal antibodies raised against amino acids 928 to 1035 and amino acids 1021 to 1035 of the C-terminus of rat kidney (rkNBC1) were developed. The affinity-purified antibodies revealed a strong band of approximately 140 kD in immunoblots of membranes from rat kidney cortex but no signal in membranes isolated from outer and inner medulla. Deglycosylation reduced the apparent molecular weight to approximately 120 kD, corresponding to the predicted molecular weight. A similar but weaker band was also present in membranes isolated from the lateral part of Ambystoma kidney. In rat kidney, immunohistochemistry confirmed the presence of rkNBC1 in convoluted segments of the proximal tubules. In ultrathin cryosections or Lowicryl HM20 sections from rat kidney cortex, distinct immunogold labeling was associated with the basolateral plasma membrane of segments S1 and S2 of proximal tubules, whereas in S3 no labeling was observed. The labeling density was similar at the basal and lateral plasma membrane and was specifically associated with the inner surface of the membrane consistent with the internal position of the C-terminus of the transporter. In contrast, rkNBC1 was absent from the apical plasma membrane and not observed in intracellular vesicles, including those closely associated with basolateral plasma membrane. In Ambystoma kidney, a weak labeling was present in the basolateral membrane of the proximal tubule and stronger labeling was observed in the late distal segment. The results demonstrate that rkNBC1 is expressed only in segment S1 and segment S2 of rat proximal tubule as well as Ambystoma proximal and late distal tubule and that rkNBC1 is present in both basal and lateral plasma membranes and absent in intracellular vesicles of the apical plasma membrane.

Reactivity of lysyl residues on the (calcium-magnesium)-ATPase to 7-amino-4-methylcoumarin-3-acetic acid succinimidyl ester

Biochemistry ◽  
1993 ◽  
Vol 32 (1) ◽  
pp. 356-362 ◽  
Author(s):  
H. I. Stefanova ◽  
A. M. Mata ◽  
J. M. East ◽  
M. G. Gore ◽  
A. G. Lee
Keyword(s):  
Acetic Acid ◽  
Magnesium Atpase ◽  
Calcium Magnesium ◽  
Succinimidyl Ester
Sign in / Sign up

Export Citation Format

Share Document