Cell membrane calcium ATPase activity in hypertension

1987 ◽  
Vol 15 (5) ◽  
pp. 854-855
Author(s):  
ABIMBOLA ADEOYA ◽  
ROBERT I. NORMAN ◽  
ROBERT F. BING
Keyword(s):  
Cell Membrane ◽  
Atpase Activity ◽  
Calcium Atpase

Calcium ATPase and intestinal calcium transport in uremic rats

1980 ◽  
Vol 238 (5) ◽  
pp. G424-G428
Author(s):  
H. Schiffl ◽  
U. Binswanger
Keyword(s):  
Enzyme Activity ◽  
Atpase Activity ◽  
Calcium Transport ◽  
Calcium Atpase ◽  
Intestinal Calcium Transport ◽  
Identical Response ◽  
Close Relationship ◽  
Intact Rats

Calcium ATPase, an enzyme involved in intestinal calcium transport, was measured in homogenates of duodenal mucosal scrapings of normal and uremic rats. The effects of calcium deprivation and treatment with 1 alpha,25-dihydroxycholecalciferol [1,25-(OH)2D3] were investigated as well. Uremia decreased the enzyme activity and impaired the rise after calcium deprivation as observed in intact rats. The 1,25-(OH)2D3 treatment increased the enzyme activity in uremic animals and resulted in an identical response to calcium deprivation as observed in intact rats; parathyroidectomy abolished this effect. A striking correlation between everted duodenal gut sac calcium transport and calcium ATPase activity could be demonstrated for all groups of rats studied. It is concluded that the calcium ATPase activity is linked to the production of 1,25-(OH)2D3 as well as to an additional factor, probably parathyroid hormone. The close relationship between enzyme activity and in vitro calcium transport, even during constant physiological supplementation with 1,25-(OH)2D3, suggests an autonomous role of the calcium ATPase activity for mediation of calcium transport in the duodenum in addition to the well-known mechanisms related to vitamin D and its metabolites.

scholarly journals Favism: disordered erythrocyte calcium homeostasis

Blood ◽  
1985 ◽  
Vol 66 (2) ◽  
pp. 294-297 ◽  
Author(s):  
A De Flora ◽  
U Benatti ◽  
L Guida ◽  
G Forteleoni ◽  
T Meloni
Keyword(s):  
Atpase Activity ◽  
Intracellular Calcium ◽  
Calcium Homeostasis ◽  
Calcium Content ◽  
Calcium Atpase ◽  
Potassium Content ◽  
Hemolytic Crisis ◽  
The Mean ◽  
Fava Beans

Abstract The biochemical events that take place during acute hemolysis of G6PD- deficient subjects in favism are far from being elucidated. Evidence is here reported for a constantly and heavily disordered calcium homeostasis in the erythrocytes from seven favic patients. The abnormality, ie, a significantly impaired calcium ATPase activity and a parallel marked increase of intracellular calcium levels, was characteristic of the acute hemolytic crisis although unrelated to the attendant reticulocytosis. Concomitantly, a remarkable decrease of intracellular potassium was also observed. The mean +/- SD Ca2+-ATPase activity in the favic patients was 20.8 +/- 7.8 mumol Pi/g Hb/h compared with 37.2 +/- 8.5 in the matched controls represented by 12 healthy G6PD-deficient subjects (P less than .001). The mean +/- SD intraerythrocytic calcium content was 288 +/- 158 mumol/L of erythrocytes in the favic patients as compared with 22.0 +/- 8.2 in the G6PD-deficient controls (P less than .001). The intraerythrocytic potassium content was 76.6 +/- 19.3 mmol/L of erythrocytes in the favic patients and 106.6 +/- 8.2 in the G6PD-deficient controls (P less than .001). In vitro incubation of normal and G6PD-deficient erythrocytes with divicine, a pyrimidine aglycone present in fava beans and strongly implicated in the pathogenesis of favism, reproduces most of these events, including drop of calcium ATPase, increased intracellular calcium, and leakage of erythrocyte potassium.

scholarly journals Calcium-ATPase Activity in Cystic Fibrosis Erythrocyte Membranes: Decreased Activity in Patients with Pancreatic Insufficiency

1984 ◽  
Vol 18 (9) ◽  
pp. 890-895 ◽  
Author(s):  
Dorr G Dearborn ◽  
Robert J Wityk ◽  
Lynelle R Johnson ◽  
Louis Poncz ◽  
Robert C Stern
Keyword(s):  
Cystic Fibrosis ◽  
Atpase Activity ◽  
Pancreatic Insufficiency ◽  
Calcium Atpase ◽  
Erythrocyte Membranes

scholarly journals Intracellular Na+ Controls Cell Surface Expression of Na,K-ATPase via a cAMP-independent PKA Pathway in Mammalian Kidney Collecting Duct Cells

2003 ◽  
Vol 14 (7) ◽  
pp. 2677-2688 ◽  
Author(s):  
Manlio Vinciguerra ◽  
Georges Deschênes ◽  
Udo Hasler ◽  
David Mordasini ◽  
Martine Rousselot ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Cell Surface ◽  
Atpase Activity ◽  
Collecting Duct ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Cortical Collecting Duct ◽  
Mammalian Kidney ◽  
Duct Cells ◽  
Collecting Duct Cells

In the mammalian kidney the fine control of Na+ reabsorption takes place in collecting duct principal cells where basolateral Na,K-ATPase provides the driving force for vectorial Na+ transport. In the cortical collecting duct (CCD), a rise in intracellular Na+ concentration ([Na+]i) was shown to increase Na,K-ATPase activity and the number of ouabain binding sites, but the mechanism responsible for this event has not yet been elucidated. A rise in [Na+]i caused by incubation with the Na+ ionophore nystatin, increased Na,K-ATPase activity and cell surface expression to the same extent in isolated rat CCD. In cultured mouse mpkCCDcl4 collecting duct cells, increasing [Na+]i either by cell membrane permeabilization with amphotericin B or nystatin, or by incubating cells in a K+-free medium, also increased Na,K-ATPase cell surface expression. The [Na+]i-dependent increase in Na,K-ATPase cell-surface expression was prevented by PKA inhibitors H89 and PKI. Moreover, the effects of [Na+]i and cAMP were not additive. However, [Na+]i-dependent activation of PKA was not associated with an increase in cellular cAMP but was prevented by inhibiting the proteasome. These findings suggest that Na,K-ATPase may be recruited to the cell membrane following an increase in [Na+]i through cAMP-independent PKA activation that is itself dependent on proteasomal activity.

Abnormal response to calmodulin in vitro of dystrophic chicken muscle membrane calcium-ATPase activity

Biochemistry ◽  
1988 ◽  
Vol 27 (19) ◽  
pp. 7519-7524 ◽  
Author(s):  
Jose Galindo ◽  
Michael S. Hudecki ◽  
Faith B. Davis ◽  
Paul J. Davis ◽  
Harshad R. Thacore ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Calcium Atpase ◽  
Muscle Membrane ◽  
Chicken Muscle ◽  
Abnormal Response ◽  
Dystrophic Chicken

Stimulatory effect of vanadate on (Na+ + K+)-ATPase activity and on 3H-ouabain-binding in a cat heart cell membrane preparation

Nature ◽  
1979 ◽  
Vol 278 (5703) ◽  
pp. 459-461 ◽  
Author(s):  
ERLAND ERDMANN ◽  
WOLFGANG KRAWIETZ ◽  
GUNTHER PHILIPP ◽  
INGELORE HACKBARTH ◽  
WILHELM SCHMITZ ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Atpase Activity ◽  
Membrane Preparation ◽  
Heart Cell ◽  
Ouabain Binding ◽  
Heart Cell Membrane ◽  
Cell Membrane Preparation ◽  
Cat Heart
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