scholarly journals Cytochemical localization and quantification of plasma membrane Ca2+-ATPase activity in mollusc digestive gland cells

10.4081/1652 ◽  
2009 ◽  
Vol 46 (1) ◽  
pp. 31 ◽  
Author(s):  
G Pons ◽  
V Evangelisti ◽  
F Caprì ◽  
S Mozzone ◽  
A Viarengo
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Digestive Gland ◽  
Cytochemical Localization ◽  
Gland Cells

Biological Activity of Pentachlorophenol on the Digestive Gland Cells of the Freshwater Mussel Unio tumidus

2003 ◽  
Vol 58 (11-12) ◽  
pp. 867-872 ◽  
Author(s):  
Katarzyna Milowska ◽  
Teresa Gabryelak ◽  
Joanna Dudala ◽  
Magdalena Labieniec ◽  
Ekaterina Slobozhanina
Keyword(s):  
Plasma Membrane ◽  
Digestive Gland ◽  
Oxidative Dna Damage ◽  
Freshwater Mussel ◽  
Lipid Peroxides ◽  
Wood Preservative ◽  
Fluorescence Probes ◽  
Chlorinated Phenols ◽  
Gland Cells ◽  
Dna Strand

Abstract Many chlorinated phenols and their derivatives are used extensively as insecticides, fungicides and herbicides by industrial and agricultural users throughout the world. Among these substances, pentachlorophenol (PCP) is a broad-spectrum biocide, which is still used as a wood preservative. In this paper, the digestive gland cells were used to assess the effect of PCP in the range of concentrations 3.75-75 μᴍ (0.01-0.2 ppm) on oxidative DNA damage, fluidity changes and peroxidation activity in the plasma membrane. The toxic property of PCP on DNA strand breakage was studied using the comet assay. The results showed that pentachlorophenol in the range of 37.5-75 μᴍ contributed to these lesions. To demonstrate the changes in the fluidity of plasma membrane we used the spectrofluorimetric method using two fluorescence probes: 1-[4-(trimethylamino)phenyl]-6-phenyl-1,3,5-hexatriene (TMAD DPH) and 12-(9-anthroyloxy) stearic acid (12-AS). It was shown that PC did not influence the surface of plasma membrane but contributed to the increase in the fluidity of the internal region of the lipid bilayer in the range of concentrations 18.75-75 μᴍ (0.05-0.2 ppm).We also examined the effect of PCP on the lipid peroxidation. To imply its peroxidation properties the spectrophotometry method was used to measure the level of malondialdehyde (MDA), one of the endpoints of the peroxidation of polyunsaturated fatty acids. The obtained results showed that PCP in the used doses did not initiate the formation of lipid peroxides. Thus, our investigation indicates that PCP can behave as a prooxidant agent but its action depends on the used doses and parameters chosen for the research.

scholarly journals Cytochemical localization of ecto-ATPases in rat neurohypophysis.

1996 ◽  
Vol 44 (2) ◽  
pp. 103-111 ◽  
Author(s):  
S Thirion ◽  
J D Troadec ◽  
G Nicaise
Keyword(s):  
Electron Microscopy ◽  
Plasma Membrane ◽  
Atpase Activity ◽  
Outer Surface ◽  
Nerve Endings ◽  
Glutaraldehyde Fixation ◽  
Cytochemical Localization ◽  
Cytochemical Method ◽  
Ca Pump ◽  
Dependent Atpase

We studied the distribution of Ca(2+)- or Mg(2+)-dependent ATPase activity in rat neurohypophysis using the lead cytochemical method of Ando et al. In electron microscopy, precipitates were found lining the outer surface of the plasma membrane surrounding nerve endings and pituicytes. These precipitates were believed to represent the activity of ecto-ATPases (as opposed to Ca pump ATPases) for the following reasons: there was equal activation by Ca2+ in the absence of Mg2+ or Mg2+ in the absence of Ca2+; the effects of the two ions were not additive; there was activation by ATP or GTP; and there was resistance to glutaraldehyde fixation, to high (10 mM) Ca2+ concentrations, and to various inhibitors such as NEM, vanadate, oligomycin, quercetin, p-chloromercuribenzoate, ouabain, and levamisole. Cytosolic activity observed in certain nerve endings in the same conditions of incubation but more sensitive to NEM is also described and discussed.

scholarly journals Cytochemical localization of ouabain-sensitive (K+)-dependent p-nitrophenyl phosphatase (transport ATPase) in human blood platelets.

1980 ◽  
Vol 28 (11) ◽  
pp. 1183-1188 ◽  
Author(s):  
L S Cutler ◽  
M B Feinstein ◽  
C P Christian
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Human Blood ◽  
Human Platelet ◽  
Blood Platelets ◽  
Cytochemical Localization ◽  
Transport Atpase ◽  
Tubular System ◽  
Membrane Compartments ◽  
Human Blood Platelets

The ultrastructural cytochemical localization of a potassium-dependent oubain-sensitive nitrophenyl phosphatase (transport ATPase) activity in human blood platelets is described. This potassium-dependent nitrophenyl phosphatase activity was not affected by 5 mM levamisole, indicating that the reaction product identified was not due to nonspecific alkaline phosphatase activity. The K+-dependent nitrophenyl phosphatase was strictly localized to the platelet plasma membrane, while the open canalicular system and dense tubular system were devoid of reaction product. In contrast, (Ca2+,Mg2+)-activated ATPase activity was predominantly localized in the open canalicular system and dense tubular system with very little cytochemical activity expressed at the plasma membrane. These data demonstrate a relative segregation of these enzymes into unique membrane compartments of the human platelet. Such data may be useful with regard to identification of purified membrane fractions from platelets and may be significant with regard to the understanding of the function(s) of the different membrane compartments of the human platelet.

Cytochemical localization of plasma membrane ATPase activity in plant cells

PROTOPLASMA ◽  
1991 ◽  
Vol 165 (1-3) ◽  
pp. 27-36 ◽  
Author(s):  
E. Chauhan ◽  
D. S. Cowan ◽  
J. L. Hall
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Plant Cells ◽  
Plasma Membrane Atpase ◽  
Cytochemical Localization ◽  
Membrane Atpase

scholarly journals Cytochemical Localization of ATPase Activity in Oat Roots Localizes a Plasma Membrane-Associated Soluble Phosphatase, Not the Proton Pump

1988 ◽  
Vol 86 (3) ◽  
pp. 841-847 ◽  
Author(s):  
Donald B. Katz ◽  
Michael R. Sussman ◽  
Robert J. Mierzwa ◽  
Ray F. Evert
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Proton Pump ◽  
Cytochemical Localization

Localization of Adenosine Triphosphatase Activity in the Phleom of Nicotiana Tabacum

1972 ◽  
Vol 30 ◽  
pp. 230-231
Author(s):  
James Cronshaw ◽  
Jamison E. Gilder
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Higher Plants ◽  
High Surface ◽  
Root Tip ◽  
Animal Cells ◽  
Physiological Processes ◽  
Tip Cells ◽  
Atpase Localization

Adenosine triphosphatase (ATPase) activity has been shown to be associated with numerous physiological processes in both plants and animal cells. Biochemical studies have shown that in higher plants ATPase activity is high in cell wall preparations and is associated with the plasma membrane, nuclei, mitochondria, chloroplasts and lysosomes. However, there have been only a few ATPase localization studies of higher plants at the electron microscope level. Poux (1967) demonstrated ATPase activity associated with most cellular organelles in the protoderm cells of Cucumis roots. Hall (1971) has demonstrated ATPase activity in root tip cells of Zea mays. There was high surface activity largely associated with the plasma membrane and plasmodesmata. ATPase activity was also demonstrated in mitochondria, dictyosomes, endoplasmic reticulum and plastids.

scholarly journals Potassium depletion increases proton pump (H+-ATPase) activity in intercalated cells of cortical collecting duct

2000 ◽  
Vol 279 (1) ◽  
pp. F195-F202 ◽  
Author(s):  
Randi B. Silver ◽  
Sylvie Breton ◽  
Dennis Brown
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Collecting Duct ◽  
Proton Pumps ◽  
Intercalated Cells ◽  
Cortical Collecting Duct ◽  
Collecting Ducts ◽  
Acid Load ◽  
Collecting Tubules ◽  
Atpase Staining

Intercalated cells (ICs) from kidney collecting ducts contain proton-transporting ATPases (H+-ATPases) whose plasma membrane expression is regulated under a variety of conditions. It has been shown that net proton secretion occurs in the distal nephron from chronically K+-depleted rats and that upregulation of tubular H+- ATPase is involved in this process. However, regulation of this protein at the level of individual cells has not so far been examined. In the present study, H+-ATPase activity was determined in individually identified ICs from control and chronically K+-depleted rats (9–14 days on a low-K+ diet) by monitoring K+- and Na+-independent H+ extrusion rates after an acute acid load. Split-open rat cortical collecting tubules were loaded with the intracellular pH (pHi) indicator 2′,7′-bis(2-carboxyethyl)-5(6)-carboxyfluorescein, and pHiwas determined by using ratiometric fluorescence imaging. The rate of pHi recovery in ICs in response to an acute acid load, a measure of plasma membrane H+-ATPase activity, was increased after K+ depletion to almost three times that of controls. Furthermore, the lag time before the start of pHirecovery after the cells were maximally acidified fell from 93.5 ± 13.7 s in controls to 24.5 ± 2.1 s in K+-depleted rats. In all ICs tested, Na+- and K+-independent pHi recovery was abolished in the presence of bafilomycin (100 nM), an inhibitor of the H+-ATPase. Analysis of the cell-to-cell variability in the rate of pHi recovery reveals a change in the distribution of membrane-bound proton pumps in the IC population of cortical collecting duct from K+-depleted rats. Immunocytochemical analysis of collecting ducts from control and K+-depleted rats showed that K+-depletion increased the number of ICs with tight apical H+ATPase staining and decreased the number of cells with diffuse or basolateral H+-ATPase staining. Taken together, these data indicate that chronic K+ depletion induces a marked increase in plasma membrane H+ATPase activity in individual ICs.

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