UTERINE MITOSIS, ALKALINE PHOSPHATASE AND ADENOSINE TRIPHOSPHATASE DURING DEVELOPMENT AND REGRESSION OF DECIDUOMATA IN PSEUDOPREGNANT MICE

1969 ◽  
Vol 44 (1) ◽  
pp. 91-NP ◽  
Author(s):  
KATHLEEN HALL
Keyword(s):  
Alkaline Phosphatase ◽  
Atpase Activity ◽  
Vascular Endothelium ◽  
Stromal Cells ◽  
Adenosine Triphosphatase ◽  
Glandular Epithelium ◽  
Histochemical Localization ◽  
Vessel Walls ◽  
The Right

SUMMARY Incidence and patterns of mitoses and histochemical localization of alkaline phosphatase (APase) and adenosine triphosphatase (ATPase) were studied from days 5 to 20 in pseudopregnant mice in which deciduomata had been induced in the left uterine horns by intrauterine injection of oil on day 4, the right horns serving as controls. In stromal cells, mitoses were very numerous throughout the endometrium of the left (but not the right) horn on days 5 and 6, in the basal, non-decidualized stroma until day 8 or day 9, and were not seen in stromal cells of either horn thereafter. In glandular epithelium, mitoses were absent from days 5 to 10, and numerous from day 11 or 12 until at least day 17 in both horns. Mitoses were present in capillaries within developing deciduomata on days 5 and 6, then seldom seen until day 12 and during the next 3 days were numerous in endothelial and pericapillary cells in the mesometrial quadrant of the left horn and around glands in both horns. The deciduoma cells reacted strongly with AP and ATP substrates from days 5 to 10, after which the intensity of the reaction weakened and had usually disappeared by day 13. ATPase activity disappeared from vascular endothelium within the deciduoma a few hours after APase had appeared within the deciduoma cells on day 5. It reappeared in the vessel walls on day 9 and thereafter was usually present until the deciduoma was shed. In the basal, non-decidualized stroma, APase was absent until about day 10, then appeared in the stroma cells nearest to the myometrium, extending gradually into the densely packed cells nearest to the regressing deciduoma. The possible role of this enzyme in reparative growth of the endometrium after regression of the deciduoma is discussed.

Histochemical studies on Raillietina (Raillietina) johri (Cestoda: Davaineidae). I. Nonspecific and specific phosphatases

1979 ◽  
Vol 53 (1) ◽  
pp. 45-49 ◽  
Author(s):  
T. K. Roy
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Atpase Activity ◽  
Functional Significance ◽  
Adenosine Triphosphatase ◽  
Vas Deferens ◽  
Gland Cells ◽  
Vitelline Gland ◽  
Receptaculum Seminis ◽  
Almost All

ABSTRACTCertain phosphatases have been localized by histochemical techniques in various tissues of a pigeon cestode, Raillietina (Raillietina) johri. Acid phosphatase (AcPase), alkaline phosphatase (AlPase) and adenosine triphosphatase (ATPase) were present in almost all structures: tegument; subtegumental muscles; subtegumental cells; excretory canal; tsetes; sperm ductules; vas deferens; cirrus sac; cirrus; ovary; receptaculum seminis; vagina; vitelline gland cells; oocytes; uterus; embryonated eggs. AlPase was absent in parenchyma, spermatocytes, spermatids and spermatozoa. AlPase activity was more intense in the tegument of mature gravid proglottides. AcPase and ATPase were visualized in various stages of spermatogenesis of the parasite. ATPase activity was also observed in chromosomes. 5'-nucleotidase (AMPase) activity was restricted to embryonated eggs only. Functional significance of these phosphatases is discussed.

scholarly journals Ouabain binding to phospholipid-dependent adenosine triphosphatase

1978 ◽  
Vol 169 (2) ◽  
pp. 313-320 ◽  
Author(s):  
S L Goodman ◽  
K P Wheeler
Keyword(s):  
Atpase Activity ◽  
Protein Complex ◽  
Adenosine Triphosphatase ◽  
Rabbit Kidney ◽  
Ouabain Binding ◽  
Equilibrium Conditions ◽  
Enzyme Preparations

The role of phospholipid in the binding of ouabain to the (Na+ + K+)-dependent adenosine triphosphatase was studied. Enzyme preparations obtained from rabbit kidney were treated with Lubrol WX to remove the phospholipid component essential for ATPase activity. Reconstituted enzyme samples were prepared by the addition of phosphatidylserine and sedimentation of an enzymically active lipid-protein complex. The binding of ouabain to both kinds of preparations was measured under equilibrium conditions with the use of 3H-labelled ouabain and initial ouabain concentrations in the range 0.01-1 micrometer. The main findings were: (i) (Mg2+ + Pi) promoted binding of significant quantities of ouabain only to the reconstituted enzyme; (ii) the absence of added Na+, (Mg2+ + ATP) similarly promoted binding only to the reconstituted samples; (iii) the addition of Na+ in the presence of (Mg2+ + ATP) increased the amount of ouabain bound to the reconstituted enzyme when the ouabain concentration was below about 0.1 micrometer, but it had no effect when the ouabain concentration was about 1 micrometer; (iv) (Mg2+ + ATP) induced ouabain binding to the depleted enzyme only when Na+ was also added; (v) the amount of ouabain bound to both depleted and reconstituted enzymes was the same in the presence of (Mg2+ + ATP + Na+); (vi) the reconstituted enzyme appeared to have a greater affinity for Na+ than did the depleted enzyme.

scholarly journals LEAD ION AND PHOSPHATASE HISTOCHEMISTRY II. EFFECT OF ADENOSINE TRIPHOSPHATE HYDROLYSIS BY LEAD ION ON THE HISTOCHEMICAL LOCALIZATION OF ADENOSINE TRIPHOSPHATASE ACTIVITY

1966 ◽  
Vol 14 (10) ◽  
pp. 702-710 ◽  
Author(s):  
HAROLD L. MOSES ◽  
ALAN S. ROSENTHAL ◽  
DAVID L. BEAVER ◽  
SHIRLEY S. SCHUFFMAN
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Lead Nitrate ◽  
Histochemical Localization ◽  
Lead Ion ◽  
Membrane Localization ◽  
Fixed Tissue ◽  
Plasma Membrane Localization ◽  
Hydrolysis Of

The lead method of Wachstein and Meisel for the histochemical localization of adenosine triphosphatase (ATPase) involves the incubation of sections of fixed tissue in reaction mixtures containing ATP, lead nitrate, magnesium sulfate and a Tris-maleate buffer, pH 7.2. Both fixation and the presence of lead ion were shown to inhibit tissue ATPase activity markedly and to inactivate the sodium- plus potassium-dependent membrane ATPase. In addition, recent studies have demonstrated that lead ion, in the concentration used in the Wachstein-Meisel system, will catalyze the hydrolysis of ATP. Studies on the effect of this nonenzymatic reaction on the histochemical localization of ATPases demonstrated that plasma membrane localization occurred only with lead and ATP concentrations which gave significant nonenzymatic hydrolysis of ATP by lead. In addition, nuclear and mitochondrial localization without accompanying plasma membrane localization could be obtained in formalin-fixed tissue with decreased concentrations of lead or with increased concentrations of ATP in the reaction mixture. The amount of lead-catalyzed hydrolysis was in the same order of magnitude as fixed tissue ATPase activity and could quantitatively account for the amount of phosphate needed to give recognizable localization of lead salt deposits in sections of fixed tissue.

Histochemical localization of phosphomonoesterases in Avhellina lahorea Woodland, 1927 (Cestoda: Anoplocephalida)

1984 ◽  
Vol 58 (2) ◽  
pp. 169-173 ◽  
Author(s):  
Rashid Farooq ◽  
H.U. Farooqi
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Adenosine Triphosphatase ◽  
Intestinal Parasite ◽  
Histochemical Localization ◽  
Sheep And Goats ◽  
Almost All ◽  
Phosphatase Alkaline

AbstractNon-specific and specific phosphatases have been histochemically localized in the tissues of Avitellina lahorea, an intestinal parasite of sheep and goats. Large quantities of acid phosphatase, alkaline phosphatase and adenosine triphosphatase were observed in almost all organs except the parenchyma where there were moderate amounts of acid phosphatase and no alkaline phosphatase; the reproductive ducts contained moderate amounts of alkaline phosphatase. 5-nucleotidase was observed only in the uterus, egg pouches and eggs and glucose-6-phosphatase activity was restricted to the tegument. The probable functions of these moieties at different sites are discussed.

Role of Na+/K+-stimulated adenosine triphosphatase in the action of dopaminergic-D2 receptors of the liver in rats

1987 ◽  
Vol 7 (11) ◽  
pp. 839-842 ◽  
Author(s):  
Abdulrahim Abu-Jayyab ◽  
Ahmed Mahgoub
Keyword(s):  
Atpase Activity ◽  
Receptor Antagonist ◽  
Dopamine Receptor ◽  
Inhibitory Activity ◽  
Receptor Agonist ◽  
Adenosine Triphosphatase ◽  
D2 Receptors ◽  
Dopamine Receptor Agonist ◽  
Dopamine Receptor Antagonist

The dopamine receptor agonist, bromocriptine, in a dose of 10 mg/kg i.p. for 14 days, in rats caused a significant increase in liver Na+/K+-ATPase activity, whereas sulpiride, a dopamine receptor antagonist, in a dose of 10 mg/kg, i.p. for 14 days, in rats, caused a significant decrease in liver Na+/K+-ATPase activity. Injection of bromocriptine and sulpiride simultaneously in a group of rats, under the same conditions and using the same doses caused a complete block of both stimulatory activity of bromocriptine and inhibitory activity of sulpiride on liver Na+/K+-ATPase activity. It is suggested that Na+/K+-ATPase may have a role in the action of dopaminergic-D2 receptors.

scholarly journals Multiple Functions of MSCA-1/TNAP in Adult Mesenchymal Progenitor/Stromal Cells

2016 ◽  
Vol 2016 ◽  
pp. 1-8 ◽  
Author(s):  
David Estève ◽  
Jean Galitzky ◽  
Anne Bouloumié ◽  
Caroline Fonta ◽  
René Buchet ◽  
...  
Keyword(s):  
Stem Cells ◽  
Alkaline Phosphatase ◽  
Mesenchymal Stem Cells ◽  
Stromal Cells ◽  
Proof Of Concept ◽  
Wide Range ◽  
Semantic Shift ◽  
Definition Of ◽  
Different Tissues

Our knowledge about mesenchymal stem cells has considerably grown in the last years. Since the proof of concept of the existence of such cells in the 70s by Friedenstein et al., a growing mass of reports were conducted for a better definition of these cells and for the reevaluation from the term “mesenchymal stem cells” to the term “mesenchymal stromal cells (MSCs).” Being more than a semantic shift, concepts behind this new terminology reveal the complexity and the heterogeneity of the cells grouped in MSC family especially as these cells are present in nearly all adult tissues. Recently, mesenchymal stromal cell antigen-1 (MSCA-1)/tissue nonspecific alkaline phosphatase (TNAP) was described as a new cell surface marker of MSCs from different tissues. The alkaline phosphatase activity of this protein could be involved in wide range of MSC features described below from cell differentiation to immunomodulatory properties, as well as occurrence of pathologies. The present review aims to decipher and summarize the role of TNAP in progenitor cells from different tissues focusing preferentially on brain, bone marrow, and adipose tissue.

scholarly journals Role of the subunits of the energy-transducing adenosine triphosphatase from Micrococcus lysodeikticus membranes studied by proteolytic digestion and immunological approaches

1980 ◽  
Vol 186 (3) ◽  
pp. 713-723 ◽  
Author(s):  
F Mollinedo ◽  
V Larraga ◽  
F J Coll ◽  
E Muñoz
Keyword(s):  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Specific Activity ◽  
Relative Proportion ◽  
Inhibitory Effect ◽  
Beta Subunit ◽  
Gamma Subunit ◽  
Micrococcus Lysodeikticus ◽  
Alpha Beta

An energy-transducing adenosine triphosphatase (ATPase, EC 3.6.1.3) that contains an extra polypeptide (delta) as well as three intrinsic subunits (alpha, beta, gamma) was purified from Micrococcus lysodeikticus membranes. The apparent subunit stoichiometry of this soluble ATPase complex is alpha 3 beta 3 gamma delta. The functional role of the subunits was studied by correlating subunit sensitivity to trypsin and effect of antibodies raised against holo-ATPase and its alpha, beta and gamma subunits with changes in ATPase activity and ATPase rebinding to membranes. A form of the ATPase with the subunit proportions 1.67(alpha):3.00(beta:0.17(gamma) was isolated after trypsin treatment of purified ATPase. This form has more than twice the specific activity of native enzyme. Other forms with less relative proportion of alpha subunits and absence of gamma subunit are not active. Of the antisera to subunits, only anti-(beta-subunit) serum shows a slight inhibitory effect on ATPase activity, but its combination with either anti-(alpha-subunit) or anti-(gamma-subunit) serum increases the effect. The results suggest that beta subunit is required for full ATPase activity, although a minor proportion of alpha and perhaps gamma subunit(s) is also required, probably to impart an active conformation to the protein. The additional polypeptide not hitherto described in Micrococcus lysodeikticus ATPase had a molecular weight of 20 000 and was found to be involved in ATPase binding to membranes. This 20 000-dalton component can be equated with the delta subunit of other energy-transducing ATPases and its association with the (alpha, beta, gamma) M. lysodeikticus ATPase complex appears to be dependent on bivalent cations. The present results do not preclude the possibility that the gamma subunit also plays a role in ATPase binding, in which, however, the major subunits do not seem to play a role.

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.

Sign in / Sign up

Export Citation Format

Share Document