Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Fibrocytes in the lateral wall and limbus of the gerbil cochlea evidenced a capacity for ion transport activity by immunostaining for transport mediating enzymes including Na,K-ATPase, carbonic anhydrase (CA) and creatine kinase (CK). Fibrocytes of the spiral ligament unlike those in the suprastrial region and limbus decreased in abundance from base to apex. Spiral ligament fibrocytes at a given position along the cochlea varied in content of transport related enzymes, and on the basis of immunostaining, location and orientation, were classified into four types. Type I fibrocytes under the stria vascularis stained for CA isozymes II and III and CK isozyme BB. Type II fibrocytes under the outer sulcus and spiral prominence epithelium were found to contain only Na,K-ATPase. Type III fibrocytes lying adjacent to bone in the inferior region of the spiral ligament contained CA II and III and CK isozymes BB and MM. Type IV fibrocytes located more superficially in the inferior part of the spiral ligament stained variably for all the enzymes. Superficial fibrocytes in the suprastrial area disclosed Na,K-ATPase whereas the underlying fibrocytes stained for CA and CK. Limbal fibrocytes reacted with antisera to all the enzymes except CA III. Most fibrocytes in stromal plates beneath the vestibular system's neurosensory epithelium contained Na,K-ATPase and CA II but not CA III. These findings point to cooperativity in fluid and ion transport between epithelial cells and neighboring fibrocytes and demonstrate functional diversity of fibrocytes of the inner ear providing a basis for classifying those in the spiral ligament.
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PMID:Differentiation of inner ear fibrocytes according to their ion transport related activity. 166 6

The distribution of two ion transport enzymes in the vestibular system was investigated immunocytochemically. Immunostaining demonstrated abundant Na+,K(+)-ATPase in the basolateral plasmalemma of all dark cells and of cuboidal (transitional) cells bordering maculae and planum semilunatum cells bordering cristae. Na+,K(+)-ATPase was also present in nerve terminals impinging on vestibular hair cells and around nerve fibers and ganglion cells. Na+,K(+)-ATPase containing cells with fine intertwining processes were found within the perilymphatic stroma beneath maculae and cristae. These cells and interspersed nerves form a distinct, highly cellular plate that lies under neurosensory epithelium selectively. The catalytic alpha subunit of Na+,K(+)-ATPase in vestibular epithelia differs antigenically from the alpha subunit in nerves and from the alpha subunit in salivary gland and renal epithelium. Carbonic anhydrase (CA) isozyme II was localized in the apex of all supporting cells in neurosensory epithelia. In contrast, CA II immunostaining varied in vestibular dark cells showing heterogeneity in ion transport activity among these cells. Immunostaining evidenced CA II also in perilymphatic stromal cells which were presumably fibroblastic in nature and which correspond in location with the Na+,K(+)-ATPase positive cells under the vestibular neurosensory epithelium.
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PMID:Immunolocalization of Na+,K(+)-ATPase and carbonic anhydrase in the gerbil's vestibular system. 169 Jan 98

Stimulation of gastric parietal cells by carbachol induces coordinate expression of the genes for two enzymes involved in the process of acid secretion, H(+)-K(+)-ATPase and carbonic anhydrase II (CA II). The basis of this coordinate expression was examined in experiments using parietal cells that had been pretreated with omeprazole. We observed a twofold increase in the steady-state mRNA levels of both H(+)-K(+)-ATPase and CA II after cells were treated with the inhibitor. The induction of CA II mRNA by carbachol followed the same kinetics in omeprazole-pretreated cells as in those that were not pretreated, suggesting that the induction of CA II gene expression by carbachol was not dependent on activation of the gastric H(+)-K(+)-ATPase. In addition, carbachol stimulation of omeprazole-pretreated cells resulted in an induction of one or more larger mRNA species that hybridized with the H(+)-K(+)-ATPase probe. The observation that carbachol-induced increases in steady-state levels of beta-actin mRNA in parietal cells could be inhibited by omeprazole pretreatment suggests a possible linkage between increased beta-actin gene expression and the process of acid secretion.
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PMID:Effect of omeprazole on gene expression in canine gastric parietal cells. 184 8

H(+)-K(+)-ATPase and carbonic anhydrase II (CA II) are two enzymes that are involved in the production and secretion of the hydrogen ion by the gastric parietal cell and maintenance of intracellular pH therein. The present studies were undertaken to examine whether H(+)-K(+)-ATPase and CA II expression change in the rat fundus in association with the development of acid secretory capacity. Changes in enzyme mRNA content in the gastric fundus of developing rat pups 1-6 wk of age were evaluated using dot blots and ribonuclease protection assays. In additional studies the localization of H(+)-K(+)-ATPase and carbonic anhydrase II mRNA was examined by in situ hybridization in Formalin-fixed gastric tissues from rats 1, 3, 6, and 8 wk of age. We observed that H(+)-K(+)-ATPase mRNA content increased with age in the developing rat fundus while CA II mRNA exhibited a reciprocal decrease. These changes in enzyme mRNA were accompanied by concomitant changes in the regional distribution of the cells expressing the genes for the two enzymes. Although the changes in H(+)-K(+)-ATPase mRNA paralleled the development of acid secretory capacity, CA II mRNA levels might be regulated by the requirement for maintenance of intracellular pH during periods of cellular proliferation and by exposure of the gastric surface epithelium to the highly acidic luminal environment of the stomach.
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PMID:H(+)-K(+)-ATPase and carbonic anhydrase II gene expression in the developing rat fundus. 216 89

Immunocytochemical detection of carbonic anhydrase (CA II), (Na+-K+)-ATPase and the anion channel (band 3) glycoprotein was used to study structural and functional heterogeneity of cells lining the collecting ducts, especially of intercalated cells, in the rat kidney. High content of CA II was found in intercalated cells as determined by morphology, although a weak diffuse cytoplasmic staining of this enzyme could be observed also in a subpopulation of principal cells. (Na+-K+)-ATPase could be detected exclusively in principal cells, whereas basolateral band 3 immunoreactivity was seen only in a subpopulation of intercalated cells. Double immunostaining experiments revealed that the weak cytoplasmic type of CA II and basolateral (Na+-K+)-ATPase immunoreactivities were colocalized in 20 to 30% (depending on the segment studied) of the collecting duct epithelial cells but, in contrast, cells rich in CA II or those with basal band 3 immunoreactivity seldom contained (Na+-K+)-ATPase. Instead, band 3 glycoprotein and the abundant CA II were colocalized in 20 to 35% of the cells in various segments of collecting ducts, whereas, band 3 and weak cytoplasmic CA II were seldom seen in the same cells. The results show that the current approach is useful for identifying and characterizing two distinct subpopulations of intercalated cells, both rich in CA II but differing in respect to the presence or absence of band 3 glycoprotein. On the basis of physiologic and biochemical data of the functions of these transport proteins we propose that the subpopulations of intercalated cells thus identified represent the acidifying and alkalinizing subtypes, respectively.
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PMID:Immunocytochemical characterization of carbonic anhydrase-rich cells in the rat kidney collecting duct. 244 Nov 37

With immunocytochemistry, we have determined distribution of sodium, potassium-adenosine triphosphatase (Na+, K+-ATPase) and of three isoenzymes of carbonic anhydrase (CA) and have shown absence of the chloride channel, Band 3 protein, in the genital tract of female rodents. Staining for Na+,K+-ATPase was strongest in the ampullary oviduct and uterine glands in the mouse. In the mouse and rat ovary, immunostaining evidenced CA I, II, and III in theca interna cells where the enzyme could affect the pH of follicular fluid. The zona pellucida of the ovary and cytoplasmic foci in follicular granulosa cells stained for content of only CA I in mouse ovary, suggesting synthesis of a zona pellucida component by granulosa cells. CA II in mouse oviductal epithelium increased from the negative infundibulum to the variably positive ampulla and isthmus to the uniformly positive interstitial segment. The content of CA III varied inversely to that of CA II. The prevalence of CA II-positive cells apparently corresponded with that of nonciliated cells, whereas abundance of CA III-positive cells concurred with that of ciliated cells in regions of the mouse oviduct. The rat oviduct lacked CA II but, like that of the mouse, showed CA III in the proximal region. The staining for CA II in surface epithelium exceeded the reactivity in glandular epithelium in the mouse uterus, except during estrus. In contrast, rat uterus evidenced CA II in glandular but not surface epithelium. These results testify to possible significance of various ion transport mechanisms for biologic activities of diverse cells in the female genital tract.
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PMID:Immunocytochemistry of ion transport mediators in the genital tract of female rodents. 245 38

Immunostaining for Na+, K+-ATPase, carbonic anhydrase (CA) II, and band 3 anion channel glycoprotein was compared in developing and mature human kidneys and in Wilms' tumors. In fetal kidneys, ATPase first appeared in proximal and distal tubules. At birth an adult pattern was present with abundant enzyme in all segments of the distal tubule and lesser amounts in proximal and collecting tubules. CA II was detected in fetal kidneys first in proximal and then in distal tubules and eventually, as in the adult, throughout the nephron. Band 3 glycoprotein was not detected in fetal kidneys and only weak staining was present in the basolateral plasmalemma of intercalated cells in newborn and infant kidneys. The number of cells reactive for band 3 and the intensity of staining in a given cell increased to near adult levels at about 2 years. This finding may provide a partial explanation for the 'physiological acidosis' characterized by a low systemic pH in newborn and young infants. ATPase was present in basolateral membranes of most epithelial cells in nonanaplastic Wilms' tumors but was absent in the epithelial component of two anaplastic Wilms' tumors. CA II was detected only in a few epithelial cells in four tumors. Neoplastic epithelial cells reactive for CA II also stained for ATPase but not vice versa. Band 3 glycoprotein was not detected in any Wilms' tumor. These findings show that the immunohistochemical assessment of protein involved in electrolyte transport provides a further means for determining the relative level of differentiation of tumor cells of epithelial origin and suggest that these methods may be a valuable aid in determining the prognosis of some carcinomas.
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PMID:Immunohistochemical localization of transport mediators in Wilms' tumor: comparison with fetal and mature human kidney. 247 91

Acid secretagogue-specific receptor activation in parietal cells triggers rapid and coordinate gene expression of gastric H+,K(+)-ATPase and of CA II. The rapid rise in steady-state levels of CA II mRNA is due to new transcription of the CA II gene in stimulated cells. Although the presumed function of CA II in activated parietal cells is to catalyze the generation of HCO3- from OH-, regulation of CA II gene expression appears to be independent of the generation of H+ (and OH-) through the action of H+,K(+)-ATPase.
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PMID:Regulation of CA II and H+,K(+)-ATPase gene expression in canine gastric parietal cells. 256 18

To identify precisely the structural and functional cell type in the collecting duct of the rat kidney expressing binding sites for Dolichos biflorus agglutinin (DBA), we stained serial paraffin sections of kidney with horseradish peroxidase-labeled DBA and with immunocytochemical methods for localizing (Na+ + K+)-ATPase and carbonic anhydrase II (CA II), enzymes found preferentially in principal and intercalated cells, respectively. Most principal cells expressing a strong basolateral staining for (Na+ + K+)-ATPase showed binding sites for DBA at their luminal surfaces. However, a minority of cells rich in CA II and showing morphologic characteristics of intercalated cells also expressed DBA binding sites at their luminal surface and apical cytoplasm. These data suggest that DBA cytochemistry can provide a useful tool for studying the functional polarity of the main cell types of the collecting duct of the rat kidney.
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PMID:Expression of binding sites for Dolichos biflorus agglutinin at the apical aspect of collecting duct cells in rat kidney. 282 51

The ontogeny of lectin-positive epithelial cell types and the maturation of polarized expression of the glycocalyx of the collecting ducts (CD) of the rat kidney were studied from samples of 18th-day fetal and neonatal kidneys of various ages. Lectins from Dolichos biflorus (DBA) and Vicia villosa (VVA), with preferential affinity to principal cells, stained virtually all CD cells of the fetal kidneys. However, within two days postnatally, the number of cells positive for DBA and VVA decreased to amounts found in the adult kidneys. Moreover, a characteristic change occurred rapidly after birth in the intracellular polarization of the reactive glycoconjugates, from a uniform plasmalemmal to a preferentially apical staining. In contrast, lectins from Arachis hypogaea (PNA), Maclura pomifera (MPA) and Lotus tetragonolobus (LTA), reacting indiscriminatively with principal and intercalated cells of adult kidneys, stained most CD cells in the fetal kidneys, and failed to show any postnatal change in the amount of positive cells or in the intracellular polarization. The immunocytochemical tests for (Na + K)-ATPase and carbonic anhydrase (CA II) revealed the characteristic postnatal decrease in the amount of principal cells and simultaneous increase in the amount of CA II rich intercalated cells. DBA and VVA reactive cells also decreased postnatally, paralleling the changes observed in the (Na + K)-ATPase positive principal cells. The present results suggest that the expression of the cell type-specific glycocalyx of principal and intercalated cells is developmentally regulated, undergoes profound changes during maturation, and is most likely associated with electrolyte transport phenomena.
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PMID:Cell type-specific glycoconjugates of collecting duct cells during maturation of the rat kidney. 284 54


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