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 usefulness of various segment and cell-type specific antibody, lectin and functional markers in the study of cystic renal lesions was evaluated. For this purpose, kidneys from recessive polycystic kidney disease (RPKD), thought to involve mainly the collecting ducts, and cystic kidneys of Meckel's syndrome (MS), which show dilation randomly along the nephron, were studied. The segment (and differentiation-stage)-specific anti-brush-border (specific for proximal tubules) antibodies stained morphologically normal proximal tubules, failed to react with cyst wall epithelium in RPKD, but readily stained some cysts in MS. Immunostaining for Tamm-Horsfall glycoprotein (distal tubules) similarly revealed normal tubular profiles, and also stained moderately dilated tubules, but not the large cysts in either disease type. Lectin markers of the distal tubules and collecting ducts (peanut agglutinin, Helix pomatia agglutinin and Dolichos biflorus agglutinin) reacted with both dilated tubules and with the cyst walls in RPKD and Meckel kidneys, suggesting that in RPKD, the dilations also occur in the distal nephron in addition to the collecting duct, and in MS in any part of the renal tubule. The cell type-specific functional marker of the collecting duct, anti-NaK-ATPase reactivity (found in principal cells) could be seen in RPKD but not in Meckel kidney cysts, suggesting a minor involvement of principal cells in MS. Consistent with this, only occasional carbonic anhydrase (found in intercalated cells) or band 3 (bicarbonate-chloride exchanger molecule of intercalated cells) of collecting ducts positive cells in the cysts could be seen, suggesting that intercalated cells are only sparsely seen in these lesions. The results show the usefulness of a panel of independent markers in studying the segment, cell-type and function-specific features of renal cystic lesions as a basis for their classification.
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PMID:Polycystic disease of the kidney. Evaluation and classification based on nephron segment and cell-type specific markers. 169 Mar 15

Sodium-potassium-stimulated adenosine triphosphatase and carbonic anhydrase isozymes I and II were localized immunocytochemically in adenomas, adenocarcinomas, and normal epithelium of human colon harboring non-neoplastic lesions. Non-neoplastic control colon showed carbonic anhydrase I and II in the cytoplasm of the columnar cells lining the upper half of the crypts. Antiserum to sodium-potassium-stimulated adenosine triphosphatase bound to the basolateral but not the apical plasmalemma of columnar epithelial cells. Staining was most intense in the superficial cells, which also contained carbonic anhydrase, but was also evident to a lesser degree in cells deep in the crypts. Adenomas and adenocarcinomas failed to stain for content of carbonic anhydrase but retained basolateral sodium-potassium adenosine triphosphatase positivity. The staining characteristics of colonic neoplasms for the two enzymes involved in the transport function of colonic epithelium thus resembled those of the less mature cells lining the base of normal crypts.
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PMID:Immunohistochemical localization of sodium-potassium-stimulated adenosine triphosphatase and carbonic anhydrase in human colon and colonic neoplasms. 169 Sep 78

Bone resorption plays an important role in bone modeling and remodeling. Osteoclasts are the cells responsible for the bone resorption. Osteoclasts are located on endosteal bone surfaces and on the periosteal surface beneath the periosteum. They are multinucleated giant cells highly polarized in their morphology and function. Among the proximal surface, the membrane and the area of the cytoplasm directly oppose to the bone surface, which are specialized into two regions. A central region consisting of many irregular cytoplasmic processes and infoldings, the ruffled border, is known to be the active site of bone resorption. Surrounding the ruffled border, a second region, the clear zone provides an area of close attachment to the mineralized bone surface. The osteoclasts secrete a large amount of protons by the action of H(+)-pump on the ruffled border into the sealed resorption cavity, resulting in the acidified microenvironment under which condition the bone matrix is dissolved. Protons are provided by the intracellular action of carbonic anhydrase. Following the secretion of the protons, several ion-transporting systems, i.e., carbonate-chloride exchanger, chloride-channel, Ca(2+)-transport systems, Na+/K(+)-ATPase, and voltage-dependent Ca(2+)-channel, are sequentially operated on both apical and basolateral cytoplasmic membranes. In addition, osteoclasts contain a large amount of lysosomal enzymes (cathepsin C, beta-glycerophosphatase, beta-glucuronidase, etc.), which contribute to degrade the bone organic matrices exposed in the resorption cavity. These enzymes bind to the mannose-6-phosphate receptor on Golgi apparatus, are transported to the ruffled border and are secreted into the extracellular compartment in an exocytotic manner. Osteoclasts also have a high tartrate-resistant acid phosphatase activity which is currently used as a marker enzyme osteoclastic differentiation. Osteoclasts are considered to develop from hematopoietic stem cells. So far, the following four different pathways of the differentiation of osteoclast are proposed: The precursors of osteoclast develop (1) from multilineage hematopoietic cells via a completely separate differentiation line, (2) from granulocyte macrophage-colony forming cells, (3) from committed but proliferative monocyte-macrophage, and (4) from mature and unproliferative monocyte-macrophage. However, the differentiation line of the osteoclasts has still to be elucidated. The formation of osteoclasts as well as that of other hematopoietic cells is strongly regulated by many cytokines [interleukin (IL)-1,IL-3,IL-6, M-colony stimulating factor (CSF), and GM-CSF]. 1,25-Dihydroxyvitamin D3 and parathyroid hormone also stimulate the differentiation of osteoclast precursors. However, the mature osteoclasts do not possess the receptors for these hormones.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:[Osteoclasts in bone metabolism]. 175 56

The progress of research in the Central Nervous System (CNS) had led to the consideration of neurons and glia as indissociable functional complexes. Neuron-glia interactions are essential for the maturation of the CNS. Glial cells release trophic factors for neurons (NGF) and neurons release trophic factors for glia (GGF). Furthermore, the latter provide a substrate for the migration of neurons and guidance of axons by mean of adhesion molecules. In adults, the interactions between neurons and glial cells serve to maintain homeostasis. Thus, the glial cells perform the restoration of the metabolic equilibrium overthrown by the transmission of the nerve impulse and provide the glucose required for neuronal activity. The nerve impulse provokes increases in the cellular space of CO2, K+, NH3 and neurotransmitters which must be taken up to allow neuronal activity to continue (in normal conditions). Astrocytes perform the uptake of the extracellular K+ by means of passive ionic channels, ionic voltage-dependent channels and a sodium-potassium-ATPase-dependent pump. The oligodendrocytes are involved in the metabolism of CO2 by converting CO2 into carbonic acid by means of carbonic anhydrase. Oligodendrocytes and astrocytes play a role in terminating neural transmission by the uptake of the amino acid neurotransmitters, such as GABA, glutamate and aspartate. The catabolism of glutamate to glutamine by means of glutamine synthetase allows both the conversion of an excitatory amino acid into a neutral amino acid (which can diffuse in the extracellular space without causing neural transmission) and the reduction of cerebral NH3 content.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Neuron-glia interactions]. 178 93

Effects of the s.c. administration of various doses of estradiol propionate (E.P.; 25-500 micrograms/kg) on the activities of carbonic anhydrase (CA), Mg(2+)-dependent ATPase and Mg(2+)-dependent, HCO3(-)-stimulated ATPase (Mg(2+)-HCO3(-)-ATPase) in rat duodenal mucosa and kidney cortex, and on body weight, organ weight and serum concentrations of testosterone and estradiol-17 beta, were examined in adult male, female, testectomized and ovariectomized rats. In normal male rats, activities of cytosol CA and brush border Mg(2+)-HCO3(-)-ATPase in the kidney were increased in a dose-dependent manner and reached 1.6- and 2-fold of controls, respectively, after consecutive administration (daily for 7 days) of 500 micrograms E.P. with no changes in either enzyme activities in duodenal mucosa. The positive correlations (P less than 0.01) were observed by linear regression analysis between serum concentration of estradiol-17 beta and kidney cytosol CA or kidney brush border Mg(2+)-HCO3(-)-ATPase activities. In normal female rats, activities of cytosol CA and brush border Mg(2+)-HCO3(-)-ATPase in the duodenal mucosa, and brush border Mg(2+)-HCO3(-)-ATPase activity in the kidney were increased by E.P. administration (100 and 500 micrograms/kg, daily for 7 days), however, kidney cytosol CA activity did not change by any dosage. Behavior of a part of both enzymes to E.P. in testectomized rats was altered almost in the same way to that observed in normal female rats and vice versa in ovariectomized rats. Body weight was decreased, in general, by consecutive administration of E.P. in a dose-dependent manner, and kidney weight was increased by E.P. in both male and female rats.
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PMID:Sexual difference and organ specificity of the effect of estradiol on carbonic anhydrase and Mg(2+)-HCO3(-)-ATPase activities isolated from duodenal mucosa and kidney cortex of male and female rats: preliminary study with crude enzyme samples. 183 40

The cytosol carbonic anhydrase (CA) and microvillus membrane Mg(2+)-dependent, HCO3-(-)stimulated ATPase (Mg(2+)-HCO3-(-)ATPase) activities implicated in ion transport were determined in duodenal mucosa and renal tubule of ovariectomized and estradiol (E2)-treated ovariectomized rats. CA and Mg(2+)-HCO3-(-)ATPase activities in duodenum remained unchanged after ovariectomy, and sc E2 200 micrograms.d-1 x 7d decreased the activity of CA. Both the enzymes in kidney exhibited a similar sensitivity to ovariectomy, and the lowered activity of Mg(2+)-HCO3-(-)ATPase following ovariectomy was restored to near normal after administration of E2. These results suggest that E2 may be a factor in regulation of the above enzymes from the duodenum and kidney of rats, the regulation of E2 on these 2 enzymes in rat duodenum is greatly different from that in rat kidney.
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PMID:Effects of estradiol on carbonic anhydrase and Mg(2+)-HCO3(-)-ATPase activities in rat duodenal microvilli and kidney tubules. 183 28

Sarcolemmal vesicles of white and red skeletal muscles of the rabbit were prepared by consecutive density gradient centrifugations in sucrose and dextran according to Seiler and Fleischer (1982, J. Biol. Chem. 257, 13,862-13,871). White and red muscle membrane fractions enriched in sarcolemma were characterized by high ouabain-sensitive Na+, K(+)-ATPase, by high Mg2(+)-ATPase activity, and by a high cholesterol content. Ca2(+)-ATPase activity, a marker enzyme for sarcoplasmic reticulum, was not detectable in the highly purified white and red muscle sarcolemmal fractions. White and red muscle sarcolemmal fractions exhibited no significant differences with regard to Na+, K(+)-ATPase, Mg2(+)-ATPase, and cholesterol. Specific activity of carbonic anhydrase in white muscle sarcolemmal fractions was 38 U.ml/mg and was 17.6 U.ml/mg in red muscle sarcolemma. Inhibition properties of sarcolemmal carbonic anhydrase were analyzed for acetazolamide, chlorzolamide, and cyanate. White muscle sarcolemmal carbonic anhydrase is characterized by inhibition constants, KI, toward acetazolamide of 4.6 X 10(-8) M, toward chlorzolamide of 0.75 X 10(-8) M, and toward cyanate of 1.3 X 10(-4) M. Red muscle sarcolemmal carbonic anhydrase is characterized by KI values toward acetazolamide of 8.1 X 10(-8) M, toward chlorzolamide of 6.3 X 10(-8) M, and toward cyanate of 0.81 X 10(-4) M. In contrast to the high specific carbonic anhydrase activities in sarcolemma, carbonic anhydrase activity in sarcoplasmic reticulum from white muscle varied between values of only 0.7 and 3.3 U.ml/mg. Carbonic anhydrase of red muscle sarcoplasmic reticulum ranged from 2.4 to 3.7 U.ml/mg.
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PMID:Sarcolemmal carbonic anhydrase in red and white rabbit skeletal muscle. 211 70

Secretin stimulation clears the cytoplasm of intralobular pancreatic duct cells in pigs of tubulovesicles and causes these cells to secrete HCO3- into the pancreatic juice. To determine whether the clearance of cytoplasmic tubulovesicles involves the microtubule system and is important for initiation of HCO3- secretion, the effect of the microtubule poison colchicine on duct cell morphology and pancreatic HCO3- secretion was measured in anaesthetized pigs. Before colchicine, secretin reduced the density of tubulovesicles in the cytoplasm of pancreatic duct cells from 92 +/- 8 U to 8 +/- 2 U and initiated pancreatic secretion of 176 +/- 21 mumols min-1 HCO3-. After colchicine, secretin failed to lower duct cell tubulovesicle density and caused the secretion of only 77 +/- 14 mumols min-1 HCO3-. By contrast, lumicolchicine, an isomer of colchicine that does not affect microtubules, did not inhibit pancreatic HCO3- secretion. Colchicine did not reduce carbonic anhydrase or Na,K-ATPase activities in in-vitro assays. The clearance of tubulovesicles from the cytoplasm of pancreatic duct cells therefore seems to be microtubule-dependent and important for the pancreatic HCO3- secretion.
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PMID:Colchicine inhibits the effects of secretin on pancreatic duct cell tubulovesicles and HCO3- secretion in the pig. 216 27

The bovine ciliary body was investigated by scanning and transmission electron microscopy. The number of cell organelles (mitochondria, rough endoplasmatic reticulum and Golgi complexes) of the nonpigmented (UPE) and the pigmented (PE) epithelium were quantitatively evaluated. Histochemically the activity of carbonic anhydrase (CA) and Na+/K(+)-ATPase was localized within the UPE and PE. As a result of this study, the bovine ciliary body was found to be organized similar to the human and primate ciliary body and can be divided into 4 zones: (1) transition zone between the iris and ciliary body; (2) prelenticular portion of the pars plicata; (3) postlenticular portion of the pars plicata; (4) pars plana. In zone 2 the UPE and PE are filled by numerous mitochondria and show extensive infoldings of the basal cell membranes, which react positively for CA and Na+/K(+)-ATPase, indicating that these cells are involved in the secretion of aequous humor. The transition zone is covered by extremely flat UPE cells and might influence the composition of the aqueous humor by reabsorption rather than secretion. In the postlenticular pars plicata, the number of mitochondria, membrane infoldings and enzyme activity decreases, while the number of rER and Golgi complexes, which are necessary for the synthesis of proteins and proteoglycans, increases. In the pars plana, the UPE is filled completely with filaments pointing to the mechanical strain caused by insertion of the zonular fibers.
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PMID:[Regional differences in the ciliary body of cattle. An electron microscopy and histochemical study]. 216 63


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