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)

Pancreas of the cat was fractionated into its subcellular components by centrifugation through an exponential ficoll-sucrose density gradient in a zonal rotor. This enables a preparation of four fractions enriched in plasma membranes, endoplasmic reticulum, mitochondria and zymogen granules, respectively. The first fraction, enriched by 9- to 15-fold in the plasma membrane marker enzymes, hormone-stimulated adenylate cyclase, (Na+K+)-ATPase, and 5'-nucleotidase, is contaminated by membranes derived from endoplasmic reticulum but is virtually free from mitochondrial and zymogen-granule contamination. The second fraction from the zonal gradient shows only moderate enrichment of the above marker enzymes but contains a considerable quantity of plasma membrane marker enzymes and represents mostly rough endoplasmic reticulum. The third fraction contains the bulk of mitochondria and the fourth mainly zymogen granules as assessed by electron microscopy and marker enzymes for both mitochondria and zymogen granules, namely succinic dehydrogenase, trypsin and amylase. Further purification of the plasma membrane fractions by differential and sucrose step-gradient centrifugation yields plasma membranes enriched 40-fold in basal and hormone-stimulated adenylate cyclase and (Na+K+)-ATPase.
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PMID:Studies on isolated subcellular components of cat pancreas. I. Isolation and enzymatic characterization. 14 36

1. Five subjects trained for 8 weeks on a bicycle ergometer for an average of 40 min/day, four times a week at a work load requiring 80% of the maximal oxygen uptake (V(O2 max.)). V(O2 max.) determinations were performed, and muscle biopsies from the quadriceps femoris muscle (vastus lateralis) were taken before, as well as repeatedly during, the training period. The muscle biopsies were histochemically stained for fibre-types (myofibrillar ATPase) and capillaries (amylase-PAS method), and analysed biochemically for succinate dehydrogenase and cytochrome oxidase activities.2. The training programme resulted in a 16% increase in V(O2 max.), a 20% increase in capillary density, a 20% increase in mean fibre area, and an approximately 40% increase in the activities of succinate dehydrogenase and cytochrome oxidase.3. The capillary supply to type I, IIA and IIB fibres, expressed as the mean number of capillaries in contact with each fibre-type, relative to fibre-type area, increased equally.4. The present study shows that endurance training constitutes a powerful stimulus for capillary proliferation in human skeletal muscle.
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PMID:Capillary supply of the quadriceps femoris muscle of man: adaptive response to exercise. 19 32

One hundred and five sexually mature male hamsters were divided in different groups. In the first experiment hamsters were administered gossypol, 10 mg/kg and 20 mg/kg/body weight/day, for twenty and thirty days. In the second experiment hamsters were administered gossypol, 5, 10 and 20 mg/kg/body weight/day, for sixty days. In the third experiment, hamsters were administered gossypol 5 mg, 10 mg, 20 mg and 40 mg/kg body weight/day for 45 days. Animals in all the groups were given gossypol by oral intubation every day. No significant effect on the body weight of hamsters following gossypol treatment was observed. At low doses the weights of testis and accessory sex organs were not statistically different from those of the controls. A significant decrease in testis and epididymis weight was however observed following high doses of gossypol. Low doses of gossypol treatment did not affect the motility of the vas deferens spermatozoa. The vas deferens spermatozoa were however immotile after 40 mg/kg/day gossypol treatment. Gossypol treatment induced a series of histological changes in the seminiferous epithelium of the hamster testis. The earliest sign of drug effect was seen in spermatids and with the increase in doses the effects became more pronounced and extended to the spermatocytes. At 40 mg/kg dose an almost complete arrest of spermatogenesis was observed. Quantitatively, the ratio of pachytene spermatocytes: resting spermatocytes and step 7 spermatids: pachytene spermatocytes decreased significantly. The step 7 spermatids did not mature to step 19 spermatids at all. Histochemically activities of ATPase, SDH and LDH decreased with the increasing doses of gossypol, the activity of 3B hydroxysteroid dehydrogenase was not affected by gossypol treatment. In testis the glucose-6-phosphatase activity was not affected significantly but the activities of fructose 1, 6-diphosphatase and glucose-6-phosphate isomerase decreased significantly with the increasing doses of gossypol. Amylase activity rose significantly at higher doses. Marked changes in LDH and LDH-X were however observed with the increase in gossypol dose. In liver the activity of glucose-6-phosphatase increased significantly while the activities of fructose 1, 6-diphosphatase, glucose-6-phosphate isomerase and amylase were not affected following gossypol treatment. The glycogen contents however increased significantly following high doses of gossypol. No changes in testosterone production and plasma levels of testosterone were observed following gossypol treatment.
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PMID:Response of hamster to the antifertility effect of gossypol. 170 27

A single dose of the synthetic proteinase inhibitor, Camostat (FOY-305; 100 mg/kg), was administered orally to rats. Pancreata were isolated and then perfused to examine the change in the level of resting fluid secretion. As early as 6 h after administration of the single dose of Camostat, the resting fluid secretion was significantly elevated. Twelve hours after administration, resting fluid secretion was maximally elevated, whereas contents of trypsinogen, chymotrypsinogen, and amylase per DNA in the pancreas were significantly decreased. After 12 h, the level of resting fluid secretion gradually decreased to the control resting level in contrast to significant increases in contents of the pancreatic enzyme and zymogens, and wet weight in acinar cells. We further examined the mechanism mediating the elevated resting fluid secretion. Our results are compatible with the view that the elevation of resting fluid secretion may be maintained by spontaneous activation of ion transporters: an ouabain-sensitive Na-K ATPase, an amiloride-sensitive Na-H antiporter, and a unique Cl transporter that is insensitive to furosemide, bumetanide, SITS, and DNDS.
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PMID:Elevation of resting fluid secretion precedes trophic responses in the rat pancreas following a single oral administration of Camostat. 205 Oct 64

The relationship between the oxygen uptake and the release of amylase and sialic acid induced by pilocarpine was investigated in dog submandibular glands. Pilocarpine dose-dependently stimulated the oxygen uptake. The dose required for the maximal response was 10 microM. The release of amylase and sialic acid induced by pilocarpine was inhibited by the addition of iodoacetic acid, malonic acid, 2, 4-dinitrophenol, antimycin A or sodium azide. The oxygen uptake induced by pilocarpine was significantly inhibited by iodoacetic acid, malonic acid, antimycin A or sodium azide. On the other hand, 2, 4-dinitrophenol further stimulated the oxygen uptake by pilocarpine. The increase in the oxygen uptake or the release of amylase and sialic acid induced by pilocarpine was significantly inhibited by ouabain. The Na+, K+-ATPase activity ratio in the microsomal fraction of dog submandibular glands was dose-dependently increased by pilocarpine. The Na+, K+-ATPase activity ratio induced by pilocarpine was significantly inhibited by ouabain, antimycin A, oligomycin or 2, 4-dinitrophenol. The pilocarpine-induced Na+, K+-ATPase activity ratio was significantly inhibited by the removal Ca2+ from the medium or the addition of 2 mM EGTA. These results suggest that the increase in the oxygen uptake by pilocarpine is profoundly involved in the energy supply for the process of amylase and sialic acid release. In particular, the energy supply demanded for the activation of Na+ pump may play a role in the mechanism by which pilocarpine induces the oxygen uptake.
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PMID:[Studies on the relationship between the oxygen uptake and the release of amylase and sialic acid]. 241

The effect of pancreatic duct obstruction on the activities of amylase and three nonexocrine pancreatic enzymes was studied in the rat. gamma-Glutamyl transferase (GGTase) activity, which is localized primarily in the plasma membrane of acinar cells, disappeared from the acinar basolateral plasma membrane and declined in specific activity by 80% over a seven-day experimental period. Mg-ATPase, localized primarily in the apical plasma membrane of acinar cells, simultaneously declined in activity in acinar cells but increased in activity in connective tissue. Mg-ATPase specific activity rose 3.5-fold. The histochemical results showed that the ductlike cells resulting from obstruction were derived primarily from acinar cells. Alkaline phosphatase (APase) activity, which is localized in vascular endothelium and the stroma of interlobular ducts, exhibited a dramatic increase in the periacinar, periductal, and interlobular stroma, and specific activity rose 11-fold. Amylase-specific activity declined as did the protein to DNA ratio. Gel electrophoresis showed that the amount of zymogen granule polypeptides declined after duct obstruction, whereas a few other polypeptides increased in amount.
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PMID:Effect of duct obstruction on histology and on activities of gamma-glutamyl transferase, adenosine triphosphatase, alkaline phosphatase, and amylase in rat pancreas. 242 7

The effects of monensin on the Na+,K+-ATPase activity and the release of amylase and sialic acid were investigated in dog submandibular gland pieces. Monensin stimulated the Na+,K+-ATPase activity and amylase release in a dose-dependent manner. Moreover, this agent increased the Na+,K+-ATPase activity and the release of amylase and sialic acid induced by pilocarpine. These results suggest that monensin increases the release of amylase and sialic acid in dog submandibular glands, in part, through the Na+ pump activated due to the Na+ influx.
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PMID:Effects of monensin on the Na+ pump activity and the release of amylase and sialic acid in dog submandibular glands. 243 68

A modified ATPase method for the simultaneous demonstration of capillaries and fiber types in skeletal muscle is presented. Muscle biopsies were obtained from mice, hamsters, rats, cats, and dogs, quick frozen, and sectioned at 8 microns in a cryostat. The frozen slides were fixed in a neutral formalin solution at 4 C for 5 min, and then incubated at 37 C for 1 hr in a medium containing ATP, Pb2+, and Ca2+ in a tris-maleate buffer (pH 7.2). Dilute (NH4)2S was used as a developer. To test the reliability of the proposed method, serial sections of each biopsy were stained separately for capillaries (amylase-PAS method) and for fiber types by a standard myosin ATPase (m-ATPase) method. Fiber type percent and capillary parameters were determined for each biopsy. No difference in results was observed for parameters determined using the modified ATPase method compared to the standard capillary and fiber type staining methods. This modified technique is therefore suitable for the simultaneous demonstration of capillaries and fiber types in skeletal muscle.
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PMID:A histochemical method for the simultaneous demonstration of capillaries and fiber type in skeletal muscle. 244 Jan 55

Pancreatic duct fragments were isolated from rat and hamster pancreas and were cultured in an agarose matrix for up to 8 weeks (rat) or 20 weeks (hamster). The fragments consisted predominantly of duct epithelium, lesser numbers of stromal and atrophied acinar cells, and small numbers of islet cells. Hamster ducts averaged 3 micrograms protein per duct while rat ducts averaged 1 microgram, and the protein:DNA ratio of both types of ducts was less than that of whole pancreas. Estimated average duct yields of 6% (hamster) and 1% (rat) were based on the protein content of the ducts. Duct viability was shown by the incorporation of 3H-thymidine and 3H-leucine into bulk DNA and protein and by autoradiography. gamma-Glutamyl transferase and (Na + K)-ATPase specific activities were slightly elevated while amylase was depressed in the ducts when compared with whole pancreas in both species. gamma-Glutamyl transferase was localized histochemically in both duct epithelium and in surviving acinar tissue, as seen in vivo. Amylase was shown by immunohistochemistry to be present within duct lumina and in atrophied acini and their lumina. Alkaline phosphatase and Mg-ATPase specific activities were elevated in the hamster, but reduced in the rat, when compared with whole pancreas. Hamster alkaline phosphatase and Mg-ATPase were localized by histochemistry to the duct stroma, where these enzymes are not detected in vivo. Carbonic anhydrase was found in the duct epithelium of both species, as in vivo, as well as in the duct stroma, unlike in vivo. Acid glycosaminoglycans, as revealed by alcian blue staining, were found at the apical surfaces and in the lumina of both kinds of ducts. Glutathione-S-transferase and glucose-6-phosphate dehydrogenase were elevated in rat ducts, but not in hamster ducts. The polypeptide compositions of cultured ducts, freshly isolated pancreatic islets, and whole pancreas were compared by one-dimensional sodium dodecyl sulfate polyacrylamide gradient gel electrophoresis. No duct-specific polypeptides were observed; the ducts were characterized mainly by the reduction or absence of polypeptides, including some zymogens, seen in whole pancreas.
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PMID:Biochemical and histochemical characterization of cultured rat and hamster pancreatic ducts. 244 50

Pancreatic ductal cell secretion has not been well characterized due to the difficulty in obtaining sufficient quantities of purified ductal cells. To determine if the MIA PaCa-2 cell line would provide a useful model for in vitro studies of pancreatic ductal cell secretion, the present study was designed to characterize these cells in greater detail. In this investigation, the human pancreatic undifferentiated cell line, MIA PaCa-2, was compared with PANC-1 cells (a human ductal cell line previously characterized), isolated rat and human ducts, acinar cells, and nonpancreatic cell lines. The results indicate that while the morphology of the MIA PaCa-2 cell line is nonpolarized and generally atypical of either ductal or acinar cells, the cell line has retained certain biochemical similarities to ductal cells. Additional morphological studies indicated (a) the presence of intermediate filaments characteristic of epithelial cells, (b) the absence of zymogen granules, and (c) an apparent basolateral plasma membrane localization of Na+, K+-ATPase. Similar to ductal cells, biochemical analyses indicated (a) the presence of Na+, K+-ATPase based on [3H]-ouabain binding assays, (b) high levels of carbonic anhydrase, (c) low levels of gamma-glutamyl transpeptidase, (d) nondetectable levels of amylase, and (e) protein composition and protein synthetic patterns comparable to PANC-1 cells. Finally, as with PANC-1 cells and isolated rat and human ducts, the major sulfated secretory product of MIA PaCa-2 cells was a protein with a molecular weight of approximately 660,000 to 1 million.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Comparative analysis of a human pancreatic undifferentiated cell line (MIA PaCa-2) to acinar and ductal cells. 247 96


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