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)

The enamel organ of growing rat incisors was perfusion-fixed with a mixture of formaldehyde and glutaraldehyde and processed for ultracytochemical demonstration of ouabain-resistant, K+-stimulated p-nitrophenylphosphatase representing the second dephosphorylative step of H-K-ATPase by use of the one-step lead method. Throughout the stages of amelogenesis, the enzymatic activity was found in the plasma membranes, mitochondrial membranes, and lysosomal structures of the cells of stratum intermedium, papillary layer, and ameloblast layer. Gap junctions and desmosomes between these cells were, however, free of reaction product or showed slight precipitates of reaction. The stellate reticulum and the outer enamel epithelium at the stage of enamel secretion were usually negative for reaction. Although secretory, transition, and ruffle-ended maturation ameloblasts showed enzymatic activity at their basolateral cell surfaces, their distal cell surfaces facing the enamel were always free of reaction product. On the other hand, the smooth-ended maturation ameloblasts seldom showed a positive reaction, except in lysosomes and along their basal cell surfaces. An energy-dispersive X-ray microanalysis of reaction products of H-K-ATPase in unosmicated tissue sections demonstrated that they were composed of lead and phosphorus, which had been released during the dephosphorylation of substrate. In cytochemical controls, the enzymatic activity was completely dependent on substrate and potassium ion, resistant to ouabain and levamisole, and inhibited by nolinium bromide, a specific inhibitor of H-K-ATPase. In addition, inorganic trimetaphosphatase as enzymatic marker of lysosome was localized in dark and pale lysosomes, phagosomes, multivesicular bodies, and ferritin-containing vesicles of the ameloblasts and the cells of stratum intermedium and papillary layer. These membrane-bound structures were also positive for H-K-ATPase reaction. These results suggest that: 1) H-K-ATPase functions to maintain an acidic internal pH of lysosomes in the enamel organ cells; and 2) H-K-ATPase localization in the plasma membranes of enamel organ cells is concerned with efflux of protons derived from cytoplasmic water.
Anat Rec 1988 Aug
PMID:H+-K+-ATPase activity in the rat incisor enamel organ during enamel formation. 284 91

The effects of starvation, feeding, and time of day on mouse gastric glands were studied by means of an enzyme histochemical method for K+-dependent p-nitrophenyl phosphatase (K+-NPPase), a partial reaction of the proton pump ATPase which drives gastric acid secretion. The stomachs of mice starved for 24 h showed very low levels of parietal cell K+-NPPase histochemical reaction. However, a brief meal following such a period of starvation produced an abrupt increase in K+-NPPase reaction within most of the parietal cell-containing glands though not all parietal cells were equally susceptible to stimulation. The number of glands containing K+-NPPase-reactive parietal cells fell slowly in the hours following a feeding stimulus. These changes were shown to be caused by feeding rather than by general arousal and to follow the feeding cycle in ad libitum fed animals. The reasons that parietal cells in the basal parts of mouse gastric glands cannot be induced to show K+-NPPase reactivity by a feeding stimulus are not understood.
Anat Rec 1988 Sep
PMID:Effects of starvation, feeding, and time of day on the activity of proton transport adenosine triphosphatase in the parietal cells of the mouse gastric glands. 284 92

Studies using thick sections stained by ATPase cytochemistry and scanning electron microscopy were carried out to determine three-dimensional ultrastructural alterations in Sertoli cell processes invading neighboring spermatids during mouse spermiogenesis. Sertoli cell processes start invading spermatid cytoplasm at the acrosomal phase of development and undergo considerable change at the maturation phase of development. At step 14, these processes elongate and begin to branch in the spermatid cytoplasm, and by step 15, they extend in various directions to form a complex of canals that the authors have designated the canal complex. The present observations also clarify that the complicated canal complex undergoes regional modification. At the late stages of maturation, the endoplasmic reticulum has gathered with other cell organelles to form aggregates of endoplasmic reticulum in the vicinity of which invading Sertoli cell processes extensively ramify further into thin tubules that intertwine with each other to form a region of thin tubules. In thin sections, each such region was a complex, consisting of small vesicles and endoplasmic reticulum, and corresponded to what has been defined as a mixed body by Morales and Clermont (Anat. Rec., 203:233-244, 1982). During the course of the formation of the region, the invading Sertoli cell processes are continuous at all times with the cell body of the surrounding Sertoli cell.
Anat Rec 1988 Jan
PMID:Dynamic changes in Sertoli cell processes invading spermatid cytoplasm during mouse spermiogenesis. 296 97

Effects of pregnancy stimulation upon histochemically assessed myofibrillar ATPase and muscle fiber diameters were analysed in the rectus abdominis (RA) muscle of guinea pig. Samples of the muscle were taken at 30, 40, 50, 60, and 70 days of pregnancy and compared with samples of the same muscle taken from nonpregnant guinea pigs. Changes in muscle fiber proportions were noted through the course of pregnancy. Starting from 50 days of gestation an increase in type I fibers and a decrease in type IIB fibers were noted. Increase in muscle fiber diameters was also observed in type I, IIA, and IIB fibers. In addition, the RA muscle of the male guinea pig was compared with that of the female guinea pig and showed more type IIA and less type IIB fibers and all the three fiber types were larger than those of the female.
Anat Rec 1987 Jan
PMID:Histochemical types and sizes of fibers in the rectus abdominis muscle of guinea pig: adaptive response to pregnancy. 297 Feb 37

Transmission electron microscopy and ultracytochemistry were employed in an attempt to localize the enzyme calcium adenosine triphosphatase (Ca-ATPase) in the rod outer segments (ROS) of the toad retina. Utilizing a one-step incubation procedure, Ca-ATPase was identified as an electron-dense precipitate in the intradiskal spaces of the rod disks (vesicles) of the ROS. Analytical microscopy identified the reaction product as lead phosphate. The formation of the reaction product was dependent on the presence of ATP (the substrate) and calcium ions. However, calcium ions could be substituted for by magnesium ions. In addition, the reaction was vanadate sensitive. The latter is known to inhibit Ca-ATPase activity. Such data appear to indicate the presence of a Ca-Mg-ATPase in association with the rod disks. Since cyclic guanosine monophosphate (cyclic GMP), rather than calcium ions, is currently believed to be the primary intracellular messenger associated with phototransduction, the presence of an ROS Ca-ATPase may indicate other functions for this cation in the physiology and biochemistry of the visual process. Ca-ATPase might play a role in directional calcium fluxes between intracellular compartments.
Anat Rec 1988 Jul
PMID:Electron microscopic cytochemical localization of Ca-ATPase in the rod outer segments of the toad Bufo marinus. 297 64

The architectural arrangement and selected histochemical properties of hepatocytes in the rainbow trout (Salmo gairdneri Richardson) were examined. Light and transmission electron microscopic (TEM) examination following fixation by portal venous perfusion revealed a tubular arrangement of hepatocytes. Lobules, as defined in the adult mammal, were absent. Biliary epithelial cells associated with bile preductules and ductules were a prominent feature of trout liver. Patterns and location of reaction products for glucose-6-phosphatase (G-6-Pase), glucose-6-phosphate dehydrogenase (G-6-PDH), and magnesium-dependent adenosine triphosphatase (ATPase), enzymes preferentially distributed in mammalian liver, were demonstrated in trout liver. A slightly heavier staining pattern for G-6-Pase was seen around presumptive portal venules but all other enzyme reaction patterns were uniform throughout the liver parenchyma. Following ATPase localization, four sizes of biliary passageways (canaliculi, bile preductules, ductules, and ducts) were visualized. Maximum glycogen retention was achieved with freeze-drying and glycolmethacrylate embedding and with this method intense, uniform glycogen staining was observed in all areas of the liver. Companion TEM examinations revealed large depots of glycogen within hepatocytes. The results are important for interpretation and description of the effects of toxic/carcinogenic alteration on trout liver.
Anat Rec 1985 Oct
PMID:Functional units in rainbow trout (Salmo gairdneri) liver: I. Arrangement and histochemical properties of hepatocytes. 300 Feb 24

Sprague-Dawley strain rats of 4-5 weeks old were perfusion-fixed with either a mixture containing 0.1 or 0.25% glutaraldehyde and 2% formaldehyde, or a 2% formaldehyde in 0.1 M sodium cacodylate buffer for 10 minutes. Non-decalcified 30-50-micron sections of the enamel organ taken from lower incisors were then processed for ultracytochemical demonstration of ouabain-sensitive, K+-dependent, p-nitrophenyl phosphatase, by use of the one-step lead method, representing the second dephosphorylative step of Na+-K+-ATPase. Throughout the secretory, transition, and maturation stages of amelogenesis, the enzymatic activity was demonstrated along the cytoplasmic side of the plasma membranes of the stratum intermedium and the papillary layer cells, especially along their numerous microvilli. The plasma membranes forming gap junctions and desmosomes were free of reaction or showed slight focal precipitates of reaction products. The stellate reticulum and the outer enamel epithelium exhibited either a weak reaction or were reaction negative. Secretory ameloblasts showed a weak trace-like reaction along the basal and lateral cell surfaces; however, the latter surfaces were sometimes completely free of reaction. Tomes' processes were usually reaction negative. Ameloblasts in the transition and maturation stages were devoid of enzymatic activity, except for a slight reaction along the plasma membranes of the basal cell surfaces of transition ameloblasts facing the papillary layer. The enzymatic activity described above was completely dependent on the presence of potassium and substrate in the incubation media and was almost completely inhibited by an addition of 10 mM ouabain to the incubation media.
Anat Rec 1986 Sep
PMID:Ultracytochemistry of ouabain-sensitive K+-dependent p-nitrophenyl phosphatase in rat incisor enamel organ. 302 Oct 21

We have identified in Bacillus subtilis an analogue of the Escherichia coli RecA protein. Its activities suggest that it has a corresponding role in general genetic recombination and in regulation of SOS (DNA repair) functions. The B. subtilis protein (B. subtilis Rec) has a Mr of 42,000 and cross-reacts with antisera raised against E. coli RecA protein. Its level is significantly reduced in the recombination-deficient recE4 mutant. B. subtilis Rec is induced 10- to 20-fold in rec+ strains following treatment with mitomycin C, whereas it is not induced in the recombination-deficient mutants recE4, recE45, and recA1. We have purified B. subtilis Rec about 2000-fold to near homogeneity and we describe its activities. It catalyzes DNA-dependent hydrolysis of dATP at a rate comparable to that of E. coli RecA protein. However, B. subtilis Rec has a negligible ATPase activity, although ATP effectively inhibits dATP hydrolysis. In the presence of dATP, B. subtilis Rec catalyzes DNA strand transfer, assayed by the conversion of phi X174 linear duplex DNA and homologous circular single-stranded DNA to replicative form II (circular double-stranded DNA with a discontinuity in one strand). ATP does not support strand transfer by this protein. B. subtilis Rec catalyzes proteolytic cleavage of E. coli LexA repressor in a reaction that requires single-stranded DNA and nucleoside triphosphate. This result suggests that an SOS regulatory system like the E. coli system is present in B. subtilis. The B. subtilis enzyme does not promote any detectable cleavage of the E. coli bacteriophage lambda repressor.
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PMID:Purification of a RecA protein analogue from Bacillus subtilis. 315 34

A cryostat retrieval method and combined adenosine triphosphatase (ATPase) and acetylcholinesterase (AChase) method were used to study the ultrastructure and innervation of histochemically identified skeletal muscle fibers in different pigeon muscles. The Z-line structure and volume percentage sarcotubular system were analyzed from different muscles selected for their composition by fiber type. Histochemically, three main fiber types were investigated: slow tonic fibers with a moderate ATPase activity after preincubation at acid or alkaline pH; fast-twitch fibers that had high activity after alkaline treatment and low activity after acid preincubation; and a type considered to be slow-twitch that had low activity after alkaline, and high after acid preincubation. Both the slow tonic and slow-twitch fibers had multiple, en grappe innervation, while the fast-twitch fibers had robust, single end plates. The Z-line of the fast-twitch and slow-twitch fibers had a regular square lattice pattern, in contrast to the granular, nonlattice structure of the slow tonic Z-line. The volume percentage sarcotubular system of the slow-twitch fibers was intermediate between and significantly different from that of the fast-twitch and slow tonic fibers. These correlative analyses suggest that the avian muscles contain not only the fast-twitch and slow tonic fibers previously known, but also a slow-twitch fiber that appears to be intermediate between the tonic and the mammalian slow-twitch fiber type. Based on the abundance of the sarcotubular system, this fiber type appears to be fast-contracting and -relaxing, in spite of being multiply innervated.
Anat Rec 1987 Jun
PMID:Quantitative ultrastructure of histochemically identified avian skeletal muscle fiber types. 361 80

Midbelly cross sections of the medial gastrocnemius muscle of young adult male laboratory mice were subjected to ATPase histochemistry with preincubation at pH 4.6. Through the use of a sampling grid and computer-assisted morphometric analysis, 26 to 35% of the total muscle fibers were sampled and classified as type I, IIa, or IIb. Photomicrographs (16 X 20 in.) of five muscles were divided into octants according to a standardized procedure. Total fiber counts and percent of fibers sampled were determined. Variability of sample size per octant was noted, but when averaged across entire muscles, it was in all instances greater than 33%. Fiber type frequency per octant was tested for goodness of fit to a random model by means of a chi-square statistic for equal expected frequencies. Deviation from random fiber type frequency was significant at the P = 0.001 level for every muscle. More importantly, when these data were pooled and again tested using the same method, the probability estimate was less than P = 0.001. This established that the variations in the fiber type proportions found in each mouse followed a common pattern. The systematic fiber type distribution confirmed by these morphometric and statistical methods supports the impression expressed by many muscle biologists that this muscle displays a consistent and complex intramuscular organization.
Anat Rec 1987 Aug
PMID:Systematic distribution of muscle fiber types in the medial gastrocnemius of the laboratory mouse: a morphometric analysis. 366 42


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