Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:Q9UIJ5 (Rec)
 58,342 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity of the electrolyte transport enzyme, sodium, potassium-activated adenosine triphosphatase (Na+,K+-ATPase), in the gills of the pinfish, Lagodon rhomboides, increased markedly following transfer of fish from brackish water to seawater. Cytochemical localization of Na+,K+-ATPase via its potassium-dependent phosphatase (K+-NPPase) activity in the branchial epithelium of pinfish adapted to seawater demonstrated that chloride cells are the major sites for the enzyme. Subcellularly, the heaviest depositions of reaction product were observed lining the cytoplasmic membrane surfaces of the labyrinth of anastomosing plasma membrane tubules that ramifies throughout the chloride cell cytoplasm. Enzyme activity was demonstrated also on the cytoplasmic surface of the apical crypt membrane and on the cytoplasmic surfaces of vesicles in the cytoplasm subjacent to the crypt. Deletion of potassium from the cytochemical incubation medium or inclusion of 10 mM ouabain abolished the reaction products associated with these membranes. The significance of these cytochemical results is discussed with reference to current hypotheses of chloride cell function.
Anat Rec 1979 Jan
PMID:Ultracytochemical localization of Na+,K+-activated ATPase in chloride cells from the gills of a euryhaline teleost. 21 85

To investigate the functional stages of osteoclasts, the ultrastructural histochemical distribution of the lysosomal enzymes [acid phosphatase (tartrate-sensitive) and neutral phosphatase], the plasma membrane enzymes [alkaline phosphatase, Ca(++)-ATPase, and alkaline ouabain-insensitive p-nitrophenylphosphatase (alkaline p-NPPase)], and the mitochondrial enzyme (cytochrome C oxidase) was evaluated in the chicken tibial metaphysis. Both active-appearing and detached (resting) osteoclasts were studied. Serial sectioning was used to identify detached osteoclasts which were present in the perivascular space. The ultrastructure of detached osteoclasts was similar to that of active osteoclasts, except for the lack of a ruffled border and clear zone, and an altered distribution pattern of small vesicles. Small vesicles were uniformly distributed in the cytoplasm of resting osteoclasts, whereas they were concentrated beneath the ruffled border of active osteoclasts. Alkaline p-NPPase, a marker enzyme for the basal ruffled border, was also apparent on the membrane of small vesicles. However, the vesicles did not possess Ca(++)-ATPase, a marker enzyme for the apical plasma membrane. These findings support the concept that small vesicles serve as a membrane reservoir for the ruffled border membrane. Pre-osteoclasts contained abundant mitochondria and lysosomes, prominent Golgi complexes, moderately developed endoplasmic reticulum, and lacked small vesicles. Pre-osteoclasts appear to fuse with osteoclasts which are attached to the bone surface, but not with detached osteoclasts. The small vesicles, from which the ruffled border arises, are absent from pre-osteoclasts, suggesting that they develop after fusion with pre-existing osteoclasts or after attachment to the bone surface. Alkaline p-NPPase appears to be a marker for differentiation of pre-osteoclasts to mature osteoclasts.
Anat Rec 1991 Nov
PMID:Characterization of the functional stages of osteoclasts by enzyme histochemistry and electron microscopy. 166 72

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

Gastric K+-NPPase represents a partial reaction of the (K+-H+)ATPase system, which is considered to be the proton pump in mammalian parietal cells. In the present paper, K+-NPPase activity was cytochemically studied by the method of Mayahara et al. (1980) in gastric glands of birds, amphibia, and mammals, either in the resting state induced by cimetidine or after stimulation of HCl secretion by histamine. The gastric K+-NPPase cytochemical reaction was localized only in oxyntic cells of the gastric mucosa in the three species tested. The subcellular distribution of the K+-NPPase reaction product drastically changes with the secretory state of HCl. In resting cells, the K+-NPPase staining is associated with the membranes of the endocellular tubular system while in HCl-secreting cells, it is associated with the plasma membrane of the elaborate secretory surface characteristic of this functional state. The above results demonstrate that the same enzymatic activity, which is associated with the gastric proton pump, is present in both membranous systems of the oxyntic cell secretory pole. This fact supports the proposal that the tubular system represents a membrane reserve that inserts the proton pump into the luminal plasma membrane in vertebrate oxyntic cells under the action of HCl secretagogues.
Anat Rec 1984 Dec
PMID:Redistribution of gastric K+-NPPase in vertebrate oxyntic cells in relation to hydrochloric acid secretion: a cytochemical study. 609 93