Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The study deals with the distribution of acid and alkaline phosphatases, ATPase, 5-nucleotidase, nonspecific esterase, specific cholinesterase, and beta-galactosidase in the diencephalon of the frog. The highlights of the present study are the following: i) Acid phosphatase is present in all the neurons, whereas the tracts and commissures are completely negative. ii) Most of the tracts and commissures are positive for 5-nucleotidase. This confirms the author's previous findings that the tracts and commissures of all the areas of frog brain are intensely positive for 5-nucleotidase. iii) beta-galactosidase activity in the nuclei of the diencephalon is either mild or completely absent, whereas the commissures and tracts show positive activity. iv) Habenulothalamic connections are intensely positive for specific cholinesterase and non-specific esterase, moderately positive for beta-galactosidase and completely negative for other enzymes. v) The epiphysis (pineal organ) shows intense reaction for adenosine triphosphatase, acid phosphatase, and 5-nucleotidase and moderate reaction for alkaline phosphatase and non-specific esterase. In contrast to the above enzymes, the specific cholinesterase and beta-galactosidase are completely missing. vi) Lateral forebrain bundles are completely negative for all the enzymes except alkaline phosphatase and beta-galactosidase. The distribution of these enzymes has been correlated with the functional aspects of various nuclei, tracts, and commissures of the diencephalon of the frog.
 ...
PMID:The chemoarchitectonics of the diencephalon of frog (Rana tigrina). 15 81

Distinct morphological regions, initial, middle and terminal segments, were distinguishable histologically; the middle segment was further subdivided into proximal, intermediated and distal parts. PAS-positive, diastase-resistant reaction was detected in the blood vessels, subepithelial tissue and stereocilia of all segments. Acid phosphatase was demonstrated in the epithelial cells with the highest activity being in the proximal part of the middle segment. Non-specific esterase gave a similar reaction but the strongest activity was in the terminal segment. Alkaline phosphatase, adenosine triphosphatase and adenosine monophosphatase were of similar activity in the subepithelial tissue, blood vessels, stereocilia and luminal contents; the strongest reaction occurred in the middle segment. Lactate, succinate, glutamate and glucose-6-phosphate dehydrogenases were examined; LDH was more active than the others particularly in the terminal segment. Some reaction was found in the epithelial cells, subepithelial tissue and luminal contents.
 ...
PMID:On the regional histology and histochemistry of the epididymis of the camel (Camelus dromedarius). 15 47

Electron microscopic cytochemistry was used to determine the localization of five phosphatase enzymes-glucose-6-phosphatase, inosine diphosphatase, thiamine pyrophosphatase, acid phosphatase, and adenosine triphosphatase-in control human testes. Glucose-6-phosphatase occurred in the endoplasmic reticulum and nuclear envelope of Sertoli cells, Leydig cells and primitive spermatogonia, but was not observed in more advanced spermatogenic cells. The presence of glucose-6-phosphatase activity paralleled the presence of glycogen in spermatogenic cells, i.e., both occurred in type AL and AD spermatogonia but not in type AP or B spermatogonia or in more advanced spermatogenic cells. Inosine diphosphatase activity was found in the endoplasmic reticulum, nuclear envelope, and Golgi complex of Sertoli cells and all spermatogenic cells except late spermatids. Additionally, inosine diphosphatase activity was localized at the junctions between Sertoli cells and late spermatids, but was not associated with any other plasma membrane. Thiamine pyrophosphatase reaction product was found in the Golgi bodies of Sertoli cells and in spermatogenic cells through immature spermatids. Neither inosine diphosphatase nor thiamine pyrophosphatase was observed in the Golgi bodies of spermatids during acrosomal formation. Acid phosphatase activity was found in lysosomes of spermatogonia, spermatocytes, and spermatids, in lysosomes of Leydig cells, and in lysosomes, lipofuscin bodies, and Golgi cisternae of Sertoli cells. It is thought that Sertoli lysosomes play a role in the phagocytosis of degenerating germ cells; however, the role of spermatogenic or Leydig lysosomes is unknown. Adenosine triphosphatase activity occurred at the interfaces between two spermatogonia, and between Sertoli cells and spermatogonia, but was not observed in the spaces between two Sertoli cells, two spermatocytes, two spermatids, or between Sertoli cells and spermatocytes, or between Sertoli cells and spermatids.
 ...
PMID:The fine structural localization of testicular phosphatases in man: the control testis. 17 58

Rats were made to drink D2O mixed water (30: 70) for 6 weeks in order to study the biological effects of orally administered D2O on the liver. Heavy water administration results in gradual decrease in the body weight whereas the liver showed marginal increase in weight throughout the experimental period. Phosphatases and dehydrogenases were analyzed biochemically. Acid phosphatase, glucose-6-phosphatase and adenosine triphosphatase registered fall in contrast to alkaline phosphatase, SDH and LDH, all of which showed a definite increase. Lipids, nucleic acids and proteins, estimated biochemically, gradually decreased throughout the experimental period in response to D2O feeding.
 ...
PMID:Biologic effects of orally administered deuterium oxide on rat liver. 19 33

Ultrastructural distribution of acid phosphatase and adenosine triphosphatase was studied in the receptor elements of HERBST and GRANDRY sensory corpuscles. Acid phosphatase activity was established in the elements of smooth and rough endoplasmic reticulum of perineural capsule cells, as well as in the secondary lysosomes of all cell types. Particular interest was paid on the activity of myelin-like dense bodies and some clear core vesicles belonging to the axoplasm of receptor nerve fibres. Adenosine triphosphatase activity was established on the membranes of receptor structures and pinocytotic vesicles. More deposits of electron dense material were localized on the axolemma of the non-myelinated portions of the receptor nerve fibres. The functional significance and importance of the both enzymes in the receptor structures was discussed.
 ...
PMID:Cytochemical localization of acid phosphatase and adenosine triphosphatase in some avian mechanoreceptors. 21 19

The central nervous systems of web-building spiders (Araneidae, Agelenidae) and hunting spiders (Lycosidae, Salticidae) were tested for non-specific and specific phosphatases. Acid phosphatase exhibited weakly to moderately positive reactions in the neuronal cell bodies and in the neuropile fibre mass of all species investigated. Alkaline phosphatase could only be demonstrated in the external and internal neural lamellae of the brain and ventral cord of several specimens of the araneid species investigated. Tests for thiamine pyrophosphatase were negative with both the lead and calcium-cobalt methods. Distinctive positive reactions for adenosine triphosphatase were visible in the nervous system of all the species used, being especially strong in the optic ganglia of the hunting spiders. The demonstration of adenosine triphosphatase was only possible when applying the calcium-cobalt method after Padykula and Herman, while the lead method after Wachstein and Meisel did not produce any staining reaction at all. Controls of the histochemical reaction showed that the enzyme was activated by Ca2+ and inhibited by sulphydryl destroying reagents (e.g. PCMB), but was insensitive to ouabain. It could be probably classified as a mitochondrial proton-translocating adenosine triphosphatase.
 ...
PMID:Phosphatases in the central nervous system of spiders (Arachnida, Araneae). 21 10

Certain phosphatases have been localized by histochemical techniques in various tissues of a pigeon cestode, Raillietina (Raillietina) johri. Acid phosphatase (AcPase), alkaline phosphatase (AlPase) and adenosine triphosphatase (ATPase) were present in almost all structures: tegument; subtegumental muscles; subtegumental cells; excretory canal; testes; sperm ductules; vas deferens; cirrus sac; cirrus; ovary; receptaculum seminis; vagina; vitelline gland cells; oocytes; uterus; embryonated eggs. AlPase was absent in parenchyma, spermatocytes, spermatids and spermatozoa. AlPase activity was more intense in the tegument of mature gravid proglottides. AcPase and ATPase were visualized in various stages of spermatogenesis of the parasite. ATPase activity was also observed in chromosomes. 5'-nucleotidase (AMPase) activity was restricted to embryonated eggs only. Functional significance of these phosphatases is discussed.
 ...
PMID:Histochemical studies on Raillietina (Raillietina) johri (Cestoda: Davaineidae). I. Nonspecific and specific phosphatases. 22 30

In order to establish whether a specific adenosine triphosphatase is present in yeast cell wall, hydrolysis rates for p-nitrophenylphosphate (acid phosphatase activity) and for ATP (ATPase activity) were compared under various conditions. Rate determinations were made with both, intact cells and with preparations containing secreted enzymes from protoplasts. Acid phosphatase and ATPase activities had the same pH profile and were susceptible in the same way to the repression by orthophosphate and to the inhibition by 2-deoxyglucose. The Lineweaver-Burk plot shows biphasic kinetic behaviour for the hydrolysis of either p-nitrophenylphosphate or ATP. This suggests the existence of two enzymes with different affinities for the substrates, or one enzyme with at least two active sites. The two activities differ in thermostability and only one activity could be completely abolished by heat treatment. The thermostable enzyme activity had K-m values of 0.475 mM for p-nitrophenylphosphate, and 0.040 mM for ATP. ATP behaved as a partially competitive inhibitor of p-nitrophenylphosphate hydrolysis. Substrate competition studies showed that only a non-specific acid phosphatase is responsible for the hydrolysis of ATP.
 ...
PMID:Acid phosphatase and adenosine triphosphatase activities in the cell wall of baker's yeast. 23 59

Cytochemical techniques associated with transmission electron microscopy were used for the localization in Tritrichomonas foetus of enzymes used as markers of different cell structures. Reaction product indicating the presence of Mg(2+)-adenosine triphosphatase (Mg(2+)-ATPase) and 5'-nucleotidase was observed in the plasma membrane. Glucose-6-phosphatase was seen in association with the endoplasmic reticulum, revealing its organization as parallel cisternae. Thiamino-pyrophosphatase was located in the cis-most region of the Golgi complex. Acid phosphatase was found within lysosomes as well as in several cisternae of the Golgi complex, in contrast to previous observations in mammalian cells. These observations provide support for the use of enzyme markers in future studies on cell fractionation of T. foetus.
 ...
PMID:Cytochemical localization of enzyme markers in Tritrichomonas foetus. 166 35

Enzyme histochemistry was assessed in semi-thin glycolmethacrylate sections after 100 mg/kg 2-bromoethanamine (BEA) hydrobromide had been given ip to male Wistar rats to induce renal papillary necrosis. Changes in the proximal tubular marker enzymes alkaline phosphatase (Alk Phos), gamma-glutamytranspeptidase (GGT) and adenosine triphosphatase (ATPase) were not apparent before 8 hr, but there was a progressive loss up to 144 hr. The proteinaceous PAS-positive casts in the loops of Henle and the collecting ducts stained for Alk Phos and GGT (from 12 hr) and for ATPase (from 18 hr). Acid phosphatase (Acid Phos) staining was increased in the proximal tubule lysosomes from 18 hr. There was a marked increase in Alk Phos in all hyperplastic upper urothelial cells from 8 to 24 hr, and a mosaic of staining remained in the pelvis adjacent to the necrosed papilla at 144 hr. At 12 hr, there was an increase in the staining of the pelvic, ureter and bladder vascular endothelial ATPase, the intensity and area of which increased progressively from 18 hr and almost occluded the capillary lumens in the worst affected areas by 144 hr. These data show several distinct series of pathological changes after the administration of BEA. The subtle degenerative changes in the proximal tubule followed the papillary lesion, but exfoliated brush border and proximal tubular cells were important components of the protein casts in the distal nephron. Similarly, the intense Alk Phos staining in the hyperplastic regions of the upper urothelium and the increased pelvic, ureteric and bladder endothelial ATPase staining suggested they develop as a consequence of the papillary lesion.
 ...
PMID:Enzyme histochemical changes in an acutely induced renal papillary necrosis. 197


1 2 Next >>