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)

Electron microscopic cytochemical localization of Mg++-activated adenosine triphosphatase (Mg++-ATPase) and 5-nucleotidase (AMPase) was investigated in bile canaliculus-rich and bile duct-containing fractions isolated from rat liver. Comparative cyochemical studies between prefixed and non-prefixed fractions revealed that the activity of both enzymes could be detected in the fractions under appropriate experimental conditions. However, the cytochemical activity of AMPase was much more sensitive to glutaraldehyde than that of Mg++-ATPase. Mg++-ATPase and AMPase reaction products were localized primarily on bile canalicular microvilli, that is, along the outer (luminal) surface of canalicular plasma membranes, but they were never observed on bile ductal microvilli. AMPase was also detectable on lateral hepatic plasma membranes. Mg++-ATPase demonstrated by the cytochemical technique described is a reliable enzyme marker for isolated bile canalicular membranes. At high magnification, Mg++-ATPase reaction product was also observed on the microfilaments surrounding isolated bile canaliculi. The possibility that the reaction product on the pericanalicular microfilaments may result from the hydrolysis of ATP byan actomyosin ATPase-like enzyme associated with these filaments is briefly discussed.
 ...
PMID:Electron microscopic cytochemical characterization of bile canaliculi and bile ducts in vitro. 12 97

In the present contribution a comparative study of histochemical mapping of the distribution of adenosine triphosphatase and 5-nucleotidase in the hind brain of mouse has been made. There are many similarities and dissimilarities between the distribution of these two enzymes in various nuclei, tracts and fiber bundles. The noteworthy differences are as follows:--1. The AP, NDNV, NI, NNH, NOAD, NOAM, NOI NPC, TS and SG are very intensely positive for ATPase whereas, in 5-NUC study none of these nuclei demonstrates intensity of such degree. 2. Nucleus ambiguus is intensely positive for ATPase and is completely negative for 5-NUC. 3. The nucleus n. facialis is intensely positive for ATPase and is moderately positive for 5-NUC. 4. NC, GN, PN, PCI and TC are completely negative for 5-NUC. In ATPase preparations only GN is negative and the rest of the areas demonstrate intensity of various degrees. Along with these differences, similarities in the intensity of both enzymes in various nuclei, tracts and fibrous bundles also exist. An attempt has been made to correlate all the aforesaid differences and similarities in the distribution of these two enzymes with the functional nature of the various areas of hind brain of mouse.
 ...
PMID:Acomparative histochemical mapping of ATPase and 5-nucleotidase in the medulla oblongata, spinal cord and cerebellum of mouse. 15 Apr 46

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

In the wall of rat's capillary blood vessels the adenosine triphosphatase is located on the endothelium, the 5'nucleotidase on the perithelial cells. The perithelial cells activities are strong during the inflammatory state, but at the beginning of the phenomenon the nucleotidasic cells become free into the oedematous tissue by preceding and accompagning the fibroblastic differenciation cells.
 ...
PMID:[Cells with phosphatase activity in the walls of subcutaneous capillaries from normal and inflamed rat tissue]. 20 49

Activity of enzymes catalizing bioenergetic processes of substance transport through cell membranes, adenosine triphosphatase and para-nitrophenyl phosphates, activity of certain enzymes of carbohydrate metabolism, lactate dehydrogenase and glucose-6-phosphate dehydrogenase, as well as to 5'-nucleotidase taking part in nucleic metabolism were determined in the pancreas of thyreoidectomized rats. Simultaneously the content of lactic acid, phosphorus, potassium and sodium, which immediately related to activation of the mentioned enzymes, was determined in the pancreas. In thyroidectomized rats the activity of Mg2+, Na+, K+-ATPase, Na+, K+-ATPase and lactate dehydrogenase in the pancreas increases, that of glucose-6-phosphate dehydrogenase, para-nitrophenylphosphatase and 5-nucleotidase decreases, the content of lactic acid, potassium, sodium and phosphorus increases.
 ...
PMID:[Adenosine triphosphatase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase activity of pancreas of thyroidectomized rats]. 20 6

A case of alveolar soft part sarcoma was studied by light and electron microscopy and by electron microscopic enzyme histochemistry of adenosine triphosphatase (ATPase) and 5'nucleotidase(5'Nase). The tumor showed distinct alveolar pattern and diastase resistant PAS positive crystalline inclusions were found in the cytoplasm. Ultrastructurally, characteristic rhomboid crystals and dense granules were observed and they were positive for Mg++- and Ca++-ATPases but negative for 5'Nase. Tumor cell membrane also showed positive activity of ATPase in addition to 5'Nase. These results would support the myogenous derivation of alveolar soft part sarcoma.
 ...
PMID:Adenosine triphosphatase activity of crystalline inclusions in alveolar soft part sarcoma. An ultrahistochemical study of a case. 301 8

The experiments were performed upon the rats aged 1, 4, 7, 15, 30, 45, 60, 90 d, and 1,5 a. The behavior of the following reactions was described: for adenosine triphosphatase stimulated by Mg++(Mg++-ATP-ase), for 5'nucleotidase (5'Nt), for alkaline phosphatase (AP), for acid phosphatase (AcP). The first 3 are markers of the transport enzymes in cells, and the 4th is a marker of lytic processes. It was estimated on the basis of the examined reactions that a full metabolic maturity of the gonad was revealed since the 45th d of post-fetal life.
 ...
PMID:Evolution of localization of the reactions of adenosine triphosphatase (Mg++-ATP-ase), 5'nucleotidase (5'nt), alkaline phosphatase (AP), and acid phosphatase (AcP) in developing rat testis. I. Physiological conditions. 301 64

The described experiments show the influence of a single dose of cadmium chloride (1.5 mg CdCl2/kg body weight applied intraperitoneally) on development of the male gonads from the 1st d of post-fetal life to 1.5 a of life. In the case of the enzymes triggering transportation processes, adenosine triphosphatase stimulated by Mg++ (Mg++-ATP-ase), alkaline phosphatase (AP), and 5'nucleotidase (5'Nt), a considerable damages begin to appear in the 15th d of life whereas in the case of acid phosphatase (AcP) already in the 1st d of life whereas in the case of acid phosphatase (AcP) already in the 1st d of life. These damages increase with age reaching their maximum in the 45th d of life.
 ...
PMID:Evolution of localization of reactions of adenosine triphosphatase (Mg++-ATP-ase), 5'nucleotidase (5'nt), alkaline phosphatase (AP), and acid phosphatase (AcP) in developing rat testis. II. After CdCl2 treatment. 303 15

Within the uterine glands, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that the activities of G-6-PDH, 6-PGDH, and cytochrome oxidase increase within secreting cells during the 2nd half of pregnancy. The activities of the other enzymes remained almost unchanged during the period of investigation. The description of our results distinguishes between gland neck, middle, and distal part of the secretory unit, respectively. In general, the enzyme activities are similar within the middle and distal gland segments, but lower in the epithelia of the neck region. The activity of dehydrogenases was medium to intensive within the middle and distal gland segments, but only low to medium within the neck portion. Of the hydrolases, the acid phosphatase, ATPase, leucine aminopeptidase, and beta-galactosidase demonstrated an intensive activity within activity secreting cells. The enzyme activities of the gland epithelia are compared with these of the uterine surface epithelia and the histochemical results are discussed in context with their significance in histiotrophic nutrition.
 ...
PMID:[Enzyme histochemistry of the pig placenta. III. Histotopics of enzymes in the uterine epithelium]. 309 49

In porcine areolar placental epithelia, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, nonspecific esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that the enzyme activities remained almost unchanged during the period of investigation. Of the dehydrogenases, the diaphorases as well as succinate and lactate dehydrogenase demonstrated generally an intensive activity within the epithelia. The activity of the other dehydrogenases was only low. The activity of unspecific esterase was very intensive within the uterine epithelia but remarkably low within chorionic epithelia. Contrarily, the reaction of adenosine triphosphatase was more intensive within chorionic than uterine epithelia. All investigated glucosidases reacted distinctly positive within chorionic epithelia, but only beta-N-acetyl-hexosaminidase and beta-galactosidase in uterine epithelia. The high activity of acid phosphatase, especially within the chorionic epithelium, seems to be connected with uteroferrin, an iron-binding protein. The histochemical results are discussed in context with the function of the areolae in histiotrophic nutrition and iron transport.
 ...
PMID:[Enzyme-histochemical studies of the pig placenta. II. Histotopics of enzymes in the areolar placenta epithelium]. 392 41


1 2 3 Next >>