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Query: UNIPROT:P01189 (
beta-endorphin
)
21,003
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The vector characteristics of the interacting Na+, K+-ATPase and ouabaine were studied in experiments on the restored ghosts of erythrocytes. It is shown that the effect of K+ on the enzyme activity is the same as in cases of using ATP and p-nitrophenylphosphate (p-NPP) as phosphorylating agents. ADP removes the p-
NPP
induced inhibition with ouabain. This effect is explained rather by addition of ADP to the enzyme substrate centre than by a decrease in the concentration of E1 approximately P phosphoform. Incorporation of labelled orthophosphate into p-nitrophenol (NP) in the presence of Na+, K+-ATPase preparations was not detected. It is shown that antibodies against the fraction of the brain microsomes inhibit K+-NPPases to a much less extent than Na+, K+-ATPase. The digitonin treatment does not remove (Na++ATP)-dependent increase in the K+-
NPPase
activity. A conclusion is drawn that the mechanisms of p-
NPP
hydrolysis differs from the mechanism of ATP hydrolysis.
...
PMID:[Interaction of p-nitrophenylphosphate with Na+,K+-ATPase]. 22 60
The specific activity of K+-dependent p-
NPPase
(paranitrophenylphosphatase) from frog (Rana ridibunda) epidermis microsomal preparation was determined. The activity was proportional to time of incubation and protein concentrations under our assays conditions. Optimal phosphatase activity was at pH from 8 to 9 and over 35 degrees C. 10(-3) M ouabain inhibited 100% of the activity and the Ki was estimated about 5 X 10(-5) M. The Km for p-
NPP
was 3.8 mM and 2.1 for K+. The lectins GSI and GSII produced 80-90% of non-competitive inhibition of the activity. 50% of inhibition by GSI was obtained at 2 micrograms/ml. The Km for p-
NPP
did not change but the Vmax of activity was clearly reduced for both GSI and GSII lectins.
...
PMID:Lectin inhibition and kinetics of microsomal K+-dependent p-nitrophenyl phosphatase of frog epidermis. 303 7
Some properties of inorganic pyrophosphatase (PPiase EC 3.6.1.1.) and para-nitrophenylphosphatase (p-
NPPase
EC 3.1.3.1) in the microsomal fraction of odontoblasts were investigated. The ratio of Mg2+:p-
NPP
and Mg2+:PPi for optimal enzyme activities was 1:1. A mutual substrate competition for PPiase and p-
NPPase
was described. In the presence of 0.1 mM EDTA, Mg2+ alone was not able to reactivate p-
NPPase
or PPiase. Instead, Zn2+ and Co2+ reactivated the PPiase, indicating they might act as cofactors for the enzyme. Mg2+ increased the PPiase activity, probably because Mg PP2-i was the true substrate for the enzyme. The diphosphonates ethane-1-hydroxy 1,1 diphosphonate (EHDP), methane diphosphonate (MDP) and dichloromethane diphosphonate (Cl2MDP) inhibited the PPiase activity.
...
PMID:Relationship of inorganic pyrophosphatase and para-nitrophenylphosphatase activities of alkaline phosphatase in the microsomal fraction of isolated odontoblasts. 612 84
Vanadate in redox state +5 inhibited the Na+K+-activated ATPase as well as the potassium-stimulated p-nitrophenylphosphatase (p-NPPase) activities of plasma membrane fragments prepared from rat brain. Vanadate exhibited a mixed type inhibition on the Na+K+-ATP-ase activity. The same type of inhibition was observed when the p-
NPPase
activity of the enzyme preparation was measured either in the presence of 20 mM K+ or with 5 mM Na+ + 1 mM K+. When the reaction mixture contained 50 microM ATP, 5 mM Na+ and 1 mM K+, inhibition of p-
NPP
hydrolised by vanadate displayed a noncompetitive character. Higher noradrenalin concentration was required for counteracting, the inhibition of p-
NPPase
by vanadate in the presence of ATP than in its absence.
...
PMID:Vanadate inhibition of Na+K+. ATPase and K+-dependent p-nitrophenylphosphatase: a kinetic analysis. 633 Oct 47
The effect of nantenine, an aporphine alkaloid, on ATPase K+-dependent dephosphorylation was evaluated using p-nitrophenylphosphate (p-NPP) as substrate. Basal K+-p-
NPPase
activity was significantly increased with 3 x 10(-4) M, remained unchanged with 3 x 10(-6) M, 3 x 10(-5) M but was reduced with 7.5 x 10(-4) M and 1 x 10(-3) M nantenine, whereas Mg2+-p-
NPPase
activity was not modified. Kinetic studies showed that K+-p-
NPPase
inhibition by nantenine is competitive to KCl but non-competitive to substrate p-
NPP
, whereas K+-p-
NPPase
stimulation by nantenine is non-competitive to KCl but competitive to p-
NPP
. These data suggest that there may be two acceptor sites for nantenine in p-
NPPase
, one eliciting stimulation and the other inhibition of K+-dependent p-
NPP
hydrolysis. Considering the biphasic action of nantenine on seizures and the correlation between decreased ATPase activity and seizure development, alkaloid anticonvulsant effect observed at low nantenine doses is attributable to the stimulation of phosphatase activity whereas the convulsant effect at high alkaloid doses seems related to Na+, K+-ATPase inhibition.
...
PMID:In vitro dose dependent inverse effect of nantenine on synaptosomal membrane K+-p-NPPase activity. 1131 51
In the search of Na+,K(+)-ATPase modulators, we have reported the isolation by gel filtration and HPLC of a brain fraction, termed endobain E, which highly inhibits Na+,K(+)-ATPase activity. In the present study we compared some properties of endobain E with those of ascorbic acid. Kinetic experiments assaying synaptosomal membrane K(+)-p-nitrophenylphosphatase (K(+)-p-
NPPase
) activity in the presence of endobain E or ascorbic acid showed that in neither case did enzyme inhibition prove competitive in nature versus K+ or p-
NPP
concentration. At pH 5.0, endobain E and ascorbic acid maximal UV absorbance was 266 and 258 nm, respectively; alkalinization to pH 14.0 led to absorption drop and shift for endobain E but to absorbance disappearance for ascorbic acid. After cysteine treatment, endobain E absorbance decreased, whereas that of ascorbic acid remained unaltered; iodine treatment led to absorbance drop and shift for endobain E but to absorbance disappearance for ascorbic acid. HPLC analysis of endobain E disclosed the presence of two components: one eluting with retention time and UV spectrum indistinguishable from those of ascorbic acid and a second, as yet unidentified, both exerting Na+,K(+)-ATPase inhibition.
...
PMID:A comparative study between a brain Na+,K(+)-ATPase inhibitor (endobain E) and ascorbic acid. 1271 44
The ecto-
nucleotide pyrophosphatase
/phosphodiesterase (E-NPP) multigene family contains five members. NPP1-3 are type II transmembrane metalloenzymes characterized by a similar modular structure composed of a short intracellular domain, a single transmembrane domain and an extracellular domain containing a conserved catalytic site. The short intracellular domain of NPP1 has a basolateral membrane-targeting signal while NPP3 is targeted to the apical surface of polarized cells. NPP4-5 detected by database searches have a predicted type I membrane orientation but have not yet been functionally characterized. E-NPPs have been detected in almost all tissues often confined to specific substructures or cell types. In some cell types, NPP1 expression is constitutive or can be induced by TGF-beta and glucocorticoids, but the signal transduction pathways that control expression are poorly documented. NPP1-3 have a broad substrate specificity which may reflect their role in a host of physiological and biochemical processes including bone mineralization, calcification of ligaments and joint capsules, modulation of purinergic receptor signalling, nucleotide recycling, and cell motility. Abnormal
NPP
expression is involved in pathological mineralization, crystal depositions in joints, invasion and metastasis of cancer cells, and type 2 diabetes. In this review we summarize the present knowledge on the structure and the physiological and biochemical functions of E-
NPP
and their contribution to the pathogenesis of diseases.
...
PMID:Physiological and pathophysiological functions of the ecto-nucleotide pyrophosphatase/phosphodiesterase family. 1275 29
Membrane glycoproteins of neural cells play crucial roles in axon guidance, synaptogenesis, and neuronal transmission. We have here characterized membrane glycoproteins containing terminal alpha-mannose residues in rat brain membranes. Affinity purification using Galanthus nivalis agglutinin, that is highly specific for terminal alpha-mannose residues, revealed a 50-kDa protein as well as 80-kDa SHPS-1 and 45-kDa beta2 subunit of Na,K-ATPase in rat brain membranes. Combination of N-terminal peptide sequencing and mass spectrometry indicated that the 50-kDa protein was rat
nucleotide pyrophosphatase
-5 (NPP-5). In contrast to other NPPs, NPP-5 was a type-I transmembrane protein. Northern blot analysis showed that NPP-5 was highly expressed in brain, but also expressed in other peripheral tissues. However, we could not detect either the
NPP
activity or the lysophospholipase D activity in the immunoprecipitates with antibodies to NPP-5 from rat brain membranes. These data, therefore, suggest that NPP-5 is a neural oligomannosidic glycoprotein that may participate in neural cell communications.
...
PMID:Characterization of nucleotide pyrophosphatase-5 as an oligomannosidic glycoprotein in rat brain. 1292 78
Ecto-
nucleotide pyrophosphatase
/phospho-diesterase-I enzyme (E-NPP), one of the type II transmembrane proteins, cleaves phosphodiester and phosphosulfate bonds of a variety of substrates including deoxynucleotides, NAD, and nucleotide sugars. Mammalian E-
NPP
consists of three closely related family proteins; E-NPP1 (PC-1), E-NPP2 (PDNP2/PD-Ialpha/autotaxin), and E-NPP3 (CD203c/PDNP3/PD-Ibeta/B10/gp130RB13-6) that express in different cells or at different locations even in the same cell. E-NPP3 is associated with malignant subversion and invasive properties. In this study, the expression and localization of E-NPP3 were investigated in human colon carcinoma. Western blotting showed strong E-NPP3 expression in cancer tissues and in the serum of colon carcinoma patients. Immunohistochemically, E-NPP3 was expressed not only in the apical but also in the basolateral plasma membranes of cancer cells. No prominent pattern of intracellular localization, and no relation between clinical stage and E-NPP3 expression were observed. Our results suggested that E-NPP3 is associated with carcinogenesis of human colon cancer and that serum E-NPP3 might be a tumor marker of colon carcinoma.
...
PMID:Expression and localization of ecto-nucleotide pyrophosphatase/phosphodiesterase I-3 (E-NPP3/CD203c/PD-I beta/B10/gp130RB13-6) in human colon carcinoma. 1453 6
The use of nucleotides and their analogs in the pharmacological studies of nucleotide receptors (P2 class) should be preceded by detailed studies on their degradation connected with ecto-enzymes of a given cell type. In the present studies we have analyzed stability of some phosphorothioate and phosphonate analogs of ATP and ADP in the HeLa epitheloid carcinoma and endothelial HUVEC cells cultures. Our studies have revealed that ecto-
nucleotide pyrophosphatase
(E-NPP) is one of the main enzymes involved in the extracellular degradation of ATP and other nucleotides in the HeLa cells. On the other hand, the ecto-ATPDase is responsible for the hydrolysis of extracellular nucleotides in human endothelial cell cultures, while the E-
NPP
-like enzymes of the HUVEC cells are not essential to this degradation. The concerted action of the aforementioned ecto-enzymes and
nucleotide pyrophosphatase
, 5'-nucleotidase and adenosine deaminase present in fetal bovine serum (FBS) supplied to the culture medium, results in partial or complete degradation of the phosphorothioate (ATPgammaS) and phosphonate analogs of adenosine nucleotides (alpha,beta-methylene-ATP and beta,gamma-methylene-ATP) in the cell cultures. Only ADPbetaS appears to be resistant to these enzymes. The influence of some nucleotides and their analogs on the proliferation of the HeLa cells in presence or absence of FBS is also discussed.
...
PMID:Degradation of extracellular nucleotides and their analogs in HeLa and HUVEC cell cultures. 1473 90
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