Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01189 (beta-endorphin)
 21,003 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Na,K-ATPase from duck salt gland and ox brain in the membrane-bound or solubilized form was studied by the radiation inactivation technique using ATP, CTP, GTP or p-NPP as substrates. The values of radiation inactivation size (RIS) were compared with the target size (TS) for the alpha-subunit of the enzyme obtained by an independent method as well as with analytical centrifugation data obtained for C12E8-solubilized enzyme. It was concluded that during ATP (CTP) hydrolysis the enzyme operates as an oligomeric structure; the complex formation requires the presence of K+ and adenosine triphosphate binding to the sites with a low affinity for the nucleotide. Specially designed experiments revealed that the degree of enzyme oligomerization increases with an increase in the microviscosity of the membrane lipid environment.
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PMID:Na,K-ATPase: radiation inactivation studies. 216 88

The effects of the putative neurotransmitters acetylcholine, adrenaline, adenosine, ATP, bombesin, 5-hydroxytryptamine, met-enkephalin, neurotensin, somatostatin, substance P and VIP have been investigated in the perfused intestine of the cod, Gadus morhua. The presence and distribution of the different types of nerves was investigated with immunohistochemistry and Falck-Hillarp fluorescence histochemistry. A spontaneous rhythmic activity of the perfused preparations usually occurred within a few minutes from the start of the experiment. This activity was diminished or abolished by addition of atropine, methysergide or tetrodotoxin to the perfusion fluid. Acetylcholine, 5-hydroxytryptamine or substance P caused a contraction of the intestinal wall. The response to acetylcholine was blocked by atropine but not by tetrodotoxin, while the response to 5-hydroxytryptamine was blocked by methysergide and usually also by tetrodotoxin. This indicates that the effect of acetylcholine is direct on the muscle cells, while the effect of 5-hydroxytryptamine may be at least partly via a second neuron. All adrenergic agonists (adrenaline, isoprenaline and phenylephrine) had a dominating inhibitory effect on the intestine. Experiments with antagonists showed that the inhibition is due to stimulation of both alpha-adrenoceptors and beta-adrenoceptors. ATP, adenosine and somatostatin also caused a relaxation of the intestinal wall, often followed by a contraction. Met-enkephalin produced variable responses, either a relaxation, a contraction or both. Bombesin caused a weak inhibition, if anything. Neurotensin and VIP did not visibly affect the intestinal motility. 5-HT-, substance P- and VIP-like immunoreactivity and catecholamine fluorescence were observed in the myenteric plexus, submucosa and muscle layers in all parts of the intestine.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Neurotransmitters in the intestine of the Atlantic cod, Gadus morhua. 241 59

There are controversial reports in the literature concerning the effects of opioids on superoxide (O2-) formation in phagocytes, these agents being either inhibitory or stimulatory. We re-examined this issue and compared the effects of the chemotactic peptide, N-formyl-L-methionyl-L-leucyl-L-phenylalanine (fMet-Leu-Phe), phorbol myristate acetate (PMA), ATP, platelet activating factor (PAF), cytochalasin B (CB) and prostaglandin E1 (PGE1) with those of various opioids on O2- formation in human neutrophils and HL-60 leukemic cells under defined experimental conditions. In the presence of CB, fMet-Leu-Phe and PAF concentration-dependently activated O2- formation in neutrophils with EC50 values of 20 nM and 100 nM, respectively. In the absence of CB, fMet-Leu-Phe and PAF were much less effective. PAF synergistically enhanced O2- formation induced by fMet-Leu-Phe. ATP at a concentration of 100 microM and the opioids, methionine enkephalin, beta-endorphin, dynorphin, [D-Ala2, N-Me-Phe4, Gly5-ol]-enkephalin, [D-Ala2-D-Leu5]-enkephalin and morphine at concentrations between 10 pM to 1 microM did not activate O2- formation. ATP but not beta-endorphin potentiated fMet-Leu-Phe-induced O2- formation. O2- formation induced by a maximally stimulatory concentration of PMA (100 ng/ml) was enhanced by fMet-Leu-Phe but was unaffected by methionine enkephalin or PGE1. PMA at a non-stimulatory concentration (2 ng/ml) potentiated the effect of fMet-Leu-Phe but did not induce responsiveness to PAF, ATP or beta-endorphin. PGE1 strongly inhibited fMet-Leu-Phe-induced O2- formation, whereas morphine, methionine enkephalin and the opioid antagonist, naloxone, were without effect.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Lack of effect of opioid peptides, morphine and naloxone on superoxide formation in human neutrophils and HL-60 leukemic cells. 255 28

Extracellular recording in guinea-pig or mouse vas deferens or rat tail artery was used to study the effects of some pharmacological agents on the nerve terminal spike (NTS) and the secretion of a sympathetic co-transmitter (presumably ATP), as reflected in the excitatory junction current (EJC). A negative-going EJCi (i for inside) was assumed to reflect release from sites inside, and a positive-going EJCo (o for outside) release from sites outside the recording electrode. Passage into or out of the electrode seemed to be slow. Tetrodotoxin (TTX) in the outer medium blocked the NTS and ECJo as well as EJCi; TTX in the pipette blocked stimulus-evoked but not spontaneous EJCi. The dihydropyridine Ca2+ channel blocking agent, nifedipine, was without effect, but Cd2+ in the external medium blocked EJCo and also, by an effect apparently 'upstream' of varicosities, inhibited EJCi (i.e. release within the patch) but not the NTS. When present in the outer medium the alpha 2-adrenoceptor agonists, clonidine and xylazine, blocked both EJCo and EJCi, but not the NTS. The effects of clonidine were blocked by yohimbine, which in itself increased the EJCo by about 50%. Neuropeptide Y and met-enkephalin in the outer medium blocked EJCo; the effect of met-enkephalin was blocked by naloxone. The K+ channel blocking agents, tetraethylammonium and 4-aminopyridine, inside or outside the electrode, increased dramatically the size of EJCi or EJCo, respectively.
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PMID:Some pharmacological applications of an extracellular recording method to study secretion of a sympathetic co-transmitter, presumably ATP. 256 19

The radiation inactivation analysis of Na+, K+-ATPase, (EC 3.6.1.37) from two different sources was carried out using ATP, CTP, GTP and p-NPP as substrates. In the case of Na+, K+-ATPase from the bovine brain the relation between the logarithm of the residual activity and the radiation dose is strictly linear, which permits calculating 75-90 kDa (for 3 mM GTP and 10 mM p-NPP). Duck salt glands Na+, K+-ATPase reveals larger target sizes: 350 kDa for ATP hydrolysis in saturating concentrations and 145-190 kDa in the case of GTP and p-NPP or low concentration of ATP (30 microM). A conclusion is drawn that while hydrolyzing substrates with complex kinetics (ATP and CTP) the enzyme functions like oligomer. The interaction of nucleotide with substrate-binding site of low affinity induces the aggregation of monomers.
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PMID:[Study of the interaction of Na+,K+-ATPase protomers using the molecular target method]. 283 45

The character of temperature dependence of hydrolytic and transport functions of Na, K-ATPase is analyzed. It is shown that the nonlinear Arrhenius plot is typical only of "allosteric" substrates ATP and CTP, the inflection of curves reflecting sensitivity of the enzyme to the phase reconstructions of membrane lipids. The linear Arrhenius plots are typical of GTP, UTP- p-NPP and acetyl phosphate, the substrates demonstrating "normal" kinetics of Michaelis and not providing the active transport of ions. A conclusion is drawn that anomalies on the Na, K-ATPase temperature dependence evidence for the lipid control of intersubunit interactions in the supermolecular complex of Na, K-ATPase which are realized during the active transport of ions.
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PMID:[Characteristics of temperature dependence of Na,K-ATPase]. 284 87

Inhibition of the phosphorylation of the synaptic plasma membrane (SPM) protein B50 by [D-Trp8]-somatostatin in vitro is time-dependent. Increasing the time of incubation of hippocampal synaptic plasma membranes with the peptide from 15 sec to 30 min prior to addition of 7.5 microM [gamma-32P]ATP results in a complete reduction of B50 phosphorylation. Incubation of synaptic plasma membranes for 30 min in the absence of peptide does not alter basal B50 phosphorylation. Neither ACTH nor beta-endorphin produces similar effects--inhibition of B50 phosphorylation by ACTH is maximal at 15 sec and beta-endorphin produces only a small inhibition, even after 30 min. [D-Trp8]-somatostatin is not activating a membrane-bound protease, since maximal inhibition of B50 phosphorylation by the peptide is seen in the presence of leupeptin or bacitracin. Hippocampal synaptic plasma membranes contain protein phosphatase activity. Assays of B50 phosphorylation in synaptic plasma membranes done under conditions that favor either net phosphorylation or dephosphorylation are consistent with inhibition of protein phosphatase activity by [D-Trp8]-somatostatin. This evidence suggests that [D-Trp8]-somatostatin interacts with SPM binding sites in the hippocampus, which may alter the activity of an endogenous protein phosphatase to determine the degree of B50 phosphorylation.
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PMID:Characteristics of [D-Trp8]-somatostatin-sensitive B50 phosphorylation. 287 46

Opioid narcotics are present in seminal plasma, although their physiological effect on spermatozoa is still unknown. This study reports data on metabolic parameters of human spermatozoa in the presence of a met-enkephalin analogue: D-Ala2-Mephe4-Met-(o)-ol-Enkephalin, FK 33824, Sandoz, Basel, Switzerland (DAMME), and its receptor antagonist naloxone hydrochloride, Endo Laboratories, Garden City, New York. Our findings indicate that the metenkephalin analogue reduces sperm motility and cellular O2 consumption without affecting cellular ATP content and viability. The hypothesis that DAMME acts on adenylate-cyclase is briefly discussed.
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PMID:Effects of a met-enkephalin analogue on motility, O2 consumption, and ATP content of human spermatozoa. 299 93

To investigate a possible role of protein phosphorylation in the mechanism of action of alpha-MSH, excised tail-fins of Xenopus tadpoles were incubated with or without alpha-MSH. After homogenization, in vitro endogenous protein phosphorylation was assayed using [gamma-32P]ATP. alpha-MSH treatment of intact tail-fins, producing full pigment dispersion, resulted in a 5-fold increase in 32P-incorporation into a 53 kDa protein band. This increase in 53 kDa phosphorylation was completely reversible. The increase was not found in homogenates from the melanophore-free part of the alpha-MSH-treated tail-fins. Phosphorylation of the 53 kDa protein could be detected in homogenates of alpha-MSH-treated primary cultured melanophores. Incubation of tail-fins with ACTH1-24, an alpha-MSH-like peptide producing full pigment dispersion, also induced an increase in 53 kDa phosphorylation. A structurally related peptide (ACTH15-24) and an unrelated peptide (LH-RH), neither of which induced pigment dispersion, were ineffective in stimulating 53 kDa phosphorylation. Injection of white adapted tadpoles with 1 micrograms of alpha-MSH or adaptation of tadpoles to a black background also resulted in a significant increase in 53 kDa phosphorylation. alpha-MSH added to the homogenates did not affect 53 kDa phosphorylation, indicating that alpha-MSH acts through a receptor-mediated mechanism. The increase in 53 kDa phosphorylation measured in vitro (post hoc), most likely reflects an alpha-MSH-induced decrease in 53 kDa phosphorylation in vivo. Our results strongly suggest that a decrease in 53 kDa phosphorylation is involved in the mechanism of action of alpha-MSH on melanophores.
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PMID:alpha-Melanotropin-induced changes in protein phosphorylation in melanophores. 299 4

In intact goldfish xanthophores, the phosphorylation of a pigment organelle (carotenoid droplet) protein, p57, appears to play an important role in adrenocorticotropin (ACTH)- or cAMP-induced pigment organelle dispersion while the dephosphorylation of this protein upon withdrawal of ACTH or cAMP is implicated in pigment aggregation. In this paper, we report the cAMP-dependent phosphorylation of this protein in cell-free extracts of xanthophores as determined by the incorporation of 32P from [gamma-32P]ATP. As is the case in intact cells, p57 is the predominant protein phosphorylated in the presence of cAMP. The cAMP-dependent protein kinase which phosphorylates p57 is not bound to the isolated organelles but is found in the soluble portion of the cell extracts. Hence, the phosphorylation of p57 requires the carotenoid droplets bearing the substrate, soluble extract containing the kinase, cAMP (half-maximal activation at 0.5 microM), and Mg2+ (optimal at 5 mM or higher). The presence of protein phosphatase(s) in these extracts was shown indirectly by the stimulation of phosphorylation by fluoride. The phosphorylation of p57 does not appear to require a cell-specific kinase as soluble extracts of goldfish dermal nonpigment cells also phosphorylate p57 associated with isolated carotenoid droplets. Furthermore, using a constant amount of carotenoid droplets, a linear relationship was demonstrated between the rate of p57 phosphorylation and the amount of extract present in the assays. These results suggest that p57 is phosphorylated directly by a cAMP-dependent protein kinase and that the activity of this enzyme is important in regulating the intracellular movement of the pigment organelles of the xanthophore.
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PMID:Regulation of pigment organelle translocation. II. Participation of a cAMP-dependent protein kinase. 300 26


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