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At least 19 recordsLinked to original sources

PubMed1984

Stimulation of prostaglandin synthesis in WI-38 human lung fibroblasts following inhibition of phospholipid acylation by p-hydroxymercuribenzoate.

The release of arachidonic acid and its metabolites, prostaglandin E2 and thromboxane A2, from WI-38 human lung fibroblasts was modulated by p-hydroxymercuribenzoate. Exposure to the inhibitor resulted in a dose-dependent decrease in [1-14C]arachidonic acid uptake and incorporation into phospholipids and neutral lipid pools. Activities of lung fibroblast arachidonyl-CoA synthetase and lysolecithin acyltransferase were inhibited by 100 microM p-hydroxymercuribenzoate. [14C]Arachidonic acid labelled fibroblasts exhibited an increased release of [14C]arachidonate and [14C]prostaglandin E2 of 54% and 112%, respectively, when exposed to 100 microM of inhibitor. The stimulatory effects of 8.0 microM delta 1-tetrahydrocannabinol on arachidonate release and prostaglandin E synthesis (Burstein, S., Hunter, S.A., Sedor, C. and Shulman, S. (1982) Biochem. Pharmacol. 31, 2361-2365) were modified by the inclusion of inhibiting agent, resulting in a 608% stimulation in arachidonic acid release, while prostaglandin E2 and thromboxane A2 synthesis increased 894% and 390%, respectively, over levels obtained by untreated cells. The levels of arachidonate metabolites were altered by inhibitor when compared to cells treated with cannabinoid alone. No significant inhibition by delta 1-tetrahydrocannabinol was found on arachidonic uptake in these cells. In unlabelled studies, p-hydroxymercuribenzoate resulted in a profound, dose-dependent stimulation of prostaglandin E synthesis of 1490% at 150 microM inhibitor concentration. These results provide evidence that free arachidonate is reincorporated via acylation, thereby implicating this pathway as a possible control mechanism for the synthesis of arachidonic acid metabolites.

1-Acylglycerophosphocholine O-Acyltransferase↗

PubMed1998

Intrathecal administration of p-hydroxymercuribenzoate or phosphoramidon/bestatin-combined induces antinociceptive effects through different opioid mechanisms.

The antinociceptive effect of intrathecally (i.t.) administered protease inhibitors was tested against capsaicin (800 ng) injected into the dorsal surface of a hindpaw. Both p-hydroxymercuribenzoate (2-8 nmol), a cysteine protease inhibitor, and phosphoramidon (1-4 nmol), an endopeptidase 24.11 inhibitor in the presence of bestatin (0.25 nmol) an aminopeptidase inhibitor, administered i.t. 60 min prior to the injection of capsaicin produced a dose-dependent reduction of the capsaicin-induced paw licking and biting response. p-Hydroxymercuribenzoate (4 nmol)-induced antinociception was significantly antagonized by nor-binaltorphimine, a selective kappa-opioid receptor antagonist, but not by naltrindole, a selective delta-opioid receptor antagonist. On the other hand, phosphoramidon (4 nmol) /bestatin-induced antinociception was significantly antagonized by naltrindole, but not by nor-binaltorphimine. The results indicate that the antinociceptive effect of p-hydroxymercuribenzoate may be due to the inhibition of a cysteine protease degrading endogenous dynorphins whereas phosphoramidon in the presence of bestatin blocks the degradation of enkephalins.

Animals↗

PubMed1984

Photosynthetic mutants of the cyanobacteria Synechocystis sp. strains PCC 6714 and PCC 6803: sodium p-hydroxymercuribenzoate as a selective agent.

Among a wide range of potential selective agents examined, sodium p-hydroxymercuribenzoate successfully enriched for mutants of Synechocystis sp. strains PCC 6714 and 6803 defective in photosynthesis. When both photosystems I and II were operating, viability of wild-type cells decreased to between 5 X 10(-5) and 1 X 10(-6) after 5 h of incubation with 500 microM p-hydroxymercuribenzoate (strain 6714), and after 8 h with 200 microM (strain 6803). Between 0.1 and 0.5% of the survivors were stable mutants defective in different steps of photosynthesis. The compound was not mutagenic. It was less toxic to cells grown chemoheterotrophically in the dark or photoheterotrophically in the presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea. p-Hydroxymercuribenzoate therefore killed only cells which were performing photosynthesis at high rates, thereby specifically selecting for mutants deficient in this process.

Chlorophyll↗

PubMed1980

Polypeptide synthesis catalyzed by p-hydroxymercuribenzoate-modified ribosomes.

The stimulation of poly(U)-directed polyphenylalanine synthesis produced by modification of Escherichia coli ribosomes with p-hydroxymercuribenzoate, at low molar ratios of reagent to ribosomes, is due to an increase in the average chain length of polyphenylalanine synthesized, and not to the activation of inactive ribosomes. At a higher molar ratio of p-hydroxymercuribenzoate to ribosomes, which produces no overall change in activity, approximately 50% of the active ribosomes present in the untreated preparation have been completely inactivated, and the remaining active ones, like the ribosomes of the stimulated preparation, synthesize polyphenylalanine at an increased rate as compared with the untreated ribosomes.

Dose-Response Relationship, Drug↗

PubMed1974

Kinetic studies on the effect of uridine diphosphate galactose and manganous ions on the reaction between lactose synthetase A protein from human milk and p-hydroxymercuribenzoate.

The inhibition of lactose synthetase A protein by p-hydroxymercuribenzoate at pH7.5 and 25 degrees C, which involves the reaction of one molecule of inhibitor with each molecule of enzyme, was decreased in rate by UDP-galactose, especially in the presence of Mn(2+). Pseudo-first-order rate constants for the reaction between 0.1mm-p-hydroxymercuribenzoate and free enzyme, the enzyme-UDP-galactose complex and the enzyme-Mn(2+)-UDP-galactose complex were 4.4x10(-2), 1.9x10(-2) and 0.3x10(-2)min(-1) respectively. The results also indicated that dissociation constants for UDP-galactose in the enzyme-UDP-galactose and enzyme-Mn(2+)-UDP-galactose complexes were 313 and 16mum respectively, the latter value being similar to the K(m) for UDP-galactose in the lactose synthetase reaction. The protective effect of UDP-galactose and the role of Mn(2+) ions in lactose synthetase are discussed.

Binding Sites↗

PubMed1976

Effects of p-hydroxymercuribenzoate binding on the visible absorption spectrum of methemoglobin.

The binding of p-hydroxymercuribenzoate to human methemoglobin causes a perturbation of the visible heme abosrption spectrum which is expressed by an increase in absorbance in the high spin band regions, 480 to 510 nm and 590 to 640 nm, concomitant with a decrease in absorbance in the alpha- and beta-band absorption regions. The pH dependence of the p-hydroxymercuribenzoate-induced difference spectrum can be accounted for quantitatively by a 5% shift toward higher spin of the aquo form of methemoglobin, a 15% shift toward higher spin of the hydroxide form, and a shift in the apparent pKa for the water to hydroxide transition from 7.92 to 8.04 when mercurial is bound. The rate of these heme abosrbance changes is consistent with the rapid second order formation of the beta93 cysteine, mercury-mercaptide bond and does not represent a change due to the dissociation of methemoglobin tetramers into dimers, even though the latter, slow process does follow mercurial binding. The observation of an increase in spin produced by the binding of a reagent which also promotes dimer formation argues strongly against any direct correlation between an increase in spin and the appearance of deoxyhemoglobin-like conformations.

Adult↗

PubMed1991

The effects of p-hydroxymercuribenzoic acid modification and heat treatment on the CuA reduction potential of cytochrome c oxidase.

p-Hydroxymercuribenzoic acid modification of cytochrome c oxidase converts the CuA center into a type 2 copper site while heat treatment of the oxidase in lauryl maltoside can transform CuA almost stoichiometrically (greater than 90%) to a blue type 1 copper site. These modifications of the protein have previously been shown to have a profound effect on the dioxygen reduction and proton pumping activities of the enzyme (Li, P. M., Morgan, J. E., Nilsson, T., Ma, M., and Chan, S. I. (1988) Biochemistry 27, 7538; Nilsson, T., Gelles, J., Li, P. M., and Chan, S. I. (1988) Biochemistry 27, 296; Sone, N., and Nicholls, P. (1984) Biochemistry 23, 6550). In this work, the intrinsic reduction potentials and the midpoint reduction potentials of the "CuA" site in both these modified oxidases have been measured under various conditions in order to clarify the intramolecular electron transfer pathways in these systems. The study reveals that the CuA intrinsic reduction potential decreases by almost 150 mV upon p-hydroxymercuribenzoic acid modification whereas it increases by 100 mV upon heat treatment. In addition, the redox interactions between CuA and the remaining metal centers are perturbed upon CuA modification. It is argued that these results bear on the role of CuA in the proton-pumping paradigm of cytochrome c oxidase.

Animals↗

PubMed1977

Nitrate reductase from Spinacea oleracea. FAD and the reactivation of the enzyme treated with p-Hydroxymercuribenzoate.

Spinach nitrate reductase complex previously inactivated by treatment with mercurials p-hydroxymercuribenzoate or p-hydroxymercuriphenyl sulphonate can be reactivated by incubation with dithioerythritol. The reactivation of NADH-diaphorase seems to be FAD-dependent, whereas that of FNH2-nitrate reductase is not. The requirement of FAD for NADH-inactivation of nitrate reductase treated with p-hydroxymercuribenzoate disappears after treatment with dithioerythritol.

Dihydrolipoamide Dehydrogenase↗

PubMed1976

The effect of p-hydroxymercuribenzoate and congeners on microsomal glucose-6-phosphatase.

Iodoacetamide, N-ethylmaleimide, p-hydroxymercuribenzoate (p-MB) and HgCl2 were tested as inhibitors of microsomal glucose-6-phosphatase. Iodoacetamide had no effect at 2 mM. N-ethylmaleimide inhibited only crude, but not purified microsomal preparations (M2) or crude microsomes exposed to deoxycholate. 14C-labelled N-ethylmaleimide was not bound by the M2 protein fraction. p-MB inhibited all types of preparations and the inhibition was not counteracted by detergent. A more detailed study was carried out with the purified M2 fraction (specific activity: 2-4 mumoles Pi/min/mg protein). Glucose-6-phosphate hydrolysis was inhibited 50% by 5 X 10(-5) M p-MB. The inhibition was completely reversible by dithiothreitol except when the enzyme was pre-incubated with p-MB in the absence of substrate. Then p-MB accelerated the temperature-dependent inactivation of glucose-6-phosphatase. Binding studies showed that around 3 mumoles 14C-p-MB were incorporated into 100 mg M2 protein regardless of the concentration of mercurial in the incubation mixture. That is, over a 25 fold range of p-MB concentration, causing up to 80% inhibition of enzyme activity, no difference was seen in the amount of labelled p-MB which was irreversibly bound to M2 protein. Kinetically p-MB behaved like a reversible inhibitor and this was confirmed by dilution experiments. Several compounds, including some amino acids, antagonized the inhibition by p-MB. The order of effectiveness was EDTA greater than barbital greater than tryptophan greater than histidine greater than lysine greater than other amino acids. Glycine, Tris and urea were ineffective competitors of p-MB inhibition. Double reciprocal plots showed that the Km for glucose-6-phosphate was increased and the Vmax reduced in the presence of p-MB. HgCl2 was a more effective inhibitor than p-MB with a Ki of 6 X 10(-6) M. We conclude that a reaction of p-MB with M2 sulfhydryls does not play a part in the inhibition of enzyme activity. It is suggested that p-MB may interact with one or more amino acid side chains in such a way that enzyme conformation is altered.

Animals↗

PubMedDate not supplied

Hyperglycemia following p-hydroxymercuribenzoate administration to mice.

p-Hydroxymercuribenzoate (PMB) administration to fed mice induced transient hyperglycemia of a few hours' duration, and an increase in mitochondrial volume and pyroantimonate precipitation in the cytoplasmic ground substance of the pancreatic islet B-cells, whereas the secretory granules were unaffected. No significant blood glucose elevation or any obvious structural alterations were observed in starved mice treated with PMB. The serum inorganic phosphate concentration was unaffected in fed mice but decreased in starved mice 10 min after PMB injection, and increased in both fed and starved mice 2 h following PMB treatment, whereas the hydrogen ion concentration was increased in both fed and straved mice 10 min after PMB administration. Mitochondrial and ionic alterations, and possible inhibited insulin release may play a role in the development of hyperglycemia in PMB-treated mice.

Animals↗

PubMedDate not supplied

p-Hydroxymercuribenzoate-induced hyperglycemia: influence of pre- and post-treatment with L-leucine, tolbutamide, D-mannoheptulose, insulin and alloxan.

The aims were to see whether p-hydroxymercuribenzoate (PMB) administration affects the serum insulin concentration in mice in vivo, whether the transitory hyperglycemia induced in fed mice by treatment with PMB is affected by L-leucine, tolbutamide, D-mannoheptulose or insulin, and whether PMB affects the B-cell toxicity of alloxan. A significant decrease in the serum insulin concentration was found 1 and 2 h following PMB injection in fed and starved mice. PMB-induced hyperglycemia was abolished by pre-treatment with L-leucine and tolbutamide, but not by pre-treatment with D-mannoheptulose, or by post-treatment with insulin. Pre-treatment of fed mice with PMB caused potentiation of the initial hyperglycemia following alloxan, but inhibited the second hyperglycemic phase. These findings indicate that PMB treatment of mice has a transient inhibitory influence upon insulin secretion, and protects against the development of alloxan diabetes.

Alloxan↗

PubMed1981

Diphenylhydantoin-induced block of the rat phrenic nerve-diaphragm preparation pretreated with p-hydroxymercuribenzoate.

Pretreatment of the rat phrenic nerve-diaphragm preparation with the sulfhydryl-(SH) blocking agent p-hydroxymercuribenzoate (pOHMB) increased the blocking efficiency of the antiepileptic drug diphenylhydantoin (DPH) during indirect stimulation. Another SH-blocking agent, N-ethyl-maleimide (NEM) did not potentiate the block, but SH-group protection with dithiothreitol (DTT) abolished the effect of pOHMB. SH-binding was thus necessary but not sufficient for enhancement of DPH-block. High Ca2+-concentration potentiated the block. Well-maintained response of the isolated phrenic nerve, and of the diaphragm during direct stimulation, located the block at the neuromuscular junction. Microelectrode records in preparations which were curarized, cut or Mg2+ paralyzed to abolish action potential activity, disclosed an abrupt cessation of end-plate potentials (EPPs) by DPH, and pOHMB pretreatment reduced the time period to abrupt EPP fallout in the curarized preparation, suggesting depressed nerve terminal excitability as the cause of the block and its potentiation. Observation of miniature EPPs beyond the time of EPP cessation excluded a postsynaptic block. The pOHMB-treated preparation is suggested as a model for testing antiepileptic drugs.

Action Potentials↗

PubMed2001

Antinociceptive effect produced by intracerebroventricularly administered dynorphin A is potentiated by p-hydroxymercuribenzoate or phosphoramidon in the mouse formalin test.

The antinociceptive effects of intracerebroventricularly (i.c.v.) administered dynorphin A, an endogenous agonist for kappa-opioid receptors, in combination with various protease inhibitors were examined using the mouse formalin test in order to clarify the nature of the proteases involved in the degradation of dynorphin A in the mouse brain. When administered i.c.v. 15 min before the injection of 2% formalin solution into the dorsal surface of a hindpaw, 1-4 nmol dynorphin A produced a dose-dependent reduction of the nociceptive behavioral response consisting of licking and biting of the injected paw during both the first (0-5 min) and second (10-30 min) phases. When co-administered with p-hydroxymercuribenzoate (PHMB), a cysteine protease inhibitor, dynorphin A at the subthreshold dose of 0.5 nmol significantly produced an antinociceptive effect during the second phase. This effect was significantly antagonized by nor-binaltorphimine, a selective kappa-opioid receptor antagonist, but not by naltrindole, a selective delta-opioid receptor antagonist. At the same dose of 0.5 nmol, dynorphin A in combination with phosphoramidon, an endopeptidase 24.11 inhibitor, produced a significant antinociceptive effect during both phases. The antinociceptive effect was significantly antagonized by naltrindole, but not by nor-binaltorphimine. Phenylmethanesulfonyl fluoride (PMSF), a serine protease inhibitor, bestatin, a general aminopeptidase inhibitor, and captopril, an angiotensin-converting enzyme inhibitor, were all inactive. The degradation of dynorphin A by mouse brain extracts in vitro was significantly inhibited only by the cysteine protease inhibitors PHMB and N-ethylmaleimide, but not by PMSF, phosphoramidon, bestatin or captopril. The present results indicate that cysteine proteases as well as endopeptidase 24.11 are involved in two steps in the degradation of dynorphin A in the mouse brain, and that phosphoramidon inhibits the degradation of intermediary delta-opioid receptor active fragments enkephalins which are formed from dynorphin A.

Animals↗

PubMed1987

Metabolism of lysophospholipids in intact rat islets. The insulin secretagogue p-hydroxymercuribenzoic acid impairs lysophosphatidylcholine catabolism and permits its accumulation.

Although recent studies implicate lysophospholipids (lyso-PLs) in stimulus-secretion coupling in the pancreatic islet, almost no data on lyso-PL metabolism therein exist. Therefore, intact rat islets were loaded with insulinotropic and non-toxic concentrations of 1-[14C]palmitoyl-lysophosphatidylcholine (lyso-PC) via transbilayer movement, and its metabolic fate was studied. The time-dependent hydrolysis of lyso-PC to fatty acid (lysophospholipase activity), its conversion to phosphatidylcholine (putative acyltransferase activity) and, to a lesser degree, the appearance of label in phosphatidylethanolamine (putative transacylase or base exchange activity) were observed. p-Hydroxymercuribenzoic acid (PHMB) at 100 microM (a concentration previously demonstrated to elicit potent exocytotic insulin release) inhibited all three activities (by 56, 46 and 75%, respectively) and led to the intracellular accumulation of lyso-PC. Antimycin A inhibited phosphatidylcholine formation but not lysophospholipase activity; lyso-PC did not accumulate, implying that blockade of both of the major metabolic pathways is required to induce a detectable increment in lyso-PC levels. Calculations derived from data using the lowest effective insulinotropic concentration of lyso-PC suggested that increments in lyso-PC accumulation at critical membrane sites of less than 10-15% above basal values are sufficient to trigger insulin release. Since PHMB elicited increments of 50-100% in lyso-PC after its translocation into islets, support is provided for the earlier contention that lyso-PLs mediate the insulinotropic effect of PHMB. In addition, these studies may provide a more precise experimental paradigm for future studies of islet lyso-PL metabolism.

Adenosine Triphosphate↗

PubMed1989

Characterization of the inositol 1,4,5-trisphosphate-induced calcium release from permeabilized endocrine cells and its inhibition by decavanadate and p-hydroxymercuribenzoate.

The inositol 1,4,5-trisphosphate (IP3)-sensitive Ca2+ compartment of endocrine cells was studied with alpha-toxin- and digitonin-permeabilized rat insulinoma (RINA2) and rat pheochromocytoma (PC12) cells. The Ca2+ uptake was ATP-dependent, and submicromolar concentrations of IP3 specifically released the stored Ca2+. Half-maximal Ca2+ release was observed with 0.25-0.5 mumol of IP3/l, and the amount of Ca2+ released due to IP3 could be enhanced by additional loading of the Ca2+ compartment. Consecutive additions of the same concentration of IP3 for 1-2 h always released the same amount of Ca2+ without desensitization, providing an ideal basis to further characterize the IP3-induced Ca2+ release. Here we describe for the first time a reversible inhibitory effect of decavanadate on the IP3-induced Ca2+ release. Among the vanadium species tested (decavanadate, oligovanadate and monovanadate), only decavanadate was inhibitory, with a half-maximal effect at 5 mumol/l in both cell types. The effect of decavanadate could be overcome by increasing the amount of sequestered Ca2+ or added IP3. Decavanadate did not affect the ATP-driven Ca2+ uptake but oligovanadate was inhibitory on Ca2+ uptake. p-Hydroxymercuribenzoate (pHMB) at concentrations between 10 and 30 mumol/l also inhibited the Ca2+ release due to IP3. Thiol compounds such as dithiothreitol (DTT; 1 mmol/l) added before pHMB removed all its inhibitory effect on the IP3-induced Ca2+ release, whereas the inhibition caused by decavanadate was unaffected by DTT. Thus, the decavanadate-dependent inhibition functions by a distinctly different mechanism than pHMB and could serve as a specific tool to analyse various aspects of the IP3-induced Ca2+ release within endocrine cells.

Adenosine Triphosphate↗

PubMed1965

COMPLEMENT: INACTIVATION OF SECOND COMPONENT BY P-HYDROXYMERCURIBENZOATE.

p-Hydroxymercuribenzoate inactivates the second component of complement whether it is in solution or is fixed to a sensitized erythrocyte together with the first and fourth components. Inactivation by the drug is blocked but not reversed by cysteine. Partial purification of the second component of complement is described.

Benzoates↗

PubMed1989

Phasic effects of glucose, p-hydroxymercuribenzoate, and lysophosphatidylcholine on insulin secretion from HIT cells.

Monolayer cultures of HIT cells were superfused to examine phasic insulin secretion. A biphasic pattern of insulin secretion was observed when cells were stimulated with a constant glucose concentration as low as 0.28 mM, with increasing stimulation at 0.56, 1.7, and 5.6 mM glucose. Higher glucose concentrations did not increase insulin secretion. In the absence of glucose, p-hydroxymercuribenzoate (15, 30, and 50 microM), which blocks the reacylation of lysophospholipids with arachidonic acid, also evoked a concentration-dependent biphasic release of insulin. Lysophosphatidylcholine (50, 75, and 100 micrograms/ml) also caused a concentration-dependent biphasic release of insulin in the absence of glucose. These observations were similar to those previously reported for superfused monolayer culture of rat islet cells and suggest that the HIT cell is a beta-cell line that may be valuable in the further examination of the relationships among glucose, phospholipid metabolism, and insulin secretion. The data are consistent with the hypothesis that glucose-stimulated release of lysophospholipids may be important in initiation of the biphasic pattern of glucose-stimulated insulin release.

Animals↗

PubMed1986

Putative roles for lysophospholipids as mediators and lipoxygenase-mediated metabolites of arachidonic acid as potentiators of stimulus-secretion coupling: dual mechanisms of p-hydroxymercuribenzoic acid-induced insulin release.

This paper explores the mechanism whereby insulin (I) secretion is stimulated by p-hydroxymercuribenzoic acid (PHMB), an agent which inhibits the esterification of arachidonic acid (AA) into phospholipids in intact rat islets. An effect of PHMB on I release could be seen even at substimulatory glucose concentrations (0-1.7 mM) and was resistant to blockade of energy flux using antimycin A, or of glucose metabolism using mannoheptulose. It was, however, inhibited by Ni++, Co++, La , replacement of chloride in the buffer by the impermeant anion isethionate or reduced ambient temperature (16 degrees C), but not by extracellular Ca++ depletion or 8-(N,N-diethylamino) octyl 3,4,5-trimethoxy-benzoate hydrochloride (a putative stabilizer of intracellular Ca++ stores); thus PHMB's effect may require the translocation of membrane-associated Ca++ stores, leading to exocytotic hormone release. Although PHMB increases the accumulation of lipoxygenase-derived metabolites of AA, I secretion at 1.7 mM glucose unexpectedly was resistant to cyclooxygenase or lipoxygenase inhibition and could not be reproduced by exogenous AA (0.18 through 262 microM). However, it could be mimicked closely by exogenous lysophosphatidylcholine, which also shared with PHMB an identical profile of reversibility and pharmacologic inhibitability. Lysophospholipid (lyso-PL)-induced I release could not be attributed to detergent effects because, for example, it occurred in the absence of significant 51Cr release. The lyso-PL effect demonstrated structural specificity (lysophosphatidyl-ethanolamine and lysophosphatidylserine being essentially inactive) and was specific for lyso-PLs as neither phosphatidylcholine itself nor glycerophosphorylcholine (the deacylation product of lysophosphatidylcholine) had any effect. In contrast to the effects of lyso-PLs, the energy-dependent effects of glucose (16.7 mM) or the amino acid alpha-ketoisocaproic acid (15 mM) on I release were abrogated by inhibitors of phospholipases or lipoxygenase. This effect of phospholipase inhibition could be circumvented by exogenous lyso-PLs. We conclude that lyso-PLs (generated by energy-dependent phospholipid deacylation or by inhibition of reacylation) may be true mediators of I release, whereas the role of concomitantly generated oxygenation products of AA is restricted to the modulation of stimulated release.

Animals↗