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Methyl ketone formation during degradation of phenoxybutyric acid by Penicillium canescens SBUG-M 1139.

Penicillium canescens SBUG-M 1139 was shown to be able to grow using phenoxybutyric acid as the sole carbon source. The rapid conversion of the phenoxyalkanoic acid resulted in the formation of phenol, which was metabolized completely. These reactions were accompanied by an accumulation of the methyl ketone phenoxypropan-2-one. Furthermore, during the metabolism of phenoxybutyric acid, 4-phenoxy-2,3-dehydrobutyric acid, 4-phenoxy-3-hydroxybutyric acid, phenoxyacetic acid, and phenoxypropan-2-ol accumulated in minor amounts. Clearly, fungi can metabolize phenoxyalkanoic acids to produce methyl ketones in a manner analogous to that used for the conversion of short- or medium-chain fatty acids by fungi.

Biodegradation, Environmental↗

Evidence for the primary role for 4-aminopyridine-sensitive K(v) channels in beta(3)-adrenoceptor-mediated, cyclic AMP-independent relaxations of guinea-pig gastrointestinal smooth muscles.

Gastrointestinal smooth muscles exhibit relaxation in response to the stimulation of beta-adrenoceptors with catecholamines. Subtypes of beta-adrenoceptors which mediate catecholamine-elicited relaxations in gastrointestinal smooth muscles are predominantly atypical beta-adrenoceptors including beta(3)-adrenoceptors. Gastrointestinal smooth muscle relaxations mediated via beta(3)-adrenoceptors can occur independently of intracellular cyclic adenosine monophosphate (AMP) elevation. One of the mechanisms responsible for cyclic AMP-independent smooth muscle relaxation following activation of G(s) protein-coupled receptors could be activation of voltage-gated K(+) channels. In the present study, possible contribution of two types of K(+) (large-conductance, Ca(2+)-sensitive and voltage-gated K(+), BK(Ca); voltage-gated, K(v)) channels to beta(3)-adrenoceptor-mediated, cyclic AMP-independent relaxations was compared in gastric fundus and duodenum smooth muscles isolated from the guinea-pig. In these gastrointestinal smooth muscles, three catecholamines ((-)-isoprenaline, (-)-noradrenaline and (-)-adrenaline) and two beta(3)-adrenoceptor agonists ((R(*), R(*))-(+/-)-4-[2-[(2-(3-chlorophenyl)-2-hydroxyethyl)amino]propyl]phenoxyacetic acid sodium (BRL37344) and (+/-)-[4-[3-[(1,1-dimethylethyl)amino]-2-hydroxypropoxy] -1,3-dihydro-2H-benzimidazol-2-one] hydrochloride ((+/-)-CGP12177A)) elicited a concentration-dependent relaxation in the presence of beta(1)- and beta(2)-adrenoceptor antagonists. The relaxations were unaffected by an adenylyl cyclase inhibitor, SQ-22536 (100 microM), which indicates their characteristic of cyclic AMP-independency. On the other hand, the SQ-22536-resistant, beta(3)-adrenoceptor-mediated relaxant components were potently attenuated when the tone was raised using high-KCl (80 mM) or in the presence of a K(v) channel blocker, 4-aminopyridine (4-AP, 1-3 mM). Iberiotoxin (100 nM), a selective blocker of BK(Ca) channels which significantly contribute to cyclic AMP-independent vascular smooth muscle relaxations induced through activation of G(s) protein-coupled receptors, did not apparently show any inhibitory effects on SQ-22536-resistant, beta(3)-adrenoceptor-mediated relaxations in these gastrointestinal smooth muscles. The present results indicate that 4-AP-sensitive K(v) channels play a primary role in beta(3)-adrenoceptor-mediated, cyclic AMP-independent relaxations of guinea-pig gastrointestinal smooth muscles. In these smooth muscles, BK(Ca) channels seem to apparently contribute insignificantly to cyclic AMP-independent relaxations following stimulation of beta(3)-type of adrenoceptors.

4-Aminopyridine↗

Tools to study beta3-adrenoceptors.

Beta(3)-adrenoceptors mediate some of the effects of catecholamines on tissues such as blood vessels or the urinary bladder and are putative targets for the treatment of diseases such as the overactive bladder syndrome. Progress in the understanding of the presence, function, and regulation of beta(3)-adrenoceptors has been hampered by a lack of highly specific tools. "Classical" beta(3)-adrenoceptor agonists such as BRL 37,344 [(R*, R*)-(+/-)-4[2-[(3-chlorophenyl)-2-hydroxyethyl) amino] propyl] phenoxyacetic acid] and CGP 12,177 [(+/-)-4-(3-t-butylamino-2-hydroxypropoxy)benzimidazol-2-one] are only partial agonists in many settings, have limited selectivity over other beta-adrenoceptor subtypes, and may additionally act on receptors other than beta-adrenoceptors. More efficacious and more selective agonists have been reported and, in some cases, are in clinical development but are not widely available for experimental studies. The widely used antagonist SR 59,230 [3-(2-ethylphenoxy)-1-[(1,S)-1,2,3,4-tetrahydronapth-1-ylamino]-2S-2-propanoloxalate] is not selective for beta(3)-adrenoceptors, at least in humans, and may actually be a partial agonist. Radioligands, which are suitable either for the selective labeling of beta(3)-adrenoceptors or for the nonselective labeling of all beta-adrenoceptor subtypes, are also missing. beta(3)- and beta(1)/beta(2) double knockout mice have been reported, but their usefulness for extrapolations in humans is questionable based upon major differences between humans and rodents with regard to the ligand recognition and expression profiles of beta(3)-adrenoceptors. While the common availability of more selective agonists and antagonists at the beta(3)-adrenoceptor is urgently awaited, the limitations of the currently available tools need to be considered in studies of beta(3)-adrenoceptor for the time being.

Adrenergic beta-3 Receptor Agonists↗

Applying non-parametric statistical methods to the classical measurements of inclusion complex binding constants.

A study on using non-parametric statistical methods was carried out to calculate the binding constant of an inclusion complex and to estimate its associated uncertainty. First, a correct evaluation of the stoichiometry was carried out in order to ensure an accurate determination of the binding constant. For this purpose, the modified Benesi-Hildelbrand method had been previously applied. Then, four statistical methods (three non-parametric methods: two bootstrap approaches, the jackknife method and a parametric one: Fieller's theorem) were employed in order to compute the binding constant. The results obtained from applying these methods and the combination of the methods: jackknife after bootstrap and bootstrap after jackknife were compared. The best results in terms of accuracy were obtained from the application of a bootstrap method: the resampling residuals approach. These procedures were applied to the inclusion complex 2-hydroxil-propyl-beta-cyclodextrin-2,4-dichloro-phenoxyacetic, which shows photochemically-induced fluorescence.

Binding Sites↗

Enhanced production of penicillin V acylase from Streptomyces lavendulae.

A 28 degrees C, Streptomyces lavendulae produced high levels of penicillin V acylase (178 IU/l of culture) when grown on skim milk as the sole nutrient source for 275 h. The enzyme showed catabolite repression by glucose and was produced in the stationary phase of growth. Penicillin V was a good inducer of penicillin V acylase formation, while phenoxyacetic acid, the side-chain moiety of penicillin V, did not alter enzyme production significantly. The enzyme was stable between pH 6 and 11 and at temperatures from 20 degrees C to 55 degrees C. This extracellular enzyme was able to hydrolyse natural penicillins and unable to hydrolyse penicillin G.

Penicillin Amidase↗

Luminal transport step of para-aminohippurate (PAH): transport from PAH-loaded proximal tubular cells into the tubular lumen of the rat kidney in vivo.

Proximal tubular cells were loaded for 10 s with [3H]para-aminohippurate ([3H]PAH) by microperfusing the peritubular capillaries with Ringer solution containing 0.05 mmol/l PAH. Immediately thereafter [3H]PAH influx from cells into a column of equilibrium solution injected into the oil-filled tubular lumen was measured by re-aspirating the fluid after 1-10 s of contact time. The rise of luminal PAH concentration within 2 s of contact time was almost linear, reaching a luminal/capillary concentration ratio of 1.6 after 2 s and of 3.2 after 5 s. The 2-s PAH concentration ratio was not changed when different manoeuvres were applied to depolarize proximal tubular cells. Also, the 2-s PAH concentration ratio was not influenced by varying the luminal pH from 6.0 to 8.0 or the luminal Cl- concentration from zero to 134 mmol/l or when either 5 mmol/l urate or 25 mmol/l lactate was in the luminal perfusate. A decrease in the 2-s PAH concentration ratio, i.e. trans-inhibition, was observed when 25 or 50 mmol/l HCO3- (-50%) was in the luminal perfusate. Trans-inhibition was also seen with 5 mmol/l of the following substituted benzoates: 2-hydroxy-benzoate (-58%), 2-methoxy-benzoate (-46%), 2-hydroxy-benzoate-acetyl ester (-36%), 2-hydroxy-3,5-dinitro-benzoate (-48%), 3,5-dichloro-benzoate (-49%), and 2,3,5-trichloro-benzoate (-45%). No effect was seen with benzoate, 3-hydroxy-benzoate, 2-chloro-benzoate, 2-nitro-benzoate, 2,5-dinitro-benzoate, 3-sulfamoyl-benzoate and 4-sulfamoyl-benzoate. However, analogues of the latter two compounds possessing two additional side groups, such as furosemide and piretanide, or a hydrophobic moiety, such as probenecid, were inhibitory (by -62, -41 and -49% respectively). Phenoxyacetate had no effect; however, it inhibited if in addition it had three chloro groups, as in 2,4,5-trichlorophenoxyacetate (-71%) or a hydrophobic carbamoyl side group, as in mersalylic acid (salyrgan, -75%). Benzene-sulfonate trans-inhibited (-33%), as did phenolsulfonphthalein (phenol red, -39%) and sulfofluorescein (-55%). However, the trans-inhibitory effect of the corresponding carboxy-compounds was absent (phenolphthalein) or weaker (fluorescein, -42%). The trans-inhibitory effect of the uricosurics ethacrynic acid (-53%), tienilic acid (-55%) indacrinone (-72%) and benzbromarone (-42%) could be attributed to two chloro or bromo side groups on the benzene ring. Other trans-inhibiting uricosuric substances were indomethacin (-42%), sulfinpyrazone (-38%), losartan (-80%) its metabolite EXP 3174 (-55%), and AA 193 (-65%). These organic acids, with pKa values between 2.8 and 4.9, possess chloro and sulfin groups, as well as heterocyclic 5-ring and hydrophobic ring or chain areas. No significant effect was seen with 5 mmol/l PAH, 2-oxo-glutarate, DIDS, cGMP, prostaglandin E2, cortisol, benzylamiloride, pyrazinoic acid and 25 mmol/l lactate. Our data indicate that in situ the secretory luminal PAH transport proceeds in a non-rheogenic fashion, per exclusionem by anion exchange. The observed trans-inhibition of PAH secretion seems to correlate with the affinity for the luminal PAH transporter and, for uricosuric substances, with their uricosuric potency.

Animals↗

Precipitation of phenyl and phenoxypenicillin from solutions using ammonium sulfate.

An easy, rapid, and available method for separating 6-aminopenicillanic acid (6-APA), benzylpenicillin (penicillin G), and other related molecules from aqueous solutions or complex industrial broths is described. A high concentration of ammonium sulphate induces partially or totally the precipitation of the penicillin present in the solutions, while 6-APA, phenylacetic, and phenoxyacetic acid always remain in the supernatant. The filtration through No. 4 Pyrex glass-fiber filter or Whatman 3MM paper permits the separation of the compounds present in the supernatant from the other ones precipitated. The precipitated product was identified, in all cases, as ammonium penicillin. This method is described here for the first time.

Ammonium Sulfate↗

Immobilization of proteins via arginine residues.

A new method for activating polyacrylamide beads to bind proteins via arginine residues is described. The linking reagent, 4-(oxyacetyl)phenoxyacetic acid (OAPA), has been synthesized and characterized. OAPA reacts with arginine or N alpha-acetyl-L-arginine with a stoichiometry of 2 to 1. As expected for an arginine-specific reagent, OAPA inactivates horse liver alcohol dehydrogenase in a time-dependent manner, with the rate of this inactivation decreasing sixfold in the presence of 1 mM NADH. The presence of the carboxyl group in the linking reagent allows efficient coupling to aminated polyacrylamide beads. These derivatized beads are capable of binding various proteins via arginine residues in a time- and pH-dependent manner. Capacities range from less than 0.5 mg/ml to greater than 11 mg/ml, depending on the protein. The proteins are bound in a stable linkage, and preblocking the beads with either arginine or N alpha-acetyl-L-arginine eliminates all protein binding. Preblocking of the protein ubiquitin with OAPA reduces binding to a level compatible with the amount of underivatized ubiquitin remaining. The specificity, water solubility, negative charge, and linking ability of OAPA make it an especially valuable tool, both as a protein-modification reagent and as a linking reagent in preparing specialized affinity chromatographic media.

Acrylic Resins↗

Inactivation of Escherichia coli 2-amino-3-ketobutyrate CoA ligase by phenylglyoxal and identification of an active-site arginine peptide.

Treatment of homogeneous preparations of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli, a pyridoxal 5'-phosphate-dependent enzyme, with phenylglyoxal, 4-(oxyacetyl)phenoxyacetic acid, 2,3-butanedione, or 1,2-cyclohexanedione results in a time- and concentration-dependent loss of enzymatic activity. Phenylglyoxal in 50 mM phosphate buffer (pH 7.0) is the most effective modifier, causing > 95% inactivation within 20 min at 25 degrees C. Controls establish that this inactivation is not due to modifier-induced dissociation or photoinduced nonspecific alteration of the ligase. The substrate, acetyl CoA, or the coenzyme, pyridoxal 5'-phosphate, gives > 50% protection against inactivation. Enzyme partially inactivated by phenylglyoxal has the same Km value for glycine but the Vmax decreases in proportion to the observed level of inactivation. Whereas the native apoligase shows good recovery of activity with time in parallel with an increase in 428-nm absorptivity when incubated with pyridoxal 5'-phosphate, no such effects are seen with the phenylglyoxal-modified apoligase. Reaction of the enzyme with [14C]phenylglyoxal allowed for the isolation of a peptide which, by amino acid composition and sequencing data, was found to correspond to residues 349-378 in the intact enzyme. These results indicate that arginine residue-366 and/or residue-368 in the primary structure of E. coli 2-amino-3-ketobutyrate ligase is at the active site.

Acetyltransferases↗

Purification and properties of penicillin acylase of Bovista plumbea.

1. A penicillin acylase (penicillin amidohydrolase, EC 3.5.1.11) formed constitutively in the basidiomycete Bovista plumbea was purifed 220-fold by a combination of two gel filtration runs, ion-exchange chromatography on DEAE-cellulose, ultrafiltration and final chromatography on hydroxyapatite. Recovery was 40%. 2. The enzyme was clearly distinguished from penicillin acylases previously characterized: the molecular weight of the purified enzyme was evaluated by gel filtration to be 88 000. Km for the best substrate phenoxymethylpenicillin was 1.67 mM. The maximum of activity occurred at 52 degrees C and pH 7.5. The activation energy calculated by Arrhenius' graphic method was 16.45 kJ/mol. 3. Neither 8-hydroxyquinoline nor EDTA, iodoacetic acid, or the products of enzymatic cleavage, 6-aminopenicillanic acid or phenoxyacetic acid, showed any characteristic inhibition effect. 4. The substrate spectrum of the enzyme was elucidated. Phenoxymethylpenicillin was the best substrate. N-Acylamino acids, dipeptides, and tripeptides were not hydrolyzed; affinity occurred only towards penicillins lacking a nitrogen atom in the side chain acid. Penicillins with aryloxy residues possessing hydrophilic groups are favoured above aryl residues and short side chains above bulky ones.

Amidohydrolases↗

Effects of anionic xenobiotics on rat kidney. I--Tissue and mitochondrial respiration.

The polar 1,1,1-trichloro-2,2-bis(p-chlorophenyl)ethane (DDT) metabolite, 2,2-bis(p-chlorophenyl)acetic acid (DDA), and the phenoxyacetic acid herbicides, 2,4-dichlorophenoxyacetic acid (2,4-D) and 2,4,5-trichlorophenoxyacetic acid (2,4,5-T), were previously shown to be accumulated to high levels in liver and kidney via the organic acid transport system, raising the possibility of organ-specific toxicity secondary to transport. In these studies, accumulation of DDA was shown to depress oxygen consumption by renal cortical slices at high doses (0.1 and 1mM). Isolated renal and hepatic mitochondria were uncoupled by low doses of DDA (5-10 nmoles/mg mitochondrial protein. Maximal uncoupling was seen at 50-70 nmoles/mg. 2,4-D and 2,4,5-T also produced uncoupling, but at doses of 70 nmoles/mg or higher. All agents were more effective with alpha-ketoglutarate or pyruvate-malate), all three agents also depressed State 3 (ADP-stimulated) respiration. Again, DDA was more effective than 2,4-D or 2,4,5-T. These results suggest that accumulation of these or other anionic xenobiotics may lead to toxicity in those tissues possessing the organic anion transport system.

2,4,5-Trichlorophenoxyacetic Acid↗

Mechanism of ticrynafen potentiation of coumarin anticoagulant action.

Administration of the antihypertensive drug ticrynafen [2,3-dichloro-4-(2-thienylcarbonyl)-phenoxyacetic acid] has been reported to potentiate the effects of coumarin anticoagulants and to have caused hemorrhagic incidents in some patients. This drug interaction has now been reproduced in the rat. Ticrynafen administration enhanced the degree of hypoprothrombinemia and altered plasma and hepatic vitamin K epoxide concentrations in warfarin-treated rats. Ticrynafen did not affect vitamin K-dependent carboxylase or vitamin K epoxide reductase activities in vitro. Cytosolic DT-diaphorase was very sensitive to ticrynafen inhibition in vitro, and inhibition of vitamin K reduction via this enzyme is a possible mechanism by which ticrynafen potentiates coumarin anticoagulant action. Inhibition of this enzyme may also contribute to the reported hepatotoxicity of ticrynafen.

Animals↗

Inhibition of purified rat liver glutathione S-transferase isozymes by diuretic drugs.

Seven soluble rat liver glutathione S-transferase isozymes were isolated and the inhibition of these isozymes by selected diuretics was investigated using 1-chloro-2,4-dinitrobenzene as substrate. All isozymes were inhibited to some extent under the experimental conditions used, but there was significant isozyme dependent selectivity of inhibition. The greatest inhibitory effect (over 80%) was found when the phenoxyacetic acid diuretics and indacrynic acid were incubated with glutathione S-transferase 3-3, 3-4 and 4-4. The sulphamoylbenzoic acid diuretics, furosemide and bumetanide, were found to have a lesser effect on the isozymes studies. As glutathione S-transferase are thought to play an important protective role in the various tissues of animals and man, by catalysing the glutathione conjugation of electrophilic drugs and drug metabolites, their inhibition may be toxicologically important.

Animals↗

Sensitivity and selectivity of compounds interacting with neuropathy target esterase. Further structure-activity studies.

Assay of neuropathy target esterase (NTE) which accounts for about 70% of paraoxon-resistant phenyl valerate (PV) esterase activity of hen brain depends on the fact that it is selectively inhibited by mipafox. A previous study of structure/activity relationships (Biochem. Pharmac. 24, 797, 1975) has been extended. Among 14 potential substrates NTE hydrolysed phenyl phenoxyacetate and phenyl thiophenoxyacetate faster (1.5-1.7X) than PV, but selectivity of these substrates for NTE among the paraoxon-resistant esterases was only 35-52%. Seventy-seven other potential inhibitors (organophosphates, phosphonates, phosphoramidates, phosphinates and carbamates) were examined to determine I50NTE and effects on both NTE and "non-NTE" at 3-4 x I50NTE (I 85-95) and, where possible, at 6-20 X I50NTE. Hydrophophic inhibitors with small/flexible leaving groups were generally very inhibitory: several 2,2-dichlorovinyl phosphates and fluorides were active at low nanomolar concentrations. In the dichlorovinyl phosphate series increasing dialkyl chain length beyond n-pentyl decreased inhibitory power, presumably due to steric hindrance since the methyl/n-decyl ester was 15X more active than di-n-decyl. Chloro-substitution of both ortho-positions of a phenyl leaving group for benzylcarbamates reduced inhibitory power more than 20X but had little effect in a phenyl leaving group of methyl phenylphosphonates where the acyl-leaving group bond is longer and less subject to steric hindrance. N-phenylbenzohydroxamyl benzylcarbamate is 10X more potent than any previously described carbamate against NTE. Among stereo-isomers differences of activity ranged from less than 2- to 15-fold. Only diphenylphosphinyl fluoride appeared to be virtually specific for NTE: at 0.5-1 microM it inhibited ca.92% of NTE and 10-13% of "non-NTE" which is similar to the specificity found for 2,6-dichlorophenyl methyl phenylphosphonate which has been claimed to be specific. Diphenylphosphinyl fluoride has an advantage in that it is easily synthesized and should be protective rather than neuropathic, but it is not stable in store. We cannot repeat experiments purporting to show a substantial proportion of a second isozyme of NTE. However, according to first-order kinetics, concentrations of inhibitor greater than 6 X I50 should inhibit NTE greater than 98% and for 19 out of 26 compounds a residue greater than 3% (limit of precision) was found under these conditions: in nearly every case the quantity was 3-5%. This quantity may not be "true NTE" but it cannot be the target for organophosphate-induced delayed neuropathy since it is resistant to various neuropathic and protective compounds.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗

Irreversible inhibition of the TXA2/PGH2 receptor of human platelets by a photoaffinity ligand.

In order to tag the TXA2/PGH2 receptor of human platelets, we synthesized azido-BSP (= 4-[2-(4-azido-benzenesulfonylamino)-ethyl]phenoxyacetic acid), a photolabile derivative of the specific TXA2/PGH2 receptor antagonist sulotroban (= BM 13.177). If protected from UV light, azido-BSP competitively inhibited the shape change of human washed platelets stimulated by the TXA2 mimetic U 46619. Schild analysis revealed a pA2 = 6.7 (apparent KD = 0.2 mumol/l). Irreversible inhibition of the U 46619-induced platelet activation was achieved by irradiating for 5 min with UV light of 254 nm a platelet suspension containing azido-BSP. After subsequent washing, the platelets were stimulated with U 46619, ADP or PAF. Under these conditions azido-BSP inhibited the shape change, aggregation and [3H]serotonin release induced by U 46619 but not the shape change induced by ADP or PAF. The concentrations of azido-BSP which blocked the U 46619-induced [3H]serotonin release and the aggregation were 0.5 mumol/l and 1.0 mumol/l, respectively, whereas even 50.0 mumol/l of azido-BSP only partially inhibited the U 46619-stimulated shape change. Obviously, increasing numbers of thromboxane receptors have to be blocked in order to inhibit the [3H]serotonin release, the aggregation and the shape change. Even at an azido-BSP concentration equal to 250 times the apparent dissociation constant, enough receptor sites remained active to allow U 46619 to induce the shape change. In sulotroban was added prior to irradiation, the blocking effect of azido-BSP decreased with increasing concentrations of sulotroban. These results show that azido-BSP is a specific and high affinity ligand of the TXA2/PGH2 receptor and that it covalently links to the receptor under irradiation. Azido-BSP is a new tool to identify and characterize the TXA2/PGH2 receptor.

15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5↗

Increased cholesterol epoxide hydrolase activity in clofibrate-fed animals.

Cholesterol epoxide hydrolase (mCE) is a microsomal enzyme that hydrolyzes cholesterol-5,6-epoxides (CE) to cholestanetriol (CT). In the present study, hepatic mCE activity was measured in mice pretreated with several different xenobiotics known to induce a variety of hepatic drug-metabolizing enzymes. Only the phenoxyacetate hypolipidemics (clofibrate and ciprofibrate, included in the diet for 14 days) were found to increase hepatic mCE activity (1.8-fold increase). Clofibrate administration also increased rabbit hepatic (2.9-fold increase) and rat and rabbit renal mCE activity (1.5- and 2.3-fold increase respectively). On a subcellular level, mCE activities in rabbit nuclear and light mitochondrial fractions were increased (3.3- and 1.8-fold increase respectively), whereas activities in the cytosolic and heavy mitochondrial fractions were unchanged. In rabbits, clofibrate administration enhanced the hepatic microsomal hydrolysis of CE without increasing the hydrolysis of arene epoxides (benzopyrene-4,5-oxide) or fatty acid epoxides (methyl cis-9,10-epoxystearate). Increase of tissue mCE activity may significantly enhance tissue CT levels. In this light, it is worth noting similarities in the mechanisms of hypocholesterolemic action caused by clofibrate or CT administration.

Animals↗

Characterization of the thromboxane receptor mediating prostacyclin release from cultured endothelial cells.

The thromboxane A2 (TXA2) mimetic, 9,11-dideoxy-11,9-epoxymethano-prostaglandin F 2 alpha (U46619), mobilized calcium in the bovine aortic endothelial cell line AG4762 and stimulated release of prostacyclin from these cells. The U46619-stimulated release of prostacyclin could be inhibited by TXA2 antagonists with the order of potency [Is-[1 less than a, 2 less than b(5z), 3 less than b, 4 less than a]]-7-[3-[[2-[(phenylamino)carbonyl]hydrazino]methyl]-7-oxabicyclo- [2.2.1]hept-2-yl]-5- heptenoic acid (SQ29548) greater than 4-[2-(4-chlorobenzene-sulphonamido) ethyl]phenylacetic acid (BM13505) greater than 4-[2-(phenylsulphonamido)-ethyl]phenoxyacetic acid (BM13177), which was consistent with release being mediated by a TXA2 (TP) receptor. The TP receptor ligands, [3H]SQ29548 and 9,11-dimethylmethano-16(3-[125I]iodo-4-hydroxyphenyl)-13,14-dih ydr o-13-aza- 15-omega-o-tetranor-thromboxane ([125I]-PTA-OH), both appeared to bind to a homogenous population of sites in AG4762 cell membranes. The affinities of [3H]SQ29548 and [125I]PTA-OH were approximately 10 nM and approximately 0.3 nM, respectively, and the density of sites labelled by either ligand was approximately 25 fmol/mg protein. Under conditions where equilibrium was approached, the specific binding of [3H] SQ29548 or [125I]PTA-OH was displaced by SQ29548, BM13505 and BM13177 with the same order of potency and similar apparent affinities as in the functional assay, suggesting that these binding sites represent bona fide TP receptors.

Bradykinin↗

Correlation of beta 3-adrenoceptor-induced activation of cyclic AMP-dependent protein kinase with activation of lipolysis in rat white adipocytes.

The lipolytic action of the beta 3-adrenoceptor-selective agonist 4-[2-[(2-hydroxy-2-(3-chlorophenyl)ethyl)-amino]propyl]-phenoxyacetic acid (BRL 37344) was compared to that of isoprenaline in adipocytes derived from rat white adipose tissue. Concentration-response curves for activation of lipolysis by each agonist correlated well with the dose-response curves for activation of cAMP-dependent protein kinase (A-Kinase). Addition of propranolol at a concentration (0.1 microM) sufficient to block beta 1- and beta 2-adrenoceptors did not affect the stimulation of either parameter by BRL 37344 or isoprenaline, indicating that lipolysis was predominantly dependent on beta 3-adrenoceptor stimulation. Blockade of beta 3-adrenoceptors by 3 microM propranolol antagonized both A-Kinase activation and glycerol release. Activation of lipolysis by BRL 37344 was blocked by treatment of the cells with N-[2-p-(bromocinnamylamino)ethyl]-5-isoquinolinesulphonamide (H89) a potent and selective isoquinolinesulphonamide inhibitor of A-Kinase activity. Taken together, these results indicate that lipolysis in rat white adipocytes is primarily controlled by beta 3-adrenoceptors, and that cyclic AMP generation alone is responsible for activation of lipolysis in this tissue.

Adenylyl Cyclases↗