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Biomedical subjects

M Waelbroeck

Publications and source records attributed to M Waelbroeck.

At least 91 records · Page 5Linked to original sources

CCK and gastrin inhibit adenylate cyclase activity through a pertussis toxin-sensitive mechanism in the tumoral rat pancreatic acinar cell line AR 4-2J.

(Thr28,Nle31)CCK(23-33) (CCK-9) and gastrin(1-17)I (gastrin) inhibited adenylate cyclase activity in membranes from the tumoral rat pancreatic acinar cell line AR 4-2J through a Bordetella pertussis toxin-sensitive mechanism. This contrasted with the stimulatory effect exerted by CCK-9 on adenylate cyclase activity in membranes from normal rat pancreas. The relative potency of CCK-9, gastrin, and related peptides in inhibiting adenylate cyclase, when confronted with previous evidence, suggests that 'non-selective CCK-gastrin CCK-B receptors' predominating over 'selective CCK-A receptors' in the AR 4-2J cell line, favored the coupling of the first receptors to adenylate cyclase through Gi, while CCK-A receptors capable of stimulating the enzyme through Gs were detected only after Bordetella pertussis toxin pretreatment.

Adenylate Cyclase Toxin↗

Stereoselectivity of the enantiomers of trihexyphenidyl and its methiodide at muscarinic receptor subtypes.

High stereoselectivity was observed for the enantiomers of trihexyphenidyl and trihexyphenidyl methiodide at muscarinic M1-receptors in field-stimulated rabbit vas deferens and at M2 alpha- and M2 beta-receptors in guinea-pig atrium and ileum, respectively. Considerably higher affinities (up to 1700-fold) were found for the (R)-(-)-enantiomers. The stereochemical demands made by the muscarinic receptor subtypes were most stringent at the M1-receptors. The (R)-(-)-enantiomers were found to be potent M1-selective antagonists (pA2 = 10.1/10.6). They showed a 91- and 45-fold selectivity for M1- over M2 alpha-receptors, respectively.

Animals↗

A new type of functional VIP receptor has an affinity for helodermin in human SUP-T1 lymphoblasts.

A new type of VIP receptor was characterized in human SUP-T1 lymphoblasts. The order of potency of unlabeled peptides, in the presence of [125I]helodermin, was: helodermin(1-35)-NH2 = helodermin(1-27)-NH2 greater than helospectin greater than VIP = PHI greater than [D-Ser2]VIP greater than [D-Asp3]VIP greater than [D-His1]VIP greater than or equal to [D-Ala4]VIP greater than or equal to secretin = GRF. This specificity was distinct from that of all VIP receptors described so far in that: (i) the affinity for helodermin (Kd = 3 nM) was higher than that of VIP (Kd = 15 nM) and PHI (Kd = 20 nM); and (ii) position 4 played an important role in ligand binding. The labeled sites were likely to be functional receptors as adenylate cyclase in crude lymphoblastic membranes (200-10,000 x g pellets) was stimulated by peptides, in the presence of GTP, with the following order of potency: helodermin(1-35)-NH2 greater than helodermin(1-27)-NH2 greater than helospectin = VIP = PHI.

Adenylyl Cyclases↗

80% of muscarinic receptors expressed by the NB-OK 1 human neuroblastoma cell line show high affinity for pirenzepine and are comparable to rat hippocampus M1 receptors.

The NB-OK 1 human neuroblastoma cell line expressed muscarinic cholinergic receptors that could be labeled with N-[3H]methylscopolamine (a nonselective antagonist). 80% of these receptors showed high affinity for pirenzepine, i.e. belonged to the M 1 subtype found in neuronal tissues. Their binding properties were identical to those of rat hippocampus M 1 receptors, and differed from those of rat pancreas and heart muscarinic receptors. The remaining (20%) muscarinic receptors showed low affinity for pirenzepine and AF-DX 116, being therefore of an M2 beta (or B) subtype, and were similar to rat pancreatic receptors.

Animals↗

Effect of freezing on the coupling of VIP receptors to adenylate cyclase in rat liver membranes.

In fresh rat liver plasma membranes, high affinity VIP receptors were specifically labelled with [125I] helodermin and were well coupled to adenylate cyclase while low affinity VIP receptors were not. After freezing and thawing low affinity VIP receptors were also coupled to adenylate cyclase. This modification of adenylate cyclase activation was specific for the VIP response as freezing and thawing did not modify Gpp (NH)p, NaF and glucagon stimulations.

Adenylyl Cyclases↗

Secretin receptors in human pancreatic membranes.

Crude membranes (27,000 g pellets) from five normal human pancreases were prepared. In the presence of GTP, the peptides of the secretin family stimulated adenylate cyclase activity, their order of potency being: secretin greater than helodermin greater than peptide histidine isoleucinamide (PHI) greater than or equal to vasoactive intestinal peptide (VIP) greater than growth hormone releasing factor (GRF) (1-29)-NH2. In addition, helodermin and PHI were more efficient than secretin. Secretin (3-27) inhibited fully the secretin stimulation and partially only the helodermin and PHI stimulation of the enzyme. Secretin receptors were investigated by the ability of secretin and related peptides to inhibit tracer binding. [125I]Secretin binding was fully inhibited by secretin (Kd 0.8 nM), helodermin (Kd 200 nM), and PHI (Kd 250 nM). VIP and GRF(1-29)-NH2 induced partial (20%) inhibition at a high 10 microM concentration. The fragments secretin (2-27), (3-27), (4-27), and (7-27) showed the same low potency and efficacy based on their ability to stimulate adenylate cyclase and to occupy secretin receptors. The analogues [Val5]secretin and [Ala2]secretin had a higher potency than secretin. Based on this comparison of adenylate cyclase stimulation and [125I]secretin binding inhibition, it is tempting to conclude that the human pancreas: (a) possesses highly specific secretin receptors and (b) such receptors could not fully account for the whole pattern of adenylate cyclase activation by related peptides, so that the presence of an added type of "helodermin-PHI-preferring" receptors is suggested.

Adenylyl Cyclases↗

Characterization of muscarinic receptors in human pancreatic membranes.

Crude membranes (27,000 x g pellets) from three normal human pancreata were prepared. Muscarinic receptors were investigated by the ability of three antagonists (atropine, pirenzepine, and AF-DX 116) and three agonists (carbamylcholine, oxotremorine, and pilocarpine) to inhibit [3H]NMS binding. These receptors showed for pirenzepine and AF-DX 116 a M2 beta specificity, typical of secretory glands and smooth muscle, that was comparable to that of rat pancreatic membranes, i.e., a low affinity for the two antagonists (Ki of 0.4 and 0.2 microM, respectively). In addition, these receptors were predominantly in a low affinity state for the agonist carbamylcholine (Ki of 100 microM).

Carbachol↗

Vasoactive intestinal peptide receptors in pancreas and liver. Structure-function relationship.

In purified rat pancreatic plasma membranes, (D-Phe4)PHI interacts as a selective VIP agonist for rat pancreatic VIP-preferring receptors, based on binding selectivity and adenylate cyclase activation, therefore allowing us to discriminate between the participation of VIP-preferring and secretin-preferring receptors in VIP stimulation. VIP-preferring receptors also bind GRF. They rely on disulfide bridges for their functional integrity. Their coupling with adenylate cyclase, based on the intrinsic activity of VIP analogues, is poor when compared to that of hepatic VIP receptors. In fresh rat liver plasma membranes, high-affinity VIP receptors are specifically labeled with [125I]helodermin and [125I]His1, D-Ala NLeu27)GRF and are well coupled to adenylate cyclase while low-affinity VIP receptors are not. The first subtype of VIP receptors is highly responsive to guanyl nucleotides and is easily altered by dithiothreitol. Only after freezing and thawing are low-affinity hepatic VIP receptors coupled to adenylate cyclase. Concerning the chemical characterization of VIP receptors, 66- and 35-kDa peptides are detected after specific [125I]VIP cross-linking with double agents in rat pancreatic membranes. In contrast, in intact pancreatic acini, the main source of radioactivity has a molecular mass of 130-180 kDa (with no contribution of intramolecular disulfide bridges), and an 80-kDa peptide is also detectable. The 66-kDa species in membranes can conceivably derive from the 80-kDa species observed in intact cells. Its molecular mass is higher than that of the 56-kDa [125I]VIP cross-linked protein previously observed in rat liver membranes. Besides, species differences between rat and guinea pig pancreas are also evident.

Adenylyl Cyclases↗

Effects of d-tubocurarine on rat cardiac muscarinic receptors: a comparison with gallamine.

Gallamine and d-tubocurarine inhibited (3H)N-methyl-scopolamine [3H)NMS) binding to rat cardiac muscarinic receptors with I50 values of 0.7 microM and 22 microM, respectively. They decreased the association and dissociation rates of the two ligands (3H)NMS and (3H)Oxotremorine M [3H)Oxo-M). Gallamine interaction with muscarinic receptors was markedly inhibited by (3H)NMS and (3H)Oxo-M binding to the receptors. We were unable to demonstrate (3H)NMS or (3H)Oxo-M binding to the muscarinic receptor-gallamine complex. By contrast, d-tubocurarine interaction with rat cardiac muscarinic receptors was facilitated by (3H)Oxo-M binding and only slightly inhibited by (3H)NMS binding to muscarinic binding sites. Furthermore, (3H)NMS and (3H)Oxo-M bound to the receptor-d-tubocurarine complex, indicating that the latter drug interacted with an allosteric site on cardiac muscarinic receptors but did not recognize the muscarinic binding site (at concentrations below 1 mM).

Animals↗

Different antagonist binding properties of rat pancreatic and cardiac muscarinic receptors.

The antagonist binding properties of rat pancreatic and cardiac muscarinic receptors were compared. In both tissues pirenzepine (PZ) had a low affinity for muscarinic receptors labelled by (3H)N-methylscopolamine [3)NMS) (KD values of 140 and 280 nM, respectively, in pancreatic and cardiac homogenates). The binding properties of pancreatic and cardiac receptors were, however, markedly different. This was indicated by different affinities for dicyclomine, (11-([(2-[diethylamino)-methyl)-1-piperidinyl] acetyl)-5, 11-dihydro-6H-pyrido(2,3-b)(1,4) benzodiazepin-6-on) (AFDX-116), 4-diphenylacetoxy-N-methyl-piperidine methobromide (4-DAMP) and hexahydrosiladifenidol (HHSiD). Pancreatic and cardiac muscarinic receptors also showed different (3H)NMS association and dissociation rates. These results support the concept of M2 receptor heterogeneity and confirm that M2 receptor subtypes have different binding kinetic properties.

Animals↗

[D-Phe4]peptide histidine-isoleucinamide ([D-Phe4]PHI), a highly selective vasoactive-intestinal-peptide (VIP) agonist, discriminates VIP-preferring from secretin-preferring receptors in rat pancreatic membranes.

The capacity of vasoactive intestinal peptide (VIP), peptide histidine-isoleucinamide (PHI), secretin, and a series of analogs to discriminate between VIP-preferring and secretin-preferring receptors that coexist in rat pancreatic plasma membranes was evaluated by their ability to inhibit [125I]iodo-VIP and [125I]iodo-secretin binding and to activate adenylate cyclase. VIP, the VIP analogs [D-His1]VIP, [D-Ser2]VIP, [D-Asp3]VIP and [D-Ala4]VIP, PHI, [D-Phe4]PHI, and secretin inhibited the binding of both ligands in a concentration range of 10(-11) M to 10(-5) M and with a selectivity factor varying from 18,000 to 0.1. The only exception was [D-Phe4]PHI that inhibited 125I-VIP binding only, with an IC50 of 7 nM, and with no inhibition of 125I-secretin binding at 10 microM. The peptides tested stimulated adenylate cyclase in the same membranes and the slope of the dose-effect curves indicated that all peptides, except [D-Phe4]PHI, interacted with at least two classes of receptors: VIP-preferring and secretin-preferring receptors. By contrast, the dose-effect curve of [D-Phe4]PHI activation of adenylate cyclase was monophasic and competitively modified by [D-Phe2]VIP (a VIP antagonist) but not by secretin(7-27) (a secretin antagonist), indicating an interaction with VIP-preferring receptors only. Thus, [D-Phe4]PHI appears to be a highly selective tool to characterize these receptors.

Adenylyl Cyclases↗

Muscarinic receptor heterogeneity in rat central nervous system. II. Brain receptors labeled by [3H]oxotremorine-M correspond to heterogeneous M2 receptors with very high affinity for agonists.

We compared the binding characteristics of muscarinic receptors labeled by [3H]oxotremorine-M ([3H]oxo-M) in homogenates of brain cortex and heart from rat. In both tissues [3H]oxo-M bound, with the same KD (6.5 nM), to a fraction of the receptors labeled by [3H]-N-methylscopolamine ([3H]NMS). This [3H]oxo-M receptor population represented, respectively, 15-20% and 35-40% of the total number of [3H]NMS receptors in cortex and heart. The three unlabeled agonists oxotremorine, carbamylcholine, and pilocarpine, when tested in competition with [3H]oxo-M, displayed a homogeneous super high affinity toward [3H]oxo-M-labeled receptors, and were unable to discriminate between brain and heart receptors labeled by [3H]oxo-M. By contrast, selective muscarinic antagonists showed some selectivity for either brain or heart [3H]oxo-M-labeled receptors. We analyzed competition curves between [3H]oxo-M and secoverine, pirenzepine, AF-DX 116, dicyclomine, or gallamine, assuming the existence of one or two receptor subclasses. Heart muscarinic receptors labeled by [3H]oxo-M were homogeneous M2 receptors of the C type with very low affinity for pirenzepine (Ki = 400 nM). Brain [3H]oxo-M-labeled receptors were heterogeneous receptors, with 30% (the B type) having a higher affinity for dicyclomine and a lower affinity for AF-DX 116 and gallamine than cardiac receptors, whereas the remaining 70% (the C type) showed "cardiac-like" binding properties. Both [3H]oxo-M-labeled subtypes in cortex homogenates had a low affinity for pirenzepine, indicating that [3H]oxo-M labeled only B and C (M2) receptors in this tissue. GTP inhibited completely [3H]oxo-M binding in heart homogenates with an IC50 at 300 nM. In cortex homogenates, GTP showed the same potency, but its efficacy was much lower (with only 30% maximal inhibition). [3H]oxo-M dissociation kinetics were monophasic in heart homogenates and biphasic in cortex homogenates. [3H]oxo-M dissociation from both tissues was slowed by gallamine and d-tubocurarine and accelerated by GTP. We found no correlation between B versus C [3H]oxo-M receptors, GTP-sensitive versus GTP-insensitive receptors, and rapidly versus slowly dissociating receptors, suggesting that [3H] oxo-M labeled a large variety of muscarinic receptor-regulatory protein complexes, all having an SH affinity for agonists.

Animals↗

Muscarinic receptor heterogeneity in rat central nervous system. I. Binding of four selective antagonists to three muscarinic receptor subclasses: a comparison with M2 cardiac muscarinic receptors of the C type.

We previously observed that [3H]NMS recognizes three types of muscarinic receptors in rat brain (one M1 subclass with high affinity for pirenzepine, and two M2 subclasses with low affinities for pirenzepine), based on distinct affinity and kinetic constants of [3H]NMS for these three subclasses. In this work, we investigated the binding of four selective antagonists to these three (the M1 and two M2) subclasses. We were able to demonstrate that cardiac-like M2 receptors with low affinity for pirenzepine and low affinity for N-methylscopolamine were present not only in cerebellum (as previously shown; see introduction) but also in cortex, striatum, and hippocampus, and the two M2 receptor subclasses were discriminated by dicyclomine, 4-DAMP, and gallamine, as well as by AF-DX 116 and [3H]NMS. Our findings also suggested that the biphasic association and dissociation kinetics of [3H]NMS observed in various brain regions reflect sequential binding to the different receptors.

Animals↗

Interaction of vasoactive intestinal peptide (VIP) and N-terminally modified VIP analogs with rat pancreatic, hepatic and pituitary membranes.

Six vasoactive intestinal peptide (VIP) analogs inhibited [125I]iodo-VIP and [125I]iodo-helodermin binding to high-affinity VIP receptors in rat hepatic membranes. They also stimulated adenylate cyclase activity through these receptors, their decreasing order of potency being VIP greater than [D-Ala4]VIP greater than [D-Asp3]VIP greater than [D-Ser2]VIP greater than [D-His1]VIP greater than [D-Phe2]VIP greater than [D-Arg2]VIP, with the latter two peptides acting as partial agonists only. All VIP analogs tested on rat pancreatic membranes were able to stimulate adenylate cyclase, their order of potency being very similar to that observed on hepatic membranes. [D-Ser2]VIP, [D-His1]VIP, [D-Arg2]VIP and [D-Phe2]VIP were partial agonists with an intrinsic activity of, respectively, 0.8, 0.7, 0.35 and 0.09 as compared to that of VIP = 1.0. [D-Phe2]VIP competitively and selectively inhibited VIP-stimulated adenylate cyclase activity (Ki = 0.1 microM). On male rat anterior pituitary homogenates the order of potency of the peptides was VIP greater than [D-Ala4]VIP greater than [D-Asp3]VIP greater than [D-Ser2]VIP greater than [D-His1]VIP. [D-Ser2]VIP and [D-His1]VIP acted as partial agonists. Besides, [D-Phe2]VIP and [D-Arg2]VIP were inactive as well as unable to inhibit VIP-stimulated adenylate cyclase activity. These results indicated that (a) the efficacy of VIP receptor/effector coupling depended on the tissue tested; (b) the possibility exists to design a VIP antagonist by appropriate modification in the N-terminal moiety of the molecule.

Adenylyl Cyclases↗

Secoverine is a non-selective muscarinic antagonist on rat heart and brain receptors.

In an attempt to determine if the selectivity of secoverine observed in vivo and in isolated tissues might be due to selective association with muscarinic receptor subtypes, we analyzed the binding of secoverine to three different receptors with specific radioligands: rat cardiac receptors (M2 receptors with low affinity for atropine), and rat cerebral cortical M1 receptors and M2 receptors with high affinity for atropine. At concentrations up to 10(-6) M, secoverine interaction with muscarinic receptors was competitive and of high affinity (Ki 4.10(-9) M) for cardiac and brain receptors. A detailed analysis using, in addition to [3H]N-methylscopolamine, the agonist [3H]oxotremorine-M (selective for high affinity binding sites at cardiac receptors) and the M1-selective antagonist [3H]pirenzepine at brain receptors, revealed identical affinities towards both receptor types, making it unlikely that secoverine distinguished the different muscarinic receptor subtypes. At concentrations between 10(-6) and 10(-3) M, secoverine interaction with an additional receptor site resulted in profound changes of tracer kinetics, suggesting the formation of a ternary complex (secoverine-radioligand-muscarinic receptor). The potency of secoverine for provoking this allosteric interaction was both tracer- and tissue-dependent. It is concluded that secoverine does not differentiate between M1, brain M2 and cardiac M2 receptors or between cardiac receptors with high, low and very low affinity for agonists. At very high concentrations secoverine recognized an allosteric site on the muscarinic receptors and reduced the dissociation rates of the 3H-ligands.

Allosteric Site↗

Alterations of rat cardiac adenylate cyclase activity with age.

Basal, 5'-guanylimidodiphosphate, GTP-, NaF-, forskolin-, D,L-isoproterenol-, glucagon- and secretin-stimulated adenylate cyclase activities were investigated in cardiac membranes from young adult (6 month old), old (20 month old) and senescent (24 month old) Sprague Dawley rats. The only significant difference between old and young adult rats was a 43% decrease of the glucagon-stimulated enzyme activity. In senescent rats compared to young adult rats, we observed a 23% decrease in forskolin-stimulated enzyme activity, a more severe (-73%) decrease in glucagon-stimulated adenylate cyclase activity and a decrease (-38%) of the response to secretin. The response to the beta-adrenoreceptor agonist D,L-isoproterenol was unaffected. These results suggest an alteration with age in the vicinity of the catalytic unit of adenylate cyclase and a selective decrease of functional glucagon and secretin receptors.

Adenylyl Cyclases↗

Modulation by n-alkanols of rat cardiac adenylate cyclase activity.

n-Alkanols (from methanol to decanol) have a biphasic effect on rat cardiac adenylate cyclase either basal or stimulated by GTP, GppNHp, NaF or hormones (isoproterenol, glucagon, secretin) in the presence of GTP. At high concentration, all the enzyme activities are inhibited. At low concentration, adenylate cyclase activity is either unchanged or potentiated depending on both the stimulus and the alkanols involved. Potentiation is due to an increase of maximum velocity with no change in the activation constant of the enzyme. Basal activity is unchanged as well as the isoproterenol- and glucagon-stimulated enzyme. The secretin-stimulated enzyme is potentiated. It is the guanyl nucleotide regulatory protein-mediated stimulation of adenylate cyclase which is mainly affected. An attempt was made to relate these effects on adenylate cyclase with physical parameters of the alkanols (partition coefficient). From the data obtained as a function of the alkanol chain-length and of temperature on the adenylate cyclase stimulated by GTP, GppNHp, NaF and permanently activated, it is concluded that the increase in efficacy observed in the presence of alkanol is due to an interaction with the protein moeity particularly with the guanyl nucleotide regulatory protein.

Adenylyl Cyclases↗

Comparative structural requirements of thirty GRF analogs for interaction with GRF- and VIP receptors and coupling to adenylate cyclase in rat adenopituitary, liver and pancreas.

The ability of 30 synthetic GRF(1-29)-NH2 analogs to stimulate adenylate cyclase activity was investigated in membranes from rat adenopituitary, rat liver and rat pancreas. In adenopituitary membranes, GRF and GRF analogs interacted with specific GRF receptors, whereas in liver and pancreatic membranes, they interacted with VIP receptors. The C-terminal moiety of GRF was responsible for GRF receptor recognition as the hybrid analog (His1, D-Ala2)-GRF(1-9), VIP(10-28) stimulated pituitary adenylate cyclase through the occupancy of VIP receptors only. When GRF or VIP receptors were occupied by GRF analogs, the N-terminal part of the ligand appeared critical for adenylate cyclase activation. This was established by testing 30 GRF analogs mono-, bi- or tri-substituted in positions 1 to 10. Major observations included: (a) the characterization of (N-Ac-Tyr1, D-Arg2)-GRF(1-29)-NH2 as an antagonist of GRF-stimulated pituitary adenylate cyclase; (b) the discovery of the (N-Ac-Tyr1, D-Phe2)-, (His1, D-Ala2, D-Ser3, NLeu27)-, and (His1, D-Ala2, D-Thr7, NLeu27)-derivatives of GRF(1-29)-NH2 as specific antagonists of VIP receptors in rat pancreatic membranes; (c) the importance of the free NH2 function of amino acid residue 1 for pancreatic adenylate cyclase activation, and (d) the decreased efficiency of iodinated (Tyr1)-GRF(1-29)-NH2 as opposed to the non iodinated form, in all systems tested.

Adenylyl Cyclases↗