Postjunctional Localization of Substance P Receptors on the Rat Portal Vein

Mastrangelo, Dominique; Mathison, Ronald; Huggel, H

doi:10.1159/000137885

Cited by 10 publications

(7 citation statements)

References 17 publications

(24 reference statements)

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“…On isolated vessels in vitro, pretreatment with the antagonists similarly inhibited the responses to the complexes and to the respective native ligand, suggesting that both complex and respective native ligand bound to the same receptor. The selectivity was further confirmed (1) by the very low number of particles observed in the pig coronary artery when the selective NK 3 agonist senktide was used instead of SP as ligand in the complex (GPSenk), and (2) by the observation that GPSenk was, as senktide alone, totally inactive on the coronary artery strips which appear devoid of NK 3 receptors [5], whereas it was as active as senktide on the rat portal vein known to possess only NK 3 receptors [1, 15, 17]. …”

Section: Discussionmentioning

confidence: 99%

“…Everted portal veins of male Sprague-Dawley rats were prepared according to a previously described method [15, 17]; they were then opened longitudinally and fixed on a plastic support. Segments 4 mm in length and 1.0 mm in width with luminal surface up were fixed on rubber pieces and left until needed in ice-cold continuously gassed Krebs solution.…”

Section: Methodsmentioning

confidence: 99%

“…Transverse strips, 2 mm in width, of pig coronary arteries were prepared as already described [13]. Everted portal veins of male Sprague-Dawley rats were prepared according to a previously described method [15, 17]; only the contractile activity of the longitudinal muscle layer was studied. Tissues were suspended in thermostated (37°C) 180-µl organ baths under a resting tension of 1 (coronary strips) or 0.5 g (portal veins) and continuously superfused with warm (37°C) and oxygenated (95% O 2 , 5% CO 2 ) Krebs solution.…”

Section: Methodsmentioning

confidence: 99%

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Binding of Gold-Protein Ligand Complexes to Neurokinin Receptors

Cathieni

Taban²,

Sors³

et al. 1999

J Vasc Res

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Active neurokinin (NK) receptors were visualized with 5-nm colloidal gold-protein-substance P (GPSP) and -senktide (GPSenk) complexes on vascular tissues. Electron micrographs of pig coronary strips incubated with GPSP showed gold particles either bound to the plasmalemma or inside intracytoplasmic vesicles of endothelial cells. Preincubation with SP or the NK₁ receptor antagonist L-703606 prevented GPSP marking. No gold particles were seen after incubation with GPSenk. On coronary strips in vitro, which had been precontracted with U46619, GPSP induced relaxations similar to those produced by equimolar concentrations of SP, both relaxations being inhibited by L-703606. Analogous to senktide, GPSenk was totally inactive on arterial strips. Incubation of rat portal veins with GPSenk showed gold particles bound to the plasmalemma or inside intracytoplasmic vesicles of smooth muscle cells. Preincubation with senktide or the NK₃ receptor antagonist R-820 prevented GPSenk marking. On portal veins in vitro GPSenk induced contractions similar to those induced by equimolar concentrations of senktide or NKB; these effects were inhibited by R-820. Our results show that colloidal gold-protein complexes present biological activity and selectivity similar to those of their respective native ligand and detect the presence of active receptors; in addition, they suggest the presence of NK-receptor-mediated endocytosis in endothelial cells of coronary artery and in smooth muscle cells of the portal vein.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Binding of Gold-Protein Ligand Complexes to Neurokinin Receptors

Cathieni

Taban²,

Sors³

et al. 1999

J Vasc Res

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“…The rat portal vein responds to a variety of neurotransmitters, hormones, and neuropeptides with a vasoconstriction [11,13,14]. Several of these vasoactive agents are localized in intramural structures; noradrenaline, acetylcholine and substance P are found in nerve fibres [6,10,11,15] and now 5-HT has been positively identified in the mast cells.…”

Section: Discussionmentioning

confidence: 99%

Immunohistochemical evidence for mast cells containing 5-hydroxytryptamine in the rat portal vein

1986

Self Cite

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Serotonin was localized to mast cells in the adventitia of the rat portal vein by indirect immunohistochemistry. The mastocytes where preferentially localized to a region delimited by the pyloric and splenic veins. Since neither 48/80 nor reaginic antibody induced a significant change in the intrinsic spontaneous activity of the portal vein it would appear that the mast cells are not involved in a direct vasomotor function. It is suggested that amines released from the mastocytes could regulate blood flow in the vasa vasorum and/or have a role associated with the sensory functions displayed by this vein.

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“…Care was taken to keep the endothe lium of the artery intact. Ligatures were attached to both ends of the preparations which were then mounted under a resting isometric tension of 1 g in previously described [15] cylindrical microbaths (85 pi). The tissues were superfused continuously at a rate of 1 ml/min with a modified Krebs solution of the following composition (mM): 118.7NaCl, 4.7 KC1, 2.5 CaCL.…”

Section: Tissue Preparationmentioning

confidence: 99%

Pharmacological Evidence that Gold-Protein-Substance P Complex Activates Neurokinin NK<sub>1</sub> Receptors

Cathieni

Mastrangelo

Taban

1995

Cell Physiol Biochem

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The biological action of gold-protein-substance P (GPSP; BSA as protein), a complex recently developed to label substance P (SP) binding sites in brain sections, was investigated in pig coronary artery. This preparation, which shows a high sensitivity and selectivity to SP, possesses NK₁ neurokinin receptors restricted to the endothelial cells. As SP, GPSP produced dose-dependent vasodilation of pig coronary strips precontracted with 10^–5M prostaglandin F_2α. Molar-equivalent concentrations of GPSP complex were determined to allow quantitative compa∼risons with native SP. The respective potencies and intrinsic activities of GPSP and SP did not show any significant differences. Gold-protein-BSA (GPBSA) complex was ineffective. The effects of SP and GPSP were similarly inhibited by the neurokinin antagonist [D-Pro⁴, D-Trp^7,9, Nle¹¹]-SP (4–11). The presence of GPSP on endothelial cell membrane was evidenced by histology. These results strongly suggest that GPSP binds to neurokinin NK₁ receptors, and support the view that such complexes represent a new tool for the histological localization of binding sites.

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Postjunctional Localization of Substance P Receptors on the Rat Portal Vein

Cited by 10 publications

References 17 publications

Binding of Gold-Protein Ligand Complexes to Neurokinin Receptors

Binding of Gold-Protein Ligand Complexes to Neurokinin Receptors

Immunohistochemical evidence for mast cells containing 5-hydroxytryptamine in the rat portal vein

Pharmacological Evidence that Gold-Protein-Substance P Complex Activates Neurokinin NK<sub>1</sub> Receptors

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