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Journal articles on the topic 'Iodocyanopindolol'

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Published: 19 February 2023

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1

Kioumis, I., D. Ukena, and Peter J. Barnes. "Effect of nedocromil sodium on down-regulation of pulmonary β-adrenoceptors." Clinical Science 76, no. 6 (June 1, 1989): 599–602. http://dx.doi.org/10.1042/cs0760599.

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1. We have studied the effect of the anti-inflammatory anti-asthma drug, nedocromil sodium, on down-regulation of pulmonary β-adrenoceptors in guinea-pig lung. 2. Incubation of minced lung with isoprenaline (10 μmol/l) resulted in a reduction in maximum binding capacity of [125I]iodocyanopindolol to lung membranes from 246 ± 4 to 169 ± 6 fmol/mg of protein (mean ± sem, P < 0.01, n = 18). 3. Nedocromil sodium, which had no direct effect on [125I]iodocyanopindolol binding, prevented isoprenaline-induced down-regulation, giving complete protection at a dose of 100 μmol/l. 4. The mechanism of this effect is not certain, but nedocromil sodium may interfere with the internalization of β-adrenoceptors in pulmonary parenchymal cells. This may have some therapeutic relevance.

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2

Hoey, Andrew, Clifford Jackson, Graham Pegg, and Martin Sillence. "Atypical responses of rat ileum to pindolol, cyanopindolol and iodocyanopindolol." British Journal of Pharmacology 117, no. 4 (February 1996): 712–16. http://dx.doi.org/10.1111/j.1476-5381.1996.tb15248.x.

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3

Tiong, Alec H. K., and J. Steven Richardson. "Characterization of Rat Cerebral Cortical Beta Adrenoceptor Subtypes Using (-)-[125I]-Iodocyanopindolol." Journal of Receptor Research 9, no. 6 (January 1989): 495–508. http://dx.doi.org/10.3109/10799898909066073.

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4

Goldie, R. G., J. M. Papadimitriou, J. W. Paterson, P. J. Rigby, and D. Spina. "Autoradiographic localization of β-adrenoceptors in pig lung using [125I]-iodocyanopindolol." British Journal of Pharmacology 88, no. 3 (July 1986): 621–28. http://dx.doi.org/10.1111/j.1476-5381.1986.tb10243.x.

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5

Van Dort, Marcian E., David L. Gildersleeve, and Donald M. Wieland. "A rapid high yield synthesis of no-carrier-added (-)-[123I]iodocyanopindolol." International Journal of Radiation Applications and Instrumentation. Part A. Applied Radiation and Isotopes 42, no. 3 (January 1991): 309–11. http://dx.doi.org/10.1016/0883-2889(91)90094-h.

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6

Plourde, G., S. Rousseau-Migneron, and A. Nadeau. "Beta-adrenoceptor adenylate cyclase system adaptation to physical training in rat ventricular tissue." Journal of Applied Physiology 70, no. 4 (April 1, 1991): 1633–38. http://dx.doi.org/10.1152/jappl.1991.70.4.1633.

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The beta-adrenergic receptor adenylate cyclase system of ventricular tissue was evaluated in a group of rats submitted to a progressive 10-wk running program on a treadmill and compared with that in a group of rats maintained sedentary during the same period. Adequate training was confirmed by a 46% increase in the gastrocnemius isocitrate dehydrogenase activity in the trained group [1.50 +/- 0.04 vs. 1.03 +/- 0.06 (SE) pmol.g-1.min-1; P less than 0.01). Binding studies with [125I]iodocyanopindolol showed a 13% reduction in the density of beta-adrenergic receptors in trained rats (42.6 +/- 2.1 vs. 49.0 +/- 2.1 fmol/mg; P less than 0.05) without any significant modification in the dissociation constant. The amount of [125I]iodocyanopindolol bound to beta-adrenoceptors in the high-affinity state was reduced by 16.6% in trained rats (12.5 +/- 0.9 vs. 15.0 +/- 0.5 fmol/mg; P less than 0.05) without any significant changes for those in the low-affinity state, indicating a decrease in the coupling between the beta-adrenergic receptors and the guanine stimulatory binding protein. Furthermore, although the basal and sodium fluoride-stimulated adenylate cyclase activities were similar in the two groups of rats, the response of adenylate cyclase maximally stimulated by 10(-5) M isoproterenol was reduced by 16% in trained rats (29.7 +/- 1.4 vs. 35.3 +/- 1.3 pmol.mg-1.min-1; P less than 0.05).(ABSTRACT TRUNCATED AT 250 WORDS)

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7

Sundaresan, P. R., T. L. Fortin, and S. L. Kelvie. "Alpha- and beta-adrenergic receptors in proximal tubules of rat kidney." American Journal of Physiology-Renal Physiology 253, no. 5 (November 1, 1987): F848—F856. http://dx.doi.org/10.1152/ajprenal.1987.253.5.f848.

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Proximal tubules were isolated from the rat kidney by collagenase digestion of the cortical tissue followed by Percoll gradient centrifugation. Microscopic and hormone-stimulated adenylate cyclase activity studies proved the purity of the preparation. [3H]Prazosin, [3H]rauwolscine, and [125I]iodocyanopindolol were used to identify and quantitate respectively the alpha 1-, alpha 2- and beta-adrenergic receptors. Proximal tubular (F4) particulate fraction was compared against other cortical nephron segment (F1, F2) fractions and the total collagenase-digested cortex particulate suspension (Ft). Proximal tubules were enriched in alpha 1- and alpha 2-adrenergic receptors compared with Ft (alpha 1-receptor, 100.4 +/- 4.5 vs. 87.4 +/- 4.9; alpha 2-receptor, 250 +/- 16.2 vs. 185.1 +/- 12 fmol/mg protein). The fractions enriched in glomeruli and distal tubular segments (F1, F2) had relatively low concentrations of alpha 1- and alpha 2-adrenergic receptors. In contrast, beta-adrenergic receptor concentration in the proximal tubules was approximately 25% of that in the Ft fraction and approximately 10% of that in the F1 fraction. Isoproterenol-stimulated adenylate cyclase activities in the different fractions corroborated well with the pattern suggested by the [125I]iodocyanopindolol binding studies. Our results suggest that whole-cortex preparation radioligand binding studies may reflect proximal tubular alpha 1- and alpha 2-adrenergic receptor changes quite well. They may, however, miss or give erroneous impressions about beta-adrenergic receptor changes occurring in different cortical nephron segments.

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8

Morin, Didier, Roland Zini, Saïk Urien, Rosa Sapena, and Jean-Paul Tillement. "Labelling of Rat Brain ß-Adrenoceptors: (3H)CGP-12177 or (125I)Iodocyanopindolol?" Journal of Receptor Research 12, no. 3 (January 1992): 369–87. http://dx.doi.org/10.3109/10799899209074801.

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9

Leurs, R., F. D. Beusenberg, A. Bast, J. G. C. van Amsterdam, and H. Timmerman. "Identification ofβ 2-adrenoceptors on guinea pig alveolar macrophages using (−)-3-[125I]iodocyanopindolol." Inflammation 14, no. 4 (August 1990): 421–26. http://dx.doi.org/10.1007/bf00914093.

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10

Pranzatelli, Michael R., and Isabel Galvan. "Ontogeny of [125I]iodocyanopindolol-labelled 5-hydroxytryptamine1B-binding sites in the rat CNS." Neuroscience Letters 167, no. 1-2 (February 1994): 166–70. http://dx.doi.org/10.1016/0304-3940(94)91053-7.

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11

Kusumoto, F. M., K. G. Lurie, J. Dutton, H. Capili, and J. B. Schwartz. "Effects of aging on AV nodal and ventricular beta-adrenergic receptors in the Fischer 344 rat." American Journal of Physiology-Heart and Circulatory Physiology 266, no. 4 (April 1, 1994): H1408—H1415. http://dx.doi.org/10.1152/ajpheart.1994.266.4.h1408.

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The effects of aging on atrioventricular (AV) nodal and right and left ventricular beta-adrenergic receptor (beta-AR) characteristics were studied in Fischer 344 rat hearts using quantitative autoradiography. Twenty-micrometer-thick cardiac sections containing the compact AV node from 16 mature (4-6 mo old) rats, 6 middle-aged (12 mo old) rats, and 16 old (24 mo old) rats were incubated with [125I]iodocyanopindolol, [125I]iodocyanopindolol plus atenolol, or ICI 118551. Saturation experiments revealed a significant age-related decrease in AV nodal beta-AR density (mature: 190 +/- 46, middle-aged: 165 +/- 27, old: 133 +/- 34 amol/mm2; P < 0.01), with no change in affinity (mature: 106 +/- 62, middle-aged: 132 +/- 46, old: 128 +/- 66 pM). No age-related changes in AV nodal beta-AR subtype ratio (55% beta 1, 45% beta 2) or estimated compact AV node volume were detected (mature: 66 +/- 17, old: 65 +/- 23 microns 3). No difference in beta-AR density or affinity was detected between mature and old rats in either left (LV) or right (RV) ventricular tissue (LV, mature: 60 +/- 11, middle-aged: 59 +/- 11, old: 62 +/- 11 amol/mm2; RV, mature: 65 +/- 9, middle-aged: 65 +/- 11, old: 58 +/- 10 amol/mm2). beta-AR subtype ratios for the left ventricle (64% beta 1, 36% beta 2) and right ventricle (63% beta 1, 37% beta 2) did not significantly differ between mature and old rats. To summarize, aging from 4 to 24 mo in the Fischer 344 rat is associated with 1) a decrease in AV nodal beta-AR density with no change in affinity; 2) no change in volume of the compact region of the AV node; 3) no change in beta-AR subtype ratio in the AV node, left ventricle, or right ventricle; and 4) no change in either RV or LV beta-AR density.

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12

Johnson, C. Carl, and Bruce A. Fuchs. "Time Dependent Uptake of (-)125I-Iodocyanopindolol but not (-)125I-Iodopindolol by Murine Splenic Lymphocytes." Journal of Receptor Research 11, no. 6 (January 1991): 959–64. http://dx.doi.org/10.3109/10799899109064690.

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13

Bree, F., T. Souchet, R. Baatard, C. Fontenaille, F. Lhoste, and J. P. Tillement. "Inhibition of (−)[125I]-iodocyanopindolol binding to rat lung beta adrenoceptors by uremic plasma ultrafiltrates." Biochemical Pharmacology 36, no. 19 (October 1987): 3121–25. http://dx.doi.org/10.1016/0006-2952(87)90621-6.

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14

Gando, Satoshi, Yuichi Hattori, Masayuki Endou, and Morio Kanno. "Influence of experimental diabetes on [125I] iodocyanopindolol (ICYP) binding to β-adrenoceptors in rat heart." Japanese Journal of Pharmacology 58 (1992): 153. http://dx.doi.org/10.1016/s0021-5198(19)48959-2.

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15

Sugasawa, Toshinari, Gerlinde Lenzen, Stéphane Simon, Jun Hidaka, Aude Cahen, Jean-Luc Guillaume, Luc Camoin, A. Donny Strosberg, and Clara Nahmias. "The iodocyanopindolol and SM-11044 binding protein belongs to the TM9SF multispanning membrane protein superfamily." Gene 273, no. 2 (August 2001): 227–37. http://dx.doi.org/10.1016/s0378-1119(01)00587-x.

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16

Hoyer, Daniel, Günter Engel, and Hans O. Kalkman. "Characterization of the 5-HTIB recognition site in rat brain: Binding studies with (−)[125I]Iodocyanopindolol." European Journal of Pharmacology 118, no. 1-2 (November 1985): 1–12. http://dx.doi.org/10.1016/0014-2999(85)90657-0.

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17

Goldie, Roy G., Domenico Spina, Paul J. Rigby, and James W. Paterson. "Autoradiographic localisation of ascorbic acid-dependent binding sites for [125I]iodocyanopindolol in guinea-pig trachea." European Journal of Pharmacology 124, no. 1-2 (May 1986): 179–82. http://dx.doi.org/10.1016/0014-2999(86)90141-x.

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18

Pinto, J. E., A. J. Nazarali, T. Torda, and J. M. Saavedra. "Autoradiographic characterization of beta-adrenoceptors in rat heart valve leaflets." American Journal of Physiology-Heart and Circulatory Physiology 256, no. 3 (March 1, 1989): H821—H827. http://dx.doi.org/10.1152/ajpheart.1989.256.3.h821.

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beta-Adrenoceptors were localized and characterized in valve leaflets of the rat heart. Sixteen micrometer-thick tissue sections containing the mitral and aortic valves were incubated with (-)3-[125I]iodocyanopindolol followed by autoradiography with computerized microdensitometry and comparison with 125I-labeled standards. beta-Adrenoceptors were present in all the valves studied. The selective beta 1-adrenoceptor antagonist CGP 20712 A (100 nM) displaced not more than 20% of the total binding sites, suggesting that most of the beta-adrenoceptors in the valve leaflets are of the beta 2-subtype. Forskolin-binding sites were detected in the mitral valve leaflet by incubation of adjacent tissue sections with [12-3H]forskolin. Our results indicate that catecholamines could regulate the function of the heart valves through stimulation of beta 2-adrenoceptors.

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19

Harmouch, A., C. Osuna, M. Rafii-El-Idrissi, J. R. Calvo, and J. M. Guerrero. "Binding of [125I]iodocyanopindolol by rat Harderian gland crude membranes: Kinetic characteristics and day—night variations." Bioscience Reports 16, no. 5 (October 1, 1996): 369–77. http://dx.doi.org/10.1007/bf01207262.

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The Harderian glands are innervated by sympathetic fibers originating in the superior cervical ganglia. The aim of this study is to characterize the β-adrenergic receptors in the rat Harderian gland. The characteristics of β-adrenergic receptors were determined in crude membrane preparations from rat Harderian gland, using [125I]iodocyanopindolol ([125I]CYP) as radioligand. The binding of the ligand to the receptor is rapid, reversible, saturable, specific and dependent on time, temperature and membrane concentration. At 30 °C, stoichiometric data suggest the presence of one binding site with a Kd value of 0.29 nM and Bmax of 32 pmol/L. The interaction shows a high degree of specificity for β-adrenergic agonists and blockers, as suggested by competitive displacement experiments with isoproterenol (IC50=19.1 nM), propranolol (IC50=28.1 nM), and norepinephrine (IC50=96.3 nM). Clonidine, yohimbine, methoxamine, and prazosin are ineffective at concentrations up to 1 μM. In the other hand, binding of [125I]CYP by Harderian gland membranes exhibits day—night variations. Binding values are low during the daytime and increase progressively late in the evening to reach a maximum at 2200 h (2 h after the onset of dark period), but decreased to the end of the dark period (0600 h). In conclusion, the results presented in this paper show the functional and pharmacological characterization of β-adrenergic receptors in the rat Harderian gland. This neurotransmitter may play a physiological role at this level regulating, at least, processes such as a thyroid hormone metabolism.

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20

Liu, Jing, Man Sung Co, and Mark I. Greene. "Reovirus type 3 and [125I]-iodocyanopindolol bind to distinct domains on the beta-adrenergic like receptor." Immunologic Research 7, no. 3 (September 1988): 232–38. http://dx.doi.org/10.1007/bf02918138.

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21

Rigby, Paul J., Marion C. Passarelli, Glenn J. Self, Janet M. H. Preuss, and Roy G. Goldie. "Ascorbic acid-induced binding of [125I]-iodocyanopindolol to non-beta-adrenoceptor sites in guinea-pig trachea." Biochemical Pharmacology 37, no. 7 (April 1988): 1421–24. http://dx.doi.org/10.1016/0006-2952(88)90804-0.

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22

Slesinger, Paul A., Pedro R. Lowenstein, Harvey S. Singer, Lary C. Walker, Manuel F. Casanova, Donald L. Price, and Joseph T. Coyle. "Development of β1 and β2 adrenergic receptors in baboon brain: An autoradiographic study using [125I]iodocyanopindolol." Journal of Comparative Neurology 273, no. 3 (July 15, 1988): 318–29. http://dx.doi.org/10.1002/cne.902730304.

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23

Hamblin, Mark W., Peter I. Adriaenssens, Kayvan A. Ariani, Grace L. Tan, and Roland D. Ciaranello. "Photoaffinity labeling with [125I]-iodocyanopindolol diazirine reveals region specific differences among rat brain 5-HT1B receptors." Biological Psychiatry 25, no. 7 (April 1989): A45. http://dx.doi.org/10.1016/0006-3223(89)91577-1.

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24

ABRAHAM, G., O. E. BRODDE, and F. R. UNGEMACH. "Identification and characterisation of β-adrenoceptors on intact equine peripheral blood lymphocytes with the radioligand (-)-[125I]-iodocyanopindolol." Equine Veterinary Journal 33, no. 5 (January 5, 2010): 487–93. http://dx.doi.org/10.2746/042516401776254862.

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25

Pranzatelli, Michael R., and Parisa Razi. "Drug-Induced Regulation of [125I]Iodocyanopindolol-labeled 5-Hydroxytryptamine1B Receptor Binding Sites in the Central Nervous System." Neuropsychopharmacology 10, no. 4 (July 1994): 259–64. http://dx.doi.org/10.1038/npp.1994.29.

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26

TSUCHIHASHI, HIROSHI, and TAKAFUMI NAGATOMO. "Binding characteristics of 125I-iodocyanopindolol to .BETA.-adrenergic receptors: Biphasic Scatchard plots. II. Effects of selective antagonists." CHEMICAL & PHARMACEUTICAL BULLETIN 35, no. 8 (1987): 3425–32. http://dx.doi.org/10.1248/cpb.35.3425.

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27

Fraeyman, N., and P. Vanscheeuwijck. "Effect of Age on the Kinetics of the Binding of Iodocyanopindolol to a Membrane Preparation of Rat Lungs." Journal of Receptor Research 11, no. 6 (January 1991): 985–99. http://dx.doi.org/10.3109/10799899109064692.

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28

Gurguis, George N. M., Jukka Turkka, and Markku Linnoila. "Effects of serotonin and metergoline on 125[I]-iodocyanopindolol binding parameters to beta-adrenergic receptors in rat brain." European Neuropsychopharmacology 8, no. 2 (May 1998): 131–40. http://dx.doi.org/10.1016/s0924-977x(97)00059-x.

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29

Bundkirchen, Andreas, Klara Brixius, Birgit Bölck, Quang Nguyen, and Robert H. G. Schwinger. "β1-adrenoceptor selectivity of nebivolol and bisoprolol. A comparison of [3H]CGP 12.177 and [125I]iodocyanopindolol binding studies." European Journal of Pharmacology 460, no. 1 (January 2003): 19–26. http://dx.doi.org/10.1016/s0014-2999(02)02875-3.

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30

Condorelli, D. F., R. Avola, N. Ragusa, S. Reale, M. Renis, R. F. Villa, and A. M. Giuffrida Stella. "G protein dependent alterations in [125I] iodocyanopindolol and ±cyanopindolol binding at 5HT1B binding sites in rat brain membranes." Neurochemical Research 14, no. 12 (December 1989): 1245. http://dx.doi.org/10.1007/bf00965517.

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31

Cervantes-Olivier, P., C. Delavier-Klutchko, O. Durieu-Trautmann, S. Kaveri, M. Desmandril, and A. D. Strosberg. "The β2-adrenergic receptors of human epidermoid carcinoma cells bear two different types of oligosaccharides which influence expression on the cell surface." Biochemical Journal 250, no. 1 (February 15, 1988): 133–43. http://dx.doi.org/10.1042/bj2500133.

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The beta 2-adrenergic receptors of the human epidermoid carcinoma A431 cells reside on two polypeptide chains revealed by photoaffinity labelling with [125I]iodocyanopindolol-diazirine. These proteins correspond to two distinct populations of N-asparagine-linked glycoproteins: the 55-52 kDa molecules are associated with complex carbohydrate chain(s), the 65-63 kDa component with polymannosidic carbohydrate chain(s). Both types of receptors are present in preconfluent cells, but only the polymannosidic type is found in the postconfluent cells. Moreover, complex chains appear to be associated with the receptors with the highest affinity for (-)-isoproterenol and polymannosidic chains with the receptors with the lowest affinity for this agonist. the carbohydrate moiety of the beta-adrenergic receptor is involved in the expression and function of the beta 2-adrenergic receptors at the surface of the A431 cells, since tunicamycin and monensin, complete and partial inhibitors of glycosylation respectively, diminish the number of binding sites at the cell surface and increase the total number of sites in the cell. In these conditions a diminution of cyclic AMP accumulation is also observed.

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32

Wang, H. Y., M. Berrios, and C. C. Malbon. "Localization of β-adrenergic receptors in A431 cells in situ. Effect of chronic exposure to agonist." Biochemical Journal 263, no. 2 (October 15, 1989): 533–38. http://dx.doi.org/10.1042/bj2630533.

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The status of beta-adrenergic receptors was investigated in A431 cells exposed to chronic stimulation by the beta-adrenergic agonist, (-)-isoproterenol. Specific binding of beta-adrenergic antagonist (-)-[125I]iodocyanopindolol declined to 60-80% below control values within 12 h of agonist treatment. This decline in ligand binding was also observed in high-speed membrane fractions prepared from agonist-treated cells. Immunoblots probed with anti-receptor antibodies revealed both that beta-adrenergic receptors from untreated and treated cells migrated as 65,000-Mr peptides and that the cellular complement of receptor was unchanged. Indirect immunofluorescence localization of beta-adrenergic receptors was comparable in control (untreated) cells and cells challenged with (-)-isoproterenol for 1, 12, or 24 h. Thus receptor complement, migration on SDS/polyacrylamide-gel electrophoresis, and localization in situ are largely unaffected by agonist stimulation. Receptor binding of antagonist radioligands, in contrast, is markedly down-regulated in cells stimulated chronically with beta-adrenergic agonists. These data argue in favour of agonist-induced alteration(s) in the conformation of the receptor that preclude radioligand binding rather than agonist-induced receptor sequestration and/or degradation.

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33

Howard, M. J., M. D. Mullen, and P. A. Insel. "Amiloride interacts with renal alpha- and beta-adrenergic receptors." American Journal of Physiology-Renal Physiology 253, no. 1 (July 1, 1987): F21—F25. http://dx.doi.org/10.1152/ajprenal.1987.253.1.f21.

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We have used radioligand binding techniques to assess whether amiloride and certain analogues of amiloride (ethylisopropyl amiloride and benzamil) can bind to adrenergic receptors in the kidney. We found that amiloride could compete for [3H]rauwolscine (alpha 2-adrenergic receptors), [3H]prazosin (alpha 1-adrenergic receptors), and [125I]iodocyanopindolol (beta-adrenergic receptors) binding in rat renal cortical membranes with inhibitor constants of 13.6 +/- 5.7, 24.4 +/- 7.4, and 83.6 +/- 13.5 microM, respectively. Ethylisopropyl amiloride and benzamil were from 2- to 25-fold more potent than amiloride in competing for radioligand binding sites in studies with these membranes. In addition, amiloride and the two analogues competed for [3H]prazosin sites on intact Madin-Darby canine kidney cells and amiloride blocked epinephrine-stimulated prostaglandin E2 production in these cells. We conclude that amiloride competes for binding to several classes of renal adrenergic receptors with a rank order of potency of alpha 2 greater than alpha 1 greater than beta. Binding to, and antagonism of, adrenergic receptors occurs at concentrations of amiloride that are lower than previously observed “nonspecific” interactions of this agent.

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34

Sundaresan, P. R., M. M. Guarnaccia, and J. L. Izzo. "Adrenal medullary regulation of rat renal cortical adrenergic receptors." American Journal of Physiology-Renal Physiology 253, no. 5 (November 1, 1987): F1063—F1067. http://dx.doi.org/10.1152/ajprenal.1987.253.5.f1063.

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The role of the adrenal medulla in the regulation of renal cortical adrenergic receptors was investigated in renal cortical particulate fractions from control rats and rats 6 wk after adrenal demedullation. The specific binding of [3H]prazosin, [3H]rauwolscine, and [125I]iodocyanopindolol were used to quantitate alpha 1-, alpha 2-, and beta-adrenergic receptors, respectively. Adrenal demedullation increased the concentration of all three groups of renal adrenergic receptors; maximal number of binding sites (Bmax, per milligram membrane protein) for alpha 1-, and alpha 2-, and beta-adrenergic receptors were increased by 22, 18.5, and 25%, respectively (P less than 0.05 for each). No differences were found in the equilibrium dissociation constants (KD) for any of the radioligands. Plasma corticosterone and plasma and renal norepinephrine levels were unchanged, whereas plasma epinephrine was decreased 72% by adrenal demedullation (P less than 0.01); renal cortical epinephrine was not detectable in control or demedullated animals. Our results suggest that, in the physiological state, the adrenal medulla modulates the number of renal cortical adrenergic receptors, presumably through the actions of a circulating factor such as epinephrine.

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35

Abrass, C. K., S. W. O'Connor, P. J. Scarpace, and I. B. Abrass. "Characterization of the beta-adrenergic receptor of the rat peritoneal macrophage." Journal of Immunology 135, no. 2 (August 1, 1985): 1338–41. http://dx.doi.org/10.4049/jimmunol.135.2.1338.

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Abstract The beta-adrenergic receptor was characterized on BCG-activated rat peritoneal macrophage membranes by radio-ligand binding studies. Saturable binding with [125I]iodocyanopindolol (125I-ICYP) was demonstrated. With Scatchard analysis, rat macrophages demonstrate approximately 1000 receptors per cell with a Kd of 5 X 10(-11) M for 125I-ICYP. Competition curves with (-) and (+) propranolol at concentrations below 10(-6) M confirmed stereospecificity. The potency of various ligands to compete for 125I-ICYP binding sites followed the order: propranolol greater than isoproterenol greater than epinephrine greater than norepinephrine with apparent Kd of 2.0 X 10(-9), 3.9 X 10(-7), 1.0 X 10(-5), and 2.5 X 10(-5) M, respectively. Isoproterenol-stimulated adenylate cyclase activity was two-fold above basal activity. The potential physiologic significance of a beta-adrenergic receptor on rat peritoneal macrophages was suggested by a dose-dependent decrease in phagocytosis of soluble, model immune complexes (aggregated gamma-globulin) by macrophages incubated with metaproterenol. We conclude that the rat macrophage has a beta-adrenergic receptor and that catecholamines may thereby modulate macrophage function.

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36

Sandnes, D., T. Westergren, T. E. Sand, G. Sager, M. Refsnes, T. Christoffersen, and S. Jacobsen. "A Comparison of the Binding Characteristics of the β-Adrenoceptor Antagonists 3H-Dihydroalprenolol and 125I-Iodocyanopindolol in Rat Liver." Acta Pharmacologica et Toxicologica 55, no. 4 (March 13, 2009): 287–96. http://dx.doi.org/10.1111/j.1600-0773.1984.tb01984.x.

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37

Sugasawa, Toshinari, Masago Matsuzaki-Fujita, Jean-Luc Guillaume, Luc Camoin, Shigeaki Morooka, and A. Donny Strosberg. "Characterization of a Novel Iodocyanopindolol and SM-11044 Binding Protein, Which May Mediate Relaxation of Depolarized Rat Colon Tonus." Journal of Biological Chemistry 272, no. 34 (August 22, 1997): 21244–52. http://dx.doi.org/10.1074/jbc.272.34.21244.

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38

Craft, C. M., W. W. Morgan, D. J. Jones, and R. J. Reiter. "Hamster and Rat Pineal Gland ?-Adrenoceptor Characterization With Iodocyanopindolol and the Effect of Decreased Catecholamine Synthesis on the Receptor." Journal of Pineal Research 2, no. 1 (January 1985): 51–66. http://dx.doi.org/10.1111/j.1600-079x.1985.tb00627.x.

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39

Ariani, Kayvan, Mark W. Hamblin, Grace L. Tan, Carol A. Stratford, and Roland D. Ciaranello. "G protein dependent alterations in [125I]iodocyanopindolol and�cyanopindolol binding at 5-HT1B binding sites in rat brain membranes." Neurochemical Research 14, no. 9 (September 1989): 835–43. http://dx.doi.org/10.1007/bf00964812.

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40

Elkins, R. P., J. F. Kelly, and B. J. Rosenberg. "A radioreceptor assay in which iodocyanopindolol is used to determine propranolol and its active metabolites in unextracted serum or plasma." Clinical Chemistry 32, no. 1 (January 1, 1986): 180–83. http://dx.doi.org/10.1093/clinchem/32.1.180.

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Abstract This rapid, sensitive, simple radioreceptor assay (RRA) for l-propranolol and its active metabolites in unextracted samples requires 5 microL of sample, a beta-adrenergic antagonist, 125-l-labeled (-)cyanopindolol (125ICYP), and turkey erythrocyte membrane receptors (Kd = 40 pmol/L). Equal volumes (100 microL) of diluted sample and 125ICYP are incubated with 500 microL of erythrocyte membranes for 30 min. Cold isotonic saline (2.5 mL) is added, and the mixture is centrifuged. The concentration of drug that inhibited receptor binding by 50% (IC50) was l-propranolol, 1.5 micrograms/L; d-propranolol, 243 micrograms/L; and 4-hydroxypropranolol, 8.8 micrograms/L. Analytical recovery of propranolol added to serum was 93 to 120%; results for 138 clinical samples tested by this method and by liquid chromatography correlated well (r = 0.96). Results correlated strongly (r = 0.98) for 23 clinical samples tested by RRA and analyzed for both propranolol and 4-hydroxypropranolol by liquid chromatography. The sensitivity of this RRA was 0.3 micrograms/L, and both intra- and interassay CVs were less than 12%. Modifications of this method could permit testing of other nonselective beta-blockers.

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41

TSUCHIHASHI, Hiroshi, Yasuo NAKASHIMA, Junji KINAMI, and Takafumi NAGATOMO. "Characteristics of 125I-iodocyanopindolol binding to .BETA.-adrenergic and serotonin-1B receptors of rat brain: Selectivity of .BETA.-adrenergic agents." Japanese Journal of Pharmacology 52, no. 2 (1990): 195–200. http://dx.doi.org/10.1254/jjp.52.195.

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42

Tsuchihashi, H., Y. Nakashima, J. Kinami, and T. Nagatomo. "Characteristics of 125I-iodocyanopindolol binding to β-adrenergic and serotonin-1B receptors of rat brain: selectivity of β-adrenergic agents." European Journal of Pharmacology 183, no. 2 (July 1990): 404. http://dx.doi.org/10.1016/0014-2999(90)93286-y.

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43

Haddad, E. B., J. C. Mak, M. G. Belvisi, M. Nishikawa, J. Rousell, and P. J. Barnes. "Muscarinic and beta-adrenergic receptor expression in peripheral lung from normal and asthmatic patients." American Journal of Physiology-Lung Cellular and Molecular Physiology 270, no. 6 (June 1, 1996): L947—L953. http://dx.doi.org/10.1152/ajplung.1996.270.6.l947.

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We used human peripheral lung from 8 mildly asthmatic patients and 11 normal donors to study the expression of muscarinic and beta-adrenergic receptors in asthma. There was no significant difference in the affinity or the density of muscarinic (labeled with [N-methyl-3H]scopolamine) and beta 1- and beta 2-adrenergic receptors (labeled with [125I]iodocyanopindolol) in peripheral lung from asthmatics compared with nonasthmatics. Only the muscarinic m1 receptor mRNA was detected in human lung using Northern blot analysis. Additionally, peripheral lung cellular mRNA hybridized to human beta 1 and beta 2 cDNA probes, giving 3.2- and 2.2-kb hands corresponding to beta 1 and beta 2-adrenergic receptors mRNA, respectively. Densitometric scanning of the autoradiograms suggests that there was no significant difference in the relative abundance of muscarinic m1 and beta 1- and beta 2-adrenergic receptor mRNA in asthmatic compared with nonasthmatic lungs. Functional experiments obtained in trachea suggest that there was an increase in the cholinergic neural response evoked by electrical field stimulation in asthmatic compared with nonasthmatic tissues which was not due to a reduction in inhibitory noncholinergic nonadrenergic relaxations.

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44

Elfont, R. M., P. R. Sundaresan, and C. D. Sladek. "Adrenergic receptors on cerebral microvessels: pericyte contribution." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 256, no. 1 (January 1, 1989): R224—R230. http://dx.doi.org/10.1152/ajpregu.1989.256.1.r224.

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R224-R230, 1989.--[125I]iodocyanopindolol ([125I]ICYP) and [3H]rauwolscine were used to quantitate, respectively, the beta- and alpha 2-adrenergic receptors in freshly isolated bovine cerebral microvessels and in pericyte cultures derived from these microvessels. Morphological and immunocytochemical criteria distinguished the pericytes from endothelial cells. Competitive binding studies established the specificity of the radioligand binding. The maximal number of binding sites (Bmax) for [125I]ICYP in the pericytes constituted only 8% of that in the microvessels (3.5 +/- 1.3 vs. 44.4 +/- 6.6 fmol/mg protein). In contrast, the Bmax for [3H]rauwolscine in the pericytes was 50% of that in the microvessels (55.4 +/- 11.8 vs. 111.1 +/- 9.5 fmol/mg protein). The dissociation constants for both [125I]ICYP and [3H]rauwolscine were similar in the two preparations. No alpha 1-adrenergic receptors, as defined by the specific binding of [3H]prazosin, were identified either in the pericytes or microvessels. Overall, our results suggest that pericytes contribute minimally to the total beta-adrenoceptor number of cerebral microvessels, and thus the beta-adrenoceptors must be located predominantly on endothelial cells. However, the contribution of pericytes to the total alpha 2-adrenoceptor number of the microvessels may be substantial.

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45

Igawa, Akihiko, Takashi Nozawa, Naohiro Yoshida, Nozomu Fujii, Minoru Inoue, Shusaku Tazawa, Hidetsugu Asanoi, and Hiroshi Inoue. "Heterogeneous cardiac sympathetic innervation in heart failure after myocardial infarction of rats." American Journal of Physiology-Heart and Circulatory Physiology 278, no. 4 (April 1, 2000): H1134—H1141. http://dx.doi.org/10.1152/ajpheart.2000.278.4.h1134.

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We examined cardiac neuronal function and β-receptor with a dual-tracer method of [131I]meta-iodobenzylguanidine (MIBG) and [125I]iodocyanopindolol (ICYP) in rat heart failure after myocardial infarction (MI). In rats with MI, left ventricular (LV) systolic function decreased, and LV dimension and right ventricular (RV) mass increased gradually. MIBG accumulations of the noninfarcted LV (remote region) and RV decreased by 15% at 1 wk compared with sham-operated rats, and these accumulations were restored by 71% and 56%, respectively, at 24 wk compared with age-matched sham rats despite sustained depletion of myocardial norepinephrine contents in these regions. ICYP accumulation of the remote region and of the RV did not decrease at any stages. Myocardial MIBG distribution was heterogeneous at 1 wk when it was lower in the peri-infarcted region than in the remote region, associated with reduced ICYP accumulation in the peri-infarcted region. The heterogeneous distribution of both isotopes disappeared at 12 wk. Thus cardiac sympathetic neuronal alteration was coupled with downregulation of β-receptors in rat heart failure after MI. The abnormal adrenergic signaling occurred heterogeneously in terms of ventricular distribution and time course after MI.

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46

Schotten, Ulrich, Karsten Filzmaier, Britta Borghardt, Simone Kulka, Friedrich Schoendube, Carlos Schumacher, and Peter Hanrath. "Changes of β-adrenergic signaling in compensated human cardiac hypertrophy depend on the underlying disease." American Journal of Physiology-Heart and Circulatory Physiology 278, no. 6 (June 1, 2000): H2076—H2083. http://dx.doi.org/10.1152/ajpheart.2000.278.6.h2076.

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In human heart failure, desensitization of the β-adrenergic signal transduction has been reported to be one of the main pathophysiological alterations. However, data on the β-adrenergic system in human compensated cardiac hypertrophy are very limited. Therefore, we studied the myocardial β-adrenergic signaling in patients suffering from hypertrophic obstructive cardiomyopathy (HOCM, n = 9) or from aortic valve stenosis (AoSt, n = 8). β-Adrenoceptor density determined by [125I]iodocyanopindolol binding was reduced in HOCM and AoSt compared with nonhypertrophied, nonfailing myocardium (NF) of seven organ donors. In HOCM the protein expression of stimulatory G protein α-subunit (Gsα) measured by immunoblotting was unchanged, whereas the inhibitory G protein α-subunit (Gαi-2) was increased. In contrast, in AoSt, Gαi-2 protein was unchanged, but Gsα protein was increased. Adenylyl cyclase stimulation by isoproterenol was reduced in HOCM but not in AoSt. Plasma catecholamine levels were normal in all patients. In conclusion, both forms of hypertrophy are associated with β-adrenoceptor downregulation but with different changes at the G protein level that occur before symptomatic heart failure due to progressive dilatation of the left ventricle develops and are not due to elevated plasma catecholamine levels.

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47

Tawada-Iwata, Y., T. Imagawa, A. Yoshida, M. Takahashi, H. Nakamura, and M. Shigekawa. "Increased mechanical extraction of T-tubule/junctional SR from cardiomyopathic hamster heart." American Journal of Physiology-Heart and Circulatory Physiology 264, no. 5 (May 1, 1993): H1447—H1453. http://dx.doi.org/10.1152/ajpheart.1993.264.5.h1447.

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We determined the contents of L-type calcium channels (LCC) and other membrane proteins in ventricular homogenates and microsomes prepared from hearts of 30- to 70-day-old Syrian cardiomyopathic (Bio 14.6) and normal hamsters. Quantitative immunoblot assay revealed that myopathic microsomes, as compared with normal controls, were enriched about twofold with the alpha 1-subunit of LCC, the ryanodine receptor calsequestrin, and Na(+)-K(+)-adenosinetriphosphatase (ATPase), whereas the contents of these proteins in ventricular homogenates were not different. In contrast, Na(+)-H+ antiporter and sarcoplasmic reticulum (SR) Ca(2+)-ATPase showed no difference in their contents in both homogenates and microsomes. Radioligand binding assay further showed no significant difference in the number of binding sites for [3H]prazosin, [125I]iodocyanopindolol, and [3H]saxitoxin between myopathic and normal microsomes. These result suggest that whereas membrane densities of LCC and the other proteins examined are not increased in myopathic cardiomyocytes, T-tubule/junctional SR membranes are more easily extracted from them by mechanical disruption. This, together with 1.5-fold higher yield of microsomal fractions from myopathic heart muscle, shows that abnormality exists in the mechanical property of cell membrane in the myopathic heart.

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48

Janssens, P. A., and P. Lowrey. "Hormonal regulation of hepatic glycogenolysis in the carp, Cyprinus carpio." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 252, no. 4 (April 1, 1987): R653—R660. http://dx.doi.org/10.1152/ajpregu.1987.252.4.r653.

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Carp (Cyprinus carpio) liver maintained normal glycogen content and enzyme complement for several days in organ culture. Epinephrine-stimulated glycogenolysis, phosphorylase activation, and cyclic AMP (cAMP) accumulation in a concentration-dependent manner with EC50s of 100, 100, and 500 nM, respectively. These actions were blocked by the beta-adrenergic antagonist, propranolol, but not by the alpha-adrenergic antagonist phentolamine. Glycogenolysis and tissue cAMP were uninfluenced by 10(-6) M arginine vasotocin, arginine vasopressin, lysine vasotocin, lysine vasopressin, mesotocin, or oxytocin, but were slightly increased by 10(-5) M isotocin and slightly decreased by 10(-6) M angiotensin II. [125I]-iodocyanopindolol (ICP), a beta-adrenergic ligand, bound to isolated carp liver membranes with a KD of 83 pM. Maximum binding of 45 fmol/mg protein was at 600 pM. Propranolol, isoprenaline, epinephrine, phenylephrine, norepinephrine, and phenoxybenzamine displaced ICP with KDs of 100 nM, 2, 20, 20, 60, and 200 microM, respectively. The alpha-adrenergic antagonists, yohimbine and prazosin, showed no specific binding. These data provide evidence that catecholamines act via beta-adrenergic receptors in carp liver and that alpha-adrenergic receptors are not present. Vasoactive peptides play no significant role in regulation of carp liver glycogenolysis.

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49

Green, A., R. M. Carroll, and S. B. Dobias. "Desensitization of beta-adrenergic receptors in adipocytes causes increased insulin sensitivity of glucose transport." American Journal of Physiology-Endocrinology and Metabolism 271, no. 2 (August 1, 1996): E271—E276. http://dx.doi.org/10.1152/ajpendo.1996.271.2.e271.

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To determine the effect of desensitization of adipocyte beta-adrenergic receptors on insulin sensitivity, rats were continuously infused with isoproterenol (50 or 100 micrograms.kg-1.h-1) for 3 days by osmotic minipumps. Epididymal adipocytes were isolated. The cells from treated animals were desensitized to isoproterenol, as determined by response of lipolysis (glycerol release). Binding of [125I]iodocyanopindolol was decreased by approximately 80% in adipocyte plasma membranes isolated from treated rats, indicating that beta-adrenergic receptors were downregulated. Cellular concentrations of Gn alpha and Gi alpha were not altered. Insulin sensitivity was determined by measuring the effect of insulin on glucose transport (2-deoxy-[3H]glucose uptake). Cells from the isoproterenol-infused rats were markedly more sensitive to insulin than those from control rats. This was evidenced by an approximately 50% increase in maximal glucose transport rate in cells from the high-dose isoproterenol-treated rats and by an approximately 40% decrease in the half-maximal effective concentration of insulin in both groups. 125I-labeled insulin binding to adipocytes was not altered by the isoproterenol infusions, indicating that desensitization of beta-adrenergic receptors results in tighter coupling between insulin receptors and stimulation of glucose transport.

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50

TSUCHIHASHI, HIROSHI, and TAKAFUMI NAGATOMO. "Biphasic binding of 125I-iodocyanopindolol to .BETA.-adrenergic receptors in rat cerebral cortical membranes. I. Assessment by the use of agonists." CHEMICAL & PHARMACEUTICAL BULLETIN 35, no. 7 (1987): 2966–72. http://dx.doi.org/10.1248/cpb.35.2966.

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