Comparison of the binding properties of A1 adenosine receptors in brain membranes of two congeneric marine fishes living at different depths

Thomas F. Murray, Joseph F. Siebenaller

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

The binding properties of A1 adenosine receptors in brain membranes were compared in two congeneric marine teleost fishes which differ in their depths of distribution. Adenosine receptors were labeled using the A1 selective radioligand [3H]cyclohexyladenosine ([3H]CHA). The A1 receptor agonist [3H]CHA bound saturably, reversibly and with high affinity to brain membranes prepared from Sebastolobus altivelis and S. alascanus; however, the mean Kd values differed significantly (Figs. 1–3, Table 1). Saturation data fit to a one site model indicated that the A1 receptor in S. alascanus exhibited a higher affinity (Kd=1.49 n M) for [3H]CHA whereas A1 receptors in S. altivelis exhibited a significantly lower affinity (Kd=3.1 n M). Moreover, S. altivelis, but not S. alascanus, parameter estimates for [3H]CHA binding to two sites of receptor were obtained (Fig. 3, Table 1). The mean dissociation constant values for the high and low affinity sites for [3H]CHA in S. altivelis were 0.43 n M and 16.3 n M, respectively. In equilibrium competition experiments the adenosine analogs R-phenylisopropyladenosine (R-PIA), N-ethylcarboxamidoadenosine (NECA) and S-phenylisopropyladenosine (S-PIA) all displayed higher affinities for A1 receptors in S. alascanus as compared to S. altivelis brain membranes (Table 2, Fig. 6). The specific binding of [3H]CHA was significantly increased by 0.1 and 1.0 m M MgCl2 in both fishes; however, the sensitivity (95–131% increase) of S. altivelis to this effect was significantly greater than that of S. alascanus (48–91% increase) (Fig. 5). The results of kinetic, equilibrium saturation and equilibrium competition experiments all suggest that A1 adenosine receptors of S. altivelis and S. alascanus brain membranes differ with respect to their affinities for selected adenosine agonists.

Original languageEnglish
Pages (from-to)267-277
Number of pages11
JournalJournal of Comparative Physiology B: Biochemical, Systemic, and Environmental Physiology
Volume157
Issue number3
DOIs
StatePublished - 1987
Externally publishedYes

Fingerprint

Adenosine A1 Receptors
binding properties
adenosine
marine fish
Fish
brain
Brain
Fishes
Phenylisopropyladenosine
membrane
Membranes
receptors
fish
Adenosine
Adenosine-5'-(N-ethylcarboxamide)
saturation
Magnesium Chloride
Purinergic P1 Receptors
Scattering parameters
teleost

All Science Journal Classification (ASJC) codes

  • Animal Science and Zoology
  • Ecology, Evolution, Behavior and Systematics
  • Biochemistry
  • Endocrinology
  • Physiology
  • Environmental Science(all)
  • Physiology (medical)

Cite this

@article{61ff2de2fb8c4d83836cdb1e4817d750,
title = "Comparison of the binding properties of A1 adenosine receptors in brain membranes of two congeneric marine fishes living at different depths",
abstract = "The binding properties of A1 adenosine receptors in brain membranes were compared in two congeneric marine teleost fishes which differ in their depths of distribution. Adenosine receptors were labeled using the A1 selective radioligand [3H]cyclohexyladenosine ([3H]CHA). The A1 receptor agonist [3H]CHA bound saturably, reversibly and with high affinity to brain membranes prepared from Sebastolobus altivelis and S. alascanus; however, the mean Kd values differed significantly (Figs. 1–3, Table 1). Saturation data fit to a one site model indicated that the A1 receptor in S. alascanus exhibited a higher affinity (Kd=1.49 n M) for [3H]CHA whereas A1 receptors in S. altivelis exhibited a significantly lower affinity (Kd=3.1 n M). Moreover, S. altivelis, but not S. alascanus, parameter estimates for [3H]CHA binding to two sites of receptor were obtained (Fig. 3, Table 1). The mean dissociation constant values for the high and low affinity sites for [3H]CHA in S. altivelis were 0.43 n M and 16.3 n M, respectively. In equilibrium competition experiments the adenosine analogs R-phenylisopropyladenosine (R-PIA), N-ethylcarboxamidoadenosine (NECA) and S-phenylisopropyladenosine (S-PIA) all displayed higher affinities for A1 receptors in S. alascanus as compared to S. altivelis brain membranes (Table 2, Fig. 6). The specific binding of [3H]CHA was significantly increased by 0.1 and 1.0 m M MgCl2 in both fishes; however, the sensitivity (95–131{\%} increase) of S. altivelis to this effect was significantly greater than that of S. alascanus (48–91{\%} increase) (Fig. 5). The results of kinetic, equilibrium saturation and equilibrium competition experiments all suggest that A1 adenosine receptors of S. altivelis and S. alascanus brain membranes differ with respect to their affinities for selected adenosine agonists.",
author = "Murray, {Thomas F.} and Siebenaller, {Joseph F.}",
year = "1987",
doi = "10.1007/BF00693353",
language = "English",
volume = "157",
pages = "267--277",
journal = "Journal of Comparative Physiology B: Biochemical, Systemic, and Environmental Physiology",
issn = "0174-1578",
publisher = "Springer Verlag",
number = "3",

}

TY - JOUR

T1 - Comparison of the binding properties of A1 adenosine receptors in brain membranes of two congeneric marine fishes living at different depths

AU - Murray, Thomas F.

AU - Siebenaller, Joseph F.

PY - 1987

Y1 - 1987

N2 - The binding properties of A1 adenosine receptors in brain membranes were compared in two congeneric marine teleost fishes which differ in their depths of distribution. Adenosine receptors were labeled using the A1 selective radioligand [3H]cyclohexyladenosine ([3H]CHA). The A1 receptor agonist [3H]CHA bound saturably, reversibly and with high affinity to brain membranes prepared from Sebastolobus altivelis and S. alascanus; however, the mean Kd values differed significantly (Figs. 1–3, Table 1). Saturation data fit to a one site model indicated that the A1 receptor in S. alascanus exhibited a higher affinity (Kd=1.49 n M) for [3H]CHA whereas A1 receptors in S. altivelis exhibited a significantly lower affinity (Kd=3.1 n M). Moreover, S. altivelis, but not S. alascanus, parameter estimates for [3H]CHA binding to two sites of receptor were obtained (Fig. 3, Table 1). The mean dissociation constant values for the high and low affinity sites for [3H]CHA in S. altivelis were 0.43 n M and 16.3 n M, respectively. In equilibrium competition experiments the adenosine analogs R-phenylisopropyladenosine (R-PIA), N-ethylcarboxamidoadenosine (NECA) and S-phenylisopropyladenosine (S-PIA) all displayed higher affinities for A1 receptors in S. alascanus as compared to S. altivelis brain membranes (Table 2, Fig. 6). The specific binding of [3H]CHA was significantly increased by 0.1 and 1.0 m M MgCl2 in both fishes; however, the sensitivity (95–131% increase) of S. altivelis to this effect was significantly greater than that of S. alascanus (48–91% increase) (Fig. 5). The results of kinetic, equilibrium saturation and equilibrium competition experiments all suggest that A1 adenosine receptors of S. altivelis and S. alascanus brain membranes differ with respect to their affinities for selected adenosine agonists.

AB - The binding properties of A1 adenosine receptors in brain membranes were compared in two congeneric marine teleost fishes which differ in their depths of distribution. Adenosine receptors were labeled using the A1 selective radioligand [3H]cyclohexyladenosine ([3H]CHA). The A1 receptor agonist [3H]CHA bound saturably, reversibly and with high affinity to brain membranes prepared from Sebastolobus altivelis and S. alascanus; however, the mean Kd values differed significantly (Figs. 1–3, Table 1). Saturation data fit to a one site model indicated that the A1 receptor in S. alascanus exhibited a higher affinity (Kd=1.49 n M) for [3H]CHA whereas A1 receptors in S. altivelis exhibited a significantly lower affinity (Kd=3.1 n M). Moreover, S. altivelis, but not S. alascanus, parameter estimates for [3H]CHA binding to two sites of receptor were obtained (Fig. 3, Table 1). The mean dissociation constant values for the high and low affinity sites for [3H]CHA in S. altivelis were 0.43 n M and 16.3 n M, respectively. In equilibrium competition experiments the adenosine analogs R-phenylisopropyladenosine (R-PIA), N-ethylcarboxamidoadenosine (NECA) and S-phenylisopropyladenosine (S-PIA) all displayed higher affinities for A1 receptors in S. alascanus as compared to S. altivelis brain membranes (Table 2, Fig. 6). The specific binding of [3H]CHA was significantly increased by 0.1 and 1.0 m M MgCl2 in both fishes; however, the sensitivity (95–131% increase) of S. altivelis to this effect was significantly greater than that of S. alascanus (48–91% increase) (Fig. 5). The results of kinetic, equilibrium saturation and equilibrium competition experiments all suggest that A1 adenosine receptors of S. altivelis and S. alascanus brain membranes differ with respect to their affinities for selected adenosine agonists.

UR - http://www.scopus.com/inward/record.url?scp=0023268114&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023268114&partnerID=8YFLogxK

U2 - 10.1007/BF00693353

DO - 10.1007/BF00693353

M3 - Article

VL - 157

SP - 267

EP - 277

JO - Journal of Comparative Physiology B: Biochemical, Systemic, and Environmental Physiology

JF - Journal of Comparative Physiology B: Biochemical, Systemic, and Environmental Physiology

SN - 0174-1578

IS - 3

ER -