Evolutionary Temperature Adaptation of Agonist Binding to the A<sub>1</sub>Adenosine Receptor

Siebenaller, Joseph F.; Murray, Thomas F.

doi:10.2307/1541733

Cited by 11 publications

(11 citation statements)

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“…1). At 5C, which approximates the body temperatures of these three species, the K^ values are similar (Siebenaller and Murray, 1988).…”

Section: Discussionmentioning

confidence: 81%

“…Assays were conducted in Tris-HCl, pH 7.6, at the incubation temperature of 5C. The procedures described in Siebenaller and Murray (1988) were followed. Brain membrane protein (0.4-1 .2 mg) was added to each assay tube.…”

Section: Equilibrium Binding Assay For Membrane Bound a Adenosine Rec...mentioning

confidence: 99%

“…At a measurement temperature of 22C, the binding affinities, specificities, and pharmacological profiles of the A i adenosine receptors in teleost fishes are similar to those of mammals (Siebenaller and Murray, 1986;Murray and Siebenaller, 1987). The binding of agonists to the high affinity state of mammalian A, receptors is disrupted by the low temperatures typical of body temperatures of many cold-adapted fishes (e.g.. Bruns et a/., 1980;Trost and Schwabe, 1981;Murphy and Snyder, 1982;Lohserfa/.. 1984;Siebenaller and Murray, 1988). However, agonist recognition and binding properties of the A, adenosine receptors are retained in evolutionary adaptation to different body temperatures.…”

Section: Introductionmentioning

confidence: 96%

“…A, adenosine receptor modulation of adenylyl cyclase was selected for two reasons as a model with which to examine pressure and temperature effects on transmembrane signal transduction. First, our previous studies had documented the widespread distribution of this receptor among the classes of chordates, including deep-occurring teleosts Murray, 1986, 1988), and we had also identified potentially adaptive differences in ligand binding among species (Murray and Siebenaller, 1987;Siebenaller and Murray, 1988). Agonist occupation of the A, adenosine receptor inhibits cAMP accumulation in mammalian central nervous tissue preparations (reviews by Wolff tv a/., 1981;Londos et a/.. 1983;Snyder, 1985;Williams, 1987).…”

Section: Introductionmentioning

confidence: 99%

“…for eight vertebrate species with body temperatures of 1 -40C, Kj values for the agonist N 6 -['H]cyclohexyladenosine <[ 3 H]CHA) measured at 5C varied 30-fold; however, the binding affinities vary only four-fold when compared at temperatures similar to the species' body temperatures (Siebenaller and Murray, 1988).…”

Section: Introductionmentioning

confidence: 99%

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A1 Adenosine Receptor Modulation of Adenylyl Cyclase of a Deep-living Teleost Fish, Antimora rostrata

Siebenaller¹,

Murray²

1990

The Biological Bulletin

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Low temperatures and high hydrostatic pressures are typical of the deep sea. The effects of these parameters on transmembrane signal transduction were determined through a study of the A1 adenosine receptor-inhibitory guanine nucleotide binding protein-adenylyl cyclase system in brain membranes of the bathyal teleost fish, Antimora rostrata (Moridae). The components of this system were analyzed at 5°C and 1 atm, and the role of the A1 receptor in the modulation of adenylyl cyclase was determined. The A1 selective radioligand N6-[3H]cyclohexyladenosine bound saturably, reversibly, and with high affinity. The Kd of N6-[3H]cyclohexyladenosine estimated from kinetic measurements was 1.11 nM; the Kd determined from equilibrium binding was 4.86 nM. [32P]ADP-ribosylation of brain membranes by pertussis toxin labeled substrates with apparent molecular masses of 39,000 to 41,000 Da. Basal adenylyl cyclase activity was inhibited in a concentration-dependent manner by the A1 adenosine receptor agonist N6-cyclopentyladenosine (IC50 = 5.08 μM). The inhibition of adenylyl cyclase activity was dependent upon GTP. Basal adenylyl cyclase activity was unaffected by 272 atm of pressure. The efficacy of 100 μM N6-cyclopentyladenosine as an inhibitor of adenylyl cyclase was the same at atmospheric pressure and at 272 atm. The inhibition of adenylyl cyclase by the agonist 5'-N-ethylcarboxamidoadenosine (100 μM) at 272 atm was twice that observed at atmospheric pressure. Although consideration of the effects of low temperature and high hydrostatic pressure on acyl chain order suggest that deep-sea conditions will perturb membrane function, signal transduction by the A1 receptor system of the bathyal fish A. rostrata is not disrupted by deep-sea conditions.

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“…1). At 5C, which approximates the body temperatures of these three species, the K^ values are similar (Siebenaller and Murray, 1988).…”

Section: Discussionmentioning

confidence: 81%

Section: Equilibrium Binding Assay For Membrane Bound a Adenosine Rec...mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

A1 Adenosine Receptor Modulation of Adenylyl Cyclase of a Deep-living Teleost Fish, Antimora rostrata

Siebenaller¹,

Murray²

1990

The Biological Bulletin

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The effects of hydrostatic pressure on the low-K m GTPase in brain membranes from two congeneric marine fishes

Siebenaller

Murray

1994

J Comp Physiol B

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Biochemical ecology of deep-sea animals

Somero

1992

Experientia

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Deep-sea ecosystems contain unique endemic species whose distributions show strong vertical patterning in the case of pelagic animals and sharp horizontal patterning in the case of benthic animals living in or near the deep-sea hydothermal vents. This review discusses the biochemical adaptations that enable deep-sea animals to exploit diverse deep-sea habitats and that help establish biogeographic patterning in the deep-sea. The abilities of deep-sea animals to tolerate the pressure and temperature conditions of deep-sea habitats are due to pervasive adaptations at the biochemical level: enzymes exhibit reduced perturbation of function by pressure, membranes have fluidities adapted to deep-sea pressures and temperatures, and proteins show enhanced structural stability relative to homologous proteins from cold-adapted shallow-living species. Animals from the warmest habitable regions of hydrothermal vent ecosystems have enzymes and mitochondria adapted to high pressure and relatively high temperatures. The low metabolic rates of bathypelagic fishes correlate with greatly reduced capacities for ATP turnover in locomotory muscle. Reduced light and food availability in bathypelagic regions select for low rates of energy expenditure in locomotory activity. Deep-sea animals thus reflect the importance of biochemical adaptations in establishing species distribution patterns and appropriate rates of metabolic turnover in different ecosystems.

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Evolutionary Temperature Adaptation of Agonist Binding to the A₁Adenosine Receptor

Cited by 11 publications

References 13 publications

A1 Adenosine Receptor Modulation of Adenylyl Cyclase of a Deep-living Teleost Fish, Antimora rostrata

A1 Adenosine Receptor Modulation of Adenylyl Cyclase of a Deep-living Teleost Fish, Antimora rostrata

The effects of hydrostatic pressure on the low-K m GTPase in brain membranes from two congeneric marine fishes

Biochemical ecology of deep-sea animals

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Evolutionary Temperature Adaptation of Agonist Binding to the A1Adenosine Receptor

Cited by 11 publications

References 13 publications

A1 Adenosine Receptor Modulation of Adenylyl Cyclase of a Deep-living Teleost Fish, Antimora rostrata

A1 Adenosine Receptor Modulation of Adenylyl Cyclase of a Deep-living Teleost Fish, Antimora rostrata

The effects of hydrostatic pressure on the low-K m GTPase in brain membranes from two congeneric marine fishes

Biochemical ecology of deep-sea animals

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Product

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Evolutionary Temperature Adaptation of Agonist Binding to the A₁Adenosine Receptor