Sub types of α2-adrenoceptors: Pharmacological and molecular biological evidence converg

  title={Sub types of $\alpha$2-adrenoceptors: Pharmacological and molecular biological evidence converg},
  author={David B. Bylund},
  journal={Trends in Pharmacological Sciences},
  • D. Bylund
  • Published 1 October 1988
  • Biology
  • Trends in Pharmacological Sciences

α‐ and β‐Adrenoceptors in Hypertension: Molecular Biology and Pharmacological Studies

The available data indicate that among the α-adrenoceptor subtypes the α 2A -adrenOceptor is the most likely candidate for an alteration specifically linked to genetic hypertension in the animal model of the spontaneously hypertensive rat and possibly in some patients.

Molecular biology of adrenergic receptors.

Additional subtypes have been characterized by molecular biology techniques, which have revealed common features in quite different G protein-coupled receptors, suggesting that these receptors might be members of a large receptor superfamily.

Characterization of Adrenoceptors

Support protocols are provided covering the preparation of membranes containing the receptor from tissue or cells in culture, calculation of Kd and Bmax from saturation experiments, and calculation of Ki from inhibition experiments.

Identification and characterization of the alpha 2D-adrenoceptor subtype in single cells prepared from guinea pig tracheal smooth muscles.

The results suggest that the alpha 2-adrenoceptor in guinea pig tracheal smooth muscle represents a single pharmacological subtype, which is designated as alpha 2D.

Molecular and cellular biology of adrenergic receptors.

  • B. Kobilka
  • Biology, Medicine
    Trends in cardiovascular medicine
  • 1991



α-Adrenoceptor-effector coupling: affinity states or heterogeneity of the α2-adrenoceptor?

There is substantial evidence supporting the concept of at least two major groups of α-adrenoceptors, which have been termed α 1 and α 2, which appear to possess different mechanisms for signal transduction.

Heterogeneity of alpha-2 adrenergic receptors

  • D. Bylund
  • Biology
    Pharmacology Biochemistry and Behavior
  • 1985

Solubilization and characterization of putative alpha-2 adrenergic isoceptors from the human platelet and the rat cerebral cortex.

It is found that the differences in the pharmacologic properties of rat cerebral cortex and human platelet alpha-2 adrenergic receptors were not due to 1) differential proteolysis of the receptor, 2) degradation of the ligand, 3) the detection of different affinity states or 4) the presence of different quantities of various affinity modulators.

Comparison of potency of α2‐adrenoceptor antagonists in vitro: evidence for heterogeneity of α2‐adrenoceptors

It is concluded that α2‐adrenoceptors are a heterogeneous population, different subgroups being more apparent between species rather than between tissue types or location.

Identification of α2‐Adrenergic Receptors in Chicken Pineal Gland Using [3H]Rauwolscine

The α2‐adrenergic receptor in the chicken pineal gland was directly identified by radioligand binding and was of the α2A subtype, since prazosin and ARC‐239 bound with low affinities and oxymetazoline bound with high affinity.

Characterization of [3H]yohimbine binding to putative alpha-2 adrenergic receptors in neonatal rat lung.

In contrast to the adult rat lung, which lacks alpha-2 adrenergic receptor binding sites, the neonatal rat lung had a high density of [3H]yohimbine binding sites and inhibition experiments indicated that the binding site had the characteristics of an alpha- 2 adrenergic receptors although yohimbines was only 5 times more potent than prazosin.

Alpha-2A and alpha-2B adrenergic receptor subtypes: antagonist binding in tissues and cell lines containing only one subtype.

Two distinct pharmacological profiles for the two alpha-2 adrenergic receptor subtypes in several different tissues are demonstrated, further support the existence and definition of these subtypes.