Properties of β-adrenergic receptors on porcine corpora lutea and granulosa cells

S. N. Perkins, M. J. Cronin, Johannes D Veldhuis

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

The nature of β-adrenergic binding by swine corpora lutea and granulosa cells was examined with the specific β-adrenergic radioligand, (±)3-[ 125I]iodocyanopindolol (ICYP). Saturation analyses revealed the presence of high affinity (K(d) = 15.2 ± 2.1 pM; n = 8 experiments) and low capacity (6.7 ± 0.8 fmol/mg protein) β-adrenergic receptors on porcine corpora lutea membranes. The properties of β-adrenergic binding were determined by computer modeling of competition studies with a variety of compounds selective for β-adrenergic subtypes. These studies disclosed predominantly β 1-adrenergic receptors on pig luteal membranes. This inference from radioligand binding studies was corroborated functionally by the approximately equipotent biological effects of L-norepinephrine and L-epinephrine on cAMP production by luteal tissue (respective EC 50s of 282 ± 31 and 187 ± 66 nM; n = 3 experiments). Physiological regulation of specific β-adrenergic receptor content in the swine ovary was indicated by prominent (up to 9-fold) variations in receptor concentrations among corpora lutea and granulosa cells at various stages of maturity. In addition, there was differential expression of β-adrenergic receptor subtype. Whereas the β-adrenergic receptor subtype was predominantly β 1 in corpora hemorrhagica and corpora lutea, granulosa cells and corpora albicantia contained principally β 2 receptors. This difference could not be accounted for by blood cell contamination of corpora lutea, since swine blood cells contained pr edominantly (>98%) β 2-receptors, which were present at less than 8.6% the concentration of total β-receptors in luteal tissue. In summary, swine corpora lutea and granulosa cells contain specific high affinity, low capacity β-adrenergic receptors that are functionally coupled to biological responses. Moreover, total receptor content as well as β-adrenergic subtype exhibit significant physiological variation in relation to maturational status of ovarian follicular and luteal tissue.

Original languageEnglish (US)
Pages (from-to)998-1005
Number of pages8
JournalEndocrinology
Volume118
Issue number3
StatePublished - 1986
Externally publishedYes

Fingerprint

Granulosa Cells
Corpus Luteum
Adrenergic Receptors
Swine
Adrenergic Agents
Blood Cells
Iodocyanopindolol
Membranes
Epinephrine
Ovary
Norepinephrine

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

Cite this

Perkins, S. N., Cronin, M. J., & Veldhuis, J. D. (1986). Properties of β-adrenergic receptors on porcine corpora lutea and granulosa cells. Endocrinology, 118(3), 998-1005.

Properties of β-adrenergic receptors on porcine corpora lutea and granulosa cells. / Perkins, S. N.; Cronin, M. J.; Veldhuis, Johannes D.

In: Endocrinology, Vol. 118, No. 3, 1986, p. 998-1005.

Research output: Contribution to journalArticle

Perkins, SN, Cronin, MJ & Veldhuis, JD 1986, 'Properties of β-adrenergic receptors on porcine corpora lutea and granulosa cells', Endocrinology, vol. 118, no. 3, pp. 998-1005.
Perkins, S. N. ; Cronin, M. J. ; Veldhuis, Johannes D. / Properties of β-adrenergic receptors on porcine corpora lutea and granulosa cells. In: Endocrinology. 1986 ; Vol. 118, No. 3. pp. 998-1005.
@article{fbc0b29c46d2490382a202acd067e3ba,
title = "Properties of β-adrenergic receptors on porcine corpora lutea and granulosa cells",
abstract = "The nature of β-adrenergic binding by swine corpora lutea and granulosa cells was examined with the specific β-adrenergic radioligand, (±)3-[ 125I]iodocyanopindolol (ICYP). Saturation analyses revealed the presence of high affinity (K(d) = 15.2 ± 2.1 pM; n = 8 experiments) and low capacity (6.7 ± 0.8 fmol/mg protein) β-adrenergic receptors on porcine corpora lutea membranes. The properties of β-adrenergic binding were determined by computer modeling of competition studies with a variety of compounds selective for β-adrenergic subtypes. These studies disclosed predominantly β 1-adrenergic receptors on pig luteal membranes. This inference from radioligand binding studies was corroborated functionally by the approximately equipotent biological effects of L-norepinephrine and L-epinephrine on cAMP production by luteal tissue (respective EC 50s of 282 ± 31 and 187 ± 66 nM; n = 3 experiments). Physiological regulation of specific β-adrenergic receptor content in the swine ovary was indicated by prominent (up to 9-fold) variations in receptor concentrations among corpora lutea and granulosa cells at various stages of maturity. In addition, there was differential expression of β-adrenergic receptor subtype. Whereas the β-adrenergic receptor subtype was predominantly β 1 in corpora hemorrhagica and corpora lutea, granulosa cells and corpora albicantia contained principally β 2 receptors. This difference could not be accounted for by blood cell contamination of corpora lutea, since swine blood cells contained pr edominantly (>98{\%}) β 2-receptors, which were present at less than 8.6{\%} the concentration of total β-receptors in luteal tissue. In summary, swine corpora lutea and granulosa cells contain specific high affinity, low capacity β-adrenergic receptors that are functionally coupled to biological responses. Moreover, total receptor content as well as β-adrenergic subtype exhibit significant physiological variation in relation to maturational status of ovarian follicular and luteal tissue.",
author = "Perkins, {S. N.} and Cronin, {M. J.} and Veldhuis, {Johannes D}",
year = "1986",
language = "English (US)",
volume = "118",
pages = "998--1005",
journal = "Endocrinology",
issn = "0013-7227",
publisher = "The Endocrine Society",
number = "3",

}

TY - JOUR

T1 - Properties of β-adrenergic receptors on porcine corpora lutea and granulosa cells

AU - Perkins, S. N.

AU - Cronin, M. J.

AU - Veldhuis, Johannes D

PY - 1986

Y1 - 1986

N2 - The nature of β-adrenergic binding by swine corpora lutea and granulosa cells was examined with the specific β-adrenergic radioligand, (±)3-[ 125I]iodocyanopindolol (ICYP). Saturation analyses revealed the presence of high affinity (K(d) = 15.2 ± 2.1 pM; n = 8 experiments) and low capacity (6.7 ± 0.8 fmol/mg protein) β-adrenergic receptors on porcine corpora lutea membranes. The properties of β-adrenergic binding were determined by computer modeling of competition studies with a variety of compounds selective for β-adrenergic subtypes. These studies disclosed predominantly β 1-adrenergic receptors on pig luteal membranes. This inference from radioligand binding studies was corroborated functionally by the approximately equipotent biological effects of L-norepinephrine and L-epinephrine on cAMP production by luteal tissue (respective EC 50s of 282 ± 31 and 187 ± 66 nM; n = 3 experiments). Physiological regulation of specific β-adrenergic receptor content in the swine ovary was indicated by prominent (up to 9-fold) variations in receptor concentrations among corpora lutea and granulosa cells at various stages of maturity. In addition, there was differential expression of β-adrenergic receptor subtype. Whereas the β-adrenergic receptor subtype was predominantly β 1 in corpora hemorrhagica and corpora lutea, granulosa cells and corpora albicantia contained principally β 2 receptors. This difference could not be accounted for by blood cell contamination of corpora lutea, since swine blood cells contained pr edominantly (>98%) β 2-receptors, which were present at less than 8.6% the concentration of total β-receptors in luteal tissue. In summary, swine corpora lutea and granulosa cells contain specific high affinity, low capacity β-adrenergic receptors that are functionally coupled to biological responses. Moreover, total receptor content as well as β-adrenergic subtype exhibit significant physiological variation in relation to maturational status of ovarian follicular and luteal tissue.

AB - The nature of β-adrenergic binding by swine corpora lutea and granulosa cells was examined with the specific β-adrenergic radioligand, (±)3-[ 125I]iodocyanopindolol (ICYP). Saturation analyses revealed the presence of high affinity (K(d) = 15.2 ± 2.1 pM; n = 8 experiments) and low capacity (6.7 ± 0.8 fmol/mg protein) β-adrenergic receptors on porcine corpora lutea membranes. The properties of β-adrenergic binding were determined by computer modeling of competition studies with a variety of compounds selective for β-adrenergic subtypes. These studies disclosed predominantly β 1-adrenergic receptors on pig luteal membranes. This inference from radioligand binding studies was corroborated functionally by the approximately equipotent biological effects of L-norepinephrine and L-epinephrine on cAMP production by luteal tissue (respective EC 50s of 282 ± 31 and 187 ± 66 nM; n = 3 experiments). Physiological regulation of specific β-adrenergic receptor content in the swine ovary was indicated by prominent (up to 9-fold) variations in receptor concentrations among corpora lutea and granulosa cells at various stages of maturity. In addition, there was differential expression of β-adrenergic receptor subtype. Whereas the β-adrenergic receptor subtype was predominantly β 1 in corpora hemorrhagica and corpora lutea, granulosa cells and corpora albicantia contained principally β 2 receptors. This difference could not be accounted for by blood cell contamination of corpora lutea, since swine blood cells contained pr edominantly (>98%) β 2-receptors, which were present at less than 8.6% the concentration of total β-receptors in luteal tissue. In summary, swine corpora lutea and granulosa cells contain specific high affinity, low capacity β-adrenergic receptors that are functionally coupled to biological responses. Moreover, total receptor content as well as β-adrenergic subtype exhibit significant physiological variation in relation to maturational status of ovarian follicular and luteal tissue.

UR - http://www.scopus.com/inward/record.url?scp=0022467930&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022467930&partnerID=8YFLogxK

M3 - Article

VL - 118

SP - 998

EP - 1005

JO - Endocrinology

JF - Endocrinology

SN - 0013-7227

IS - 3

ER -