Follicle-stimulating hormone regulation of A-Kinase Anchoring Proteins in granulosa cells

Daniel Carr, Deborah A. DeManno, Angela Atwood, Mary Hunzicker-Dunn, John D. Scott

Research output: Contribution to journalArticle

66 Citations (Scopus)

Abstract

It has been well established that the biochemical and morphological changes during maturation of granulosa cells that are induced by follicle-stimulating hormone (FSH) occur through the elevation of intracellular cAMP and consequent activation of the cAMP-dependent protein kinase (PKA). In this report we show that FSH action alters the expression of A-Kinase Anchoring Proteins (AKAPs), which function to target the subcellular distribution of the type II PKA. Exposure of granulosa cells grown in primary culture with FSH and estradiol for 72 h resulted in the up-regulation of an 80-kDa AKAP and the RIIβ subunit of PKA, whereas cells grown in control medium containing only estradiol produced a time-dependent increase of a 140-kDa AKAP. RII overlays performed with [32P]RIIα preferentially detected RII-binding bands of 80 and 95 kDa compared to blots probed with [32P]RIIβ, suggesting that FSH may alter the subcellular location of PKA in an isoform-specific manner. FSH treatment causes a translocation of RIIα from the particulate to the cytosolic fraction coincident with the induction of the 80-kDa AKAP, which is also predominately cytosolic. These data suggest that FSH promotes a redistribution of the type II PKA holoenzyme through the selective induction of an RII isoform-specific AKAP.

Original languageEnglish (US)
Pages (from-to)20729-20732
Number of pages4
JournalJournal of Biological Chemistry
Volume268
Issue number28
StatePublished - Oct 5 1993

Fingerprint

Granulosa Cells
Follicle Stimulating Hormone
Protein Kinases
Phosphotransferases
Proteins
Estradiol
Protein Isoforms
Cells
Holoenzymes
Cyclic AMP-Dependent Protein Kinases
Cell culture
Protein Subunits
Chemical activation
Up-Regulation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Carr, D., DeManno, D. A., Atwood, A., Hunzicker-Dunn, M., & Scott, J. D. (1993). Follicle-stimulating hormone regulation of A-Kinase Anchoring Proteins in granulosa cells. Journal of Biological Chemistry, 268(28), 20729-20732.

Follicle-stimulating hormone regulation of A-Kinase Anchoring Proteins in granulosa cells. / Carr, Daniel; DeManno, Deborah A.; Atwood, Angela; Hunzicker-Dunn, Mary; Scott, John D.

In: Journal of Biological Chemistry, Vol. 268, No. 28, 05.10.1993, p. 20729-20732.

Research output: Contribution to journalArticle

Carr, D, DeManno, DA, Atwood, A, Hunzicker-Dunn, M & Scott, JD 1993, 'Follicle-stimulating hormone regulation of A-Kinase Anchoring Proteins in granulosa cells', Journal of Biological Chemistry, vol. 268, no. 28, pp. 20729-20732.
Carr D, DeManno DA, Atwood A, Hunzicker-Dunn M, Scott JD. Follicle-stimulating hormone regulation of A-Kinase Anchoring Proteins in granulosa cells. Journal of Biological Chemistry. 1993 Oct 5;268(28):20729-20732.
Carr, Daniel ; DeManno, Deborah A. ; Atwood, Angela ; Hunzicker-Dunn, Mary ; Scott, John D. / Follicle-stimulating hormone regulation of A-Kinase Anchoring Proteins in granulosa cells. In: Journal of Biological Chemistry. 1993 ; Vol. 268, No. 28. pp. 20729-20732.
@article{3afacd6da42c4b72abe47276b9223c48,
title = "Follicle-stimulating hormone regulation of A-Kinase Anchoring Proteins in granulosa cells",
abstract = "It has been well established that the biochemical and morphological changes during maturation of granulosa cells that are induced by follicle-stimulating hormone (FSH) occur through the elevation of intracellular cAMP and consequent activation of the cAMP-dependent protein kinase (PKA). In this report we show that FSH action alters the expression of A-Kinase Anchoring Proteins (AKAPs), which function to target the subcellular distribution of the type II PKA. Exposure of granulosa cells grown in primary culture with FSH and estradiol for 72 h resulted in the up-regulation of an 80-kDa AKAP and the RIIβ subunit of PKA, whereas cells grown in control medium containing only estradiol produced a time-dependent increase of a 140-kDa AKAP. RII overlays performed with [32P]RIIα preferentially detected RII-binding bands of 80 and 95 kDa compared to blots probed with [32P]RIIβ, suggesting that FSH may alter the subcellular location of PKA in an isoform-specific manner. FSH treatment causes a translocation of RIIα from the particulate to the cytosolic fraction coincident with the induction of the 80-kDa AKAP, which is also predominately cytosolic. These data suggest that FSH promotes a redistribution of the type II PKA holoenzyme through the selective induction of an RII isoform-specific AKAP.",
author = "Daniel Carr and DeManno, {Deborah A.} and Angela Atwood and Mary Hunzicker-Dunn and Scott, {John D.}",
year = "1993",
month = "10",
day = "5",
language = "English (US)",
volume = "268",
pages = "20729--20732",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "28",

}

TY - JOUR

T1 - Follicle-stimulating hormone regulation of A-Kinase Anchoring Proteins in granulosa cells

AU - Carr, Daniel

AU - DeManno, Deborah A.

AU - Atwood, Angela

AU - Hunzicker-Dunn, Mary

AU - Scott, John D.

PY - 1993/10/5

Y1 - 1993/10/5

N2 - It has been well established that the biochemical and morphological changes during maturation of granulosa cells that are induced by follicle-stimulating hormone (FSH) occur through the elevation of intracellular cAMP and consequent activation of the cAMP-dependent protein kinase (PKA). In this report we show that FSH action alters the expression of A-Kinase Anchoring Proteins (AKAPs), which function to target the subcellular distribution of the type II PKA. Exposure of granulosa cells grown in primary culture with FSH and estradiol for 72 h resulted in the up-regulation of an 80-kDa AKAP and the RIIβ subunit of PKA, whereas cells grown in control medium containing only estradiol produced a time-dependent increase of a 140-kDa AKAP. RII overlays performed with [32P]RIIα preferentially detected RII-binding bands of 80 and 95 kDa compared to blots probed with [32P]RIIβ, suggesting that FSH may alter the subcellular location of PKA in an isoform-specific manner. FSH treatment causes a translocation of RIIα from the particulate to the cytosolic fraction coincident with the induction of the 80-kDa AKAP, which is also predominately cytosolic. These data suggest that FSH promotes a redistribution of the type II PKA holoenzyme through the selective induction of an RII isoform-specific AKAP.

AB - It has been well established that the biochemical and morphological changes during maturation of granulosa cells that are induced by follicle-stimulating hormone (FSH) occur through the elevation of intracellular cAMP and consequent activation of the cAMP-dependent protein kinase (PKA). In this report we show that FSH action alters the expression of A-Kinase Anchoring Proteins (AKAPs), which function to target the subcellular distribution of the type II PKA. Exposure of granulosa cells grown in primary culture with FSH and estradiol for 72 h resulted in the up-regulation of an 80-kDa AKAP and the RIIβ subunit of PKA, whereas cells grown in control medium containing only estradiol produced a time-dependent increase of a 140-kDa AKAP. RII overlays performed with [32P]RIIα preferentially detected RII-binding bands of 80 and 95 kDa compared to blots probed with [32P]RIIβ, suggesting that FSH may alter the subcellular location of PKA in an isoform-specific manner. FSH treatment causes a translocation of RIIα from the particulate to the cytosolic fraction coincident with the induction of the 80-kDa AKAP, which is also predominately cytosolic. These data suggest that FSH promotes a redistribution of the type II PKA holoenzyme through the selective induction of an RII isoform-specific AKAP.

UR - http://www.scopus.com/inward/record.url?scp=0027452329&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027452329&partnerID=8YFLogxK

M3 - Article

C2 - 8407895

AN - SCOPUS:0027452329

VL - 268

SP - 20729

EP - 20732

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 28

ER -