Follicle-stimulating hormone regulation of A-kinase anchoring proteins in granulosa cells

• Published in: The Journal of biological chemistry 1993-10, Vol.268 (28), p.20729-20732
• Main Authors: Carr, D W, DeManno, D A, Atwood, A, Hunzicker-Dunn, M, Scott, J D
• Format: Article
• Language: English
• Subjects: A Kinase Anchor Proteins; Adaptor Proteins, Signal Transducing; Animals; Base Sequence; Carrier Proteins; Cells, Cultured; Colforsin - pharmacology; Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit; Cyclic AMP-Dependent Protein Kinase RIIbeta Subunit; Cyclic AMP-Dependent Protein Kinase Type II; Cyclic AMP-Dependent Protein Kinases - chemistry; Cyclic AMP-Dependent Protein Kinases - metabolism; DNA, Single-Stranded; Female; Follicle Stimulating Hormone - pharmacology; Granulosa Cells - drug effects; Granulosa Cells - metabolism; Kinetics; Molecular Sequence Data; Proteins - metabolism; Rats; Rats, Sprague-Dawley; Subcellular Fractions
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(19)36841-3

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 RII beta 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]RII alpha preferentially detected RII-binding bands of 80 and 95 kDa compared to blots probed with [32P]RII beta, suggesting that FSH may alter the subcellular location of PKA in an isoform-specific manner. FSH treatment causes a translocation of RII alpha 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.