Follicle-stimulating hormone promotes histone H3 phosphorylation on serine-10

D A DeManno; J E Cottom; M P Kline; C A Peters; E T Maizels; M Hunzicker-Dunn

doi:10.1210/me.13.1.91

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Follicle-stimulating hormone promotes histone H3 phosphorylation on serine-10

Journal article

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Peer reviewed

Follicle-stimulating hormone promotes histone H3 phosphorylation on serine-10

D A DeManno, J E Cottom, M P Kline, C A Peters, E T Maizels and M Hunzicker-Dunn

Molecular endocrinology (Baltimore, Md.), Vol.13(1), pp.91-105

01/1999

DOI: https://doi.org/10.1210/me.13.1.91

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https://hdl.handle.net/2376/116079

PMID: 9892015

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Abstract

Histones - chemistry

Culture Media, Serum-Free

Phosphoproteins - metabolism

Granulosa Cells - drug effects

Granulosa Cells - metabolism

Phosphoproteins - chemistry

Follicle Stimulating Hormone - pharmacology

Isoquinolines - pharmacology

Peptide Mapping

Phosphoamino Acids - analysis

Female

Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors

Phosphorylation - drug effects

Cyclic AMP-Dependent Protein Kinases - drug effects

Cyclic AMP-Dependent Protein Kinases - metabolism

Follicle Stimulating Hormone - metabolism

Cells, Cultured

Enzyme Inhibitors - pharmacology

Solubility

Rats

Enzyme Activation - drug effects

Rats, Sprague-Dawley

Serine - metabolism

Histones - drug effects

Animals

Cell Differentiation - drug effects

Sulfonamides

Cell Extracts

Histones - metabolism

FSH promoted the rapid phosphorylation of the nuclear protein histone H3 in immature rat ovarian granulosa cells under experimental conditions that lead to cellular differentiation and not proliferation. FSH-stimulated histone H3 phosphorylation correlated with cAMP-dependent protein kinase A (PKA) activation and translocation of the PKA catalytic subunit to a nuclear-enriched fraction and was inhibited by the PKA inhibitor H89, and histone H3 phosphorylation was stimulated in cells treated with agents that raise intracellular cAMP levels such as forskolin and 8-bromo-cAMP. FSH-stimulated histone H3 phosphorylation in granulosa cells mapped to ser-10, a site previously identified as the PKA phosphorylation site in various mitotically active cells as the mitosis-specific phosphorylation site. Injection of the FSH analog PMSG to immature rats, which is known to stimulate granulosa cell proliferation as well as differentiation, also promoted histone H3 phosphorylation on ser-10 in granulosa cells. These results establish that FSH-stimulated histone H3 phosphorylation in granulosa cells is linked not only to granulosa cell mitosis but also to granulosa cell differentiation and that FSH-stimulated histone H3 phosphorylation on ser-10 in isolated granulosa cells is mediated by PKA. These results also identify the PKA-dependent histone H3 phosphorylation as an early nuclear protein marker for FSH-stimulated differentiation of granulosa cells. Based on the recently described function of histone H3 as a coactivator of transcription, these results are consistent with the hypothesis that phosphorylated histone H3 may facilitate PKA-dependent gene transcription in granulosa cells leading to the preovulatory phenotype.

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Title: Follicle-stimulating hormone promotes histone H3 phosphorylation on serine-10
Creators: D A DeManno - Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611, USA
J E Cottom
M P Kline
C A Peters
E T Maizels
M Hunzicker-Dunn
Publication Details: Molecular endocrinology (Baltimore, Md.), Vol.13(1), pp.91-105
Academic Unit: Molecular Biosciences, School of
Publisher: United States
Grant note: HD-28048 / NICHD NIH HHS F32 HD-07244 / NICHD NIH HHS P01 HD-21921 / NICHD NIH HHS
Identifiers: 99900547564301842
Language: English
Resource Type: Journal article