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Mol. Hum. Reprod. Advance Access originally published online on June 20, 2009
Molecular Human Reproduction 2009 15(8):499-506; doi:10.1093/molehr/gap048
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© The Author 2009. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

MATER protein as substrate of PKC{varepsilon} in human cumulus cells

T. Maraldi1,4, M. Riccio1, P. Sena1, L. Marzona1, A. Nicoli2, A. La Marca3, S. Marmiroli1, J. Bertacchini1, G. La Sala2 and A. De Pol1

1Department of Anatomy and Histology, University of Modena and Reggio Emilia, Via Del Pozzo 71, 41100 Modena, Italy 2Department of Obstetrics and Gynecology, Arcispedale Santa Maria Nuova, V.le Risorgimento 80, 42100 Reggio Emilia, Italy 3Mother-Infant Department, Unit of Obstetrics and Gynecology, University of Modena and Reggio Emilia, Via Del Pozzo 71, 41100 Modena, Italy

4 Correspondence address. Fax: +39-059-4224861; E-mail: tullia.maraldi{at}unimo.it

High activity of the phosphoinositide 3-kinase/Akt pathway in cumulus cells plays an important role in FSH regulation of cell function and Protein Kinase C epsilon (PKC{varepsilon}) collaborates with these signalling pathways to regulate cell proliferation. Relevant roles in follicular development are played by Maternal Antigen That Embryos Require (MATER) that is a cumulus cell- and oocyte-specific protein dependent on the maternal genome. We recently demonstrated that human MATER localizes at specific domains of oocytes and, for the first time, also in cumulus cells. MATER contains a carboxy-terminal leucine-rich repeat domain involved in protein–protein interactions regulating different cellular functions. Here we investigated the functional role of MATER. Thus, we performed coimmunoprecipitation experiments using HEK293T cells expressing human MATER; a similar approach was then followed in human cumulus/follicular cells. In MATER+HEK293T cells, we observed that this protein acts as a phosphorylation substrate of PKC{varepsilon}. Western blot experiments indicate that, unlike oocytes, human cumulus cells express PKC{varepsilon}. Immunoprecipitation and confocal analysis suggest for the first time that MATER protein interacts with this protein kinase in cumulus cells under physiological conditions. Since PKC{varepsilon} is known to collaborate with antiapoptotic signalling pathways, this suggests a novel mechanism for the function of MATER in follicular maturation.

Key words: cumulus cells/follicular development/human ovary/MATER/PKC

Submitted on May 5, 2009; resubmitted on June 16, 2009; accepted on June 16, 2009.


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