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First published online June 25, 2007

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Oocytes trigger glycolysis

Mammalian oocytes cannot perform the essential metabolic process of glycolysis and so rely on their companion cumulus cells to provide them with glycolysis products. To facilitate this, oocytes secrete paracrine factors that promote the expression of glycolytic enzymes, such as platelet phosphofructokinase (PFKP) and lactate dehydrogenase A (LDHA), in cumulus cells. John Eppig and colleagues now show that oocyte-derived BMP15 and FGF8 cooperatively promote Pfkp and Ldha expression and glycolysis in mouse cumulus cells (see p. 2593). In Bmp15^-/- and Bmp15^-/- Gdf9^+/- mutant mice, both Pfkp and Ldha expression and glycolysis are reduced in cumulus cells. Moreover, oocytes from these mutant mice are unable to promote glycolysis in wild-type cumulus cells. The co-culture of cumulus cells (without an oocyte) with BMP15 and FGF8 promotes Pfkp and Ldha expression and glycolysis, whereas the co-culture of cumulus cells with GDF9 and either BMP15 or FGF8 does not induce glycolysis. Understanding how BMP and FGF signals cooperate in this setting will clarify our knowledge of oocyte and follicular development.

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Oocyte-derived BMP15 and FGFs cooperate to promote glycolysis in cumulus cells

Koji Sugiura, You-Qiang Su, Francisco J. Diaz, Stephanie A. Pangas, Shweta Sharma, Karen Wigglesworth, Marilyn J. O'Brien, Martin M. Matzuk, Shunichi Shimasaki, and John J. Eppig
Development 2007 134: 2593-2603. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in Development Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?