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Role of focal adhesion kinase in oocyte-follicle communication.

ABSTRACT: Germ cells require communication with associated somatic cells for normal gametogenesis, as exemplified by an oocyte that interacts with granulosa cells via paracrine factors as well as gap junctions located at sites of contact between these two cell types. The objective of the present study was to define the mechanisms by which cell-cell contact with the oocyte is controlled and to determine the extent that the oocyte actively participates in this association. Proline-rich tyrosine kinase 2 (PTK2), a focal adhesion kinase, was found to be activated at sites of contact between the oocyte and trans-zonal cell processes from the surrounding granulosa cells. In order to determine the functional significance of oocyte-derived PTK2 signaling in oocyte-follicle communication, an oocyte-specific Ptk2 knockout was produced through a breeding strategy pairing a floxed Ptk2-CAT-eGFP mouse with the Zp3-Cre line. Since Ptk2-null mice never develop to birth, this represents the first opportunity to define the role of PTK2 in oocyte-follicle communication. Ablation of Ptk2 within the developing oocyte resulted in lower fertility with reduced numbers of pups, lower rates of blastocyst formation, and reduced cell numbers per blastocyst. Follicles containing Ptk2-null oocytes exhibited reduced oocyte diameter, reduced numbers of connexin 37 and 43 foci at the oocyte surface, and impaired dye coupling between oocyte and granulosa cells. These findings are consistent with a model in which PTK2 plays a critical role in establishing or maintaining oocyte-granulosa cell contacts that are essential for gap junction-mediated communication between granulosa cells and the oocyte.

SUBMITTER: McGinnis LK

PROVIDER: S-EPMC4324459 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature

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Role of focal adhesion kinase in oocyte-follicle communication.

McGinnis Lynda K LK Kinsey William H WH

Molecular reproduction and development 20141223 2

Germ cells require communication with associated somatic cells for normal gametogenesis, as exemplified by an oocyte that interacts with granulosa cells via paracrine factors as well as gap junctions located at sites of contact between these two cell types. The objective of the present study was to define the mechanisms by which cell-cell contact with the oocyte is controlled and to determine the extent that the oocyte actively participates in this association. Proline-rich tyrosine kinase 2 (PT ...[more]

PMID: 25536210

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Project description:The survival of endothelial cells is dependent on interactions between the matrix and integrins mediated through focal adhesions. Focal adhesion kinase (FAK) is thought to play a key role in maintaining focal adhesion function and cell survival, whereas caspase-mediated FAK proteolysis is implicated in focal adhesion disassembly during apoptosis. We examined the relationship between changes in FAK phosphorylation and proteolysis during apoptosis of primary porcine aortic endothelial cells (PAEC) induced by staurosporine, a widely used apoptogenic agent in diverse cell types. Staurosporine-induced PAEC apoptosis was detected after 1 h and was preceded by disruption and loss of FAK localization to focal adhesions within a few minutes, whereas staurosporine-induced cleavage of FAK occurred only after 8-24 h. Staurosporine induced a very rapid dephosphorylation of FAK at Tyr(861) and Tyr(397) and caused dissociation of phosphorylated FAK from focal adhesions as early as 30 s. The effect of staurosporine was very potent with striking inhibition of Tyr(861) and Tyr(397) phosphorylation and focal adhesion disruption occurring in the range 10-100 nM. Selective inhibition of a known target of staurosporine, protein kinase C, using GF109203X, and of phosphoinositide 3'-kinase using wortmannin, did not reduce FAK tyrosine phosphorylation at Tyr(861) and Tyr(397), or cause disruption of focal adhesions. Cycloheximide, the protein synthesis inhibitor, induced PAEC apoptosis more slowly than staurosporine, but did not induce FAK dephosphorylation or rapid focal adhesion disruption, and instead caused a slower loss of focal adhesions and a marked increase in FAK proteolysis. These studies show that FAK dephosphorylation and focal adhesion disassembly are very early events mediating the onset of staurosporine-induced endothelial cell apoptosis and are dissociated from FAK proteolysis. Cycloheximide induces apoptosis through a pathway involving FAK proteolysis without dephosphorylation.

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Role of focal adhesion kinase in oocyte-follicle communication.

Publications

Role of focal adhesion kinase in oocyte-follicle communication.

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