Antibody Microarray Analyses of Signal Transduction Protein Expression and Phosphorylation during Porcine Oocyte Maturation

Pelech, Steven; Jelínková, Lucie; Šušor, Andrej; Zhang, Hong; Shi, Xianglin; Pavlok, A.; Kubelka, Michal; Kovářová, Hana

doi:10.1021/pr800082a

Cited by 30 publications

(30 citation statements)

References 137 publications

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“…This disagrees with previous studies showing no change in overall levels of pTyr proteins between GV and MII [16]. Interestingly, a recent study examining changes in protein phosphorylation and the kinome of porcine oocytes during maturation found that the number of tyrosine phosphorylated proteins increased was equal to the number that decreased during transitions from GV-MI and MI-MII [22]. This may explain why traditional global protein Fig.…”

Section: Intracellular Localization and Dynamics Of Protein Phosphorycontrasting

confidence: 90%

Dynamics of protein phosphorylation during meiotic maturation

McGinnis

Albertini

2010

J Assist Reprod Genet

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Purpose To ask whether distinct kinase signaling pathways mediate cytoplasmic or nuclear maturation of mouse oocytes and if in vitro maturation influences the distribution and timing of these phosphorylation events. Methods Mouse cumulus oocyte complexes (COCs) were matured under conditions known to influence oocyte quality (basal or supplemented media) and assayed with epitope specific antibodies that would distinguish between Cdk1 or tyrosine kinase targets at 0, 2, 4, 8, and 16 hrs. Semi-quantitative image analysis was used to assess the topographical patterns of protein phosphorylation during in vitro maturation. In vitro fertization and embryo culture were used to examine the effects of culture conditions on developmental potential. Results Protein tyrosine phosphorylation increased during meiotic progression from methaphase-I to metaphase-II. Levels were significantly higher in the oocyte cortex. Levels of cortical staining are enhanced in oocytes matured in supplemented media that displayed higher developmental competence. In contrast, bulk substrates for Cdk1 kinase localize to the meiotic spindle while cytoplasmic levels of kinase activity increase throughout meiotic progression; culture media had no measurable effect. Ablation of the tyrosine kinase Fyn significantly reduced cortical levels of tyrosine phosphorylation. Conclusions The findings indicate that distinct signaling pathways mediate nuclear and cytoplasmic maturation during in vitro maturation in a fashion consistent with a role for tyrosine kinases in cortical maturation and oocyte quality.

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Section: Intracellular Localization and Dynamics Of Protein Phosphorycontrasting

confidence: 90%

Dynamics of protein phosphorylation during meiotic maturation

McGinnis

Albertini

2010

J Assist Reprod Genet

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“…However, few data are currently available on GSK3 expression in ovary of human or large domestic animals and its involvement in oocyte maturation control. By antibody microarray analysis, GSK3A and GSK3B isoforms were recently detected in pig and bovine oocytes (Pelech et al 2008).…”

Section: Introductionmentioning

confidence: 99%

Glycogen synthase kinase 3B in bovine oocytes and granulosa cells: possible involvement in meiosis during in vitro maturation

Uzbekova¹,

Salhab²,

Perreau³

et al. 2009

Reproduction

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Glycogen synthase kinase 3 (GSK3) regulates cellular metabolism and cell cycle via different signalling pathways. In response to insulin and growth factors GSK3 is serine-phosphorylated and inactivated. We analysed GSK3B expression and activation in bovine cumulus cells (CC) and oocytes at different meiotic stages in vitro in parallel with MAP kinases ERK (MAPK3/MAPK1) and p38 (MAPK14). GSK3B localised to cytoplasm in granulosa cells and in oocytes throughout folliculogenesis. In mature metaphase-II (MII) oocytes, GSK3B was concentrated to the region of midzone between the oocyte and the first polar body, as well as active phospho-Thr Aurora A kinase (AURKA). During in vitro maturation (IVM), in oocytes, phospho-Ser 9 -GSK3B level increased as well as phospho-MAPK3/MAPK1, while phospho-MAPK14 decreased. In CC, phospho-MAPK14 increased upon germinal vesicle breakdown (GVBD)/metaphase-I (MI) and then decreased during transition to MII. Administration of inhibitors of GSK3 activity (lithium chloride or 2 0 Z,3 0 E -6-bromoindirubin-3 0 -oxime) rapidly increased phospho-Ser 9 -GSK3B, and led to transient decrease of phospho-MAPK3/MAPK1 and to durable enhancing of phospho-MAPK14 in granulosa primary cell culture. GSK3 inhibitors during IVM diminished cumulus expansion and delayed meiotic progression. In cumulus, phospho-MAPK14 level was significantly higher in the presence of inhibitors, comparing with control, through the time of MI/MII transition. In oocytes, phospho-GSK3B was increased and phospho-MAPK3/MAPK1 was decreased before GVBD and oocytes were mainly arrested at MI. Therefore, GSK3B might regulate oocyte meiosis, notably MI/MII transition being the part of MAPK3/1 and MAPK14 pathways in oocytes and CC. GSK3B might be also involved in the local activation of AURKA that controls this transition.

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“…Additionally, tyros-doi: 10.17221/8580-VETMED ine phosphorylated proteins increased in both the cell cortex and cytoplasm after oocytes fully developed in disagreement with previous findings (BenYosef et al 1998). However, an increasing number of phosphorylated proteins during the G-MI stage corresponded with their decreasing number in the transition to the MI-MII stage (Pelech et al 2008).…”

Section: Molecular Markers Of Oocyte Developmental Competencementioning

confidence: 90%

Developmental competence of mammalian oocytes-insights into molecular research and the promise of microfluidic technology: a review

Kempisty¹,

Zawierucha²,

Ciesiółka³

et al. 2015

Vet. Med. - Czech

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Developmental competence of female gametes determines their maturation ability, successful fertilisation, and proper zygote formation. Oocyte quality may be assessed by expression profiling of several gene markers such as Cx43, TGFB, GDF9, BMP, Lox and Pdia5 that determine the biological features of oocytes. Conversely, several other extrinsic factors, including follicular size or heat shock may significantly influence oocyte quality and ability to grow and develop during folliculo-and oogenesis. However, using molecular methods for evaluation of oocyte quality often leads to destruction of an analysed cell. Therefore, there is an increased requirement to seek new non-invasive methods of oocyte-embryo quality assessment. Here we describe the Lab-on-Chip system based on microfluidic technology, which is the first parametric and objective device for evaluation of oocyte developmental competence using spectral images. In this review several extrinsic factors and molecular markers of oocyte developmental competence are discussed. Furthermore, based on our previous studies, we discuss the possibility of applying the spectrophotometric system (Lab-on-Chip) in both biomedical and reproductive research in domestic animals.

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Antibody Microarray Analyses of Signal Transduction Protein Expression and Phosphorylation during Porcine Oocyte Maturation

Cited by 30 publications

References 137 publications

Dynamics of protein phosphorylation during meiotic maturation

Dynamics of protein phosphorylation during meiotic maturation

Glycogen synthase kinase 3B in bovine oocytes and granulosa cells: possible involvement in meiosis during in vitro maturation

Developmental competence of mammalian oocytes-insights into molecular research and the promise of microfluidic technology: a review

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