The involvement of Fyn kinase in resumption of the first meiotic division in mouse oocytes

Levi, Mattan; Maro, Bernard; Shalgi, Ruth

doi:10.4161/cc.9.8.11299

Cited by 32 publications

(38 citation statements)

References 63 publications

(130 reference statements)

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“…We have previously demonstrated that rat oocytes activation, triggered by SrCl 2 , puromycin, or ionomycin, is inhibited in the presence of SFK inhibitors, PP2 and SU6656 (Talmor-Cohen et al 2004, Tomashov-Matar et al 2007 and have recently shown that the same applies to mouse oocytes (Levi & Shalgi 2009, Levi et al 2010. We were able to demonstrate the localization of Fyn to the cytoplasm, cortex, and MII spindle of immunostained rat oocytes (Talmor-Cohen et al 2004).…”

Section: Introductionsupporting

confidence: 48%

“…Furthermore, our previous data indicate that the rate of extrusion of PBI and its size were also affected by the inhibition of cortical Fyn (Levi et al 2010). Interestingly, the TII spindle in DN-Fyn-FLAG cRNA-microinjected oocytes was longer than in control oocytes.…”

Section: Discussionmentioning

confidence: 99%

“…When the spindle was fully rotated, cleavage took place and the PBII was extruded. Unlike the symmetric localization of Fyn around the spindle midzone during the extrusion of PBI (Levi et al 2010) and PBII, Fyn concentrated asymmetrically at the cortical area closest to the spindle midzone, the area designated for ingression of the cleavage furrow, where F-actin have also been accumulated. Fyn resumed its homogenous cortical distribution pattern before translocating again to the area above the spindle midzone designated for ingression of the cortical cleavage furrow during the first mitotic cleavage.…”

Section: Discussionmentioning

confidence: 99%

“…MII oocytes were removed from the oviductal ampullae, their cumulus cells were dispersed by hyaluronidase (H-3631; Sigma), and the oocytes were cultured in 20 ml drops of M2 medium under mineral oil at 37 8C. (Levi et al 2010). All plasmids were sequenced and analyzed and they were linearized using SfiI restriction enzyme (New England Biolabs, Ipswich, MA, USA).…”

Section: Ovulated MII Oocytesmentioning

confidence: 99%

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Fyn kinase is involved in cleavage furrow ingression during meiosis and mitosis

Levi¹,

Maro²,

Shalgi³

2010

Reproduction

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Fertilization of mammalian oocytes triggers their exit from the second meiotic division metaphase arrest. The extrusion of the second polar body (PBII) that marks the completion of meiosis is followed by the first mitotic cleavage of the zygote. Several lines of evidence in somatic cells imply the involvement of Fyn, an Src family kinase (SFK), in cell cycle control and actin functions. In this study, we demonstrate, using live cell confocal imaging and microinjection of Fyn cRNAs, the recruitment of Fyn to the oocyte's cortical area overlying the chromosomes and its colocalization with filamentous actin (F-actin) during exit from the meiotic metaphase. Fyn concentrated asymmetrically at the cortical site designated for ingression of the PBII cleavage furrow, where F-actin had already been accumulated, and then redispersed throughout the entire cortex only to be recruited again to the cleavage furrow during the first mitotic division. Although microinjection of dominant negative Fyn did not affect initiation of the cleavage furrow, it prolonged the average duration of ingression, decreased the rates of PB extrusion and of the first cleavage, and led to the formation of bigger PBs and longer spindles. Extrusion of the PBII was blocked in oocytes exposed to SU6656, an SFK inhibitor. Our results demonstrate, for the first time, a continuous colocalization of Fyn and F-actin during meiosis and imply a role for the SFKs, in general, and for Fyn, in particular, in regulating pathways that involve actin cytoskeleton, during ingression of the meiotic and mitotic cleavage furrows.

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Section: Introductionsupporting

confidence: 48%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Ovulated MII Oocytesmentioning

confidence: 99%

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Fyn kinase is involved in cleavage furrow ingression during meiosis and mitosis

Levi¹,

Maro²,

Shalgi³

2010

Reproduction

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“…The ZP-free oocytes were fixed by 3% paraformaldehyde (Merck, Gibbstown, NJ, USA), washed in blocking solution (3% fetal bovine serum in Dulbecco's phosphate buffer (DPBS)) and permeabilized (10 min in 0.05% Nonidet P-40; Sigma). Oocytes were further incubated for 1.5 h with anti-PPM1A antibody, washed in blocking solution and incubated for an additional 1 h with Cy3-conjugated secondary antibody [38] together with Hoechst 33342. Stained oocytes were visualized and photographed by a Leica laser confocal microscope (SP5, Wetzlar, Germany).…”

Section: Immunofluorescencementioning

confidence: 99%

De novo synthesis of protein phosphatase 1A, magnesium dependent, alpha isoform (PPM1A) during oocyte maturation

Chuderland

Dvashi

Kaplan-Kraicer

et al. 2012

Cellular and Molecular Biology Letters

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Oocyte maturation in mammals is a multiple-stage process that generates fertilizable oocytes. Ovarian oocytes are arrested at prophase of the first meiotic division characterized by the presence of a germinal vesicle. Towards ovulation, the oocytes resume meiosis and proceed to the second metaphase in a process known as maturation; they undergo nuclear and cytoplasmic changes that are accompanied by translation and degradation of mRNA. Protein phosphatase 1A, magnesium dependent, alpha isoform (PPM1A), which belongs to the metal-dependent serine/threonine protein phosphatase family, is highly conserved during evolution. PPM1A plays a significant role in many cellular functions such as cell cycle progression, apoptosis and cellular differentiation. It works through diverse signaling pathways, including p38 MAP kinase JNK and transforming growth factor beta (TGF-β). Herein we report that PPM1A is expressed in mouse oocytes and that its mRNA level rises during oocyte maturation. Using quantitative real-time polymerase chain reaction (qPCR) and western blot analysis, we found that PPM1A mRNA is synthesized at the beginning of the maturation process and remains elevated in the mature oocytes, promoting the accumulation of PPM1A

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Protein tyrosine kinase signaling during oocyte maturation and fertilization

McGinnis

Carroll

Kinsey

2011

Molecular Reproduction Devel

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The oocyte is a highly specialized cell capable of accumulating and storing energy supplies as well as maternal transcripts and pre-positioned signal transduction components needed for zygotic development, undergoing meiosis under control of paracrine signals from the follicle, fusing with a single sperm during fertilization, and zygotic development. The oocyte accomplishes this diverse series of events by establishing an array of signal transduction pathway components that include a select collection of protein tyrosine kinases (PTKs) that are expressed at levels significantly higher than most other cell types. This array of PTKs includes cytosolic kinases such as SRC-family PTKs (FYN and YES), and FAK kinases, as well as FER. These kinases typically exhibit distinct patterns of localization and in some cases are translocated from one subcellular compartment to another during meiosis. Significant differences exist in the extent to which PTK-mediated pathways are used by oocytes from species that fertilize externally versus internally. The PTK activation profiles as well as calcium signaling pattern seems to correlate with the extent to which a rapid block to polyspermy is required by the biology of each species. Suppression of each of the SRC-family PTKs as well as FER kinase results in failure of meiotic maturation or zygote development, indicating that these PTKs are important for oocyte quality and developmental potential. Future studies will hopefully reveal the extent to which these factors impact clinical assisted reproductive techniques in domestic animals and humans.

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The involvement of Fyn kinase in resumption of the first meiotic division in mouse oocytes

Cited by 32 publications

References 63 publications

Fyn kinase is involved in cleavage furrow ingression during meiosis and mitosis

Fyn kinase is involved in cleavage furrow ingression during meiosis and mitosis

De novo synthesis of protein phosphatase 1A, magnesium dependent, alpha isoform (PPM1A) during oocyte maturation

Protein tyrosine kinase signaling during oocyte maturation and fertilization

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