Behavior of the Components of Maturation-Promoting Factor, cdc2 Kinase and Cyclin B, during Oocyte Maturation of Goldfish

Katsu, Yoshinao; Yamashita, Masakane; Kajiura, Hiroko; Nagahama, Yoshitaka

doi:10.1006/dbio.1993.1289

Cited by 74 publications

(37 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This increased synthesis of cyclin B may control the correct timing of the first meiotic cleavage. In goldfish oocytes, synthesis of new cyclin B is required for oocyte maturation (Katsu et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

Requirement for phosphorylation of cyclin B1 for Xenopus oocyte maturation.

Meyer

Donoghue

1995

MBoC

View full text Add to dashboard Cite

Maturation-promoting factor, consisting of cdc2 protein kinase and a regulatory B-type cyclin, is a universal regulator of meiosis and mitosis in eukaryotes. In Xenopus, there are two subtypes of B-type cyclins, designated Bi and B2, both of which are phosphorylated.In this study, we have investigated the biological significance of this phosphorylation for Xenopus cyclin Bi during meiotic maturation. We have used a combination of sitedirected mutagenesis and phosphopeptide-mapping to identify serine residues 2, 94, 96, 101, and 113 as presumptive phosphorylation sites, and together these sites account for all cyclin Bi phosphorylation in oocytes before germinal vesicle breakdown (GVBD). Single Ser-* Ala mutants as well as multiple site mutants have been constructed and characterized. Phosphorylation of cyclin Bi appears to be required for Xenopus oocyte maturation, based on the significantly diminished ability of the quintuple Ala mutant to induce oocyte maturation. Furthermore, partial phosphorylation of these five sites is sufficient to meet this requirement. Phosphorylation of cyclin Bi is not required for cdc2 kinase activity, for binding to cdc2 protein, for stability of cyclin Bi before GVBD, or for destruction of cyclin Bi after GVBD or after egg activation. A quintuple Glu mutant was also constructed, with serine residues 2, 94, 96, 101, and 113 mutated to Glu. In contrast to the quintuple Ala mutant, the quintuple Glu mutant was able to induce oocyte maturation efficiently, and with more rapid kinetics than wild-type cyclin Bi. These data confirm that phosphorylation, as mimicked by Ser->Glu mutations, confers enhanced biological activity to cyclin Bi. Possible roles of cyclin Bi phosphorylation are discussed that might account for the increased biological activity of the quintuple Glu mutant.

show abstract

Section: Introductionmentioning

confidence: 99%

Requirement for phosphorylation of cyclin B1 for Xenopus oocyte maturation.

Meyer

Donoghue

1995

MBoC

View full text Add to dashboard Cite

show abstract

“…Menurut Krassel et al (2003), keberadaan molekul inhibin dalam darah mamalia berfungsi untuk menghambat sekresi FSH dan LH sehingga tidak terjadi superovulasi, tetapi hasil penelitian Wu et al (2000) menyimpulkan bahwa secara in vitro inhibin dapat mematurasi oosit pada ikan zebra (Danio rerio). Katsu et al (1993) mengemukakan ekspresi mRNA inhibin pada ikan salmon berbeda dengan ekspresi mRNA inhibin pada mamalia, sehingga diduga inhibin adalah salah faktor yang berperan mematangkan telur ikan. Hasil penelitian tersebut juga menunjukkan inhibin yang ada pada ikan zebra dan ikan salmon homolog dengan inhibin yang ada pada manusia dan mamalia lain.…”

Section: Pendahuluanunclassified

“…Mekanisme intraselluler maturasi akhir pada prinsipnya diawali dengan adanya fosforilasi. Katsu et al (1993) dan Yamashita dan Nagahama (1995) menjelaskan mekanisme kejadian maturasi akhir pada ikan dimulai dengan adanya aksi MIH dari sel granulosa yang merangsang terjadinya aktivasi MPF, MPF kemudian mem-fosforilasi protein-protein target termasuk lamin dan histon.…”

Section: Kondisi Gonadunclassified

Maturation of Nile-Tilapia (Oreochromis niloticus) Oocytes With Exposed by Goat Inhibin Isolated from Granulose Cells

Linggi¹,

Aulanni’am

Risjani

et al. 2007

J Kedokt Hewan

View full text Add to dashboard Cite

ABSTRAKTujuan penelitian adalah mengetahui peran regulasi inhibin pada proses maturasi telur ikan nila (Oreochromis niloticus). Inhibin yang digunakan berasal dari isolasi sel granulosa ovarium kambing yang disuntikkan ke dalam induk betina. Setelah 3 hari perlakuan, gonad dikeluarkan dengan cara pembedahan, kemudian dilakukan evaluasi maturasi di bawah mikroskop stereo. Hasil penelitian menunjukkan rata-rata persentase telur yang mengalami maturasi pada dosis 0, 20, 40, dan 60 µg/ekor secara berurutan masing-masing sebesar 50,05; 29,44; 21,46; dan 30,83%. Dari hasil penelitian disimpulkan bahwa pemaparan isolat inhibin dari sel granulosa ovarium kambing dapat menginduksi maturasi oosit (telur) ikan nila.Kata kunci: inhibin, maturasi, oosit ABSTRACTThe present study aimed to investigate the role of inhibin in the regulation of oocytes maturation. Inhibin was isolated from goat granulose cells and injected by intraperitoneal in to female Nile-Tilapia. Three days later its gonad was taken by decapitation and the change of oocyte was evaluated under microscope. Results showed that average of percentages of oocytes that undergo maturated after exposed with inhibin of 0, 20, 40, and 60 µg/individual 50. 05, 29.44, 21.46, and 30.83%, respectively.The exposure of doses of goat inhibin in Nile-Tilapia showed significantly different (P<0.01) to percentages of mature oocytes. It was conluded that exposition of goat inhibin from granulose cells can inducing the maturation of Nile-Tilapia oocytes.

show abstract

“…MPF has been purified from the eggs of several species and shown to consist of Cdc2 and cyclin B Gautier et al, 1988Gautier et al, , 1990Labbé et al, 1988Labbé et al, , 1989Yamashita et al, 1992a, b;Katsu et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

“…To date, the molecular mechanisms of MPF formation and activation during oocyte maturation have been investigated in detail for Xenopus (Gautier and Maller, 1991;Kobayashi et al, 1991;Minshull et al, 1991) and goldfish (Hirai et al, 1992;Kajiura et al, 1993;Katsu et al, 1993) (see also review by Yamashita, 1998). Cyclin B is absent in immature goldfish oocytes, and its synthesis through translational activation of dormant mRNA in immature oocytes by stimulation of MIH (17α, is prerequisite for initiating oocyte maturation in this species Katsu et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Immunological Detection and Characterization of Poly(A) Polymerase, Poly(A)-Binding Protein and Cytoplasmic Polyadenylation Element-Binding Protein in Goldfish and Xenopus Oocytes

Nakahata¹,

Mita

Katsu

et al. 2001

Zoological Science

Self Cite

View full text Add to dashboard Cite

ABSTRACT-Cytoplasmic polyadenylation regulates translational activation of dormant cyclin B1 mRNA stored in immature oocytes, a process required for the initiation of oocyte maturation in goldfish and Xenopus. As a first step towards understanding the molecular mechanisms of translational activation of cyclin B1 during oocyte maturation, we have isolated cDNA clones encoding proteins involved in cytoplasmic polyadenylation and produced specific antibodies against recombinant proteins. These include poly(A) polymerase (PAP), poly(A)-binding protein (PABP) and cytoplasmic polyadenylation element-binding protein (CPEB). Monoclonal antibodies raised against goldfish PAP recognized several forms of PAP in goldfish and Xenopus oocytes. Besides ordinary PAPs with high molecular weight (ca. 100 kDa), the antibodies also detected those with low molecular weight (ca. 40 kDa) that are present specifically in the cytoplasm, raising new players that might be responsible for cytoplasmic polyadenylation. An antibody against goldfish PABP showed for the first time in Xenopus oocytes the protein expression of PABPII, another PABP distinct from the well-characterized PABPI. Monoclonal antibodies raised against Xenopus CPEB recognized both unphosphorylated 62-kDa and phosphorylated 64-kDa forms but did not cross-react with goldfish CPEB, which was specifically detected by anti-goldfish CPEB monoclonal antibodies produced previously. The cDNAs, recombinant proteins and antibodies produced in this study are expected to provide useful tools for investigating the regulatory mechanisms of cyclin B1 translation during oocyte maturation in goldfish and Xenopus.

show abstract

Behavior of the Components of Maturation-Promoting Factor, cdc2 Kinase and Cyclin B, during Oocyte Maturation of Goldfish

Cited by 74 publications

References 0 publications

Requirement for phosphorylation of cyclin B1 for Xenopus oocyte maturation.

Requirement for phosphorylation of cyclin B1 for Xenopus oocyte maturation.

Maturation of Nile-Tilapia (Oreochromis niloticus) Oocytes With Exposed by Goat Inhibin Isolated from Granulose Cells

Immunological Detection and Characterization of Poly(A) Polymerase, Poly(A)-Binding Protein and Cytoplasmic Polyadenylation Element-Binding Protein in Goldfish and Xenopus Oocytes

Contact Info

Product

Resources

About