נגישות
menu      
Advanced Search
Syntax
Search...
Volcani treasures
About
Terms of use
Manage
Community:
אסיף מאגר המחקר החקלאי
Powered by ClearMash Solutions Ltd -
Selective degradation of cyclin B1 mRNA in rat oocytes by RNA interference (RNAi)
Year:
2004
Source of publication :
Journal of Molecular Endocrinology
Authors :
Gershon, Eran
;
.
Volume :
33
Co-Authors:
Lazar, S., Department of Biological Regulation, Weizmann Institute of Science, Rehovot 76100, Israel
Gershon, E., Department of Biological Regulation, Weizmann Institute of Science, Rehovot 76100, Israel
Dekel, N., Department of Biological Regulation, Weizmann Institute of Science, Rehovot 76100, Israel
Facilitators :
From page:
73
To page:
85
(
Total pages:
13
)
Abstract:
Cyclic adenosine monophosphate (cAMP) keeps oocytes in meiotic arrest, thereby preventing activation of the key regulators of meiosis, p34cdc2/cyclin B1, (known as maturation-promoting factor (MPF)) and Erk 1 and 2, members of the mitogen-activated protein kinase (MAPK) family. The activity of MAPK in oocytes is upregulated by Mos. We previously demonstrated that Mos translation in rat oocytes is negatively regulated by a PKA-mediated cAMP action, which inhibits c-mos mRNA polyadenylation and is associated with the suppression of p34 cdc2 kinase. The goal of the present study was to provide definitive evidence that Mos translation is subjected to MPF regulation. In order to inhibit MPF activity, we employed the double-stranded (ds) RNA interference (RNAi) of gene expression. We demonstrated that the introduction of cyclin B1 dsRNA into rat oocytes selectively depleted the corresponding mRNA, further ablating its protein product. These oocytes, which exhibit low MPF activity, failed to elongate the c-mos mRNA poly(A) tail, did not accumulate Mos and were unable to activate MAPK. We conclude that an active MPF in rat oocytes is necessary for c-mos mRNA polyadenylation and Mos translation. © 2004 Society for Endocrinology.
Note:
Related Files :
animal cell
Animals
animal tissue
Base Sequence
Cyclin B
mitogen activated protein kinase
Show More
Related Content
More details
DOI :
10.1677/jme.0.0330073
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
24458
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:07
You may also be interested in
Scientific Publication
Selective degradation of cyclin B1 mRNA in rat oocytes by RNA interference (RNAi)
33
Lazar, S., Department of Biological Regulation, Weizmann Institute of Science, Rehovot 76100, Israel
Gershon, E., Department of Biological Regulation, Weizmann Institute of Science, Rehovot 76100, Israel
Dekel, N., Department of Biological Regulation, Weizmann Institute of Science, Rehovot 76100, Israel
Selective degradation of cyclin B1 mRNA in rat oocytes by RNA interference (RNAi)
Cyclic adenosine monophosphate (cAMP) keeps oocytes in meiotic arrest, thereby preventing activation of the key regulators of meiosis, p34cdc2/cyclin B1, (known as maturation-promoting factor (MPF)) and Erk 1 and 2, members of the mitogen-activated protein kinase (MAPK) family. The activity of MAPK in oocytes is upregulated by Mos. We previously demonstrated that Mos translation in rat oocytes is negatively regulated by a PKA-mediated cAMP action, which inhibits c-mos mRNA polyadenylation and is associated with the suppression of p34 cdc2 kinase. The goal of the present study was to provide definitive evidence that Mos translation is subjected to MPF regulation. In order to inhibit MPF activity, we employed the double-stranded (ds) RNA interference (RNAi) of gene expression. We demonstrated that the introduction of cyclin B1 dsRNA into rat oocytes selectively depleted the corresponding mRNA, further ablating its protein product. These oocytes, which exhibit low MPF activity, failed to elongate the c-mos mRNA poly(A) tail, did not accumulate Mos and were unable to activate MAPK. We conclude that an active MPF in rat oocytes is necessary for c-mos mRNA polyadenylation and Mos translation. © 2004 Society for Endocrinology.
Scientific Publication
You may also be interested in