Cleavage stage porcine embryos may have differing developmental requirements for karyopherins α2 and α3
Identifieur interne : 001B04 ( Istex/Corpus ); précédent : 001B03; suivant : 001B05Cleavage stage porcine embryos may have differing developmental requirements for karyopherins α2 and α3
Auteurs : Ryan A. Cabot ; Randall S. PratherSource :
- Molecular Reproduction and Development [ 1040-452X ] ; 2003-03.
Abstract
Numerous cellular proteins are able to localize to the nucleus due to the fact that they possess a nuclear localization signal (NLS) in their amino acid sequence. Nuclear localization sequences recognized by the importin α/β heterodimer are found in cellular proteins capable of performing many diverse functions, ranging from chromatin remodeling to cell cycle regulation. Evidence has been presented that suggests individual importin α homologues are present at varying levels in different adult tissues. Other data have shown that specific subsets of NLSs found in different cellular proteins are recognized by individual importin α homologues with varying affinities. This evidence led us to hypothesize that due to the specific cargoes they carry, the mammalian embryo has different developmental requirements for individual importin α homologues. The results of the studies presented here indicate that importin α/β‐mediated import occurs throughout early cleavage in the porcine embryo, as determined by a reporter protein microinjection assay, and that multiple importin α homologues are present throughout early cleavage, as determined by immunocytochemical analysis. An RNA interference approach was used in an attempt to determine the developmental requirements for specific importin α homologues during early cleavage in the porcine embryo. Results from this study showed that fertilized porcine embryos injected with double stranded RNA (dsRNA) corresponding to the importin α homologue karyopherin α3 had significantly fewer nuclei following four days of culture than did embryos injected with dsRNA for another importin α homologue, karyopherin α2, or two control groups. This is the first report indicating that mammalian embryos may have differential developmental requirements for specific nuclear trafficking pathways. Mol. Reprod. Dev. 64: 292–301, 2003. © 2003 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/mrd.10238
Links to Exploration step
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<front><div type="abstract" xml:lang="en">Numerous cellular proteins are able to localize to the nucleus due to the fact that they possess a nuclear localization signal (NLS) in their amino acid sequence. Nuclear localization sequences recognized by the importin α/β heterodimer are found in cellular proteins capable of performing many diverse functions, ranging from chromatin remodeling to cell cycle regulation. Evidence has been presented that suggests individual importin α homologues are present at varying levels in different adult tissues. Other data have shown that specific subsets of NLSs found in different cellular proteins are recognized by individual importin α homologues with varying affinities. This evidence led us to hypothesize that due to the specific cargoes they carry, the mammalian embryo has different developmental requirements for individual importin α homologues. The results of the studies presented here indicate that importin α/β‐mediated import occurs throughout early cleavage in the porcine embryo, as determined by a reporter protein microinjection assay, and that multiple importin α homologues are present throughout early cleavage, as determined by immunocytochemical analysis. An RNA interference approach was used in an attempt to determine the developmental requirements for specific importin α homologues during early cleavage in the porcine embryo. Results from this study showed that fertilized porcine embryos injected with double stranded RNA (dsRNA) corresponding to the importin α homologue karyopherin α3 had significantly fewer nuclei following four days of culture than did embryos injected with dsRNA for another importin α homologue, karyopherin α2, or two control groups. This is the first report indicating that mammalian embryos may have differential developmental requirements for specific nuclear trafficking pathways. Mol. Reprod. Dev. 64: 292–301, 2003. © 2003 Wiley‐Liss, Inc.</div>
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<abstract lang="en">Numerous cellular proteins are able to localize to the nucleus due to the fact that they possess a nuclear localization signal (NLS) in their amino acid sequence. Nuclear localization sequences recognized by the importin α/β heterodimer are found in cellular proteins capable of performing many diverse functions, ranging from chromatin remodeling to cell cycle regulation. Evidence has been presented that suggests individual importin α homologues are present at varying levels in different adult tissues. Other data have shown that specific subsets of NLSs found in different cellular proteins are recognized by individual importin α homologues with varying affinities. This evidence led us to hypothesize that due to the specific cargoes they carry, the mammalian embryo has different developmental requirements for individual importin α homologues. The results of the studies presented here indicate that importin α/β‐mediated import occurs throughout early cleavage in the porcine embryo, as determined by a reporter protein microinjection assay, and that multiple importin α homologues are present throughout early cleavage, as determined by immunocytochemical analysis. An RNA interference approach was used in an attempt to determine the developmental requirements for specific importin α homologues during early cleavage in the porcine embryo. Results from this study showed that fertilized porcine embryos injected with double stranded RNA (dsRNA) corresponding to the importin α homologue karyopherin α3 had significantly fewer nuclei following four days of culture than did embryos injected with dsRNA for another importin α homologue, karyopherin α2, or two control groups. This is the first report indicating that mammalian embryos may have differential developmental requirements for specific nuclear trafficking pathways. Mol. Reprod. Dev. 64: 292–301, 2003. © 2003 Wiley‐Liss, Inc.</abstract>
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