Matches in SemOpenAlex for { <https://semopenalex.org/work/W1978356064> ?p ?o ?g. }
Showing items 1 to 66 of
66
with 100 items per page.
- W1978356064 endingPage "170" @default.
- W1978356064 startingPage "170" @default.
- W1978356064 abstract "Oocyte growth, maturation, and activation are complex processes that include transcription, heterochromatin formation, chromosome condensation and decondensation, two consecutive chromosome separations, and genomic imprinting for producing the mature egg. The first sign of oocyte maturation is phosphorylation of histone H3, which leads to the chromosome condensation (Bui et al. 2004 Biol. Reprod. 70, 1843-1851). The objective of this study was to investigate the change in chromosome morphology in relation to histone modifications in pig oocytes during growth, maturation, and activation. Growing oocytes were collected from follicles at various diameters (from 0.1 to 6 mm) in pig ovaries. For maturation, oocyte-cumulus-granulosa cell complexes (OCGC) were collected from follicles that were 3 to 6 mm in diameter and cultured in modified TCM 199 for different periods of time to obtain meiotic stages of oocytes. For activation, oocytes were cultured for maturation in 42 h and were activated using a protocol that was described previously (Nguyen et al. 2003 Theriogenology 59, 719-734). Then, oocytes were examined by immunostaining with antibodies: anti-phospho-histone H3 at serine 10 or serine 28 (S10 or S28), anti-trimethyl-histone H3 at lysine 9 (K9), and anti-acetyl-histone H3 at lysine 9, 14, or 28 (K9, K14, or K28). Some oocytes were examined for double assay of Cdc2 and H3 kinase, which were measured by phosphorylation of histone H1 and myelin basic protein as their substrates. To examine the effects of histone deacetylase (HDAC) inhibition, OCGC were cultured in maturation medium supplemented with or without 100 nM trichostatin A for 42 h. The results show that, during the growth phase, histone H3 became methylated at K9 and is acetylated at K9, K14, and K18. When the fully grown oocytes start maturation, histone H3 becomes phosphorylated at S28 and then S10 and is deacetylated at K9, K14, and K18. After oocyte activation, reacetylation and dephosphorylation of histone H3 correlates to the decondensation of chromosomes. We also found that the activity of histone H3 kinase occurred at a similar time course to that of phosphorylation of histone H3-S28. This suggests that phosphorylation of H3-S28 might be one of the key events initiating meiotic chromosome condensation. The inhibition of HDAC induces maintenance of acetylation of H3-K14 and dephosphorylation of histone H3 at S10 and S28. Therefore, the chromosome could not condense and affect meiotic progression. It is possible that deacetylation is required for the phosphorylation of histone H3. The results suggest that chromatin morphology of pig oocytes is regulated by acetylation/deacetylation and phosphorylation/dephosphorylation of histone H3 and that histone deacetylase activity is essential for the process of chromatin remodeling in pre-ovulatory oocytes. Although histone acetylation and phosphorylation were reversible, histone methylation has energetic stability and is established during the oocyte growth phase. It is also suggested that the ordered phosphorylation of histone H3 at S10 and S28 is influenced by acetylation of neighboring lysines in the histone H3 molecule." @default.
- W1978356064 created "2016-06-24" @default.
- W1978356064 creator A5009730530 @default.
- W1978356064 creator A5033838383 @default.
- W1978356064 creator A5034366887 @default.
- W1978356064 creator A5078093234 @default.
- W1978356064 date "2006-01-01" @default.
- W1978356064 modified "2023-09-22" @default.
- W1978356064 title "123 HISTONE H3 MODIFICATIONS IN PIG OOCYTES DURING GROWTH, MATURATION, AND ACTIVATION" @default.
- W1978356064 doi "https://doi.org/10.1071/rdv18n2ab123" @default.
- W1978356064 hasPublicationYear "2006" @default.
- W1978356064 type Work @default.
- W1978356064 sameAs 1978356064 @default.
- W1978356064 citedByCount "0" @default.
- W1978356064 crossrefType "journal-article" @default.
- W1978356064 hasAuthorship W1978356064A5009730530 @default.
- W1978356064 hasAuthorship W1978356064A5033838383 @default.
- W1978356064 hasAuthorship W1978356064A5034366887 @default.
- W1978356064 hasAuthorship W1978356064A5078093234 @default.
- W1978356064 hasConcept C153911025 @default.
- W1978356064 hasConcept C163949779 @default.
- W1978356064 hasConcept C178108356 @default.
- W1978356064 hasConcept C196843134 @default.
- W1978356064 hasConcept C2776690073 @default.
- W1978356064 hasConcept C2776745794 @default.
- W1978356064 hasConcept C2779085176 @default.
- W1978356064 hasConcept C54355233 @default.
- W1978356064 hasConcept C552990157 @default.
- W1978356064 hasConcept C64927066 @default.
- W1978356064 hasConcept C83640560 @default.
- W1978356064 hasConcept C86803240 @default.
- W1978356064 hasConcept C95444343 @default.
- W1978356064 hasConceptScore W1978356064C153911025 @default.
- W1978356064 hasConceptScore W1978356064C163949779 @default.
- W1978356064 hasConceptScore W1978356064C178108356 @default.
- W1978356064 hasConceptScore W1978356064C196843134 @default.
- W1978356064 hasConceptScore W1978356064C2776690073 @default.
- W1978356064 hasConceptScore W1978356064C2776745794 @default.
- W1978356064 hasConceptScore W1978356064C2779085176 @default.
- W1978356064 hasConceptScore W1978356064C54355233 @default.
- W1978356064 hasConceptScore W1978356064C552990157 @default.
- W1978356064 hasConceptScore W1978356064C64927066 @default.
- W1978356064 hasConceptScore W1978356064C83640560 @default.
- W1978356064 hasConceptScore W1978356064C86803240 @default.
- W1978356064 hasConceptScore W1978356064C95444343 @default.
- W1978356064 hasIssue "2" @default.
- W1978356064 hasLocation W19783560641 @default.
- W1978356064 hasOpenAccess W1978356064 @default.
- W1978356064 hasPrimaryLocation W19783560641 @default.
- W1978356064 hasRelatedWork W1932794209 @default.
- W1978356064 hasRelatedWork W1965813621 @default.
- W1978356064 hasRelatedWork W1978356064 @default.
- W1978356064 hasRelatedWork W1986693701 @default.
- W1978356064 hasRelatedWork W2060366628 @default.
- W1978356064 hasRelatedWork W2064378826 @default.
- W1978356064 hasRelatedWork W2093320357 @default.
- W1978356064 hasRelatedWork W2374097975 @default.
- W1978356064 hasRelatedWork W2939457231 @default.
- W1978356064 hasRelatedWork W4240070910 @default.
- W1978356064 hasVolume "18" @default.
- W1978356064 isParatext "false" @default.
- W1978356064 isRetracted "false" @default.
- W1978356064 magId "1978356064" @default.
- W1978356064 workType "article" @default.