title: Changes in acetylation on lysine 12 of histone H4 (acH4K12) of murine oocytes during maternal aging may affect fertilization and subsequent embryo development.
abstract: OBJECTIVE
  To compare acH4K12 levels in oocytes during mouse aging and then assess how such changes might affect the developmental potential of oocytes.
  
  
  METHODS
  Experimental animal study.
  
  
  METHODS
  State key laboratory and university research laboratory.
  
  
  METHODS
  Kunming white strain mice.
  
  
  METHODS
  Oocytes obtained from TSA treated group or aging mouse group were fertilized and the formation of pronuclei and subsequently developmental potential in vitro or in vivo were assessed.
  
  
  METHODS
  AcH4K12 levels in oocytes were assessed using fluorescence staining, and confocal microscopy and oocyte developmental potentials were determined by in vitro or in vivo methods.
  
  
  RESULTS
  The AcH4K12 levels in oocytes statistically significantly increased during mouse aging. When histone acetylation of oocytes of young mice was artificially increased by trichostatin A (TSA) treatment, the acH4K12 levels in male and female pronuclei in fertilized oocytes showed statistically significant changes. About 38.9% of TSA-treated oocytes failed to form pronuclei or formed morphologically abnormal pronuclei 6 hours after fertilization, which statistically significantly decreased the blastocyst rate of TSA-treated oocytes when compared with the control group (41.5% vs. 60.5%). A similar reduction in blastocyst development was also observed when oocytes collected in older mice were compared with younger mice (17.3% vs. 69.4%).
  
  
  CONCLUSIONS
  The AcH4K12 levels in oocytes statistically significantly increased during the aging process in mice, and such changes may affect the acetylation patterns and morphology of pronuclei during fertilization and lead to a reduction in oocyte developmental potential.
authors.affiliation: Laboratory of Animal Embryonic Biotechnology, College of Animal Science and Technology, China Agricultural University, Beijing 100193, People's Republic of China.
authors.forename: Lun
authors.initials: L
authors.lastname: Suo
authors.forename: Qing-Gang
authors.initials: QG
authors.lastname: Meng
authors.forename: Yan
authors.initials: Y
authors.lastname: Pei
authors.forename: Chang-Liang
authors.initials: CL
authors.lastname: Yan
authors.forename: Xiang-Wei
authors.initials: XW
authors.lastname: Fu
authors.forename: Thomas D
authors.initials: TD
authors.lastname: Bunch
authors.forename: Shi-En
authors.initials: SE
authors.lastname: Zhu
mesh_terms: D000107:Acetylation / Q000187:drug effects; D000375:Aging / Q000502:physiology*; D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism; D047108:Embryonic Development / Q000502:physiology*; D005260:Female; D005306:Fertilization / Q000502:physiology*; D056572:Histone Deacetylase Inhibitors / Q000494:pharmacology; D006657:Histones / Q000378:metabolism*; D006877:Hydroxamic Acids / Q000494:pharmacology; D008239:Lysine / Q000378:metabolism; D008297:Male; D008540:Meiosis / Q000502:physiology; D051379:Mice; D008815:Mice, Inbred Strains; D009865:Oocytes / Q000166:cytology* / Q000378:metabolism*; D008941:Spindle Apparatus / Q000502:physiology; D013480:Superovulation; D015053:Zygote / Q000166:cytology / Q000502:physiology
chemical_list: D056572:Histone Deacetylase Inhibitors; D006657:Histones; D006877:Hydroxamic Acids; C012589:trichostatin A; D008239:Lysine