title: In spermatozoa, Stat1 is activated during capacitation and the acrosomal reaction.
abstract: A role for sperm-specific proteins during the early embryonic development has been suggested by a number of recent studies. However, little is known about the participation of transcription factors in that stage. Here, we show that the signal transducer and activator of transcription 1 (Stat1), but not Stat4, was phosphorylated in response to capacitation and the acrosomal reaction (AR). Moreover, Stat1 phosphorylation correlated with changes in its localization: during capacitation, Stat1 moved from the cytoplasm to the theca/flagellum fraction. During AR, Stat1 phosphorylation increased again. In addition, blocking protein kinase A (PKA) and PKC during capacitation abolished both phosphorylation and migration of Stat1. Our results show tight spatio-temporal rearrangements of Stat1, suggesting that after fertilization Stat1 participates in the first rounds of transcription within the male pronucleus.
authors: Departamento de Biología Celular, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional, México DF, Mexico.
authors: Yadira
authors: Y
authors: Bastián
authors: Armando
authors: A
authors: Zepeda-Bastida
authors: Salvador
authors: S
authors: Uribe
authors: Adela
authors: A
authors: Mújica
mesh_terms: D020101:Acrosome Reaction / Q000502:physiology*; D000818:Animals; D001692:Biological Transport; D015153:Blotting, Western / Q000379:methods; D002118:Calcium / Q000494:pharmacology; D002478:Cells, Cultured; D017868:Cyclic AMP-Dependent Protein Kinases / Q000037:antagonists & inhibitors / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D004533:Egtazic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D019833:Genistein / Q000494:pharmacology; D006168:Guinea Pigs; D007211:Indoles / Q000494:pharmacology; D007529:Isoflavones / Q000494:pharmacology; D007546:Isoquinolines / Q000494:pharmacology; D008297:Male; D008301:Maleimides / Q000494:pharmacology; D010766:Phosphorylation; D011493:Protein Kinase C / Q000037:antagonists & inhibitors / Q000378:metabolism; D011505:Protein-Tyrosine Kinases / Q000037:antagonists & inhibitors; D050794:STAT1 Transcription Factor / Q000032:analysis / Q000378:metabolism*; D050797:STAT4 Transcription Factor / Q000032:analysis / Q000378:metabolism; D013075:Sperm Capacitation / Q000502:physiology*; D013082:Sperm Tail / Q000378:metabolism; D013094:Spermatozoa / Q000378:metabolism*; D013449:Sulfonamides / Q000494:pharmacology; D015533:Transcriptional Activation / Q000187:drug effects
chemical_list: D007211:Indoles; D007529:Isoflavones; D007546:Isoquinolines; D008301:Maleimides; D050794:STAT1 Transcription Factor; D050797:STAT4 Transcription Factor; D013449:Sulfonamides; C040641:genistin; D004533:Egtazic Acid; D019833:Genistein; D011505:Protein-Tyrosine Kinases; D017868:Cyclic AMP-Dependent Protein Kinases; D011493:Protein Kinase C; C070515:bisindolylmaleimide I; C063509:N-(2-(4-bromocinnamylamino)ethyl)-5-isoquinolinesulfonamide; D002118:Calcium