{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,4,30]],"date-time":"2024-04-30T23:11:23Z","timestamp":1714518683686},"reference-count":35,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2002,2,25]],"date-time":"2002-02-25T00:00:00Z","timestamp":1014595200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[2002,5]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>P2P\u2010R is a nuclear protein that can bind both p53 and Rb1. Its functions include roles in the control of RNA metabolism, apoptosis, and p53\u2010dependent transcription. The expression of P2P\u2010R also is repressed in G<jats:sub>1<\/jats:sub> arrested terminally differentiated cells. The current studies therefore evaluated if P2P\u2010R undergoes cell cycle\u2010associated changes in its abundance and\/or localization. Western blots show that relative to G<jats:sub>0<\/jats:sub> quiescent cells, P2P\u2010R protein levels are higher in populations of G<jats:sub>2<\/jats:sub>\/M cells prepared by the physiological parasynchronization technique of serum deprivation followed by serum stimulation. More striking is the &gt;\u200910\u2010fold enrichment of P2P\u2010R protein in specimens of highly purified mitotic cells prepared by the mitotic shake\u2010select technique, or by synchrony with the mitotic spindle disruption agents nocodazole or vinblastine. These changes in P2P\u2010R protein occur without a concomitant change in P2P\u2010R mRNA expression suggesting that P2P\u2010R immunoreactivity increases during mitosis. Confocal microscopy next established the localization of P2P\u2010R to nucleoli in interphase cells and at the periphery of chromosomes in mitotic cells that lack nucleoli. The high levels of P2P\u2010R localized to the periphery of chromosomes in mitotic cells suggest that P2P\u2010R shares characteristics with other nucleolar proteins that associate with the periphery of chromosomes during mitosis. These include: nucleolin, B23, Ki67, and fibrillarin. J. Cell. Physiol. 191: 145\u2013154, 2002. \u00a9 2002 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/jcp.10084","type":"journal-article","created":{"date-parts":[[2002,8,25]],"date-time":"2002-08-25T23:45:33Z","timestamp":1030319133000},"page":"145-154","source":"Crossref","is-referenced-by-count":22,"title":["P2P\u2010R protein localizes to the nucleolus of interphase cells and the periphery of chromosomes in mitotic cells which show maximum P2P\u2010R immunoreactivity"],"prefix":"10.1002","volume":"191","author":[{"given":"Sizhi","family":"Gao","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael M.","family":"Witte","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robert 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