title: Tumour suppressor protein p53 released by nuclease digestion increases at the onset of rat liver regeneration.
abstract: OBJECTIVE
  Protein kinase CK2 (CK2) increases when cells are committed to proliferate, as in liver regeneration. This enzyme phosphorylates the tumour suppressor protein p53, whose expression controls the levels of many other cell cycle proteins. The aim of this study was to determine if CK2 was affected by p53.
  
  
  METHODS
  Male Sprague-Dawley rats (200-250 g) were subjected to either partial hepatectomy or laparotomy and the levels and subcellular distribution of p53 were studied, following the approach used earlier for CK2. The levels of both proteins were also studied in the human cell lines HL-60 (devoid of p53) and HepG2 (with normal p53 levels) and in fibroblasts from transgenic p53-deficient mice (p53-/-) or homozygous for wild-type p53 (p53+/+). Computer-assisted search was used to detect p53 consensus sequences in genes for CK2 subunits Binding of p53 protein to some of these sequences was assayed by electrophoretic mobility shift assay.
  
  
  RESULTS
  Rat liver p53 protein was present mainly in the fraction extracted from intact nuclei by nucleases (S1) and showed a transient increase at 6 h post partial hepatectomy, as observed previously with nuclear CK2. The human CK2a gene presents the consensus sequence for trans-activation by p53 and specific binding of p53 protein to some of these sequences was detected in vitro. Total CK2a was higher in HepG2 than in HL-60 cells but total CK2 and its cytosolic/ nuclear distribution was similar in mice (p53+/+) fibroblasts and (p53-/-) fibroblasts.
  
  
  CONCLUSIONS
  p53 is present in the nuclease-extracted S1 fraction from liver cells, as described for CK2, and undergoes similar changes at the beginning of rat liver regeneration. However, the data on cultured cells suggest that the expression of CK2 and its subcellular localization are p53-independent events.
authors.affiliation: Department de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Bellaterra, Spain.
authors.forename: F
authors.initials: F
authors.lastname: Miró
authors.forename: J C
authors.initials: JC
authors.lastname: Lelong
authors.forename: F
authors.initials: F
authors.lastname: Pancetti
authors.forename: N
authors.initials: N
authors.lastname: Roher
authors.forename: A
authors.initials: A
authors.lastname: Duthu
authors.forename: M
authors.initials: M
authors.lastname: Plana
authors.forename: J C
authors.initials: JC
authors.lastname: Bourdon
authors.forename: O
authors.initials: O
authors.lastname: Bachs
authors.forename: E
authors.initials: E
authors.lastname: May
authors.forename: E
authors.initials: E
authors.lastname: Itarte
mesh_terms: D000818:Animals; D015153:Blotting, Western; D047390:Casein Kinase II; D002460:Cell Line; D002478:Cells, Cultured; D003851:Deoxyribonucleases / Q000032:analysis / Q000378:metabolism*; D005347:Fibroblasts / Q000378:metabolism*; D018922:HL-60 Cells / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D008115:Liver Regeneration / Q000502:physiology*; D008297:Male; D051379:Mice; D008822:Mice, Transgenic; D017346:Protein Serine-Threonine Kinases / Q000096:biosynthesis*; D051381:Rats; D017207:Rats, Sprague-Dawley; D016159:Tumor Suppressor Protein p53 / Q000096:biosynthesis* / Q000172:deficiency
chemical_list: D016159:Tumor Suppressor Protein p53; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases; D003851:Deoxyribonucleases