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NCL  -  nucleolin

Bos taurus

 
 
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High impact information on NCL

  • Here, we show that FGF-2 added to nuclear extract binds to protein kinase CK2 and nucleolin, a CK2 natural substrate [1].
  • Fibroblast growth factor-2 binds to the regulatory beta subunit of CK2 and directly stimulates CK2 activity toward nucleolin [1].
  • The kinase activity, in isolated nuclei, was estimated by endogenous phosphorylation of a specific substrate, nucleolin [2].
  • The aim of this study was to describe the dynamic changes in the localization of the key nucleolar protein markers, fibrillarin, B23/nucleophosmin, C23/nucleolin, protein Nopp140, during the final stages of bovine oocyte growth [3].
  • On completion of the growth phase, nucleolin and nucleophosmin appeared to migrate to the periphery of the nucleolus and into the nucleoplasm, and the proportion of oocytes displaying RNA pol I localization had decreased [4].
 

Biological context of NCL

  • During the second cell cycle (2-cell stage), the findings were similar except for a lack of nucleolin and RNA polymerase I labeling [5].
  • The aim of this study was to evaluate the expression pattern of fibroblast growth factor 2 (FGF2), its receptor variants (FGFR1IIIc, FGFR2IIIc) and nucleolin in time-defined follicle classes before and after GnRH application and after ovulation in the cow [6].
 

Anatomical context of NCL

 

Regulatory relationships of NCL

  • Using purified proteins, FGF-2 is shown to directly interact with CK2 and to stimulate CK2 activity toward nucleolin [1].
 

Other interactions of NCL

 

Analytical, diagnostic and therapeutic context of NCL

  • In addition, immunocytochemical localization by confocal microscopy of nucleolin, a key protein involved in processing rRNA transcripts, was performed on early 8-, late 8-, and 16-cell embryos for both groups of SCNT embryos [7].

References

  1. Fibroblast growth factor-2 binds to the regulatory beta subunit of CK2 and directly stimulates CK2 activity toward nucleolin. Bonnet, H., Filhol, O., Truchet, I., Brethenou, P., Cochet, C., Amalric, F., Bouche, G. J. Biol. Chem. (1996) [Pubmed]
  2. Protein kinase NII and the regulation of rDNA transcription in mammalian cells. Belenguer, P., Baldin, V., Mathieu, C., Prats, H., Bensaid, M., Bouche, G., Amalric, F. Nucleic Acids Res. (1989) [Pubmed]
  3. Immunolocalization of upstream binding factor and pocket protein p130 during final stages of bovine oocyte growth. Baran, V., Pavlok, A., Bjerregaard, B., Wrenzycki, C., Hermann, D., Philimonenko, V.V., Lapathitis, G., Hozak, P., Niemann, H., Motlik, J. Biol. Reprod. (2004) [Pubmed]
  4. Immunolocalization of nucleolar proteins during bovine oocyte growth, meiotic maturation, and fertilization. Fair, T., Hyttel, P., Lonergan, P., Boland, M.P. Biol. Reprod. (2001) [Pubmed]
  5. Nucleolar proteins and nuclear ultrastructure in preimplantation bovine embryos produced in vitro. Laurincik, J., Thomsen, P.D., Hay-Schmidt, A., Avery, B., Greve, T., Ochs, R.L., Hyttel, P. Biol. Reprod. (2000) [Pubmed]
  6. Changes in fibroblast growth factor 2 and its receptors in bovine follicles before and after GnRH application and after ovulation. Berisha, B., Steffl, M., Amselgruber, W., Schams, D. Reproduction (2006) [Pubmed]
  7. Ovine ooplasm directs initial nucleolar assembly in embryos cloned from ovine, bovine, and porcine cells. Hamilton, H.M., Peura, T.T., Laurincik, J., Walker, S.K., Maddocks, S., Maddox-Hyttel, P. Mol. Reprod. Dev. (2004) [Pubmed]
 
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