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Journal of Cell Science, Vol 104, Issue 1 19-30, Copyright © 1993 by Company of Biologists
JOURNAL ARTICLES |
K Rothbarth, C Petzelt, X Lu, IT Todorov, G Joswig, R Pepperkok, W Ansorge and D Werner
Division of Cellular Biochemistry, German Cancer Research Center, Heidelberg.
Differential screening of a murine RNA-based cDNA library with cell cycle phase-specific transcripts released a cDNA clone (lambda CCD41) to a mRNA (1.349 kb) which, according to the mode of its detection, increases as expected during the cell cycle. The molecular characteristics of the protein (27 x 10(3) M(r)) encoded by this mRNA were deduced from the cDNA sequence and antibodies were prepared against the recombinant protein. Immunofluorescence studies performed with PtK2 cells revealed that the amount of the antigen specified by the CCD41 sequence increases during the cell cycle out of proportion with the DNA content. In G1 phase cells, the antigen is exclusively located at the site of the centrosome. During cell cycle progression the antigen becomes also detectable in perinuclear vesicles that increase in number and size, reaching a maximum in G2 phase cells. The centrosomal location of the CCD41 antigen was investigated in relation to another centrosomal antigen, centrosomin A. Since the latter antigen is detected by a monoclonal antibody reacting specifically and permanently with the centrosomes in PtK2 cells throughout the cell cycle it was possible to investigate the relative positions of the two proteins at the site of the centrosome and to add new information about the general architecture of the organelle and its changes during the cell cycle. While the centrosomin A antibody detects the pronounced cell cycle stage-dependent shape changes of the centrosome, the CCD41-encoded protein appears to be localized as a compact structure inside the centrosome. Its epitopes are exposed throughout the cell cycle except during a brief period immediately after the formation of the daughter centrosome.
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  C Petzelt, G Joswig, A Mincheva, P Lichter, H Stammer, and D Werner The centrosomal protein centrosomin A and the nuclear protein centrosomin B derive from one gene by post-transcriptional processes involving RNA editing J. Cell Sci., January 10, 1997; 110(20): 2573 - 2578. [Abstract] [PDF]
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 K. Fukudome, S. Kurosawa, D. J. Stearns-Kurosawa, X. He, A. R. Rezaie, and C. T. Esmon The Endothelial Cell Protein C Receptor. CELL SURFACE EXPRESSION AND DIRECT LIGAND BINDING BY THE SOLUBLE RECEPTOR J. Biol. Chem., July 19, 1996; 271(29): 17491 - 17498. [Abstract] [Full Text] [PDF]
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V Bouckson-Castaing, M Moudjou, D. Ferguson, S Mucklow, Y Belkaid, G Milon, and P. Crocker Molecular characterisation of ninein, a new coiled-coil protein of the centrosome J. Cell Sci., January 1, 1996; 109(1): 179 - 190. [Abstract] [PDF]
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K. Fukudome and C. T. Esmon Molecular Cloning and Expression of Murine and Bovine Endothelial Cell Protein C/Activated Protein C Receptor (EPCR) J. Biol. Chem., March 10, 1995; 270(10): 5571 - 5577. [Abstract] [Full Text] [PDF]
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J. Dominguez, B Buendia, C Lopez-Otin, C Antony, E Karsenti, and J Avila A protein related to brain microtubule-associated protein MAP1B is a component of the mammalian centrosome J. Cell Sci., January 2, 1994; 107(2): 601 - 611. [Abstract] [PDF]
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