Using immunohistochemical analysis, Fukawa et al. (2002) showed that the radioresistance associated with FGF2 overexpression was mediated by increased expression of this NPM1 isoform. By transfection of the C-terminally truncated NPM1 variant (NPM2) into radiosensitive HeLa cells, Dalenc et al. They concluded that overexpression of FGF2 caused the redistribution of both NPM1 isoforms. (2002) found nuclear staining for NPM1 in control HeLa cells and cytoplasmic staining following transfection with FGF2. (2000) concluded that NPM1 is a target of CDK2/cyclin E in the initiation of centrosome duplication.īy immunohistochemistry using antibodies that did not differentiate between NPM1 isoforms, Dalenc et al. Moreover, expression of a nonphosphorylatable mutant NPM1 in cells effectively blocked centrosome duplication. An anti-NPM1 antibody, which blocked this phosphorylation, suppressed the initiation of centrosome duplication in vivo. NPM1 associated with unduplicated centrosomes, and dissociated from centrosomes by CDK2/cyclin E-mediated phosphorylation. (2000) identified nucleophosmin as a substrate of CDK2 ( 116953)/cyclin E ( 123837) in centrosome duplication. Electron microscopic study indicated that nucleophosmin is concentrated in the granular region of the nucleolus, where ribosome assembly occurs. They stated that nucleophosmin is likely involved in the assembly of ribosomal proteins into ribosomes. Stimulation of the growth of normal cells, e.g., mitogen activation of B lymphocytes, was accompanied by an increase in nucleophosmin protein level. (1989) found that nucleophosmin is a nucleolar phosphoprotein that is more abundant in tumor cells than in normal resting cells.
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