Abstract:
:An established melanoma cell line (MM96L) was transfected with selectable plasmid constructs encoding either whole SV40 large T antigen, or beta-galactosidase fusions with the retinoblastoma protein (Rb)-binding region of SV40 large T antigen and a nonbinding mutant derivative of it. Both of the beta-galactosidase fusions also encoded the large T nuclear targeting signal. Transcription of inserted genes was regulated through a Zn+2-inducible metallothionein IA promoter, which provides tight but not absolute control of expression. Only the wild-type large T segment fusion was functionally active in the binding of Rb protein. Stable lines derived from primary transfectants with the expression plasmid encoding the mutant large T segment fusion showed a normal FACS scan profile, a normal growth rate, and (upon induction) high levels of nuclear staining for beta-galactosidase. However, cells transfected with the wild-type (Rb-binding) large T segment fusion grew slowly, with surviving clones assuming a predominantly tetraploid karyotype and relatively much lower levels of beta-galactosidase activity upon Zn+2 induction. The latter cells, but not those transfected with the corresponding non-Rb-binding fusion construct, also exhibited elevated cell death and apoptosis in response to the inducer Zn+2. These results implied that expression of an Rb-binding protein has deleterious effects on the melanoma cell line growth and may reflect a role for Rb of a related pocket protein in maintaining the differentiation state of these transformed cells.
journal_name
Exp Cell Resjournal_title
Experimental cell researchauthors
Khan S,Collins RJ,Dunn ISdoi
10.1006/excr.1996.0071subject
Has Abstractpub_date
1996-02-25 00:00:00pages
171-82issue
1eissn
0014-4827issn
1090-2422pii
S0014482796900713journal_volume
223pub_type
杂志文章abstract::Ezrin-Radixin-Moesin (ERM) binding phosphoprotein 50 (EBP50, a.k.a. NHERF-1) is a scaffold protein essential for the localization and coordinated activity of apical transporters, enzymes and receptors in epithelial cells. EBP50 acts via multiple protein binding interactions, including oligomerization through interacti...
journal_title:Experimental cell research
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journal_title:Experimental cell research
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journal_title:Experimental cell research
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journal_title:Experimental cell research
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journal_title:Experimental cell research
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journal_title:Experimental cell research
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journal_title:Experimental cell research
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journal_title:Experimental cell research
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journal_title:Experimental cell research
pub_type: 杂志文章
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journal_title:Experimental cell research
pub_type: 杂志文章,评审
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journal_title:Experimental cell research
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journal_title:Experimental cell research
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journal_title:Experimental cell research
pub_type: 杂志文章
doi:10.1016/s0014-4827(02)00056-3
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