N-Oct 5 is generated by in vitro proteolysis of the neural POU-domain protein N-Oct 3.

Details

Serval ID
serval:BIB_61F768DCBD3B
Type
Article: article from journal or magazin.
Collection
Publications
Title
N-Oct 5 is generated by in vitro proteolysis of the neural POU-domain protein N-Oct 3.
Journal
Oncogene
Author(s)
Atanasoski S., Schreiber E., Fontana A., Herr W.
ISSN
0950-9232
Publication state
Published
Issued date
03/1997
Peer-reviewed
Oui
Volume
14
Number
11
Pages
1287-1294
Language
english
Abstract
The neural POU-domain proteins N-Oct 3 and N-Oct 5 were first identified in electrophoretic mobility retardation assays through their ability to bind to the octamer sequence ATGCAAAT. These two N-Oct factors are detected in extracts from tumor-derived and normal neural cells. They are present differentially, however, in extracts from melanocytes and melanoma cells: N-Oct 3 is present in extracts from both melanocytes and melanoma cells, whereas N-Oct 5 is more evident in extracts from metastatic melanoma cells. We show here that a cDNA encoding N-Oct 3 directs synthesis of both the N-Oct 3 and N-Oct 5 proteins and that the N-Oct 5 protein in neural and melanoma-cell extracts is also related to N-Oct 3. N-Oct 5, however, is apparently not expressed in vivo: It is not detected if cells are rapidly lysed in SDS or if extracts are prepared with a cocktail of protease inhibitors that includes the serine-protease inhibitor 4-(2-Aminoethyl)benzenesulfonyl fluoride hydrochloride (AEBSF). These data suggest that N-Oct 5 is a specific in vitro proteolytic cleavage product of N-Oct 3 and is not directly related to melanocyte malignancy.
Keywords
Animals, Astrocytes, COS Cells, Cell Transformation, Neoplastic, DNA, Complementary, Homeodomain Proteins, Humans, Hydrolysis, Melanoma, POU Domain Factors, Transcription Factors, Tumor Cells, Cultured
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 16:36
Last modification date
20/08/2019 15:18
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