scholarly journals Activation of a Nuclear DNA-binding Protein Recognized by a Transcriptional Element, bcn-1, from the Laminin B2 Chain Gene Promoter

1996 ◽  
Vol 271 (31) ◽  
pp. 18981-18988 ◽  
Author(s):  
Hideaki Suzuki ◽  
Bruce C. O'Neill ◽  
Yu Suzuki ◽  
Oleg N. Denisenko ◽  
Karol Bomsztyk
1998 ◽  
Vol 275 (4) ◽  
pp. F518-F526 ◽  
Author(s):  
Hideaki Suzuki ◽  
Oleg N. Denisenko ◽  
Yu Suzuki ◽  
Daniel S. Schullery ◽  
Karol Bomsztyk

Laminin is a major component of the extracellular matrix whose expression is regulated by growth factors. The laminin γ1-chain promoter contains a newly identified transcriptional element denoted bcn-1 that is both active and inducible in mesangial cells. In this study, we explored activation of the bcn-1 element in other renal and nonrenal cells. Treatment of rat glomerular epithelial cells (GEC) with phorbol 12-myristate 13-acetate (PMA) increased activity of the bcn-1 transcriptional element, within the context of the native laminin γ1-chain promoter or when cloned upstream of a heterologous promoter. Treatment of GEC with PMA induced nuclear DNA-binding activity, BCN-1, which was recognized by the bcn-1 motif in a gel shift assay. These results provide evidence that the bcn-1 motif and its cognate BCN-1 factor(s) may regulate transcription of the laminin γ1-chain in GEC. The bcn-1 element and its cognate BCN-1 DNA-binding activity were also inducible in monkey kidney COS-7 and in human T cell Jurkat lines. SDS-PAGE of in situ ultraviolet cross-linked nucleoproteins from GEC, COS, and Jurkat cells revealed one major 110–115 kDa adduct in all three cell lines. These results demonstrate that the bcn-1 element is active in renal and nonrenal cells from different mammalian species where the same protein contributes to the inducible BCN-1 DNA-binding activity.


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