Recombinant thrombomodulin improved Stevens-Johnson syndrome with high serum high-mobility group-B1 DNA-binding protein induced by lenalidomide administered to treat multiple myeloma

2013 ◽  
Vol 132 (4) ◽  
pp. 493-494 ◽  
Author(s):  
Yasuyuki Inoue ◽  
Tasuku Saito ◽  
Yuka Tsuruoka ◽  
Kazuyuki Sato ◽  
Yuji Nishio ◽  
...  
Keyword(s):  
Multiple Myeloma ◽  
Dna Binding ◽  
Binding Protein ◽  
High Mobility ◽  
Dna Binding Protein ◽  
High Serum ◽  
High Mobility Group ◽  
Stevens Johnson Syndrome ◽  
Johnson Syndrome ◽  
Recombinant Thrombomodulin

Purification and characterization of a high-mobility-group-like DNA-binding protein that stimulates rRNA synthesis in vitro

1988 ◽  
Vol 8 (8) ◽  
pp. 3406-3414
Author(s):  
H F Yang-Yen ◽  
L I Rothblum
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
High Mobility ◽  
Dna Binding Protein ◽  
High Mobility Group ◽  
Rrna Synthesis ◽  
Rrna Gene ◽  
Hmg Proteins ◽  
Novikoff Hepatoma

A 16,000-dalton, high-mobility-group-like (HMG-like) DNA-binding protein, referred to as p16, has been purified to homogeneity from Novikoff hepatoma ascites cells. p16 binds specifically to a portion of the 5' flanking region of the rat rRNA gene (-620 to -417), which is part of the upstream activator sequence identified previously (B. G. Cassidy, H.-F. Yang-Yen, and L. I. Rothblum, Mol. Cell. Biol. 6:2766-2773, 1986). p16 also binds to a segment of the external transcribed spacer (+352 to +545). In vitro reconstituted transcription experiments demonstrated that the addition of p16 stimulated rRNA synthesis up to ca. fourfold. The stimulation was dose dependent and saturable. The effect of p16 on ribosomal gene transcription was also dependent on the presence of either the upstream or the downstream DNA-binding site, or both. The amino acid composition of p16 is very similar to that of HMG-I, suggesting that p16 may be a member of the HMG-I family of proteins. In this case, our results suggest that HMG proteins may play an important role in the regulation of the rRNA gene expression.

scholarly journals Purification and characterization of a high-mobility-group-like DNA-binding protein that stimulates rRNA synthesis in vitro.

1988 ◽  
Vol 8 (8) ◽  
pp. 3406-3414 ◽  
Author(s):  
H F Yang-Yen ◽  
L I Rothblum
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
High Mobility ◽  
Dna Binding Protein ◽  
High Mobility Group ◽  
Rrna Synthesis ◽  
Rrna Gene ◽  
Hmg Proteins ◽  
Novikoff Hepatoma

A 16,000-dalton, high-mobility-group-like (HMG-like) DNA-binding protein, referred to as p16, has been purified to homogeneity from Novikoff hepatoma ascites cells. p16 binds specifically to a portion of the 5' flanking region of the rat rRNA gene (-620 to -417), which is part of the upstream activator sequence identified previously (B. G. Cassidy, H.-F. Yang-Yen, and L. I. Rothblum, Mol. Cell. Biol. 6:2766-2773, 1986). p16 also binds to a segment of the external transcribed spacer (+352 to +545). In vitro reconstituted transcription experiments demonstrated that the addition of p16 stimulated rRNA synthesis up to ca. fourfold. The stimulation was dose dependent and saturable. The effect of p16 on ribosomal gene transcription was also dependent on the presence of either the upstream or the downstream DNA-binding site, or both. The amino acid composition of p16 is very similar to that of HMG-I, suggesting that p16 may be a member of the HMG-I family of proteins. In this case, our results suggest that HMG proteins may play an important role in the regulation of the rRNA gene expression.

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