scholarly journals An Essential Role of the CAAT/Enhancer Binding Protein-α in the Vitamin D-Induced Expression of the Human Steroid/Bile Acid-Sulfotransferase (SULT2A1)

2006 ◽  
Vol 20 (4) ◽  
pp. 795-808 ◽  
Author(s):  
Chung S. Song ◽  
Ibtissam Echchgadda ◽  
Young-Kyo Seo ◽  
Taesung Oh ◽  
Soyoung Kim ◽  
...  
Keyword(s):  
Vitamin D ◽  
Binding Site ◽  
Essential Role ◽  
Binding Protein ◽  
Water Soluble ◽  
Induced Expression ◽  
Composite Element ◽  
Deoxyribonuclease I ◽  
Enhancer Binding Protein

Abstract The vitamin D receptor (VDR) regulates steroid and drug metabolism by inducing the genes encoding phase I and phase II enzymes. SULT2A1 is a liver- and intestine-expressed sulfo-conjugating enzyme that converts the alcohol-OH of neutral steroids, bile acids, and drugs to water-soluble sulfated metabolites. 1α,25-Dihydroxyvitamin D3 [1,25-(OH)2D3] induces SULT2A1 gene transcription after the recruitment of VDR to the vitamin D-responsive chromatin region of SULT2A1. A composite element in human SULT2A1 directs the 1,25-(OH)2D3-mediated induction of natural and heterologous promoters. This element combines a VDR/retinoid X receptor-α-binding site [vitamin D response element (VDRE)], which is an imperfect inverted repeat 2 of AGCTCA, and a CAAT/enhancer binding protein (C/EBP)-binding site located 9 bp downstream to VDRE. The binding sites were identified by EMSA, antibody supershift, and deoxyribonuclease I footprinting. C/EBP-α at the composite element plays an essential role in the VDR regulation of SULT2A1, because 1) induction was lost for promoters with inactivating mutations at the VDRE or C/EBP element; 2) SULT2A1 induction by 1,25-(OH)2D3 in C/EBP-α-deficient cells required the expression of cotransfected C/EBP-α; and 3) C/EBP-β did not substitute for C/EBP-α in this regulation. VDR and C/EBP-α were recruited concurrently to the composite element along with the coactivators p300, steroid receptor coactivator 1 (SRC-1), and SRC-2, but not SRC-3. VDR and C/EBP-α associated endogenously as a DNA-dependent, coimmunoprecipitable complex, which was detected at a markedly higher level in 1,25-(OH)2D3-treated cells. These results provide the first example of the essential role of the interaction in cis between C/EBP-α and VDR in directing 1,25-(OH)2D3-induced expression of a VDR target gene.

Comparison between the human serum growth hormone-binding protein and the water-soluble growth hormone-binding site released from IM-9 lymphocytes

1993 ◽  
Vol 129 (6) ◽  
pp. 559-564 ◽  
Author(s):  
Guy Massa ◽  
Mapoko Ilondo ◽  
Magda Vanderschueren-Lodeweyckx
Keyword(s):  
Growth Hormone ◽  
Human Serum ◽  
Binding Site ◽  
Binding Protein ◽  
Water Soluble ◽  
Hormone Binding ◽  
Serum Growth Hormone ◽  
Gh Receptor ◽  
Growth Hormone Binding Protein ◽  
Hormone Binding Protein

The characteristics of the human serum growth hormone-binding protein (GHBP) were compared with those of a water-soluble GH-binding site prepared by incubating cultured IM-9 lymphocytes in assay buffer with 25 mmol/l iodoacetamide. High-performance liquid chromatography gel filtration of the water-soluble GH-binding site incubated with 125I-labeled human GH ([125I]hGH) revealed a large peak of bound [125I]hGH eluting at the same position as the peak of [125I]hGH bound to the GHBP in serum. The estimated Mr of the peak was 120 000, presumably representing one [125I]hGH bound to two binding sites. The binding specificities of the serum GHBP, the water-soluble GH-binding site and the GH receptor on IM-9 lymphocytes were identical. The binding affinities for 22 000 hGH and for 20 000 hGH of the serum GHBP were similar to the binding affinity of the water-soluble GH-binding site but lower than those of the cellular GH receptor. These findings show that the characteristics of the serum GHBP are comparable to those of the water-soluble GH-binding site released from IM-9 cells and support the hypothesis that in man the serum GHBP is produced by proteolytic cleavage of the cellular GH receptor.

scholarly journals An essential role for CCAAT/enhancer binding protein β in bleomycin-induced pulmonary fibrosis

2007 ◽  
Vol 211 (4) ◽  
pp. 455-462 ◽  
Author(s):  
B Hu ◽  
MR Ullenbruch ◽  
H Jin ◽  
M Gharaee-Kermani ◽  
SH Phan
Keyword(s):  
Pulmonary Fibrosis ◽  
Essential Role ◽  
Binding Protein ◽  
Enhancer Binding Protein ◽  
Ccaat Enhancer Binding Protein

scholarly journals An Essential Role of Polymeric Adhesives in the Reinforcement of Acidified Paper Relics

Polymers ◽  
2022 ◽  
Vol 14 (1) ◽  
pp. 207
Author(s):  
Jiaojiao Liu ◽  
Huiping Xing ◽  
Yajun Zhou ◽  
Xiaolian Chao ◽  
Yuhu Li ◽  
...  
Keyword(s):  
Essential Role ◽  
Polyvinyl Butyral ◽  
Scientific Basis ◽  
Water Soluble ◽  
Wheat Starch ◽  
Protective Effects ◽  
Ft Ir ◽  
Starch Paste

Paper acidification causes paper relics to undergo embrittlement and decay, to form dregs, and even to break upon a single touch; therefore, reinforcement and deacidification treatments are essential steps for paper conservation and to retard the deterioration and prolong the life of objects. Polymeric adhesives play an essential role in reinforcement and deacidification treatments, although it is not well studied. In this work, the effect of polymeric adhesives on the conservation process and their protective effects on acidified paper relics were studied. Firstly, three polymeric adhesives, including wheat starch paste, polyvinyl butyral (PVB), and polyvinyl alcohol (PVA), were selected as research objects. Subsequently, their effects on four popular conservation methods were further discussed, including traditional mounting, hot-melt with silk net, alcohol-soluble cotton mesh, and water-soluble cotton mesh. Additionally, as an example, the reversibility and long-term durability of water-soluble adhesive PVA-217 were assessed. Using a computer measured and controlled folding endurance tester, pendulum tensile strength tester, tear tester, burst tester, FT-IR, video optical contact angle tester, and other instruments, the conservation application of water-soluble adhesives in paper relics was evaluated. This study provides a scientific basis and experimental data for the application of polymeric adhesives in the conservation of paper relics.

scholarly journals Associations between Vitamin D and Type 2 Diabetes Mellitus: The Role of Vitamin D Receptor and Binding Protein

2020 ◽  
Vol 10 (04) ◽  
pp. 222-235
Author(s):  
Eman S. Arafat ◽  
Inass M. Taha ◽  
Shahad W. Kattan ◽  
Nouf Abubakr Babteen ◽  
Iman Fawzy
Keyword(s):  
Diabetes Mellitus ◽  
Type 2 Diabetes ◽  
Vitamin D ◽  
Type 2 Diabetes Mellitus ◽  
Vitamin D Receptor ◽  
Binding Protein

Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein

1994 ◽  
Vol 14 (11) ◽  
pp. 7256-7264
Author(s):  
Y W Kim ◽  
G A Otterson ◽  
R A Kratzke ◽  
A B Coxon ◽  
F J Kaye
Keyword(s):  
Binding Site ◽  
Binding Protein ◽  
Tata Binding Protein ◽  
Binding Activity ◽  
Reversible Binding ◽  
Complex Interactions ◽  
Differential Binding ◽  
Cellular Transcription

The growth suppressor activities of the RB and p107 products are believed to be mediated by the reversible binding of a heterogeneous family of cellular proteins to a conserved T/E1A pocket domain that is present within both proteins. To study the functional role of these interactions, we examined the properties of cellular retinoblastoma binding protein 2 (RBP2) binding to RB, p107, and the related TATA-binding protein (TBP) product. We observed that although RBP2 bound exclusively to the T/E1A pocket of p107, it could interact with RB through independent T/E1A and non-T/E1A domains and with TBP only through the non-T/E1A domain. Consistent with this observation, we found that a mutation within the Leu-X-Cys-X-Glu motif of RBP2 resulted in loss of ability to precipitate p107, while RB- and TBP-binding activities were retained. We located the non-T/E1A binding site of RBP2 on a 15-kDa fragment that is independent from the Leu-X-Cys-X-Glu motif and encodes binding activity for RB and TBP but does not interact with p107. Despite the presence of a non-T/E1A binding site, however, recombinant RBP2 retained the ability to preferentially precipitate active hypophosphorylated RB from whole-cell lysates. In addition, we found that cotransfection of RBP2 can reverse in vivo RB-mediated suppression of E2F activity. These findings confirm the differential binding specificities of the related RB, p107, and TBP proteins and support the presence of multifunctional domains on the nuclear RBP2 product which may allow complex interactions with the cellular transcription machinery.

Role of transcription factor CCAAT/enhancer-binding protein alpha in human fetal liver cell typesin vitro

2014 ◽  
Vol 45 (8) ◽  
pp. 919-932 ◽  
Author(s):  
Jörg C. Gerlach ◽  
Patrick Over ◽  
Hubert G. Foka ◽  
Morris E. Turner ◽  
Robert L. Thompson ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Liver Cell ◽  
Fetal Liver ◽  
Binding Protein ◽  
Human Fetal Liver ◽  
Fetal Liver Cell ◽  
Enhancer Binding Protein ◽  
Ccaat Enhancer Binding Protein
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