期刊
JOURNAL OF CELLULAR BIOCHEMISTRY
卷 83, 期 3, 页码 414-425出版社
WILEY-LISS
DOI: 10.1002/jcb.1239
关键词
retinoblastoma protein; C/EBP; transcription; differentiation; surfactant protein D
资金
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL044015] Funding Source: NIH RePORTER
- NHLBI NIH HHS [P01HL474049, HL44015] Funding Source: Medline
The retinoblastoma protein (RB) recruits histone deacetylase (HDAC) to repress E2F-mediated transactivation that plays a critical role in cell cycle regulation. RB is also involved in activation of expression of a number of tissue specific- and differentiation-related genes. In this study, we examined the mechanism by which RB stimulated the expression of a differentiation-related gene, the surfactant protein D (SP-D), which plays important roles in innate host defense and the regulation of surfactant homeostasis. We demonstrated that RB specifically stimulated the activity of human SP-D gene promoter. The RB family member, p107 but not p130, also increased SP-D promoter activity, Activation by RB was mediated through a NF-IL6 (C/EBP beta) binding motif in the human SP-D promoter, and this sequence specifically bound to C/EBP alpha, C/EBP beta, and C/EBP delta. RB formed stable complexes with all three C/EBP family members. RB small pocket (amino acid residues 379-792), but not the C-pocket (amino acid residues 792-928), was necessary and sufficient for its interaction with C/EBP proteins. Furthermore, we demonstrated that the complexes containing RB and C/EBP proteins directly interacted with C-EBP binding site on DNA. These findings indicate that RB plays a positive, selective, and direct role in the C/EBP-dependent transcriptional regulation of human SP-D expression. J. Cell. Biochem. 83: 414-425, 2001. (C) 2001 Wiley-Liss, Inc.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据