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A Carboxy Terminal BMP/TGF-beta Binding Site in Secreted Phosphoprotein 24 kD Independently Affects BMP-2 Activity
Tian, Haijun1,2; Li, Chen-Shuang3; Zhao, Ke-Wei4; Wang, Jeffrey C.2; Duarte, M. Eugenia L.5; David, Cynthia L.6; Phan, Kevin2; Atti, Elisa7; Brochmann, Elsa J.4,8,9; Murray, Samuel S.4,8,9
关键词SECRETED PHOSPHOPROTEIN 24 kD BONE MORPHOGENETIC PROTEIN 2 BONE RESEARCH
刊名JOURNAL OF CELLULAR BIOCHEMISTRY
2015-04-01
DOI10.1002/jcb.25023
116期:4页:667-676
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Biochemistry & Molecular Biology ; Cell Biology
研究领域[WOS]Biochemistry & Molecular Biology ; Cell Biology
关键词[WOS]RODENT MODEL ; PROTEIN ; PEPTIDE ; SPP24 ; GROWTH
英文摘要

Secreted phosphoprotein 24kD (spp24) is a bone matrix protein isolated during attempts to identify osteogenic proteins. It is not osteogenic but performs other important roles in the regulation of bone metabolism, at least in part, by binding to and affecting the activity of members of the BMP/TGF- family of cytokines. Spp24 exists in a number of forms that preserve the N-terminus and are truncated at the C-terminus. The hypothesized cytokine binding domain is present within the cystatin domain which is preserved in all of the N-terminal products. In this report, we describe a C-terminal fragment that is distinct from the cystatin domain and which independently binds to BMP-2 and TGF-. This fragment inhibited BMP-2 activity in an ectopic bone forming assay. A shorter C-terminal product did not inhibit BMP-2 activity but improved bone quality induced by BMP-2 and produced increased calcium deposition outside of bone. Spp24 has been used to develop several potential therapeutic proteins. These results provide more information on the function of spp24 and provide other materials that can be exploited for clinical interventions. J. Cell. Biochem. 116: 667-676, 2015. (c) 2014 Wiley Periodicals, Inc.

语种英语
WOS记录号WOS:000349163000020
引用统计
被引频次:6[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/66438
专题北京大学口腔医学院_牙周科
作者单位1.Second Mil Med Univ, Shanghai Changzheng Hosp, Dept Orthopaed Surg, Shanghai 200003, Peoples R China
2.Univ Calif Los Angeles, Dept Orthopaed Surg, Los Angeles, CA 90024 USA
3.Peking Univ Sch & Hosp Stomatol, Dept Orthodont, Beijing 100081, Peoples R China
4.VA Greater Los Angeles Healthcare Syst, Res Serv, North Hills, CA 91343 USA
5.Univ Fed Rio de Janeiro, Natl Inst Traumatol & Orthopaed, BR-21941 Rio De Janeiro, Brazil
6.Univ Arizona, Ctr Toxicol, Tucson, AZ 85721 USA
7.Univ Calif Los Angeles, Sch Dent, Los Angeles, CA 90024 USA
8.VA Greater Los Angeles Healthcare Syst, Geriatr Res Educ & Clin Ctr, North Hills, CA 91343 USA
9.Univ Calif Los Angeles, Dept Med, Los Angeles, CA 90024 USA
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GB/T 7714
Tian, Haijun,Li, Chen-Shuang,Zhao, Ke-Wei,et al. A Carboxy Terminal BMP/TGF-beta Binding Site in Secreted Phosphoprotein 24 kD Independently Affects BMP-2 Activity[J]. JOURNAL OF CELLULAR BIOCHEMISTRY,2015,116(4):667-676.
APA Tian, Haijun.,Li, Chen-Shuang.,Zhao, Ke-Wei.,Wang, Jeffrey C..,Duarte, M. Eugenia L..,...&Murray, Samuel S..(2015).A Carboxy Terminal BMP/TGF-beta Binding Site in Secreted Phosphoprotein 24 kD Independently Affects BMP-2 Activity.JOURNAL OF CELLULAR BIOCHEMISTRY,116(4),667-676.
MLA Tian, Haijun,et al."A Carboxy Terminal BMP/TGF-beta Binding Site in Secreted Phosphoprotein 24 kD Independently Affects BMP-2 Activity".JOURNAL OF CELLULAR BIOCHEMISTRY 116.4(2015):667-676.
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