The Bioactive Acidic Serine- and Aspartate-Rich Motif Peptide

Current Protein & Peptide Science 16 巻 3 号 196-202 頁 2015 発行
アクセス数 : 342
ダウンロード数 : 73

今月のアクセス数 : 3
今月のダウンロード数 : 3
ファイル情報(添付)
CurrProteinPeptSci_16_196.pdf 844 KB 種類 : 全文
タイトル ( eng )
The Bioactive Acidic Serine- and Aspartate-Rich Motif Peptide
作成者
収録物名
Current Protein & Peptide Science
16
3
開始ページ 196
終了ページ 202
抄録
The organic component of the bone matrix comprises 40% dry weight of bone. The organic component is mostly composed of type I collagen and small amounts of non-collagenous proteins (NCPs) (10-15% of the total bone protein content). The small integrin-binding ligand N-linked glycoprotein (SIBLING) family, a NCP, is considered to play a key role in bone mineralization. SIBLING family of proteins share common structural features and includes the arginine-glycine-aspartic acid (RGD) motif and acidic serine- and aspartic acid-rich motif (ASARM). Clinical manifestations of gene mutations and/or genetically modified mice indicate that SIBLINGs play diverse roles in bone and extraskeletal tissues. ASARM peptides might not be primary responsible for the functional diversity of SIBLINGs, but this motif is suggested to be a key domain of SIBLINGs. However, the exact function of ASARM peptides is poorly understood. In this article, we discuss the considerable progress made in understanding the role of ASARM as a bioactive peptide.
著者キーワード
Acidic serine- and aspartic acid-rich motif (ASARM)
bone mineralization
matrix extracellular phosphoglycoprotein (MEPE)
small integrin-binding ligand N-linked glycoprotein (SIBLING)
言語
英語
資源タイプ 学術雑誌論文
出版者
Bentham Science Publishers
発行日 2015
権利情報
The published manuscript is available at EurekaSelect via http://www.eurekaselect.com/openurl/content.php?genre=article&doi=10.2174/1389203716666150206122839.
This is not the published version. Please cite only the published version. この論文は出版社版ではありません。引用の際には出版社版をご確認、ご利用ください。
出版タイプ Author’s Original(十分な品質であるとして、著者から正式な査読に提出される版)
アクセス権 オープンアクセス
収録物識別子
[ISSN] 1389-2037
[ISSN] 1875-5550
[DOI] 10.2174/1389203716666150206122839
[PMID] 25693768
[DOI] https://doi.org/10.2174/1389203716666150206122839