The Bioactive Acidic Serine- and Aspartate-Rich Motif Peptide

Current Protein & Peptide Science Volume 16 Issue 3 Page 196-202 published_at 2015
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Title ( eng )
The Bioactive Acidic Serine- and Aspartate-Rich Motif Peptide
Creator
Source Title
Current Protein & Peptide Science
Volume 16
Issue 3
Start Page 196
End Page 202
Abstract
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.
Keywords
Acidic serine- and aspartic acid-rich motif (ASARM)
bone mineralization
matrix extracellular phosphoglycoprotein (MEPE)
small integrin-binding ligand N-linked glycoprotein (SIBLING)
Language
eng
Resource Type journal article
Publisher
Bentham Science Publishers
Date of Issued 2015
Rights
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。
Publish Type Author’s Original
Access Rights open access
Source Identifier
[ISSN] 1389-2037
[ISSN] 1875-5550
[DOI] 10.2174/1389203716666150206122839
[PMID] 25693768
[DOI] https://doi.org/10.2174/1389203716666150206122839