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).
Current Protein & Peptide Science
Title:The Bioactive Acidic Serine- and Aspartate-Rich Motif Peptide
Volume: 16 Issue: 3
Author(s): Tomoko Minamizaki and Yuji Yoshiko
Affiliation:
Keywords: Acidic serine- and aspartic acid-rich motif (ASARM), bone mineralization, matrix extracellular phosphoglycoprotein (MEPE), small integrin-binding ligand N-linked glycoprotein (SIBLING).
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.
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Cite this article as:
Minamizaki Tomoko and Yoshiko Yuji, The Bioactive Acidic Serine- and Aspartate-Rich Motif Peptide, Current Protein & Peptide Science 2015; 16 (3) . https://dx.doi.org/10.2174/1389203716666150206122839
DOI https://dx.doi.org/10.2174/1389203716666150206122839 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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