Periostin and its interacting proteins in the construction of extracellular architectures

Periostin is a matricellular protein that is composed of a multi-domain structure with an amino-terminal EMI domain, a tandem repeat of four FAS 1 domains, and a carboxyl-terminal domain. These distinct domains have been demonstrated to bind to many proteins including extracellular matrix proteins (...

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Vydáno v:	Cellular and molecular life sciences : CMLS Ročník 74; číslo 23; s. 4269 - 4277
Hlavní autoři:	Kii, Isao, Ito, Harumi
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	Cham Springer International Publishing 01.12.2017 Springer Nature B.V
Témata:	Amino acids Assembly Binding sites Biochemistry Biomedical and Life Sciences Biomedicine Bone Morphogenetic Protein 1 - genetics Bone Morphogenetic Protein 1 - metabolism Bone morphogenetic proteins Cell Adhesion Molecules - genetics Cell Adhesion Molecules - metabolism Cell Biology chemical interactions collagen Collagen (type I) Collagen - genetics Collagen - metabolism Connective Tissue - anatomy & histology Connective Tissue - metabolism Connective tissues Construction Crosslinking disease course Electromagnetic interference enzymes Extracellular matrix Fibronectin fibronectins Fibronectins - genetics Fibronectins - metabolism Gene Expression Homeostasis Humans Laminin Laminin - genetics Laminin - metabolism Life Sciences Lysyl oxidase Multi-Author Review Nephroblastoma Overexpressed Protein - genetics Nephroblastoma Overexpressed Protein - metabolism Protein Binding Protein Interaction Domains and Motifs Protein Interaction Mapping Protein Isoforms - genetics Protein Isoforms - metabolism Proteins Proteoglycans - metabolism Signal Transduction Tenascin Tenascin - genetics Tenascin - metabolism EMI FAS 1 Tenascin Collagen Fibronectin BMP-1
ISSN:	1420-682X, 1420-9071, 1420-9071
On-line přístup:	Získat plný text
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Popis
Shrnutí:	Periostin is a matricellular protein that is composed of a multi-domain structure with an amino-terminal EMI domain, a tandem repeat of four FAS 1 domains, and a carboxyl-terminal domain. These distinct domains have been demonstrated to bind to many proteins including extracellular matrix proteins (Collagen type I and V, fibronectin, tenascin, and laminin), matricellular proteins (CCN3 and βig-h3), and enzymes that catalyze covalent crosslinking between extracellular matrix proteins (lysyl oxidase and BMP-1). Adjacent binding sites on periostin have been suggested to put the interacting proteins in close proximity, promoting intermolecular interactions between each protein, and leading to their assembly into extracellular architectures. These extracellular architectures determine the mechanochemical properties of connective tissues, in which periostin plays an important role in physiological homeostasis and disease progression. In this review, we introduce the proteins that interact with periostin, and discuss how the multi-domain structure of periostin functions as a scaffold for the assembly of interacting proteins, and how it underlies construction of highly sophisticated extracellular architectures.
Bibliografie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 ObjectType-Review-3 content type line 23
ISSN:	1420-682X 1420-9071 1420-9071
DOI:	10.1007/s00018-017-2644-4