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Text
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URL Address
<a href="http://doi.org/10.1002/jcb.24760" target="_blank" rel="noreferrer noopener">http://doi.org/10.1002/jcb.24760</a>
Pages
1243–1253
Issue
7
Volume
115
Dublin Core
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Title
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Osteoactivin promotes osteoblast adhesion through HSPG and alphavbeta1 integrin.
Publisher
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Journal of cellular biochemistry
Date
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2014
2014-07
Subject
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3T3 Cells; Actin Cytoskeleton/physiology; ADHESION; Alkaline Phosphatase/biosynthesis; Animals; Antibodies/immunology; Cell Adhesion; Cell Differentiation; Cell Line; Cell Proliferation; Chlorates/pharmacology; Extracellular Signal-Regulated MAP Kinases/biosynthesis; Eye Proteins/genetics/immunology/*metabolism; Focal Adhesion Kinase 1/biosynthesis; Focal Adhesions; Heparan Sulfate Proteoglycans/*metabolism; Heparin/pharmacology; Inbred C57BL; INTEGRIN; Membrane Glycoproteins/genetics/immunology/*metabolism; Mice; OSTEOACTIVIN; OSTEOBLAST; OSTEOBLAST DIFFERENTIATION; Osteoblasts/*physiology; Osteogenesis/physiology; Protein Binding; Rats; Receptors; Recombinant Proteins; Vitronectin/immunology/*metabolism
Creator
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Moussa Fouad M; Hisijara Israel Arango; Sondag Gregory R; Scott Ethan M; Frara Nagat; Abdelmagid Samir M; Safadi Fayez F
Description
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Osteoactivin (OA), also known as glycoprotein nmb (gpnmb) plays an important role in the regulation of osteoblast differentiation and function. OA induced osteoblast differentiation and function in vitro by stimulating alkaline phosphatase (ALP) activity, osteocalcin production, nodule formation, and matrix mineralization. Recent studies reported a role for OA in cell adhesion and integrin binding. In this study, we demonstrate that recombinant osteoactivin (rOA) as a matricellular protein stimulated adhesion, spreading and differentiation of MC3T3-E1 osteoblast-like cells through binding to alphav beta1 integrin and heparan sulfated proteoglycans (HSPGs). MC3T3-E1 cell adhesion to rOA was blocked by neutralizing anti-OA or anti-alphav and beta1 integrin antibodies. rOA stimulated-osteoblast adhesion was also inhibited by soluble heparin and sodium chlorate. Interestingly, rOA stimulated-osteoblast adhesion promoted an increase in FAK and ERK activation, resulting in the formation of focal adhesions, cell spreading and enhanced actin cytoskeleton organization. In addition, differentiation of primary osteoblasts was augmented on rOA coated-wells marked by increased alkaline phosphatase staining and activity. Taken together, these data implicate OA as a matricellular protein that stimulates osteoblast adhesion through binding to alphav beta1 integrin and cell surface HSPGs, resulting in increased cell spreading, actin reorganization, and osteoblast differentiation with emphasis on the positive role of OA in osteogenesis.
Identifier
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<a href="http://doi.org/10.1002/jcb.24760" target="_blank" rel="noreferrer noopener">10.1002/jcb.24760</a>
Rights
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Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
2014
3T3 Cells
Abdelmagid Samir M
Actin Cytoskeleton/physiology
ADHESION
Alkaline Phosphatase/biosynthesis
Animals
Antibodies/immunology
Cell Adhesion
Cell Differentiation
Cell Line
Cell Proliferation
Chlorates/pharmacology
Department of Anatomy & Neurobiology
Extracellular Signal-Regulated MAP Kinases/biosynthesis
Eye Proteins/genetics/immunology/*metabolism
Focal Adhesion Kinase 1/biosynthesis
Focal Adhesions
Frara Nagat
Heparan Sulfate Proteoglycans/*metabolism
Heparin/pharmacology
Hisijara Israel Arango
Inbred C57BL
integrin
Journal of cellular biochemistry
Membrane Glycoproteins/genetics/immunology/*metabolism
Mice
Moussa Fouad M
NEOMED College of Medicine
OSTEOACTIVIN
OSTEOBLAST
OSTEOBLAST DIFFERENTIATION
Osteoblasts/*physiology
Osteogenesis/physiology
Protein Binding
Rats
Receptors
Recombinant Proteins
Safadi Fayez F
Scott Ethan M
Sondag Gregory R
Vitronectin/immunology/*metabolism