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Cited by 64Cell Adhesion Molecules ResearchBone Metabolism and DiseasesBone and Dental Protein Studies

Activation of αvβ3Integrin on Human Osteoclast-like Cells Stimulates Adhesion and Migration in Response to Osteopontin

Faccio, R., Grano, M., Colucci, S., Zallone, A.Zambonin, Quaranta, V., Pelletier, A.J.·1998·Biochemical and Biophysical Research Communications
DOI 10.1006/bbrc.1998.9180
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Abstract

Integrins mediate cell adhesion and can induce different cellular responses, including changes in intracellular pH, changes and oscillation in intracellular free calcium, and protein phosphorylation on tyrosine. During bone resorption, the integrin alphav beta3 regulates adhesion of osteoclasts to bone extracellular matrix proteins, such us osteopontin (Opn). Adhesion via alphav beta3 is followed by osteoclast polarization onto the bone surface and by the onset of bone resorption. To characterize these events at the molecular level, we investigated the state of activation of alphav beta3 on the human osteoclast-like cell line GCT23 using the monoclonal antibody AP5 which binds to and can induce, under low calcium conditions, activated alphav beta3. By flow cytometry, approximately 50% of alphav beta3 on the surface of the osteoclast-like cell line GCT23 was reactive with AP5 and was therefore in the activated state. Incubation with AP5 in the presence of low calcium concentrations increased activated alphav beta3 to 90-100%. Activation of alphav beta3 increased the efficiency of GCT23 adhesion to Opn by 2-fold. Furthermore, haptotactic migration on Opn was also enhanced about 40% compared to control. We propose that changes in the activation state of alphav beta3 may be a regulation point for osteoclasts during bone resorption.

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Crossref · 10.1006/bbrc.1998.9180

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  • Interaction with the matrix is mediated by the integrin complex α5β3, which recognizes RGD motifs in proteins such as fibronectin, osteopontin and bone sialoprotein.

    “The interaction with the matrix is mediated by the integrin complex α5β3, which recognizes RGD motifs in proteins such as fibronectin,190 osteopontin (OPN)191 and bone sialoprotein.192”

    From Bone remodeling: an operational process ensuring survival and bone mechanical competence (2022) · cites this paper as [191]

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Authors
Faccio, R., Grano, M., Colucci, S., Zallone, A. Z., Quaranta, V., & Pelletier, A. J.
Affiliations
  • University of Bari Aldo Moro (IT)
  • Scripps Research Institute (US)
ORCID
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
1998-08
Volume
249
Issue
2
Pages
522-525
ISSN
0006-291X (ISSN-L)
DOI
10.1006/bbrc.1998.9180
OpenAlex
W2064705331
Cited by
64
References
12
Citations by year
2026: 1 · 2023: 1 · 2022: 1 · 2019: 3 · 2017: 1 · 2016: 3 · 2015: 2 · 2014: 1 · 2013: 1 · 2012: 1
FWCI
2.07
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Biochemical and Biophysical Research Communications (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5r01de010063-04, 5r29gm053489-05)
  • National Institute of General Medical Sciences (GM53489)
  • National Institute of Dental and Craniofacial Research (DE10063)
Topics
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
  • Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
Keywords
integrin αvβ3, integrin activation, osteoclast-like cells, osteopontin, cell adhesion, bone resorption, low calcium
MeSH terms
Antibodies, Monoclonal, Epitopes, Bone Neoplasms, Calcium, Cell Adhesion, Cell Movement, Humans, Kinetics, Osteoclasts, Sialoglycoproteins, Tumor Cells, Cultured, Receptors, Vitronectin, Osteopontin

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