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Cited by 140Bone Metabolism and DiseasesCell Adhesion Molecules ResearchBone and Dental Protein Studies

β1 integrins and osteoclast function: Involvement in collagen recognition and bone resorption

Helfrich, M.H., Nesbitt, S.A., Lakkakorpi, P.T., Barnes, M.J., Bodary, S.C., Shankar, G., Mason, W.T., Mendrick, D.L. +2 more·1996·Bone
DOI 10.1016/s8756-3282(96)00223-2
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Abstract

The extracellular matrix of bone is composed mainly of type I collagen. In this report we studied the role and collagen-binding properties of osteoclast integrins (alpha v, alpha 2, beta 1, and beta 3). Cell adhesion assays with rat osteoclasts and affinity chromatography/SDS-PAGE analysis with purified human osteoclast membranes demonstrated adhesion of osteoclasts to native type I collagen in a divalent cation and Arg-Gly-Asp (RGD)-dependent way via alpha 2 beta 1 integrin, whereas osteoclast adhesion to denatured collagen predominantly involved alpha v beta 3. In receptor-binding assays, the involvement of human recombinant alpha v beta 3 in adhesion to denatured collagen was confirmed. Additionally, osteoclasts adhered to type I collagen fibers and to monomeric types II-V collagen with characteristics similar to those on native monomeric type I collagen. Osteoclastic bone resorption in vitro was inhibited (> 40%) in the presence of alpha 2 and beta 1 antibodies. Using scanning laser confocal microscopy, alpha v beta 3, alpha 2, and beta 1 integrin were detected within podosomes in nonresorbing osteoclasts and in the ruffled border area and basolateral membrane in resorbing osteoclasts, but not in the sealing zone of resorbing osteoclasts. These results demonstrate that alpha 2 beta 1, in addition to alpha v beta 3, has an important role in osteoclast function and acts as a receptor for native, but not denatured, collagen.

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  • During bone resorption osteoclasts express αvβ3 and α2β1 integrins to interact with the extracellular matrix, in which the former bind to bone-enriched RGD-containing proteins such as bone sialoprotein and osteopontin, whereas β1 integrins bind to collagen fibrils.

    “Thus, during bone resorption osteoclasts express α v β 3 and α 2 β 1 integrins to interact with the extracellular matrix, in which the former bind to bone-enriched RGD-containing proteins, such as bone sialoprotein and osteopontin, whereas β 1 integrins bind to collagen fibrils [133, 134].”

    From Biology of Bone Tissue: Structure, Function, and Factors That Influence Bone Cells (2015) · cites this paper as [134]

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Authors
Helfrich, M. H., Nesbitt, S. A., Lakkakorpi, P. T., Barnes, M. J., Bodary, S. C., Shankar, G., Mason, W. T., Mendrick, D. L., Väänänen, H. K., & Horton, M. A.
Affiliations
  • University of Aberdeen (GB)
  • University College London (GB)
  • University of Oulu (FI)
  • University of Cambridge (GB)
  • Genentech (US)
  • Babraham Institute (GB)
  • Brigham and Women's Hospital (US)
Corresponding author
Helfrich, M.H.
ORCID
Venue
Bone
Publisher
Elsevier BV
Published
1996-10
Volume
19
Issue
4
Pages
317-328
ISSN
  • 1873-2763 (ISSN-L)
  • 8756-3282
DOI
10.1016/s8756-3282(96)00223-2
OpenAlex
W2107556429
Cited by
139
References
55
Citations by year
2026: 2 · 2024: 6 · 2023: 1 · 2022: 2 · 2021: 3 · 2020: 5 · 2019: 4 · 2018: 6 · 2017: 3 · 2016: 1 · 2015: 5 · 2014: 5 · 2013: 5 · 2012: 7
FWCI
2.40
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Bone (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
  • Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
Keywords
beta1 integrin, osteoclasts, bone resorption, type I collagen, alpha2beta1 integrin, integrin αvβ3, RGD motif, cell adhesion, podosomes, ruffled border, sealing zone, denatured collagen, integrin antibodies
MeSH terms
Amino Acid Sequence, Animals, Antibodies, Monoclonal, Binding, Competitive, Bone Resorption, Cations, Divalent, Cell Adhesion, Chromatography, Affinity, Collagen, Electrophoresis, Polyacrylamide Gel, Humans, Immunohistochemistry, Membrane Proteins, Oligopeptides, Osteoclasts, Peptide Fragments, Receptors, Immunologic, Integrins, Rats

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