The DOI matches its Crossref record; 149 of the 149 references it cites were found in a registry or an index.
αvβ3and macrophage colony‐stimulating factor: partners in osteoclast biology
Abstract
Summary: Osteoclasts, the sole bone‐resorbing cells, arise by fusion and differentiation of monocyte/macrophage precursors. Matrix degradation requires adhesion of the osteoclast to bone, an integrin α v β 3‐mediated event that also stimulates signals which polarize the cell and secrete resorptive molecules such as hydrochloric acid and acidic proteases. Two cytokines are necessary and sufficient for osteoclastogenesis, receptor activator of nuclear factor κB ligand (RANKL) and macrophage colony‐stimulating factor (M‐CSF), both produced by mesenchymal cells in the bone marrow environment. M‐CSF promotes survival and proliferation of osteoclast precursors. It also contributes to their differentiation and regulates the cytoskeletal changes that accompany bone resorption. Binding of M‐CSF to c‐Fms, its receptor, recruits adapter proteins and cytosolic kinases, thereby activating a variety of intracellular signals. We herein review how α v β 3 and M‐CSF, alone and in concert, impact production, survival, and function of the osteoclast, thereby controlling skeletal mass. Signals from α v β 3 and/or c‐Fms activate Syk and Vav3, originally defined by their function in lymphoid cells. Genetic depletion of either protein generates a strong bone phenotype, underscoring the promise of osteoimmunobiology.
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Cites
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Cited by
Normal Bone Anatomy and Physiology
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Osteoimmunology: shared mechanisms and crosstalk between the immune and bone systems
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Estrogens and androgens in skeletal physiology and pathophysiology
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Metadata
- Authors
- Ross, F. P., & Teitelbaum, S. L.
- Venue
- Immunological Reviews
- Publisher
- Wiley
- Published
- 2005-11-22
- Volume
- 208
- Issue
- 1
- Pages
- 88-105
- ISSN
- 0105-2896 (ISSN-L)
- 1600-065X
- OpenAlex
- W1838439206
- Cited by
- 303
- References
- 149
- FWCI
- 0.88
- Type
- journal article
- Language
- en
- Open access
- closed
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