RGD-directed attachment of isolated rat osteoclasts to osteopontin, bone sialoprotein, and fibronectin

Flores, Myra E.; Norgård, Maria; Heinegård, Dick; Reinholt, Finn P.; Andersson, Göran

doi:10.1016/0014-4827(92)90305-r

Cited by 167 publications

(80 citation statements)

References 20 publications

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“…The bone-cell interaction is mediated in part by integrin αvβ3 (161) (Figure 4), which recognizes the RGD sequence present in various bone matrix proteins such as osteopontin, vitronectin, and bone sialoprotein (162)(163)(164). Interaction of integrin αvβ3 with the bone matrix induces cytoskeleton organization that polarizes the osteoclast's resorptive machinery to the bone-cell interface, where it creates an isolated resorptive compartment consisting of an actin ring surrounding a ruffled border.…”

Section: Establishment Of the Resorption Compartmentmentioning

confidence: 99%

Osteoclasts: New Insights

2013

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Osteoclasts, the bone-resorbing cells, play a pivotal role in skeletal development and adult bone remodeling. They also participate in the pathogenesis of various bone disorders. Osteoclasts differentiate from cells of the monocyte/macrophage lineage upon stimulation of two essential factors, the monocyte/ macrophage colony stimulating factor (M-CSF) and receptor activation of NF-кB ligand (RANKL). M-CSF binds to its receptor c-Fms to activate distinct signaling pathways to stimulate the proliferation and survival of osteoclast precursors and the mature cell. RANKL, however, is the primary osteoclast differentiation factor, and promotes osteoclast differentiation mainly through controlling gene expression by activating its receptor, RANK. Osteoclast function depends on polarization of the cell, induced by integrin αvβ3, to form the resorptive machinery characterized by the attachment to the bone matrix and the formation of the bone-apposed ruffled border. Recent studies have provided new insights into the mechanism of osteoclast differentiation and bone resorption. In particular, c-Fms and RANK signaling have been shown to regulate bone resorption by cross-talking with those activated by integrin αvβ3. This review discusses new advances in the understanding of the mechanisms of osteoclast differentiation and function.

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Section: Establishment Of the Resorption Compartmentmentioning

confidence: 99%

Osteoclasts: New Insights

2013

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“…36 EkRylander et al 31 found that osteopontin is a substrate for the phosphoprotein phosphatase activity of osteoclast TRAP in vitro, resulting in dephosphorylation of serine residues. Other phosphatase enzymes, including alkaline phosphatase and prostatic acid phosphatase, lacked this enzymic activity.…”

Section: Trap As a Phosphoprotein Phosphatasementioning

confidence: 99%

Structure, function, and regulation of tartrate-resistant acid phosphatase

Oddie

Schenk

Angel

et al. 2000

Bone

200

198

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“…Several other integrin based drugs such as the peptides containing the integrin-binding RGD sequence (Ruoslahti, 1996), and mimics of such peptides that speci®cally block individual integrins are also under development. These drugs target thrombosis (a IIb b 3 in platelets (Pierschbacher et al, 1994), osteoporosis (a v b 3 in osteoclsts (Flores et al, 1992)) and tumor-induced angiogenesis (a v b 3 in neovascular endothelial cells (Brooks et al, 1994). In a recent exciting study, Ruoslahti's group used the in vivo selection of phage display libraries to isolate peptides that home speci®cally to tumor blood vessels.…”

Section: Summary and Therapeutic Applicationsmentioning

confidence: 99%

Signaling by integrin receptors

Kumar¹

1998

Oncogene

257

181

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Adhesive interactions are critical for the proliferation, survival and function of all cells. Integrin receptors as the major family of adhesion receptors have been the focus of study for more than a decade. These studies have tremendously enhanced our understanding of the integrin-mediated adhesive interactions and have unraveled novel integrin functions in cell survival mechanisms and in the activation of divergent signaling pathways. The signals from integrin receptors are integrated from those originating from growth factor receptors in order to organize the cytoskeleton, stimulate cell proliferation and rescue cells from matrix detachment-induced programmed cell death. These functions are critical in the regulation of multiple processes such as tissue development, in¯ammation, angiogenesis, tumor cell growth and metastasis and programmed cell death.

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RGD-directed attachment of isolated rat osteoclasts to osteopontin, bone sialoprotein, and fibronectin

Cited by 167 publications

References 20 publications

Osteoclasts: New Insights

Osteoclasts: New Insights

Structure, function, and regulation of tartrate-resistant acid phosphatase

Signaling by integrin receptors

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