Osteopontin adhesion receptors on gingival fibroblasts.

  title={Osteopontin adhesion receptors on gingival fibroblasts.},
  author={John A. D'Errico and John J. Sauk and Charles W. Prince and Martha J. Somerman},
  journal={Journal of periodontal research},
  volume={30 1},
Osteopontin (OPN) promotes attachment and spreading of cells in an RGD dependent fashion, suggesting that OPN interacts with integrins on cell surfaces. Here in, we show that LM-609, a monoclonal antibody to the alpha v beta 3 integrin (a vitronectin receptor), inhibited OPN-mediated attachment of gingival fibroblasts. To characterize the cell surface receptors responsible for this interaction, we performed OPN-sepharose affinity chromatography using detergent extracts of 35S-methionine or 125I… 

CD44 is not an adhesive receptor for osteopontin

It is suggested that CD44‐osteopontin interactions may not be common in vivo and may be limited to a specific CD44 isoform(s), and/or a particular modified form of osteopontIn interactions.

Osteopontin N-terminal Domain Contains a Cryptic Adhesive Sequence Recognized by α9β1 Integrin*

The data show that the N-terminal osteopontin fragment, which contains the RGD domain, supports adhesion of a melanoma cell line that is unable to bind native osteopontoin, which suggests that osteoponin adhesive interactions may be regulated by thrombin cleavage.

Structural Requirements for α9β1-Mediated Adhesion and Migration to Thrombin-Cleaved Osteopontin

It is demonstrated that alpha 9 beta 1 is one of the few integrin receptors that can interact with two distinct RGD-containing ligands through different adhesive domains.

Transforming JB6 cells exhibit enhanced integrin‐mediated adhesion to osteopontin

Flow cytometric analyses, blocking adhesion assay using anti‐αv antibody, and co‐immunoprecipitation assay all indicate that transforming JB6 cells adhere to OPN through its RGD sequence, and the most likely OPN receptor is the αvβ5 integrin, which increases the affinity or avidity for OPNthrough a PKC‐dependent pathway rather than increasing the number of receptors.

The role of osteopontin in tumorigenesis and metastasis.

Osteopontin has binding affinity for several different cellular receptors, potentially allowing it to stimulate various signaling pathways and influence distinct cellular events which may ultimately favor tumorigenesis or metastasis.

Coordinate expression of OPN and associated receptors during monocyte/macrophage differentiation of HL‐60 cells

The data suggest that induction of OPN and associated receptors may play a role during monocytic differentiation of HL‐60 cells.

Osteopontin Expression May Be Induced by c-Src in Papillary Thyroid Carcinoma

Results suggested that the induction of the expression of OPN invasiveness in papillary thyroid carcinoma was one of the important downstream events of increased c-Src expression.

Mechanical stimulation of osteopontin mRNA expression and synthesis in bone cell cultures

The severe loss of OPN expression in primary bone cells cultured without mechanical stimulation suggests that disuse conditions down‐regulate the differentiated osteoblastic phenotype, and suggests a role for OPN in the reaction of bone cells to mechanical stimuli.

Effects of irradiation on cementum matrix cytokins function during periodontal regeneration

The results imply that some cytokine in intact cementum prevents the attachment (differentiation) of bone cells onto the root surface, which may explain why the introduction of CGM following gingival flap surgery induces new cementum, new ligament and new bone formation, but CGM irradiated with γ-rays for clinical use causes ankylosis.

Upregulation of osteopontin expression in rat spinal cord microglia after traumatic injury.

Osteopontin expression in the model preceded that shown in the previously reported cerebral infarction models, and was localized in activated microglia surrounded by astrocytes.



The nature and significance of osteopontin.

  • W. Butler
  • Biology, Medicine
    Connective tissue research
  • 1989
This conclusion is supported by a number of studies showing that the protein promotes attachment and spreading of fibroblasts and osteoblasts to substratum, and that this attachment is inhibited by RGD-containing peptides.

New perspectives in cell adhesion: RGD and integrins.

Together, the adhesion proteins and their receptors constitute a versatile recognition system providing cells with anchorage, traction for migration, and signals for polarity, position, differentiation, and possibly growth.

Immunohistological localization of cell adhesion proteins and integrins in the periodontium.

The distribution of the cell adhesion proteins vitronECTin, fibronectin, tenascin, and laminin as well as several integrin subunits, alpha 2, alpha 5, and alpha v, was studied in primate periodontal tissues in order to localize the molecules studied in both soft and hard tissues.

The vitronectin receptor alpha v beta 3 binds fibronectin and acts in concert with alpha 5 beta 1 in promoting cellular attachment and spreading on fibronectin

It is concluded that fibronectin binds to the alpha v beta 3 vitronECTin receptor specifically and with high affinity, and that this interaction is biologically relevant in supporting cell adhesion to matrix proteins.

Identification of a bone sialoprotein receptor in osteosarcoma cells.

Results show that BSP is recognized by an RGD-directed receptor and that both vitronectin and BSP can bind to this receptor.

Integrin subunit expression by human osteoblasts and osteoclasts in situ and in culture.

Staining patterns observed in situ show that osteoblasts and osteoclasts possess different integrin subunits, a family of transmembrane proteins composed of non-covalently linked alpha and beta subunits.