Osteopontin at the Tumor/Host Interface

Senger, Donald R.; Brown, Lawrence F.; Perruzzi, Carole; Papadopoulos-Sergiou, A; Water, Livingston Van De

doi:10.1111/j.1749-6632.1995.tb44622.x

Cited by 26 publications

(18 citation statements)

References 34 publications

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“…The major thrombin cleavage site is at residues Arg 169 -Ser 170 , which is 6 amino acids C-terminal from the RGD domain. A second potential thrombin-cleavage site is within the RGD domain (Arg 160 -Gly 161 ) (17). Previous studies have shown that osteopontin proteolytic fragments are found in vivo and may have physiological importance (17,18).…”

mentioning

confidence: 99%

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

Smith

Cheung

Ling

et al. 1996

Journal of Biological Chemistry

237

186

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Osteopontin is an adhesive glycoprotein implicated in numerous diseases associated with inflammation and remodeling. There are several structural domains in osteopontin that are of particular interest. The RGD motif is a cell attachment sequence shown to be critical for cell adhesion through ␣ v -containing integrins. In close proximity to the RGD domain is the thrombin cleavage site. Previous observations suggest that thrombin cleavage of osteopontin occurs in vivo and may be physiologically important. To study the functional significance of osteopontin cleavage by thrombin, we made glutathione S-transferase-osteopontin fusion proteins. These proteins contain either the N-or C-terminal domains expected to be formed following thrombin cleavage at the Arg 169 -Ser 170 peptide bond. We compared these osteopontin fragments with native osteopontin in their ability to support adhesion of several different cell lines and identified the receptors mediating these interactions. Our 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 osteopontin. This suggests that osteopontin adhesive interactions may be regulated by thrombin cleavage. We also demonstrate that osteopontin contains a cryptic binding activity, which can be recognized by a novel osteopontin receptor. This receptor has been identified as the ␣ 9 ␤ 1 integrin.

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mentioning

confidence: 99%

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

Smith

Cheung

Ling

et al. 1996

Journal of Biological Chemistry

237

186

View full text Add to dashboard Cite

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“…In vitro, thrombin stimulates each event previously described to be necessary in the formation of a functional blood vessel. Thrombin directly and/or indirectly increases the expression of metalloproteinases (Duhamel-Clerin et al, 1997;Galis et al, 1997;Nguyen et al, 1999;Zucker et al, 1995Zucker et al, , 1998, diminishes the ability of endothelial cells to adhere to the extracellular matrix (Maragoudakis and Tsopanoglou, 2000), increases vascular permeability Garcia and Schaphorst, 1995), and induces proliferation and migration of endothelial cells (Herbert et al, 1994;Pankonin and Teuscher, 1991;Senger et al, 1996;Wang et al, 1997). Whether the eect of thrombin on proliferation and migration is direct remains to be determined.…”

Section: Direct Modulationmentioning

confidence: 99%

Angiogenesis and G-protein-coupled receptors: signals that bridge the gap

Richard¹,

Vouret‐Craviari²,

Pouysségur³

2001

Oncogene

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Angiogenesis is a mechanism that has repercussions in a number of physiological and pathological situations. Vascular endothelial growth factor and basic ®broblast growth factor have understandably received enormous research coverage for being the major mediators of new blood vessel growth, often overshadowing other agonist that also have strong angiogenic potential. We wish to put the spotlight on GPCR agonists that undoubtedly have their word to say on the subject of angiogenesis. In this short review, we will discuss our ®ndings along with the work from other groups on the mechanisms by which GPCR agonists, like thrombin and angiotensin II, control a number of angiogenic signals. A complete understanding of these mechanisms could, by the design of new therapeutic strategies, have a strong impact in clinical oncology. Oncogene (2001) 20, 1556 ± 1562.

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“…In addition, BSP peptides are potent inhibitors of breast cancer cell adhesion to bone (82,83). OPN is expressed in breast cancer (4,7,16,23), as well as in prostate cancer (21), thyroid cancer (84), skin cancer (85), and several other types of cancer (6,86,87).…”

Section: Figmentioning

confidence: 99%

“…It is a protein of ϳ60 kDa, and shares with BSP high sialic acid content, highly acidic sequences (but these are aspartic acid-rich), multiple residues with consensus for phosphorylation as well as an integrin-binding RGD motif (6,12,14). Because of its RGD tripeptide and adhesive properties, it has been proposed that OPN plays a role in metastasis in certain tumors (20 -22).…”

mentioning

confidence: 99%

“…Osteopontin (OPN) 1 and bone sialoprotein (BSP) are produced by trophoblasts (1,2) and are induced in certain neoplasms (3)(4)(5)(6)(7)(8)(9)(10)(11). BSP is a phosphoprotein of molecular mass ϳ70 -80 kDa, about half of which is sialic acid rich N-and O-linked carbohydrates, and also contains several glutamic acid-rich domains, tyrosine sulfates, as well as an integrinbinding arginine-glycine-aspartate (RGD) domain (12)(13)(14).…”

mentioning

confidence: 99%

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