?v?3, ?v?5, and osteopontin are coordinately upregulated at early time points in a rabbit model of neointima formation

Corjay, Martha H.; Diamond, Sheila; Schlingmann, Karen; Gibbs, Sandra K.; Stoltenborg, Janet K.; Racanelli, Adrienne L.

doi:10.1002/(sici)1097-4644(19991201)75:3<492::aid-jcb13>3.0.co;2-z

Cited by 42 publications

(12 citation statements)

References 33 publications

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“…OPN is an adhesion molecule and a growth promoter that binds to specific ␤3 integrin receptors, leading to stimulation of cell spreading and proliferation (32). In addition to OPN, ␤3 integrin receptors are also upregulated in models of atherosclerosis and are suggested to play an important role in atherosclerosis (33,34).…”

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confidence: 99%

Hypoxia Stimulates Osteopontin Expression and Proliferation of Cultured Vascular Smooth Muscle Cells

et al. 2001

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We examined the effect of hypoxia on proliferation and osteopontin (OPN) expression in cultured rat aortic vascular smooth muscle (VSM) cells. In addition, we determined whether hypoxia-induced increases in OPN and cell proliferation are altered under hyperglycemic conditions. Quiescent cultures of VSM cells were exposed to hypoxia (3% O 2 ) or normoxia (18% O 2 ) in a serum-free medium, and cell proliferation as well as the expression of OPN was assessed. Cells exposed to hypoxia for 24 h exhibited a significant increase in [ 3 H]thymidine incorporation followed by a significant increase in cell number at 48 h in comparison with respective normoxic controls. Exposure to hypoxia produced significant increases in OPN protein and mRNA expression at 2 h followed by a gradual decline at 6 and 12 h, with subsequent significant increases at 24 h. Neutralizing antibodies to either OPN or its receptor ␤3 integrin but not neutralizing antibodies to ␤5 integrin prevented the hypoxia-induced increase in T he first descriptions of a link between systemic hypoxia and pulmonary artery smooth muscle cell proliferation came from both in vivo and in vitro models of pulmonary hypertension (1-3). Increased proliferation of aortic vascular smooth muscle (VSM) cells is also a key feature in the progression of atherosclerosis (4). Both systemic and local hypoxia contributes to the development of atherosclerotic lesions (5-11). Recent in vivo studies found a direct correlation of local arterial wall hypoxia, VSM cell proliferation, and atherosclerosis (12,13). However, the underlying signaling mechanisms whereby hypoxia induces VSM cell proliferation and subsequent atherosclerotic lesions remain poorly defined. Part of the problem has been in the demonstration of a mitogenic effect of hypoxia in cultured VSM cells in vitro. Hypoxia has only been shown to induce the proliferation of bovine pulmonary artery smooth muscle cells in culture when they are costimulated either with an activator of protein kinase C (PKC) or serum (3,14). To examine the effect of local hypoxia on cell proliferation, our laboratory has developed an appropriate cell culture model system in which cultured cells exhibited differentiated morphology and function by improved oxygenation (15). Using this culture model, we reported that hypoxia induces proliferation, dedifferentiation, and/or extracellular matrix synthesis in cultured renal tubular epithelial and glomerular mesangial cells (16 -18). In the present study, we examined the effect of hypoxia on the proliferation of cultured rat aortic VSM cells to determine whether hypoxia directly alters their proliferative behavior.Enhanced proliferation of VSM cells has also been demonstrated in both human and experimental models of diabetes (19,20). In addition, cultured VSM cells grown in high media glucose concentration (to mimic hyperglycemia of diabetes) have exhibited increased cell proliferation (21). The pathophysiological mechanisms responsible for accelerated VSM cell proliferation and progression into diabetic...

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Hypoxia Stimulates Osteopontin Expression and Proliferation of Cultured Vascular Smooth Muscle Cells

et al. 2001

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“…2,3 After vascular injury, ␣ v ␤ 3 expression increases markedly, a finding that has been consistent across numerous animal models including baboons, rats, rabbits, mice, and pigs. 4 ␣ v ␤ 3 expression is observed rapidly in the media after injury and is found in the neointima within 7 days, with peak levels at 14 to 28 days.…”

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confidence: 55%

“…4 ␣ v ␤ 3 expression is observed rapidly in the media after injury and is found in the neointima within 7 days, with peak levels at 14 to 28 days. [2][3][4][5][6][7] ␣ v ␤ 3 integrin expression colocalizes with ␣-actin in the injured arteries, suggesting that SMCs within the vessel wall express ␣ v ␤ 3 integrins after vascular injury. 2,7 Recently, Sadeghi et al, using an 111 In-labeled radiotracer, found that expression of activated ␣ v ␤ 3 increased after carotid injury in Apo E Ϫ/Ϫ mice; the increase was maximal 1 week after injury with levels remaining elevated at 3 and 4 weeks.…”

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confidence: 99%

Down But Not Out

Stouffer

Pathak

Zhao

et al. 2005

ATVB

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“…10 Using animal models of neointima formation, several groups have observed increased expression of osteopontin and ␣ v ␤ 3 in such lesions. 11 More direct evidence supporting the potential role of osteopontin in the process of intimal thickening stems from the observation that neutralizing antibodies to osteopontin limit neointimal thickening in rat carotid artery after balloon injury. 12 RGD and ␣ v ␤ 3 antagonists have been shown to inhibit neointima formation in rabbit, hamster, porcine, and guinea pig vascular injury models, an effect that has been interpreted to be mediated via the disruption of osteopontin-␣ v ␤ 3 interaction.…”

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Bone Sialoprotein and the Paradox of Angiogenesis Versus Atherosclerosis

Dong

Goldschmidt‐Clermont

2000

Circulation Research

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Bone sialoprotein (BSP) is a protein thought to be highly specific for bone. BSP contains an arginine-glycineaspartic acid (RGD) cell attachment sequence involved in osteoclast adhesion to bone matrix via the vitronectin receptor and plays an important role in the early process of bone mineralization and resorption. The study by Bellahcène et al 1 in this issue of Circulation Research indicates that BSP mediates adhesion and chemotactic migration of endothelial cells and promotes angiogenesis, suggesting that BSP may be an important factor in angiogenesis and the initiation of atherosclerosis, two processes that are probably related.In earlier studies, Folkman 2 hypothesized that tumor growth beyond a few millimeters requires recruitment and growth of a new microcirculation, or angiogenesis, which is induced by tumors as lifelines for oxygen and nutrients. New blood vessels also provide exits for cancer cells to spread to other parts of the body. Angiogenesis is also involved in physiological conditions, such as embryogenesis, and other pathological conditions, such as wound healing. The process of angiogenesis requires a highly coordinated series of events, including endothelial cell proliferation, migration, tube and lumen formation, and, in some cases, recruitment of smooth muscle cells (SMCs) and other adventitial cells.Adhesive interaction of cells with components of the extracellular matrix is a recognized requirement for cell proliferation and migration. Evidence indicates that many of the adhesive interactions are mediated by members of the integrin family of heterodimeric adhesion receptors. Among these integrins, ␣ v ␤ 3 , which is expressed by a variety of cell types, has been shown to play a key role in the cell migration involved in metastasis and angiogenesis. 3 The work presented by Bellahcène et al 1 indicates that BSP, a bone-associated protein that contains the RGD sequence, a common recognition sequence for most integrins, binds ␣ v ␤ 3 in endothelial cells and mediates the migration of such cells, extending the study by Byzova et al. 4 Furthermore, Bellahcène et al 1 show that another integrin, ␣ v ␤ 5 , does not bind BSP, suggesting that there is a certain degree of specificity for the interaction between BSP and ␣ v ␤ 3 .The in vivo data indicating that BSP promotes angiogenesis via its interaction with ␣ v ␤ 3 integrin and that such an angiogenic effect is probably even greater than that of basic fibroblast growth factor (bFGF) 1 are intriguing. These data underscore the physiological and pathophysiological consequences of the interaction between BSP and ␣ v ␤ 3 integrin and define BSP as a novel angiogenic factor. These findings may provide an explanation for the previously established association of BSP expression levels in tumors with the development of bone metastases. 5 Higher BSP expression in the tumor correlates with an increased risk of metastasis of carcinomas to bone tissue, which could be due to angiogenesis enhancement by BSP. In addition, BSP expression in the tumor may facil...

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?v?3, ?v?5, and osteopontin are coordinately upregulated at early time points in a rabbit model of neointima formation

Cited by 42 publications

References 33 publications

Hypoxia Stimulates Osteopontin Expression and Proliferation of Cultured Vascular Smooth Muscle Cells

Hypoxia Stimulates Osteopontin Expression and Proliferation of Cultured Vascular Smooth Muscle Cells

Down But Not Out

Bone Sialoprotein and the Paradox of Angiogenesis Versus Atherosclerosis

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