Periostin mediates vascular smooth muscle cell migration through the integrins ανβ3 and ανβ5 and focal adhesion kinase (FAK) pathway

Li, Guohong; Jin, Rong; Norris, Russell A.; Zhang, Lin; Yu, Shiyong; Wu, Fengbo; Markwald, Roger R.; Nanda, Anil; Conway, Simon J.; Smyth, Susan S.; Granger, D. Neil

doi:10.1016/j.atherosclerosis.2009.07.046

Cited by 138 publications

(134 citation statements)

References 36 publications

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“…Overexpression of periostin in aortic SMCs induced migration together with increased integrin-b3 expression and FAK phosphorylation. 7 In addition, periostin expression was increased in vascular SMCs subjected to mechanical strain, and this increase was followed by FAK activation and MCP-1 secretion, which were inhibited by a periostin-neutralizing antibody. 31 In agreement with these studies, induction of periostin in the NTS model was determinant for the de novo expression of integrin-b3 followed by downstream FAK and AKT activation.…”

Section: Discussionmentioning

confidence: 96%

“…[3][4][5] Interaction of periostin with cell-surface integrins avb3 and avb5 has been associated with increased adhesion and migration of cancer cells and vascular smooth muscle cells (SMCs). 6,7 Periostin is highly induced in vitro by TGF-b1, 1,5,8 and it was also found to be upregulated by angiotensin II in cardiac fibroblasts. 8 IL-4 and IL-13 increased periostin in lung fibroblasts and bronchial epithelial cells, associating its induction with asthma.…”

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confidence: 99%

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NFκB-Induced Periostin Activates Integrin-β3 Signaling to Promote Renal Injury in GN

Prakoura

Kavvadas

Kormann

et al. 2016

JASN

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De novo expression in the kidney of periostin, a protein involved in odontogenesis and osteogenesis, has been suggested as a biomarker of renal disease. In this study, we investigated the mechanism(s) of induction and the role of periostin in renal disease. Using a combination of bioinformatics, reporter assay, and chromatin immunoprecipitation analyses, we found that NFkB and other proinflammatory transcription factors induce periostin expression in vitro and that binding of these factors on the periostin promoter is enriched in glomeruli during experimental GN. Mice lacking expression of periostin displayed preserved renal function and structure during GN. Furthermore, delayed administration of periostin antisense oligonucleotides in wild-type animals with GN reversed already established proteinuria, diminished tissue inflammation, and improved renal structure. Lack of periostin expression also blunted the de novo renal expression of integrin-b3 and phosphorylation of focal adhesion kinase and AKT, known mediators of integrin-b3 signaling that affect cell motility and survival, observed during GN in wild-type animals. In vitro, recombinant periostin increased the expression of integrin-b3 and the concomitant phosphorylation of focal adhesion kinase and AKT in podocytes. Notably, periostin and integrin-b3 were highly colocalized in biopsy specimens from patients with inflammatory GN. These results demonstrate that interplay between periostin and renal inflammation orchestrates inflammatory and fibrotic responses, driving podocyte damage through downstream activation of integrin-b3 signaling. Targeting periostin may be a novel therapeutic strategy for treating CKD.

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Section: Discussionmentioning

confidence: 96%

mentioning

confidence: 99%

NFκB-Induced Periostin Activates Integrin-β3 Signaling to Promote Renal Injury in GN

Prakoura

Kavvadas

Kormann

et al. 2016

JASN

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“…Recent reports have shown that the activation of FAK is essential for cell migration (11). To determine whether FAK has a role in ANG II-dependent SMC migration, we performed the scratch and Boyden chamber assays on SMCs treated with the FAK inhibitor, PF-573228, in the presence or absence of ANG II (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The activation of FAK has been implicated in vascular cell migration, both in cardiovascular disease and in angiogenic vasculature that accompanies metastatic lesions; however, little is known about the mechanism of FAK activation in vascular SMCs (11,18). FAK has over 20 phosphorylation sites; however, Y 397 is considered the primary site and is activated by autophosphorylation (6).…”

Section: Discussionmentioning

confidence: 99%

Both AT₁and AT₂receptors mediate proliferation and migration of porcine vascular smooth muscle cells

Louis

Saward

Zahradka

2011

American Journal of Physiology-Heart and Circulatory Physiology

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Louis S, Saward L, Zahradka P. Both AT1 and AT2 receptors mediate proliferation and migration of porcine vascular smooth muscle cells. Am J Physiol Heart Circ Physiol 301: H746 -H756, 2011. First published May 27, 2011 doi:10.1152/ajpheart.00431.2010.-Angiotensin receptor antagonists have shown clinical promise in modulating vascular disease, in part by limiting smooth muscle cell proliferation and migration. The majority of studies examining the contribution of these receptors have been undertaken in cells derived from rat aorta, which primarily express the ANG II type 1 (AT1) receptor. This investigation studied the relative contribution of AT1 and ANG II type 2 (AT2) receptors to the mitogenic program of porcine smooth muscle cells. Smooth muscle cells were derived from porcine coronary artery explants. The presence of both AT1 and AT2 receptors was demonstrated through ligand binding and RT-PCR analysis. Biochemical and cellular markers of proliferation were monitored in the presence of selective receptor antagonists. Smooth muscle cell migration was measured using both wound healing and Boyden chamber migration assays. Visualization of the AT1 and AT2 receptors in growing and quiescent porcine smooth muscle cells with epifluorescence microscopy demonstrated that their subcellular distribution varied with growth state. An examination with several growth assays revealed that both AT1-specific losartan and AT2-specific PD-123319 receptor antagonists inhibited ANG II-stimulated RNA and DNA synthesis, PCNA expression, and hyperplasia. ANG II induced both directional and nondirectional cell migration. AT1 receptor antagonist treatment significantly decreased ANG II-induced directional migration only, whereas AT2 receptor antagonist treatment significantly reduced both modes of migration. Interestingly, the focal adhesion kinase inhibitor PF-573228 also blocked migration but not proliferation. Furthermore, focal adhesion kinase activation in response to ANG II was prevented only by PD-123319, indicating that this activation is downstream of the AT2 receptor. The observed role of the AT2 receptor in ANG II-induced migration was confirmed with smooth muscle cells depleted of the AT2 receptor with short hairpin RNA treatment.focal adhesion kinase; angiotensin II types 1 and 2 receptors; losartan; PD-123319; PF-573228 EXCESSIVE SMOOTH MUSCLE CELL (SMC) growth has been implicated in the development and progression of cardiovascular diseases such as atherosclerosis and hypertension. A critical mediator of these disease processes is angiotensin II (ANG II), a biologically active peptide with a broad range of physiological effects on the cardiovascular system (8). The actions of ANG II are mediated by at least two different ANG II receptors, ANG II types 1 (AT 1 ) and 2 (AT 2 ) receptors; however, the AT 1 receptor is typically regarded as the primary mediator of the vascular response to ANG II. As a consequence, many studies of SMCs have not included an analysis of the AT 2 receptor and fewer details of its biological f...

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“…Predominantly, periostin has been shown to mediate its effects through integrins (such as avb3) and adhesive signaling. [29][30][31][32] Although Nishiyama's proposal requires intracellular interactions between periostin and BMP-1, the ability of rhPN to increase MMP2 expression, thereby facilitating laminin5c2 cleavage, may represent an alternative mechanism for keratinocyte proliferation based on avb3 ligation and adhesion signaling. 14 As in the previous studies, a full-thickness excisional wound model was used, although it is unclear whether an 8 or 10 mm punch was used since both are stated in the methods (Table 1).…”

Section: Excisional Repair In the Postn 2/2 Mousementioning

confidence: 99%

Functional significance of periostin in excisional skin repair

Elliott

Kim

Hamilton

2012

Cell Adhesion & Migration

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Periostin mediates vascular smooth muscle cell migration through the integrins ανβ3 and ανβ5 and focal adhesion kinase (FAK) pathway

Cited by 138 publications

References 36 publications

NFκB-Induced Periostin Activates Integrin-β3 Signaling to Promote Renal Injury in GN

NFκB-Induced Periostin Activates Integrin-β3 Signaling to Promote Renal Injury in GN

Both AT₁and AT₂receptors mediate proliferation and migration of porcine vascular smooth muscle cells

Functional significance of periostin in excisional skin repair

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Periostin mediates vascular smooth muscle cell migration through the integrins ανβ3 and ανβ5 and focal adhesion kinase (FAK) pathway

Cited by 138 publications

References 36 publications

NFκB-Induced Periostin Activates Integrin-β3 Signaling to Promote Renal Injury in GN

NFκB-Induced Periostin Activates Integrin-β3 Signaling to Promote Renal Injury in GN

Both AT1and AT2receptors mediate proliferation and migration of porcine vascular smooth muscle cells

Functional significance of periostin in excisional skin repair

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Both AT₁and AT₂receptors mediate proliferation and migration of porcine vascular smooth muscle cells