Inhibition of Cell Adhesion to Lens Capsule by LCM 1910, an RGD-Derived Peptide

Palmade, F.; Sechoy-Chambon, O.; Vains, J.B. Regnouf De; Coquelet, C.; Bonne, C.

doi:10.1089/jop.1994.10.623

Cited by 11 publications

(5 citation statements)

References 19 publications

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“…Integrin antagonists show clinical promise for the treatment of TGF‐β‐induced EMT‐associated disorders such as inflammation, fibrosis and cancer [106]. Most of the therapeutic approaches currently under investigation target integrin function using anti‐integrin agents including both naturally occurring and engineered peptides that can mimic their RGD ligand, or antibodies that can act as integrin antagonists [107–109]. For example, clinical administration of a peptide antagonist of the αVβ3 receptor successfully inhibits pathological angiogenesis seen in cancer, proliferative retinopathy, rheumatoid arthritis and psoriasis [110, 111].…”

Section: Disease Perspectivesmentioning

confidence: 99%

aV integrins and TGF‐β‐induced EMT: a circle of regulation

Mamuya

Duncan

2012

J Cellular Molecular Medi

131

117

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Transforming growth factor-β (TGF-β) has roles in embryonic development, the prevention of inappropriate inflammation and tumour suppression. However, TGF-β signalling also regulates pathological epithelial-to-mesenchymal transition (EMT), inducing or progressing a number of diseases ranging from inflammatory disorders, to fibrosis and cancer. However, TGF-β signalling does not proceed linearly but rather induces a complex network of cascades that mutually influence each other and cross-talk with other pathways to successfully induce EMT. Particularly, there is substantial evidence for cross-talk between αV integrins and TGF-β during EMT, and anti-integrin therapeutics are under development as treatments for TGF-β-related disorders. However, TGF-β’s complex signalling network makes the development of therapeutics to block TGF-β-mediated pathology challenging. Moreover, despite our current understanding of integrins and TGF-β function during EMT, the precise mechanism of their role during physiological versus pathological EMT is not fully understood. This review focuses on the circle of regulation between αV integrin and TGF-β signalling during TGF-β induced EMT, which pose as a significant driver to many known TGF-β-mediated disorders.

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Section: Disease Perspectivesmentioning

confidence: 99%

aV integrins and TGF‐β‐induced EMT: a circle of regulation

Mamuya

Duncan

2012

J Cellular Molecular Medi

131

117

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“…The expression of β1-integrin is upregulated during epithelial-mesenchymal transitions occurring as a consequence of lens epithelial cell suspension in collagen I gels (Zuk and Hay, 1994) and in response to TGFβ treatment. In fact, it has been proposed that interference with β1-integrin function may be clinically useful to block epithelial-mesenchymal transition of lens cells leading to posterior capsular opacification, a common side effect of modern cataract surgery (Kim et al, 2002;Mathew et al, 2003;Palmade et al, 1994). However, the function of β1-integrin in the lens in vivo is not well understood.…”

Section: Introductionmentioning

confidence: 99%

Conditional deletion of β1-integrin from the developing lens leads to loss of the lens epithelial phenotype

Симирский

Wang

Duncan

2007

Developmental Biology

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Beta1-integrins are cell surface receptors that participate in sensing the cell's external environment. We used the Cre-lox system to delete beta1-integrin in all lens cells as the lens vesicle transitions into the lens. Adult mice lacking beta1-integrin in the lens are microphthalmic due to apoptosis of the lens epithelium and neonatal disintegration of the lens fibers. The first morphological alterations in beta1-integrin null lenses are seen at 16.5 dpc when the epithelium becomes disorganized and begins to upregulate the fiber cell markers beta- and gamma-crystallins, the transcription factors cMaf and Prox1 and downregulate Pax6 levels demonstrating that beta1-integrin is essential to maintain the lens epithelial phenotype. Furthermore, beta1-integrin null lens epithelial cells upregulate the expression of alpha-smooth muscle actin and nuclear Smad4 and downregulate Smad6 suggesting that beta1-integrin may brake TGFbeta family signaling leading to epithelial-mesenchymal transitions in the lens. In contrast, beta1-integrin null lens epithelial cells show increased E-cadherin immunoreactivity which supports the proposed role of beta1-integrins in mediating complete EMT in response to TGFbeta family members. Thus, beta1-integrin is required to maintain the lens epithelial phenotype and block inappropriate activation of some aspects of the lens fiber cell differentiation program.

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“…Palmade et al [24] reported that Ac-Arg-Gly-Asp-NH-CH2-Bzl (LCM 1910) which is an RGD-derived peptide signifi cantly decreased cell attachment on the lens capsule at a concentrationdependent effect, and cell proliferation was decreased on a plastic dish in the presence of LCM 1910 in bovine LEC culture. Sasabe et al [25] reported that 0.5 mg/ml of RGDS and GRGDS RGD peptide showed inhibitory effects on cell attachment in rabbit LEC culture, but 0.5, 1.0 and 2.0 mg/ml of the RGD sequence alone had no effect.…”

Section: Discussionmentioning

confidence: 99%

Inhibitory Effects of Arg-Gly-Asp (RGD) Peptide on Cell Attachment and Migration in a Human Lens Epithelial Cell Line

Oharazawa¹,

Ibaraki²,

Ohara³

et al. 2005

Ophthalmic Res

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Posterior capsule opacification (PCO) after cataract surgery is caused by growth of residual human lens epithelial (HLE) cells on the posterior capsule. We have shown that extracellular matrix (ECM) is an essential factor for HLE cell attachment and migration. The purpose of this study was to examine the inhibitory effects of Arg-Gly-Asp (RGD) peptide on cell attachment and migration in an HLE cell line. HLE cell line cells (SRA 01/04) that were obtained by transfection of large T antigen of SV40 were cultured in the absence of serum. The culture dishes were coated with type IV collagen, laminin or fibronectin, and Gly-Arg-Gly-Asp-Ser-Pro (GRGDSP) RGD peptide (0.1, 0.3, 1.0, 2.0 mg/ml) was added to the medium. The number of attached cells was counted after 90 min of incubation, and the inhibitory effects of GRGDSP RGD peptide on cell attachment were calculated. Cell attachment on the fibronectin-coated dishes was inhibited by GRGDSP RGD peptide at concentrations higher than 0.3 mg/ml; the inhibitory rate was 80% at a concentration of 2.0 mg/ml. The inhibition of cell attachment by GRGDSP RGD peptide on laminin-coated dishes appeared only at a concentration of 2.0 mg/ml, whereas no effects were observed on the type IV collagen-coated dishes. The inhibitory effects of GRGDSP RGD peptide on cell migration were measured in medium containing 2.0 mg/ml of GRGDSP RGD peptide after 1, 3, 5 and 7 days of culture. Cell migration was inhibited by GRGDSP RGD peptide from 1 day of culture on the fibronectin-coated dishes and from 5 days of culture on the laminin-coated dishes, whereas no effects were observed on the type IV collagen-coated dishes. GRGDSP RGD peptide inhibited cell attachment and migration on laminin and fibronectin that have RGD sequences. These data suggested that RGD peptide may have the potential to prevent PCO.

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Inhibition of Cell Adhesion to Lens Capsule by LCM 1910, an RGD-Derived Peptide

Cited by 11 publications

References 19 publications

aV integrins and TGF‐β‐induced EMT: a circle of regulation

aV integrins and TGF‐β‐induced EMT: a circle of regulation

Conditional deletion of β1-integrin from the developing lens leads to loss of the lens epithelial phenotype

Inhibitory Effects of Arg-Gly-Asp (RGD) Peptide on Cell Attachment and Migration in a Human Lens Epithelial Cell Line

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