Interplay between αvβ3 Integrin and Nucleolin Regulates Human Endothelial and Glioma Cell Migration

Κουτσιούμπα, Μαρίνα; Polytarchou, Christos; Courty, José; Zhang, Yue; Kieffer, Nelly; Mikelis, Constantinos M.; Skandalis, Spyros S.; Hellman, Ulf; Iliopoulos, Dimitrios; Papadimitriou, Evangelia

doi:10.1074/jbc.m112.387076

Cited by 58 publications

(72 citation statements)

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“…It has also been shown that cell surface nucleolin is implicated in the migration of endothelial and glioma cells (Koutsioumpa et al, 2013). Our results clearly indicate that the knockdown of nucleolin markedly attenuates the spreading and migration of A375 cells on fibronectin, suggesting a key role of lipid raft-dependent β1 integrin-nucleolin interaction in cell migration on fibronectin.…”

Section: Discussionsupporting

confidence: 65%

“…For example, Kang et al (2009) reported that although only partially colocalized, αvβ3 integrin and nucleolin protein are highly coexpressed in HeLa cells. Interestingly, Koutsioumpa et al (2013) recently indicated that the interplay between αvβ3 integrin and nucleolin regulates human endothelial and glioma cell migration. Reyes-Reyes and Akiyama (2008) have also shown the important role of surface nucleolin in p-selectin-mediated α5β1 integrin activation and colo-320 cell adhesion on fibronectin.…”

Section: Discussionmentioning

confidence: 99%

“…These data suggest that β1 integrin and nucleolin constitutively interact in the cells, and their association depends on intact lipid rafts. Nucleolin, a eukaryotic nucleolar protein, is located mainly in the nucleolus, but an increasing number of studies have confirmed that the localization of nucleolin in the membrane is important for various cell processes (Koutsioumpa et al, 2013;Reyes-Reyes and Akiyama, 2008;Said et al, 2002). This prompted us to investigate whether nucleolin is present on the A375 cell surface by flow cytometric analysis.…”

Section: Lipid Rafts Are Necessary For Interaction Between β1 Integrimentioning

confidence: 99%

“…However, by liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS), we demonstrated the effect of lipid raft disruption on the β1 integrin complex and identified potential β1-integrin-interacting proteins that are closely-related to lipid rafts. Among these proteins, nucleolin is proposed to be present in lipid rafts Said et al, 2002) and is implicated in adhesion and migration of cancer cells (Koutsioumpa et al, 2013;ReyesReyes and Akiyama, 2008). After further confirming the lipidraft-dependent interaction between nucleolin and β1 integrin, we explored the biological role of nucleolin in β1-integrinmediated A375 cell spreading and migration on fibronectin.…”

Section: Introductionmentioning

confidence: 99%

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Identification of Nucleolin as a Lipid-Raft-Dependent β1-Integrin-Interacting Protein in A375 Cell Migration

Wang

Zhang

et al. 2013

Molecules and Cells

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Lipid rafts are related to cell surface receptor function. Integrin is a major surface receptor protein in cell adhesion and migration on the extracellular matrix (ECM). Here, we showed that lipid rafts played a critical role in human melanoma A375 cell spreading and migration on fibronectin; an important component of the ECM that interacts with β1 integrin. We found that the disruption of lipid rafts did not markedly inhibit the expression and activation of β1 integrin. By coimmunoprecipitation and mass spectrometry, we investigated the influence of lipid rafts on the β1 integrin complex and identified nucleolin as a potential lipid-raft-dependent β1-integrin-interacting protein. Upon confirmation of the interaction between β1 integrin and nucleolin, further studies revealed that nucleolin colocalized with β1 integrin in lipid rafts and raft disruption interrupted their association. In addition, knockdown of nucleolin markedly attenuated A375 cell spreading and migration on fibronectin. Taken together, we demonstrated that nucleolin is a critical lipid-raft-dependent β1-integrin-interacting protein in A375 cell spreading and migration on fibronectin.

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Section: Discussionsupporting

confidence: 65%

Section: Discussionmentioning

confidence: 99%

Section: Lipid Rafts Are Necessary For Interaction Between β1 Integrimentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Identification of Nucleolin as a Lipid-Raft-Dependent β1-Integrin-Interacting Protein in A375 Cell Migration

Wang

Zhang

et al. 2013

Molecules and Cells

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“…Furthermore, NCL enhances translation of many mRNA encoding for oncogenic proteins [42]. Cell surface NCL has been reported to act as a receptor for several growth factor such as midkine [43] and pleiotrophin [43][44][45] involved in angiogenesis and tumor growth, hepatocyte growth factor (HGF) involved in the mechanisms of metastasis and cell adhesion [46] and P-selectin that induces signaling pathways of cell adhesion and invasion [47]. In addition, the implication of cell surface NCL in proliferative diseases may be related to the fact that it exists in a protein complex of 500-kDa, including several proteins involved in cancer progression.…”

Section: Ncl: a Promising Target For Cancer Therapymentioning

confidence: 99%

Nanoparticles Functionalized with Ligands of Cell Surface Nucleolin for Cancer Therapy and Diagnosis

Destouches¹

2015

J Nanomed Nanotechnol

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Conventional cancer chemotherapies are often limited by their non-targeted nature and their inadequate delivery to the tumor affecting the normal tissues and leading to toxic adverse effects. In order to improve the anticancer efficacy and safety of these drugs, as well as the diagnosis capacity of imaging agents, nanoparticles drug delivery system has been developed combining ligands enabling tumor targeting at a cellular level and drug carrier capacity. Nucleolin (NCL) is a multifunctional protein that could shuttle from nucleolus to nucleoplasm, cytoplasm and cell surface. This ribonucleo protein over expressed at the cell surface of cancer cells is involved in many cancer processes supporting tumorigenesis such as cell proliferation and apoptosis. Additionally, NCL expression is enhanced in angiogenic vessels, enabling multi-targeting strategies toward the tumor microenvironment. In this context, several compounds targeting NCL, such as the aptamer AS1411, the peptide F3 and the multivalent pseudopeptide N6L, have been developed and investigated for cancer therapy. Due to their cancer cell targeting capacities, these compounds have been evaluated to mediate highly specific and effective nanoparticles for drug delivery to the tumor. In this report, we present a review of literature focusing on drug-loaded nanoparticles conjugated with these nucleolin ligands, strikingly emphasizing the success of such a strategy.

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Pleiotrophin interacts with glycosaminoglycans in a highly flexible and adaptable manner

2021

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Pleiotrophin (PTN) is a potent mitogenic cytokine whose activities are controlled by its interactions with glycosaminoglycan (GAG). We examined the specificity of PTN for several types of GAG oligosaccharides. Our data indicate that the interaction of PTN with GAGs is dependent on the sulfation density of GAGs. Surprisingly, an acidic peptide also had similar interactions with PTN as GAGs. This shows that the interaction of PTN with anionic polymers is flexible and adaptable and that the charge density is the main determinant of the interaction. In addition, we show that PTN can compensate for the loss of its termini in interactions with heparin oligosaccharides, allowing it to maintain its affinity for GAGs in the absence of the termini. Taken together, these data provide valuable insight into the interactions of PTN with its proteoglycan receptors.

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Interplay between αvβ3 Integrin and Nucleolin Regulates Human Endothelial and Glioma Cell Migration

Cited by 58 publications

References 60 publications

Identification of Nucleolin as a Lipid-Raft-Dependent β1-Integrin-Interacting Protein in A375 Cell Migration

Identification of Nucleolin as a Lipid-Raft-Dependent β1-Integrin-Interacting Protein in A375 Cell Migration

Nanoparticles Functionalized with Ligands of Cell Surface Nucleolin for Cancer Therapy and Diagnosis

Pleiotrophin interacts with glycosaminoglycans in a highly flexible and adaptable manner

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