Role of Afadin in Vascular Endothelial Growth Factor– and Sphingosine 1-Phosphate–Induced Angiogenesis

Tawa, Hideto; Rikitake, Yoshiyuki; Takahashi, Motonori; Amano, Hideharu; Miyata, Muneaki; Satomi‐Kobayashi, Seimi; Kinugasa, Mitsuo; Nagamatsu, Yasunori; Mizutani, Takashi; Ogita, Hisakazu; Miyoshi, Jun; Hirata, Ken‐ichi; Takai, Yoshimi

doi:10.1161/circresaha.110.216747

Cited by 77 publications

(84 citation statements)

References 39 publications

(37 reference statements)

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“…Thus, it was believed that cell-cell adhesion is initiated depending on the random interaction of the extracellular regions of cell adhesion molecules. However, we have shown here that the transinteraction of nectins is enhanced by the interaction of nectin with afadin, and we showed previously that afadin localizes at the leading edge of a moving cell (4,5). Taken together, these results indicate that when the leading edge of a moving cell makes a contact with another cell, the nectin-based cell-cell adhesion is initiated at the contact site.…”

Section: Discussionsupporting

confidence: 79%

“…However, it is conceivable that the trans-interaction of nectin-3 with nectin-1 or Necl-5 may induce a conformational change in the intracellular region of nectin-3 to facilitate the binding to afadin and that the interaction of afadin with nectin-3 may induce a conformational change in the extracellular region of nectin-3 to promote the trans-interaction. In a moving single cell, afadin localizes at the leading edge by binding to Rap1, which is activated there by the actions of PDGF and VEGF (4,5). Afadin does not likely interact with nectins because nectins are present diffusely on the plasma membrane.…”

Section: Discussionmentioning

confidence: 99%

“…In addition to the role of afadin in cell-cell adhesion, afadin is involved in directional cell movement (4,5). It was shown previously that the PDGF receptor and integrin ␣ v ␤ 3 cooperatively induce movement of NIH3T3 cells (6).…”

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confidence: 99%

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Cooperative Role of Nectin-Nectin and Nectin-Afadin Interactions in Formation of Nectin-based Cell-Cell Adhesion

Kurita

Ogita²,

Takai

2011

Journal of Biological Chemistry

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The nectin cell adhesion molecules interact in trans with each other through their extracellular regions and with afadin through their cytoplasmic tails, forming adherens junctions in cooperation with cadherins. In a single cell, Necl-5 (nectin-like molecule-5) localizes at the leading edge and regulates directional cell movement in response to a chemoattractant. In such a single cell, afadin also localizes at the leading edge without interacting with nectins or Necl-5. It remains unknown how the nectin-nectin and nectin-afadin interactions are initiated when moving cells contact each other to initiate the formation of adherens junctions. We show here that the Necl-5-nectin interaction induced by cell-cell contact enhances the nectin-afadin interaction. This interaction then enhances the nectin-nectin interaction, which further enhances the nectin-afadin interaction in a positive feedback manner. Thus, the Necl-5-nectin, nectin-nectin, and nectin-afadin interactions cooperatively increase the clustering of the nectin-afadin complex at the cellcell contact sites, promoting the formation of the nectin-based cell-cell adhesion.

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Section: Discussionsupporting

confidence: 79%

Section: Discussionmentioning

confidence: 99%

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Cooperative Role of Nectin-Nectin and Nectin-Afadin Interactions in Formation of Nectin-based Cell-Cell Adhesion

Kurita

Ogita²,

Takai

2011

Journal of Biological Chemistry

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“…For example, it has been reported that EC proliferation, EC permeability, and/or cell migration require Rap1A only, 29,41 Rap1B, 36 or both Rap1A and 1B. 39,42 The results have varied depending on cell type (epithelial vs. endothelial), subtype (microvascular endothelial vs. HUVEC) or method of knockdown (genetic knockout vs. various siRNA methods).…”

Section: Isoform-specific Differences Between Rap1amentioning

confidence: 99%

Isoform-specific differences between Rap1A and Rap1B GTPases in the formation of endothelial cell junctions

Wittchen¹,

Aghajanian²,

Burridge³

2011

Small GTPases

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“…S1P plays important roles in diverse physiological and pathological processes in cancer cells. It regulates cell growth, proliferation, differentiation, cell survival, migration, and angiogenesis [8,10,[19][20][21][22][23] . S1P exerts most of its function as a specific ligand for a family of G-protein-coupled receptors (GPCRs), termed S1P1-S1P5 [24][25][26][27] .…”

Section: Dual Messenger Signalings Of S1pmentioning

confidence: 99%

Roles of sphingosine 1-phosphate on tumorigenesis

Huang

Lee³

2011

WJBC

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Sphingosine 1-phosphate (S1P) is a bioactive sphingolipid with a variety of biological activities. It is generated from the conversion of ceramide to sphingosine by ceramidase and the subsequent conversion of sphingosine to S1P, which is catalyzed by sphingosine kinases. Through increasing its intracellular levels by sphingolipid metabolism and binding to its cell surface receptors, S1P regulates several physiological and pathological processes, including cell proliferation, migration, angiogenesis and autophagy. These processes are responsible for tumor growth, metastasis and invasion and promote tumor survival. Since ceramide and S1P have distinct functions in regulating in cell fate decision, the balance between the ceramide/sphingosine/S1P rheostat becomes a potent therapeutic target for cancer cells. Herein, we summarize our current understanding of S1P signaling on tumorigenesis and its potential as a target for cancer therapy.

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Role of Afadin in Vascular Endothelial Growth Factor– and Sphingosine 1-Phosphate–Induced Angiogenesis

Cited by 77 publications

References 39 publications

Cooperative Role of Nectin-Nectin and Nectin-Afadin Interactions in Formation of Nectin-based Cell-Cell Adhesion

Cooperative Role of Nectin-Nectin and Nectin-Afadin Interactions in Formation of Nectin-based Cell-Cell Adhesion

Isoform-specific differences between Rap1A and Rap1B GTPases in the formation of endothelial cell junctions

Roles of sphingosine 1-phosphate on tumorigenesis

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