Nectin-like Molecule-5/Tage4 Enhances Cell Migration in an Integrin-dependent, Nectin-3-independent Manner

Ikeda, Wataru; Kakunaga, Shigeki; Takekuni, Kyoji; Shingai, Tatsushi; Satoh, Keiko; Morimoto, Koji; Takeuchi, Masami; Imai, Toshio; Takai, Yoshimi

doi:10.1074/jbc.m312969200

Cited by 99 publications

(126 citation statements)

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“…32 Mouse Necl-5 probably works as a homo-cis-dimer, 14 and when completely lacking its cytoplasmic region (Necl-5-DCP), demonstrates dominant negative effects on the wild-type Necl-5-mediated enhancement of cell migration and cell growth. 15,16 A conserved ITIM region (aa 396-401) is also present in the cytoplasmic region of Necl-5, 9 and we therefore constructed a corresponding mutant of human CD155 (CD155DCP) and established cells that stably express this truncated receptor. The expression of CD155DCP results in decreased levels of the serum responsiveness in ras3T3 cells when compared with wild-type CD155.…”

Section: Discussionmentioning

confidence: 99%

“…15 Integrins are transmembrane proteins whose cytoplasmic domains interact with proteins such as talin, FAK, a-actinin, vinculin and paxillin. 19 Among these interacting factors, activated/phosphorylated FAK plays an especially important role in integrin-mediated signal transduction pathways.…”

Section: Discussionmentioning

confidence: 99%

“…A Necl-5 species lacking intracytoplasmic region (Necl-5-DCP) has been shown to serve as a dominant negative mutant and inhibit cell motility and proliferation. 15,16 We thus predicted that CD155DCP, expressed in cells which express endogenous CD155, might also function as a dominant negative mutant of CD155. As expected, the serum responsiveness of DLD-1/CD155DCP cells was markedly decreased when compared with DLD-1/Mock cells (Fig.…”

Section: Rt-pcr Of Endogenous Necl-5 and Exogenous Cd155 In Ras3t3 Cellsmentioning

confidence: 99%

“…2,13 Necl-5 shows an approximately 60% identity in its cDNA nucleotide sequence and 41% identity in its amino acid sequence with CD155, 4,13 heterophilically trans-interacts with nectin-3, a molecule which is involved in the formation of adherens junction, and also enhances serum-or platelet-derived growth factor (PDGF)-induced cell migration in an integrin-dependent manner. 14,15 Recently, it has been reported that mouse Necl-5 enhances cell proliferation by serum-or PDGF-stimulation through the Ras-Raf-MEK-ERK signaling pathway. 16 Its structural and functional similarities with human CD155 prompted us to investigate whether CD155 had similar effects on cell proliferation.…”

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confidence: 99%

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The CD155/poliovirus receptor enhances the proliferation of ras‐mutated cells

Kono

Imai

Yasuda

et al. 2007

Intl Journal of Cancer

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Stimulation of the CD155/poliovirus receptor, which localizes in the cell-matrix and at cell-cell junctions, inhibits cell adhesion and enhances cell migration. Necl-5, a mouse homolog of CD155, is implicated in the formation of adherence junctions. Recently, Necl-5 has also been found to enhance cell proliferation via the stimulation of serum and platelet-derived growth factor through the Ras-Raf-MEK-ERK signaling pathway. In our present study, we find that CD155 significantly enhances the serum-induced cell proliferation of NIH3T3 cells which have been transformed by an oncogenic Ras (V12Ras-NIH3T3), but not the parental cells. CD155 expression in V12Ras-NIH3T3 cells is also found to upregulate cyclin D2, downregulate p27 Kip1 and shorten the G 0 /G 1 phase of the cell cycle. An inhibitor of focal adhesion kinase does not reduce this CD155-mediated enhancement of V12Ras-NIH3T3 cell proliferation. The expression of CD155DCP, which lacks the cytoplasmic region including the immunoreceptor tyrosine-based inhibitory motif (ITIM), has a reduced ability to enhance the serum responsiveness of V12Ras-NIH3T3 cells, suggesting that the ITIM might be required for this effect of CD155. In addition, the overexpression of exogenous CD155 enhances the serum responsiveness of HT1080 cells, which harbor a mutant N-ras gene. On the other hand, siRNA-induced knockdown of endogenous CD155 and/or CD155DCP expression significantly repress the serum responsiveness of DLD-1 cells, which express endogenous CD155 and harbor a mutant K-ras gene, suggesting that this mutant may function in a dominant negative manner. Taken together, our present data suggest that CD155, at least in part, enhances the proliferation of ras-mutated cells. ' 2007 Wiley-Liss, Inc.Key words: CD155; Necl-5; ras; proliferation CD155 is an immunoglobulin-like molecule containing a domain structure that comprises 1 extracellular region with 3 immunoglobulin-like loops, 1 single transmembrane region and 1 short cytoplasmic region. 1 CD155 is ubiquitously expressed in many human tissues, including the brain, kidney, ileum, liver, lung, placenta and leukocytes, 1,2 and was originally identified as the receptor for the human poliovirus, which causes the characteristic flaccid paralysis of poliomyelitis. 1-3 CD155 has 4 spliced variants, 2 a and d membrane-bound forms, which serve as the poliovirus receptor, and the b and g forms which are secreted versions of this protein. 2 The transmembrane isoform CD155a, however, is the principle variant, and comprises 65-70% of the gene transcripts. 4 In our present study, the term ''CD155'' denotes the a variant unless otherwise stated.CD155 has been reported to be involved in cell-cell adhesion via a heterophilic trans-interaction with nectin-3 and stimulation of this receptor has been shown to inhibit cell adhesion and enhance cell migration. 5,6 CD155 is also overexpressed in many human cancer cells, 4,6,7 but the significance of this has remained elusive.Mouse nectin-like molecule-5 (Necl-5)/tumor-associated glycoprotein E4 i...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Rt-pcr Of Endogenous Necl-5 and Exogenous Cd155 In Ras3t3 Cellsmentioning

confidence: 99%

mentioning

confidence: 99%

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The CD155/poliovirus receptor enhances the proliferation of ras‐mutated cells

Kono

Imai

Yasuda

et al. 2007

Intl Journal of Cancer

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“…Integral transmembrane proteins of Ig superfamily are implicated in cell adhesion and migration. For example, JAM-C was described to promote neutrophil trans-endothelial migration [11], whereas nectin-like molecule-5 has been shown to enhance cell movement in NIH3T3 cells [12].…”

Section: Introductionmentioning

confidence: 99%

Coxsackie and adenovirus receptor (CAR) is a product of Sertoli and germ cells in rat testes which is localized at the Sertoli–Sertoli and Sertoli–germ cell interface

Wang

Mruk

Lee

et al. 2007

Experimental Cell Research

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The coxsackie and adenovirus receptor (CAR), a putative cell-cell adhesion molecule, has attracted wide interest due to its importance in viral pathogenesis and in mediating adenoviral gene delivery. However, the distribution pattern and physiological function of CAR in the testis is still not clear. Here, we identified CAR in Sertoli cells and germ cells of rats. In vivo studies have shown that CAR resides at the blood-testis barrier as well as at the ectoplasmic specialization. The persistent expression of CAR in rat testes from neonatal period throughout adulthood implicates its role in spermatogenesis. Using primary Sertoli cell cultures, we observed a significant induction of CAR during the formation of Sertoli cell epithelium. Furthermore, CAR was seen to be concentrated at inter-Sertoli cell junctions, colocalizing with tight junction protein marker ZO-1 and adherens junction protein N-cadherin. CAR was also found to be associated with proteins of Src kinase family and its protein level declined after TNFα treatment in Sertoli cell cultures. Immunofluorescent staining of isolated germ cells has revealed the presence of CAR on spermatogonia, spermatocytes, round spermatids and elongate spermatids. Taken together, we propose that CAR functions as an adhesion molecule in maintaining the inter-Sertoli cell junctions at the basal compartment of the seminiferous epithelium. In addition, CAR may confer adhesion between Sertoli and germ cells at the Sertoli-germ cell interface. It is possible that the receptor utilized by viral pathogens to breakthrough the epithelial barrier was also employed by developing germ cells to migrate through the inter-Sertoli cell junctions.

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The importance of reporting disease activity states in rheumatoid arthritis clinical trials

Aletaha

Funovits

Smolen

2008

Arthritis & Rheumatism

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Objective. To compare the value of reporting treatment effects in rheumatoid arthritis (RA) as relative change from baseline (e.g., American College of Rheumatology [ACR] responder status) with the value of evaluating absolute disease activity states (e.g., remission).Methods. We pooled data from several recent RA clinical trials and evaluated patients who had completed a 1-year treatment period (n ‫؍‬ 629). We compared levels of functional impairment and radiographic progression among patients meeting the ACR 50% or 70% improvement criteria (ACR50 and ACR70 responders, respectively) who attained remission of disease, low disease activity, or moderate disease activity after 1 year, as assessed by the Simplified Disease Activity Index and the Disease Activity Score in 28 joints.Results. Within the ACR50 and ACR70 responder groups, functional disability and radiographic progression were lowest in patients who had attained disease remission at 1 year, compared with those who had attained low or moderate disease activity. When patients attained the same disease activity category, physical function and radiographic progression did not differ significantly with different response states.

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Nectin-like Molecule-5/Tage4 Enhances Cell Migration in an Integrin-dependent, Nectin-3-independent Manner

Cited by 99 publications

References 73 publications

The CD155/poliovirus receptor enhances the proliferation of ras‐mutated cells

The CD155/poliovirus receptor enhances the proliferation of ras‐mutated cells

Coxsackie and adenovirus receptor (CAR) is a product of Sertoli and germ cells in rat testes which is localized at the Sertoli–Sertoli and Sertoli–germ cell interface

The importance of reporting disease activity states in rheumatoid arthritis clinical trials

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