A decrease in the expression of CD63 tetraspanin protein elevates invasive potential of human melanoma cells

Jang, Hwa-In; Lee, Hansoo

doi:10.1038/emm.2003.43

Cited by 48 publications

(49 citation statements)

References 18 publications

(24 reference statements)

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“…3, black bars, CD63, C compared to Vector, C). This greater adherence to the substratum in cells overexpressing CD63 is expected if, in hBRIE 380i cells, CD63 has its reported role in cell adhesion (42,43). Reduction of the CD63 transcript level in cells transfected with antisense CD63 cDNA conversely resulted in a significant decrease in cell adhesion (Fig.…”

Section: Reduced Expression Of Cd63 Increases Pyy-and Npy-induced Celmentioning

confidence: 55%

“…The expression levels of CD63 affect those of I-FABP. Because CD63 is necessary for cell adhesion in melanoma KM3 and MelJuso cell lines (42,43), we tested whether CD63 also mediates adhesion of non-tumorigenic small intestinal hBRIE 380i cells and whether CD63 effects on the expression of differentiation markers such as I-FABP are a consequence of the role of CD63 in cell adhesion.…”

Section: Resultsmentioning

confidence: 99%

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Peptide YY and Neuropeptide Y Induce Villin Expression, Reduce Adhesion, and Enhance Migration in Small Intestinal Cells through the Regulation of CD63, Matrix Metalloproteinase-3, and Cdc42 Activity

Lee

Hadi

Halldén

et al. 2005

Journal of Biological Chemistry

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Peptide YY (PYY) and neuropeptide Y (NPY) are regulatory peptides synthesized in the intestine and brain, respectively, that modify physiological functions affecting nutrient assimilation and feeding behavior. Because PYY and NPY also alter the expression of intestine-specific differentiation marker proteins and the tetraspanin CD63, which is involved in cell adhesion, we investigated whether intestinal cell differentiation could be linked to mucosal cell adhesion and migration through these peptides. PYY and NPY significantly decreased cell adhesion and increased cell migration in a dose-dependent manner prior to cell confluency in our model system, non-tumorigenic small intestinal hBRIE 380i cells. Both peptides reduced CD63 expression and CD63-dependent cell adhesion. CD63 overexpression increased and antisense CD63 cDNA decreased intestinal cell adhesion. In parallel, both PYY and NPY increased expression of matrix metalloproteinase-3 (MMP-3) to a level sufficient to induce cell migration by activating the Rho GTPase Cdc42. The effects of both peptides on cell migration were blocked in cells constitutively overexpressing dominant-negative Cdc42. PYY and NPY also significantly induced the expression of the differentiation marker villin, which could be eliminated by an MMP inhibitor at a concentration that inhibits cell migration. Increased MMP-3 activity, which enhanced cell migration, also induced villin mRNA levels. Therefore, these data indicate that the alteration of adhesion and migration by PYY and NPY occurs in part by synchronous modulation of three proteins that are involved in extracellular matrix-basolateral membrane interactions, CD63, MMP-3 and Cdc42, and that PYY/NPY regulation of expression of mucosal proteins such as villin is linked to the process of cell migration and adhesion.

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Section: Reduced Expression Of Cd63 Increases Pyy-and Npy-induced Celmentioning

confidence: 55%

Section: Resultsmentioning

confidence: 99%

Peptide YY and Neuropeptide Y Induce Villin Expression, Reduce Adhesion, and Enhance Migration in Small Intestinal Cells through the Regulation of CD63, Matrix Metalloproteinase-3, and Cdc42 Activity

Lee

Hadi

Halldén

et al. 2005

Journal of Biological Chemistry

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“…The matrix-degrading activity of MMP-9 was assayed by zymography as described previously (Jang and Lee, 2003). Briefly, aliquots of conditioned medium (1 µ g per lane with volumes adjusted according to protein content) were denatured at room temperature for 10 min in an equal volume of electrophoresis sample buffer and run on 10% gelatin gels.…”

Section: Zym Ogram Assaymentioning

confidence: 99%

Ox-LDL suppresses PMA-induced MMP-9 expression and activity through CD36-mediated activation of PPAR-γ

Lee¹,

Kim²,

Kim³

et al. 2004

Exp Mol Med

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Abbreviations: AP-1, activating factor-1; BCIP, bromochloroindolyl phosphate; 15d-PGJ2, 15-Deoxy-12,14 -Prostaglandin J2; HODE, hydroxyoctadecadienoic acid; LXR, liver X receptor; MMP-9, matrix metalloproteinase-9; NBT, nitro blue tetrazolium; NF-κB, nuclear factor-kappa B; ox-LDL, oxidized low-density lipoprotein; PGF2α , prostaglandin F2α ; PPAR-γ, peroxisome proliferator-activated factor receptor-γ; RXR, retinoid X receptor; STAT, signal transducers and activators of transcription; TZD, thiazolidinedione

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“…It was studied for its role in cellular spreading (16) and in the pathogenesis of melanoma (17,18). Furthermore, CD63 is known as a marker of activation of several cell types including granulocytes and platelets (19 -22).…”

mentioning

confidence: 99%

CD63 as an Activation-Linked T Cell Costimulatory Element

Pfistershammer

Majdic

Stöckl

et al. 2004

The Journal of Immunology

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Dendritic cells (DC) are unique in their capacity to either stimulate or regulate T cells, and receptor/ligand pairs on DC and T cells are critically involved in this process. In this study we present such a molecule, which was discovered by us when analyzing the functional effects of an anti-DC mAb. This mAb, 11C9, reacted strongly with DC, but only minimally with lymphocytes. In MLR it constantly reduced DC-induced T cell activation. Therefore, we assumed that mAb 11C9 primarily exerts its functions by binding to a DC-structure. This does not seem to be the case, however. Preincubation of DC with mAb 11C9 before adding T cells had no inhibitory effect on T cell responses. Retroviral expression cloning identified the 11C9 Ag as CD63. This lysosomal-associated membrane protein (LAMP-3), is only minimally expressed on resting T cells but can, as we show, quickly shift to the surface upon stimulation. Cross-linkage of that structure together with TCR-triggering induces strong T cell activation. CD63 on T cells thus represents an alternative target for mAb 11C9 with its binding to activated T cells rather than DC being responsible for the observed functional effects. This efficient CD63-mediated costimulation of T cells is characterized by pronounced induction of proliferation, strong IL-2 production and compared with CD28 enhanced T cell responsiveness to restimulation. Particularly in this latter quality CD63 clearly surpasses several other CD28-independent costimulatory pathways previously described. CD63 thus represents an activation-induced reinforcing element, whose triggering promotes sustained and efficient T cell activation and expansion.

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A decrease in the expression of CD63 tetraspanin protein elevates invasive potential of human melanoma cells

Cited by 48 publications

References 18 publications

Peptide YY and Neuropeptide Y Induce Villin Expression, Reduce Adhesion, and Enhance Migration in Small Intestinal Cells through the Regulation of CD63, Matrix Metalloproteinase-3, and Cdc42 Activity

Peptide YY and Neuropeptide Y Induce Villin Expression, Reduce Adhesion, and Enhance Migration in Small Intestinal Cells through the Regulation of CD63, Matrix Metalloproteinase-3, and Cdc42 Activity

Ox-LDL suppresses PMA-induced MMP-9 expression and activity through CD36-mediated activation of PPAR-γ

CD63 as an Activation-Linked T Cell Costimulatory Element

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