Localization of the Transmembrane 4 Superfamily (TM4SF) Member PETA-3 (CD151) in Normal Human Tissues: Comparison with CD9, CD63, and α5β1 Integrin

Sincock, Paul M.; Mayrhofer, Graham; Ashman, Leonie K.

doi:10.1177/002215549704500404

Cited by 185 publications

(176 citation statements)

References 31 publications

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“…Although initially identified as a platelet/leukocyte surface glycoprotein, CD151 is expressed in a wide variety of tissues and cell types including megakaryoctes, endothelial cells, and myocytes (Fitter et al 1995(Fitter et al , 1998Hasegawa et al 1997). We present here the first observations on the regional distribution of CD151 transcripts in rat brain, which is in marked contrast to that reported in earlier studies which showed very low level of expression in mouse and human brain (Sincock et al 1997;Hasegawa et al 1997). The presence of CD151 mRNA in rat brain is unlikely due only to expression in the vascular endothelial compartment because the transcripts are also present at high levels in cultured cortical neurons.…”

Section: Discussioncontrasting

confidence: 89%

“…We present here the first observations on the regional distribution of CD151 transcripts in rat brain, which is in marked contrast to that reported in earlier studies which showed very low level of expression in mouse and human brain (Sincock et al 1997;Hasegawa et al 1997). The presence of CD151 mRNA in rat brain is unlikely due only to expression in the vascular endothelial compartment because the transcripts are also present at high levels in cultured cortical neurons.…”

Section: Discussioncontrasting

confidence: 89%

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Tetraspan Protein CD151 A Common Target of Mood Stabilizing Drugs?

Hua

Green

Wong

et al. 2001

Neuropsychopharmacology

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The latency in onset of antimanic and mood stabilizing effects of lithium suggest that long-term neuronal adaptations mediated by changes in gene expression may be important to the therapeutic action of lithium treatment. Using differential display-polymerase chain reaction, several novel, hitherto unexpected lithium-regulated genes have been isolated, all of which would not have beenAlthough lithium is widely used in the treatment of acute mania and the prophylaxis for bipolar affective disorder, the cellular and molecular mechanisms underlying its therapeutic action remain unclear. However, significant progress has been made over the past decade with cumulative evidence indicating that modulation of postreceptor signaling mechanisms in critical regions of the brain may be essential to the mood stabilizing properties of this agent (reviewed in Jope 1999;Li et al. 2000;Manji and Lenox 1999).Many signal transduction cascades are known to induce long-term cellular responses through regulation of gene transcription. Moreover, the delayed onset of therapeutic action of lithium has led to the hypothesis that regulation of gene expression may be important for its mood stabilizing effects (Jope 1999;Li et al. 2000). In line with this hypothesis, several studies have demonstrated that chronic lithium treatment alters the expression of an array of genes, including G protein ␣ -subunits, adenylyl cyclase subtypes, neuropeptides (reviewed in Jope 1999;Li et al. 2000;Manji and Lenox 1999) NO . 5 et al. 2000). The modulatory effects of lithium on gene expression have been suggested to be mediated, at least in part, through the cAMP response element binding protein (CREB) or activator protein-1 (AP-1) transcriptional factor pathway (Ozaki and Chuang 1997;Asghari et al. 1998;Yuan et al. 1998). It is thus conceivable that other genes containing the consensus sequences for these transcription factors in their promoter region may also be the potential targets of lithium. Therefore, the identification of other lithium-regulated genes is important in better understanding the spectrum of cellular and molecular mechanisms that contribute to the therapeutic and/or side effects of this drug.Using differential display-polymerase chain reaction (ddPCR), several novel lithium-regulated genes have been identified that would not otherwise have been considered using a candidate gene approach. These novel lithium-regulated targets included 2 Ј , 3 Ј -cyclic nucleotide 3 Ј -phosphodiesterase type II (Wang and Young 1996), polyomavirus enhancer-binding protein 2 ␤ (Chen et al. 1999), nitrogen permease regulator 2 (Wang et al. 1999), aldolase A (Hua et al. 2000, and diphosphoinositol polyphosphate phosphohydrolase II (Hua et al. 2001). Unexpectedly, during the course of experiments amplifying the 5 Ј end of a putative lithium-regulated ddPCR fragment, we isolated another cDNA clone, a homolog of human/mouse transmembrane-4-superfamily (TM4SF) protein, CD151. The transcript levels of CD151 were significantly decreased in the rat frontal corte...

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Section: Discussioncontrasting

confidence: 89%

Section: Discussioncontrasting

confidence: 89%

Tetraspan Protein CD151 A Common Target of Mood Stabilizing Drugs?

Hua

Green

Wong

et al. 2001

Neuropsychopharmacology

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“…We observed the decrease in the expression of CD151, which is well known to be an important molecule for invasion and metastasis of tumors (25). It is also reported that CD151 associates with the integrin family and modulates cell adhesion (33,34). Our data indicate the effectiveness of PPARg antagonists in the prevention of squamous cell carcinoma invasion via the down-regulation of cell surface adhesion molecules.…”

Section: Discussionsupporting

confidence: 66%

Critical Role of Peroxisome Proliferator-Activated Receptor γ on Anoikis and Invasion of Squamous Cell Carcinoma

Masuda

Wada

Nakajima

et al. 2005

Clinical Cancer Research

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Purpose: Peroxisome proliferator-activated receptor g (PPARg) plays a important role in various physiological functions.We examined whether PPARg is expressed in primary squamous cell carcinoma and lymph node metastasis and whether PPARg is a potential target for tumor therapy. Experimental Design and Results: A high-level expression of PPARg was observed in tumor cells of human primary squamous cell carcinoma, lymph node metastasis, and squamous cell carcinoma cell lines. Treatment with PPARg-specific antagonists, but not agonists, caused apoptotic cell death on squamous cell carcinoma cell lines in a concentration-dependent manner. Small interfering RNA for PPARg also inhibited cell adhesion and growth of squamous cell carcinomas. The phosphorylation of focal adhesion kinase (FAK) was decreased by treatment with PPARg antagonists, and resulted in decreases in phosphorylation of Erk and mitogen-activated protein kinase. Furthermore, PPARg antagonists decreased the adhesion of squamous cell carcinomas into fibronectin-coated plates, indicating the inhibition of interaction between squamous cell carcinomas and fibronectin. Expression of integrin a5, a counter adhesion molecule for fibronectin, was inhibited by the treatment with PPARg antagonists.These results indicate that the decrease in integrin a5 and following inhibition of cell adhesion may cause the inhibition of FAK signaling pathways. PPARg antagonists also strongly inhibited invasion of squamous cell carcinoma via down-regulation of CD151expression. Conclusions: The cell death caused by the PPARg antagonists was a result of direct interference with cell adhesion ''anoikis'' involving intracellular FAK signaling pathways. These results imply a potentially important and novel role for the inhibition of PPARg function via the use of specific antagonists in the treatment of squamous cell carcinoma and the prevention of tumor invasion and metastasis.

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“…20,21 Other integrins (a5b1, a6b1, a6b4 and aIIbb3) are also known to interact with CD151 depending on cell types, [22][23][24][25] although information about the binding sites is not available. Since CD151 is located at the periphery of the thin invasive protrusions (invadopodia) of cancer cells and treatment of the cells with anti-CD151 monoclonal antibody inhibits metastasis, 26 this molecule is considered to play an important role in invasion and metastasis.…”

mentioning

confidence: 99%

Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151

Shiomi

Inoki

Kataoka

et al. 2005

Laboratory Investigation

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Matrix metalloproteinase-7 (MMP-7) (also known as matrilysin-1) is secreted as a proenzyme (proMMP-7) and plays a key role in the degradation of various extracellular matrix (ECM) and non-ECM molecules after activation. To identify the binding proteins related to proMMP-7 activation, a human lung cDNA library was screened by yeast two-hybrid system using proMMP-7 as bait. We identified a candidate molecule CD151, which is a member of the transmembrane 4 superfamily. Complex formation of proMMP-7 with CD151 was demonstrated by immunoprecipitation of the molecules from CaR-1 cells, a human rectal carcinoma cell line, expressing both proMMP-7 and CD151, and CD151 stable transfectants incubated with proMMP-7. Yeast twohybrid assays using deletion mutants of proMMP-7 and CD151 suggested an interaction between the propeptide of proMMP-7 and the COOH-terminal extracellular loop of CD151. The binding activity of 125 I-labeled proMMP-7 to CD151 on the cell membranes was shown with CD151 stable transfectants. Laser-scanning confocal microscopy demonstrated that proMMP-7 colocalizes with CD151 on the cell membranes of CD151 stable transfectants and CaR-1 cells. In situ zymography using crosslinked carboxymethylated transferrin, a substrate of MMP-7, demonstrated proteinase activity on and around CD151 stable transfectants and CaR-1 cells, while the activity was abolished by their treatment with MMP inhibitors, anti-MMP-7 antibody or anti-CD151 antibody. In human lung adenocarcinoma tissues, colocalization of MMP-7 and CD151 was demonstrated on the carcinoma cells. Metalloproteinase activity was present in these tissues and could be inhibited by antibodies to MMP-7 or CD151. These data demonstrate for the first time that proMMP-7 is captured and activated on the cell membranes through interaction with CD151, and suggest the possibility that similar to the MT1-MMP/MMP-2 system, MMP-7 is involved in the pericellular activation mechanism mediated by CD151, a crucial step in proteolysis on the cell membranes under various pathophysiological conditions including cancer invasion and metastasis.

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Localization of the Transmembrane 4 Superfamily (TM4SF) Member PETA-3 (CD151) in Normal Human Tissues: Comparison with CD9, CD63, and α5β1 Integrin

Cited by 185 publications

References 31 publications

Tetraspan Protein CD151 A Common Target of Mood Stabilizing Drugs?

Tetraspan Protein CD151 A Common Target of Mood Stabilizing Drugs?

Critical Role of Peroxisome Proliferator-Activated Receptor γ on Anoikis and Invasion of Squamous Cell Carcinoma

Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151

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