Syndecan-1-Dependent Homotypic Cell Adhesion in HT58 Lymphoma Cells

Sebestyén, Anna; Tótth, Árpád; Rudolf, Martin; Szakács, Orsolya; Paku, Sándor; Kopper, László

doi:10.1159/000030140

Cited by 13 publications

(8 citation statements)

References 33 publications

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“…These cellular aggregations were observed in all species of SDCs and GPC1 (data not shown), indicating that the expression of HSPGs induced cell-cell adhesion. Similar to our observation, HS-dependent cell-cell adhesion has been reported in B lymphoid cell lines and cells transduced with SDC1 (36,56,60). To determine whether this increased cell-cell contact mediated by HSPG is related to the fusion activity with an HTLV-1-producing cell line, we conducted a syncytium assay as described in Materials and Methods.…”

Section: Preparation Of Vsv Pseudotypes Bearing Htlv-1 Env Proteinssupporting

confidence: 92%

Entry of Human T-Cell Leukemia Virus Type 1 Is Augmented by Heparin Sulfate Proteoglycans Bearing Short Heparin-Like Structures

Tanaka

Jinno-Oue

Shimizu

et al. 2012

J Virol

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bThree molecules have been identified as the main cellular factors required for binding and entry of human T-cell leukemia virus type 1 (HTLV-1): glucose transporter 1 (GLUT1), heparan sulfate (HS), and neuropilin 1 (NRP-1). However, the precise mechanism of HTLV-1 cell tropism has yet to be elucidated. Here, we examined the susceptibilities of various human cell lines to HTLV-1 by using vesicular stomatitis virus pseudotypes bearing HTLV-1 envelope proteins. We found that the cellular susceptibility to HTLV-1 infection did not correlate with the expression of GLUT1, HS, or NRP-1 alone. To investigate whether other cellular factors were responsible for HTLV-1 susceptibility, we conducted expression cloning. We identified two HS proteoglycan core proteins, syndecan 1 and syndecan 2, as molecules responsible for susceptibility to HTLV-1. We found that treatment of syndecan 1-transduced cells (expressing increased HS) with heparinase, a heparin-degradative enzyme, reduced HTLV-1 susceptibility without affecting the expression levels of HS chains. To further elucidate these results, we characterized the expression of HS chains in terms of the mass, number, and length of HS in several syndecan 1-transduced cell clones as well as human cell lines. We found a significant correlation between HTLV-1 susceptibility and the number of HS chains with short chain lengths. Our findings suggest that a combination of the number and the length of HS chains containing heparin-like regions is a critical factor which affects the cell tropism of HTLV-1. Human T-cell leukemia virus type 1 (HTLV-1) is the causative agent of adult T-cell leukemia (16, 49) and HTLV-1-associated myelopathy, also known as tropical spastic paraparesis (10,24,45). Previous investigations revealed that HTLV-1 infects not only human T lymphocytes and central nervous system cells but also cells of other tissues (6,17,21,34,51,69). To date, glucose transporter 1 (GLUT1), neuropilin-1 (NRP-1), and heparan sulfate proteoglycans (HSPGs) have been implicated as being involved in HTLV-1 infection (reviewed in reference 12). The expression of GLUT1, which is responsible for viral binding and fusion mediated by the gp46 surface envelope (Env) protein (3,26,39), is ubiquitous, and it is also known that various cells express HSPGs. Although these findings might be able to explain the broad host cell range of HTLV-1, they are not sufficient to explain the variance of HTLV-1 cell tropism.It was previously reported that HTLV-1 spreads from cell to cell via virological synapses (22, 38); however, recent studies by Pais-Correia and colleagues showed that the HTLV-1 virions retaining extracellular structures are important for HTLV-1 cell transmission (46). That study implied that the viral particle mediates HTLV-1 transmission and suggested the importance of the interaction between viral particles and the target cell surface. In this study, we investigated the susceptibilities of various human cell lines to cell-free HTLV-1 infection using highly infectious vesicular stomatiti...

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Section: Preparation Of Vsv Pseudotypes Bearing Htlv-1 Env Proteinssupporting

confidence: 92%

Entry of Human T-Cell Leukemia Virus Type 1 Is Augmented by Heparin Sulfate Proteoglycans Bearing Short Heparin-Like Structures

Tanaka

Jinno-Oue

Shimizu

et al. 2012

J Virol

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“…The growth of carcinoma cells was inhibited by antisense syndecan-1 [34]. Elimination of HS chains and inhibition of syndecan-1 synthesis induced apoptosis in HT58 cells [35]. The differences reported in these studies suggest that apoptosis in response to syndecan-1 may be modulated by various factors depending on cell type.…”

Section: Discussionmentioning

confidence: 82%

Syndecan-2 expression increases serum-withdrawal-induced apoptosis, mediated by re-distribution of Fas into lipid rafts, in stably transfected Swiss 3T3 cells

et al. 2006

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To examine the function of syndecan-2, one of the most abundant heparan sulfate proteoglycans in fibroblasts, we obtained stably transfected Swiss 3T3 clones. We examined the effects of stable syndecan-2 overexpression on programmed cell death, finding that syndecan-2 transfected cells were more sensitive to apoptosis induced by serum-withdrawal than control cells. In addition, overexpression of syndecan-2 correlates with increased membrane levels of the Fas/CD95 receptor, suggesting that the increased serum-withdrawal apoptosis observed in Swiss 3T3 cells might be Fas receptor-dependent. Differences in Fas membrane levels between both control and syndecan-2 transfected cells result from a redistribution of the Fas receptor. Our data clearly demonstrate that increased Fas levels are primarily related to lipid rafts and that this increase is a key factor in Fas/CD95-mediated apoptosis. Moreover, disruption of lipid rafts with methyl-beta-cyclodextrin or filipin significantly reduced apoptosis in response to serum withdrawal. The differences in Fas/CD95 membrane distribution could explain why syndecan-2 transfected cells have a higher susceptibility to serum-withdrawal-induced apoptosis.

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“…Syndecan-1 is expressed in various human cancers (Table 1; Bayer-Garner et al, 2000;Conejo et al, 2000;Harada et al, 2003;Naganuma et al, 2004;Sebestyen et al, 2000) and correlates with tumor recurrence in human prostate cancer (Chen et al, 2004a;Zellweger et al, 2003). Syndecan-1 is upregulated in human breast cancer samples compared to normal breast tissue, and in some breast cancer patients, increased syndecan-1 mRNA and protein correlate with higher histologic tumor grading, increased mitotic index, increased tumor size, and poor prognosis (Barbareschi et al, 2003;Tsanou et al, 2004).…”

Section: Syndecan-1mentioning

confidence: 99%