The impact of N- and O-glycosylation on the functions of Glut-1 transporter in human thyroid anaplastic cells

Samih, Nezha; Hovsépian, Sonia; Notel, Frédéric; Prorok, Maëlle; Zattara-Cannoni, Hélène; Mathieu, Sylvie; Lagadic‐Gossmann, Dominique; Fayet, Guy; El‐Battari, Assou

doi:10.1016/s0304-4165(03)00050-3

Cited by 48 publications

(40 citation statements)

References 35 publications

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“…This discrepancy between GLUT1 expression levels and 3 HPage 13 of 28 A c c e p t e d M a n u s c r i p t 13 DG uptake could be due to a defect of N-glycosylation status as already observed in primary anaplastic thyroid cell lines by other authors (Samih et al, 2003).…”

Section: Analysis Of Glut1 and Glut3 Proteins On Cell Membrane And Cymentioning

confidence: 59%

Expression analysis of facilitative glucose transporters (GLUTs) in human thyroid carcinoma cell lines and primary tumors

Ciampi

Vivaldi

Romei

et al. 2008

Molecular and Cellular Endocrinology

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Expression analysis of facilitative glucose transporters (GLUTs) in human thyroid carcinoma cell lines and primary tumors, Molecular and Cellular Endocrinology (2007), doi:10.1016/j.mce.2008 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. We studied several GLUT isoforms expression in thyroid tumor cell lines deriving from anaplastic (ARO, FRO), papillary (NPA), follicular (WRO) and medullary (TT) human thyroid carcinoma. GLUT1 and GLUT3 were also studied in 157 human thyroid malignant and benign tissues.Quantitative Real-time RT-PCR analysis revealed that GLUT1 mRNA levels were higher in less-differentiated cells (ARO, FRO) while GLUT3 mRNA levels were prevalent in well-differentiated cells (NPA, WRO). Accordingly, Western blot showed high expression and correct membrane targeting of GLUT1 protein in ARO and FRO and of GLUT3 protein in NPA and WRO. All cell lines were able to take-up different rates of 3 H-Deoxy-Glucose. The analysis of GLUT1 and GLUT3 mRNA expression in human thyroid tissues showed the prevalence of GLUT1, but not of GLUT3, in malignant with respect to normal tissues. Finally, both GLUT1 and GLUT3 showed a slightly higher expression in anaplastic than in well-differentiated tumors.In conclusion, we showed that GLUT1 and GLUT3 were the most important glucose transporters in the thyroid tumoral cells. In particular GLUT1 was the most prevalent in less-differentiated cells (ARO and FRO) while GLUT3 was the most prevalent in welldifferentiated cells (NPA and WRO). A similar pattern of expression was found for GLUT1 but not for GLUT3 in human thyroid tumors.

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Section: Analysis Of Glut1 and Glut3 Proteins On Cell Membrane And Cymentioning

confidence: 59%

Expression analysis of facilitative glucose transporters (GLUTs) in human thyroid carcinoma cell lines and primary tumors

Ciampi

Vivaldi

Romei

et al. 2008

Molecular and Cellular Endocrinology

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“…[25][26][27] Cell type-specific posttranslational modifications of EGF domains 28 may provide a general mechanism for regulating ligand-receptor interactions. Aspartyl betahydroxylation and O-fucose glycosylation of EGF domains modulate Notch-receptor signaling.…”

Section: Discussionmentioning

confidence: 99%

N‐glycosylation of CD97 within the EGF domains is crucial for epitope accessibility in normal and malignant cells as well as CD55 ligand binding

Wobus

Vogel

Schmücking

et al. 2004

Intl Journal of Cancer

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CD97 is an EGF-TM7 receptor found on various carcinomas where expression levels correlate with dedifferentiation and tumor stage, smooth muscle cells and leukocytes. CD97 acts as an adhesion molecule by binding to its cellular ligand, CD55. In this study, we demonstrate that 2 immunodominant CD97 epitopes are not equally present in the various cell types. Differences were apparent in gastrointestinal tumors and smooth muscle cells where monoclonal antibodies (mAbs) to the first epidermal growth factor (EGF) domain (CD97 EGF ) showed a more restricted staining pattern than mAbs to the stalk region (CD97 stalk ). This discrepancy was not detectable in cultured gastrointestinal tumor cell lines. In fact, the selection of the CD97 mAb influences the result of clinical studies. Thus, we clarified the reason(s) for these differences in CD97 mAb staining on various cell types. We provide evidence that epitope accessibility for CD97 EGF Key words: CD97; colorectal cancer; smooth muscle cell; epitope accessibility; glycosylation CD97 is a member of a subfamily of 7-span transmembrane (TM7) receptors referred to as EGF-TM7 proteins. 1,2 In normal tissues, CD97 is abundantly expressed in smooth muscle cells, macrophages, granulocytes, dendritic cells and in some T and B cells. 3 Carcinomas of different origin showed higher CD97 expression compared to the corresponding normal cell types. 4 -7 CD97 consists of an extended extracellular region with several N-terminal epidermal growth factor (EGF) domains coupled to the TM7 domain by a stalk. 1,8 Various CD97 isoforms exist possessing 3 (EGF 1,2,5), 4 (EGF 1,2,3,5), or 5 (EGF 1,2,3,4,5) EGF domains. CD97 binds to membrane receptor CD55. 9 This interaction is mediated by the first 2 CD97 EGF domains. 9 -11 Chondroitin sulfate glycosaminoglycan, present in cell membranes and the extracellular matrix, is a new ligand to the longest CD97 isoform (EGF 1,2,3,4,5). 12 The ability of CD97 EGF domains to interact with cellular and/or extracellular matrix ligands suggests that the molecule is involved in cell-cell or cell-matrix interactions. Various lines of evidence have shown an important role for CD97 in tumor dedifferentiation, migration, invasiveness and metastasis. CD97 levels correlate with the in vitro migration and invasion capacity of colorectal tumor cell lines and CD97-transfected cells. 6 Colorectal carcinomas with more strongly CD97-stained, scattered tumor cells at the invasion front showed a poorer clinical stage as well as increased lymph vessel invasion compared to cases with uniform CD97 staining. 6 In thyroid cancers, CD97 expression parallels the aggressiveness and lymph node involvement of these tumors. 4,5 Our previous data revealed that CD97 has prognostic and therapeutic potential in cancer. However, analyzing CD97 expression brings up the phenomenon that different staining patterns, depending on which CD97 monoclonal antibody (mAb) has been used for immunohistology, can be readily observed in pancreatic tissues. 7,13 Based on this observation, one aim of ...

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“…32 Cells were cultured for 72 hr with the drugs and assayed for E-selectin-IgM binding and analysed by FACS as described. 14 As shown in Figure 6d, benzyl-GalNAc strongly inhibits E-selectin binding (9.6% remaining activity) whereas dMJ showed no effect.…”

Section: E-selectin Ligand Characterizationmentioning

confidence: 99%

Introducing α(1,2)‐linked fucose into hepatocarcinoma cells inhibits vasculogenesis and tumor growth

Mathieu¹,

Gerolami²,

Luis³

et al. 2007

Intl Journal of Cancer

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The glycoantigen sialyl-Lewis x (sLex) and its isomer sialy-Lewis a (sLea) are frequently associated with advanced states of cancer and metastasis. In a previous work, we have shown that hepatocarcinoma cells (HCC) HepG2 interact with the endothelial Eselectin exclusively through sLe x oligosaccharides, the synthesis of which could be completely prevented by the a(1,2)-fucosyltransferase-I (FUT1), thus resulting in a strong inhibition of adhesion and rolling on activated endothelial cells. The purpose of the present study was to evaluate the impact of inhibiting sLex synthesis and the subsequent E-selectin adhesion, on HCC tumor growth in nude mice. Four weeks after subcutaneous transplantation of cells, no FUT1-derived tumor could be detected, whereas 75% of control animals developed large size tumor nodules. Between the 4th and the 8th week postinoculation, 33% tumors arose from FUT1-transduced cells but showed a slow growth (nodule volumes less than 500 mm 3 ), while more than 50% of control tumors reached volumes between 1,500 and 3,000 mm 3 . Several parameters were examined, including cell division and proliferation, apoptosis, adhesion to extracellular matrix components and angiogenesis/vasculogenesis. We provide evidence that among all, vasculogenesis was the most clearly affected by FUT1 expression, suggesting that tumor angiomorphogenesis may, at least partly, depend on Eselectin-mediated interaction between HCC and endothelial cells, the inhibition of which remarkably retards tumor growth. ' 2007 Wiley-Liss, Inc.Key words: a(1,2)-fucosyltransferase-I; E-selectin; sialyl-Lewis; antitumor; vasculogenesisThe sialyl-Lewis antigens (sLex and sLea) are blood grouprelated antigens naturally expressed on leukocytes to initiate leukocyte-endothelium interaction mediated by the cytokine-inducible endothelial adhesion molecule E-selectin. 1,2 In addition to this physiological role in inflammation, sialyl-Lewis antigens are also considered as tumor markers expressed on many cancer cells and therefore, they are thought to be involved in metastasis by initiating tumor cell-endothelium adhesion. 3 Indeed, the expression of sialyl-Lewis antigens on carcinoma cells is frequently associated with advanced states of cancer and a statistically relevant relationship has been established between the postoperative prognosis of patients and the degree of expression of sialyl-Lewis antigens on cancer tissues. 3 Besides, several lines of evidence from selectin-deficient mice studies pointed out the contribution of selectins in facilitating tumor growth and progression. 4,5 In particular, E-selectin and its sLex-containing glycoconjugate ligands have been shown to be involved in the essential events of tumor angiogenesis, 6-9 including the fact that coinjection of tumor cells expressing high level of sLe x together with endothelial cells constitutively expressing E-selectin, has been found to promote tumor angiogenesis and growth. 10 We have recently succeeded in strongly blocking the expression of sLex on digestive cancer cells...

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The impact of N- and O-glycosylation on the functions of Glut-1 transporter in human thyroid anaplastic cells

Cited by 48 publications

References 35 publications

Expression analysis of facilitative glucose transporters (GLUTs) in human thyroid carcinoma cell lines and primary tumors

Expression analysis of facilitative glucose transporters (GLUTs) in human thyroid carcinoma cell lines and primary tumors

N‐glycosylation of CD97 within the EGF domains is crucial for epitope accessibility in normal and malignant cells as well as CD55 ligand binding

Introducing α(1,2)‐linked fucose into hepatocarcinoma cells inhibits vasculogenesis and tumor growth

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