Glycosylation of the laminin receptor (α3β1) regulates its association with tetraspanin CD151: Impact on cell spreading, motility, degradation and invasion of basement membrane by tumor cells

Ranjan, Amit; Bane, Sanjay M.; Kalraiya, Rajiv D.

doi:10.1016/j.yexcr.2014.02.004

Cited by 29 publications

(23 citation statements)

References 52 publications

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“…The expression of both CD44 and β 1 integrin did not correlate with invasive potential of the cells as both B16F10 and B16BL6 cells express them in almost equal amounts (Figure 3(a)). Their expression on the surface of these two cell lines is also identical for CD44 as shown in Figure 3(b) and for β 1 integrin as shown previously [9]. Lectin L-PHA precipitation and western blotting of proteins from cell lysates of both B16F10 and B16BL6 cells showed that both β 1 integrin and CD44 carry β 1,6 branched N-oligosaccharides.…”

Section: Resultssupporting

confidence: 84%

“…Proteins from B16BL6 cells showed higher levels of precipitation of both CD44 and β 1 integrin with L-PHA suggesting that these proteins carry higher levels of β 1,6 branched N-oligosaccharides. However, inhibition of glycosylation with swainsonine (SW) did not have any effect on the surface expression of CD44 (Figures 3(c) and 3(d)) and even β 1 integrin [9]. However, role of β 1,6 branched N-oligosaccharides on the motility receptors in regulating their association with MT1-MMP needs to be assessed.…”

Section: Resultsmentioning

confidence: 99%

“…Increased expression of β 1,6 branched N-oligosaccharides on integrin receptors like β 1 appears to promote adhesion and thus MMP9 expression [9]. The present studies aim to investigate the expression and localization of MT1-MMP and uPAR with receptors carrying β 1,6 branched N-oligosaccharides and the role of these oligosaccharides in regulating their association with receptors involved in motility.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Invasive Potential of Melanoma Cells Correlates with the Expression of MT1-MMP and Regulated by Modulating Its Association with Motility Receptors via N-Glycosylation on the Receptors

Ranjan

Kalraiya

2014

BioMed Research International

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Matrix remodeling and invasion of basement membrane are the major determinants of malignant progression. Matrix degrading enzymes play a pivotal role in this process and have been shown to be regulated at multiple levels. Using high metastatic B16F10 and its invasive variant B16BL6 cells, we previously demonstrated that the expression of β1,6 branched N-oligosaccharides promotes cellular adhesion on different matrix components which in turn induces secretion of MMP9. The present investigations report that although the two cell lines do not differ in the expression of uPAR, expression of MT1-MMP is significantly higher on B16BL6 cells. Analysis of the transcripts of tissue inhibitors of matrix metalloproteinases (TIMPs) showed that expression of both TIMP1 and TIMP2 correlates negatively with the invasive potential of cells. CD44 and β1 integrin, the two important receptors involved in motility, were identified to carry β1,6 branched N-oligosaccharides in an invasive potential dependent manner. However, their glycosylation status did not appear to influence their surface expression. Although glycosylation on CD44 had no effect, that on β1 integrin significantly affected association of β1 integrin with MT1-MMP. The results thus demonstrate that the cancer cells use multiple mechanisms for degradation of matrix in a controlled manner to couple it with movement for effective invasion.

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Section: Resultssupporting

confidence: 84%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Invasive Potential of Melanoma Cells Correlates with the Expression of MT1-MMP and Regulated by Modulating Its Association with Motility Receptors via N-Glycosylation on the Receptors

Ranjan

Kalraiya

2014

BioMed Research International

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“…Note that most of the highly reactive, prevalent autoantibodies shown in Table I have some association with cancer-related selfAgs, including BIRC2 (41), CA125 (43), MUC1 (54), stem cell factor (60), S-100 (61), myosin (56), GHRH (26,27), glucagon (29), HGH (31), leptin (33), F3 coagulation factor III (36), EEF1A1 (45), fibronectin (48,49), neurotrophin-3 (58), BCMO1 (63), citrate synthase (66), GST (68), PTGDS (70), laminin (83), and MIF (85). Indeed, we have found that dynamic changes in autoantibody repertoires mark the natural history in mice of variants of a syngeneic, transplantable tumor (112).…”

Section: Discussionmentioning

confidence: 99%

Tumor-Associated and Disease-Associated Autoantibody Repertoires in Healthy Colostrum and Maternal and Newborn Cord Sera

Madi

Bransburg-Zabary

Maayan-Metzger

et al. 2015

The Journal of Immunology

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In this work, we studied autoantibody repertoires and Ig isotypes in 71 mothers and their 104 healthy newborns (including twins and triplets delivered term or premature). Newborns receive maternal IgG Abs via the placenta before birth, but developing infants must produce their own IgM and IgA Abs. We used an Ag microarray analysis to detect binding to a selection of 295 self-Ags, compared with 27 standard foreign Ags. The magnitude of binding to specific self-Ags was found to be not less than that to the foreign Ags. As expected, each newborn shared with its mother a similar IgG repertoire—manifest as early as the 24th week of gestation. IgM and IgA autoantibody repertoires in cord sera were highly correlated among the newborns and differed from their mothers’ repertoires; the latter differed in sera and milk. The autoantibodies bound to self-Ags known to be associated with tumors and to autoimmune diseases. Thus, autoantibody repertoires in healthy humans—the immunological homunculus—arise congenitally, differ in maternal milk and sera, and mark the potential of the immune system to attack tumors, beneficially, or healthy tissues, harmfully; regulation of the tissue site, the dynamics, and the response phenotype of homuncular autoimmunity very likely affects health.

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“…Glycosylation of α3β1 integrin was demonstrated to regulate its association with the tetra spanin CD151, modulating cell spreading and motility 143 . Therefore, changes in the N-glycosylation profile of integrins modulate tumour cell motility and migration through interference with the supramolecular complex formation (tumour cell focal adhesions) on the cell surface.…”

Section: O-glcnacylationmentioning

confidence: 99%

Glycosylation in cancer: mechanisms and clinical implications

2015

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Despite recent progress in understanding the cancer genome, there is still a relative delay in understanding the full aspects of the glycome and glycoproteome of cancer. Glycobiology has been instrumental in relevant discoveries in various biological and medical fields, and has contributed to the deciphering of several human diseases. Glycans are involved in fundamental molecular and cell biology processes occurring in cancer, such as cell signalling and communication, tumour cell dissociation and invasion, cell-matrix interactions, tumour angiogenesis, immune modulation and metastasis formation. The roles of glycans in cancer have been highlighted by the fact that alterations in glycosylation regulate the development and progression of cancer, serving as important biomarkers and providing a set of specific targets for therapeutic intervention. This Review discusses the role of glycans in fundamental mechanisms controlling cancer development and progression, and their applications in oncology.

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Glycosylation of the laminin receptor (α3β1) regulates its association with tetraspanin CD151: Impact on cell spreading, motility, degradation and invasion of basement membrane by tumor cells

Cited by 29 publications

References 52 publications

Invasive Potential of Melanoma Cells Correlates with the Expression of MT1-MMP and Regulated by Modulating Its Association with Motility Receptors via N-Glycosylation on the Receptors

Invasive Potential of Melanoma Cells Correlates with the Expression of MT1-MMP and Regulated by Modulating Its Association with Motility Receptors via N-Glycosylation on the Receptors

Tumor-Associated and Disease-Associated Autoantibody Repertoires in Healthy Colostrum and Maternal and Newborn Cord Sera

Glycosylation in cancer: mechanisms and clinical implications

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