Bisecting GlcNAc Residues on Laminin-332 Down-regulate Galectin-3-dependent Keratinocyte Motility

Kariya, Yoshinobu; Kawamura, Chihiro; Tabei, Toshiki; Gu, Jianguo

doi:10.1074/jbc.m109.038836

Cited by 64 publications

(62 citation statements)

References 63 publications

(44 reference statements)

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“…3. Furthermore, we found that galectin-3, which is a β-galactoside binding protein, strongly bound to unmodified Lm332 but not to the Lm332 modified by GnT-III, and that binding of galectin-3 was completely blocked by lactose [23]. Coimmunoprecipitation revealed that galectin-3 associated with both β4 integrin and EGFR, thereby cross-linking the two molecules.…”

Section: Roles Of N-glycosylation On α5β1 Integrinmentioning

confidence: 87%

“…For example, it could also be explained that the bisecting GlcNAc might be recognized by an unidentified endogenous lectin, which is similar to E4-PHA, to regulate cell behavior of animal cells. Alterations of N-glycans on integrins could also regulate their cis-interactions with membrane-associated proteins including the epidermal growth factor receptor (EGFR) [22,23], and the tetraspanin family of proteins in microdomain [24,25] as well as endocytosis [10,26,27]. In addition, GnT-III also contributes to suppress some other important glycoproteins, such as EGFR.…”

Section: N-glycans Regulate Integrin Functionsmentioning

confidence: 99%

“…Similarly, tetraspanin CD82 with incomplete Nglycosylation exhibits an enhanced association with the α3 and α5 integrin subunits [45]. A modest association between Lm332 and α6β4 integrin mediated by galectin-3 through the N-glycans on both molecules promoted cell adhesion and migration on Lm332 as well as α6β4 integrin clustering on Lm332 [23,43]. Accordingly, an appropriate intermolecular interaction through N-glycan is important for the efficient cellular signaling and the following cellular function.…”

Section: Roles Of N-glycosylation On α5β1 Integrinmentioning

confidence: 99%

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Potential roles of N-glycosylation in cell adhesion

Isaji

et al. 2012

Glycoconj J

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128

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The functional units of cell adhesion are typically multiprotein complexes made up of three general classes of proteins; the adhesion receptors, the cell-extracellular matrix (ECM) proteins, and the cytoplasmic plaque/peripheral membrane proteins. The cell adhesion receptors are usually transmembrane glycoproteins (for example E-cadherin and integrin) that mediate binding at the extracellular surface and determine the specificity of cell-cell and cell-ECM recognition. E-cadherin-mediated cell-cell adhesion can be both temporally and spatially regulated during development, and represents a key step in the acquisition of the invasive phenotype for many tumors. On the other hand, integrin-mediated cell-ECM interactions play important roles in cytoskeleton organization and in the transduction of intracellular signals to regulate various processes such as proliferation, differentiation and cell migration. ECM proteins are typically large glycoproteins, including the collagens, fibronectins, laminins, and proteoglycans that assemble into fibrils or other complex macromolecular arrays. The most of these adhesive proteins are glycosylated. Here, we focus mainly on the modification of N-glycans of integrins and laminin-332, and a mutual regulation between cell adhesion and bisected N-glycan expression, to address the important roles of N-glycans in cell adhesion.

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Section: Roles Of N-glycosylation On α5β1 Integrinmentioning

confidence: 87%

Section: N-glycans Regulate Integrin Functionsmentioning

confidence: 99%

Section: Roles Of N-glycosylation On α5β1 Integrinmentioning

confidence: 99%

See 1 more Smart Citation

Potential roles of N-glycosylation in cell adhesion

Isaji

et al. 2012

Glycoconj J

Self Cite

128

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“…A mechanism by which galectin-3 promotes keratinocyte cell motility is through association with N-glycan ligands on laminin-332 and a3b1 integrin, resulting in enhanced cellular signaling and the formation of lamellopodia, respectively (Kariya et al, 2010;Saravanan et al, 2009). In cancer cells, galectin-3 also facilitates cell motility by inducing MMPs (Kim et al, 2011;Wang et al, 2012), but the molecular mechanism associated with this process is unknown.…”

Section: Introductionmentioning

confidence: 99%

Molecular basis for MMP9 induction and disruption of epithelial cell-cell contacts by galectin-3

Mauris

Woodward

Cao

et al. 2014

Journal of Cell Science

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Dynamic modulation of the physical contacts between neighboring cells is integral to epithelial processes such as tissue repair and cancer dissemination. Induction of matrix metalloproteinase (MMP) activity contributes to the disassembly of intercellular junctions and the degradation of the extracellular matrix, thus mitigating the physical constraint to cell movement. Using the cornea as a model, we show here that a carbohydrate-binding protein, galectin-3, promotes cellcell detachment and redistribution of the tight junction protein occludin through its N-terminal polymerizing domain. Notably, we demonstrate that galectin-3 initiates cell-cell disassembly by inducing matrix metalloproteinase expression in a manner that is dependent on the interaction with and clustering of the matrix metalloproteinase inducer CD147 (also known as EMMPRIN and basigin) on the cell surface. Using galectin-3-knockout mice in an in vivo model of wound healing, we further show that increased synthesis of MMP9 at the leading edge of migrating epithelium is regulated by galectin-3. These findings establish a new galectin-3-mediated regulatory mechanism for induction of metalloproteinase expression and disruption of cellcell contacts required for cell motility in migrating epithelia.

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“…Thus, N-glycans can be considered to be either a positive or negative regulator of the biological functions of integrin. Zhao et al reported a similar type of regulation in α3 integrin (27), α5 integrin (28) and laminin 332 (29). Therefore GnT-III and GnT-V have adverse effects on cancer invasion and metastasis by adding bisecting GlcNAc or β1-6GlcNAc branching (Fig.…”

Section: Figmentioning

confidence: 90%