Vimentin and desmin possess GlcNAc-binding lectin-like properties on cell surfaces

Abstract

Vimentin and desmin are intermediate filament proteins found in various mesenchymal and skeletal muscle cells, respectively. These proteins play an important role in the stabilization of the cytoplasmic architecture. Here, we found, using artificial biomimicking glycopolymers, that vimentin and desmin possess N-acetylglucosamine (GlcNAc)-binding lectin-like properties on the cell surfaces of various vimentin- and desmin-expressing cells such as cardiomyocytes and vascular smooth muscle cells. The rod II domain of these proteins was demonstrated to be localized to the cell surface and to directly bind to the artificial biomimicking GlcNAc-bearing polymer, by confocal laser microscopy and surface plasmon resonance analysis. These glycopolymers strongly interact with lectins and are useful tools for the analysis of lectin-carbohydrate interactions, since glycopolymers binding to lectins can induce the clustering of lectins due to multivalent glycoside ligand binding. Moreover, immunocytochemistry and pull-down assay with His-tagged vimentin-rod II domain protein showed that the vimentin-rod II domain interacts with O-GlcNAc proteins. These results suggest that O-GlcNAc proteins might be one candidate for physiological GlcNAc-bearing ligands with which vimentin and desmin interact. These findings demonstrate a novel function of vimentin and desmin that does not involve stabilization of the cytoplasmic architecture by which these proteins interact with physiological GlcNAc-bearing ligands such as O-GlcNAc proteins on the cell surface through their GlcNAc-binding lectin-like properties.

Platelet adhesion involves a novel interaction between vimentin and von Willebrand factor under high shear stress

“…36 Several studies have indicated that this cytoskeletal protein can be found on the surface of different cell types, including platelets. [20][21][22]24 Vimentin is not the only cytoskeletal protein found on the cell surface because $3 other intermediate filaments are also expressed on the surface of various cells. 37 Because vimentin is a component of the platelet cytoskeleton, 25 it is unclear the mechanism by which it is translocated to the cell surface.…”

“…Emerging studies indicate that this cytoskeletal protein can be found on the surface of different cell types, including platelets. [20][21][22][23][24][25] This study reports that vimentin expressed on platelets may function as a receptor for VWF, and this interaction apparently works in concert with the classical GPIba-VWF binding in mediating platelet adhesion at high shear stress. …”

Integrin-independent Cell Adhesion Substrates: Possibility of Applications for Mechanobiology Research

“…60 In particular, Hepatic stellate cells can adhere on PVGlcNAc-coated substrates via these intermediate filament proteins. The expression of α-smooth actin, a marker of activated hepatic stellate cells, was suppressed on PVGlcNAc-coated substrates suggesting that hepatic stellate cells can maintain a quiescent state.…”

Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1) is regulated by O-GlcNAc transferase

“…Unlike other forms of glycosylation in cells that occurs within the secretory pathway, O-GlcNAc modifications occur in the nucleus and cytoplasm [3]. O-GlcNAc glycosylation has been shown to play a role in regulating protein function by influencing enzymatic activity, stability and subcellular localization of proteins [4][5][6][7]. O-GlcNAcylation is sensitive to the nutritional state of the cell as components used for synthesis of uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), the substrate for OGT, are generated from nutrients.…”