Transglutaminase-2 in cell adhesion

Png, Evelyn; Tong, Louis

doi:10.4161/cam.26344

Cited by 9 publications

(7 citation statements)

References 39 publications

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“…This enzyme is located primarily in the cytosol, but it can be externalized and can play an essential role in the extracellular matrix organization, e.g., in fibronectin crosslinking 46 . Tissue transglutaminase co-localizes with beta 1 -integrin adhesion receptors 47 , and it has a positive influence on the phosphorylation of paxillin, which is vital for cell adhesion and migration 48 . Increased activity of tissue transglutaminase accompanied the increased resistance to trypsinization in murine sarcoma RIF-1 cells, HT29 human colonic carcinoma cells, and ECV304 human umbilical vein endothelial cells after photodynamic therapy using pyridinium zinc (II) phthalocyanine as sensitizer 37 .…”

Section: Discussionmentioning

confidence: 99%

Cell type specific adhesion to surfaces functionalised by amine plasma polymers

Černochová

Blahová

Medalová

et al. 2020

Sci Rep

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Our previously-obtained impressive results of highly increased C2C12 mouse myoblast adhesion to amine plasma polymers (PPs) motivated current detailed studies of cell resistance to trypsinization, cell proliferation, motility, and the rate of attachment carried out for fibroblasts (LF), keratinocytes (HaCaT), rat vascular smooth muscle cells (VSMC), and endothelial cells (HUVEC, HSVEC, and CPAE) on three different amine PPs. We demonstrated the striking difference in the resistance to trypsin treatment between endothelial and non-endothelial cells. The increased resistance observed for the non-endothelial cell types was accompanied by an increased rate of cellular attachment, even though spontaneous migration was comparable to the control, i.e., to the standard cultivation surface. As demonstrated on LF fibroblasts, the resistance to trypsin was similar in serum-supplemented and serum-free media, i.e., medium without cell adhesion-mediating proteins. The increased cell adhesion was also confirmed for LF cells by an independent technique, single-cell force spectroscopy. This method, as well as the cell attachment rate, proved the difference among the plasma polymers with different amounts of amine groups, but other investigated techniques could not reveal the differences in the cell behaviour on different amine PPs. Based on all the results, the increased resistance to trypsinization of C2C12, LF, HaCaT, and VSMC cells on amine PPs can be explained most probably by a non-specific cell adhesion such as electrostatic interaction between the cells and amine groups on the material surface, rather than by the receptor-mediated adhesion through serum-derived proteins adsorbed on the PPs.

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Section: Discussionmentioning

confidence: 99%

Cell type specific adhesion to surfaces functionalised by amine plasma polymers

Černochová

Blahová

Medalová

et al. 2020

Sci Rep

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“…Although the signaling mechanism driving Ser178 phosphorylation is poorly explored, paxillin phosphorylation at this residue facilitates the binding of FAK, which in turn promotes Tyr31 and Tyr118 phosphorylation and the subsequent binding of vinculin to paxillin. This evidence suggests that phosphorylation of paxillin Ser178 may be upstream FAK and vinculin, which may be sufficient to interfere with post-translational changes downstream FAK and vinculin [ 80 ].…”

Section: Paxillin Function In Specific Cells and Tissuesmentioning

confidence: 99%

Paxillin: a crossroad in pathological cell migration

et al. 2017

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Paxilllin is a multifunctional and multidomain focal adhesion adapter protein which serves an important scaffolding role at focal adhesions by recruiting structural and signaling molecules involved in cell movement and migration, when phosphorylated on specific Tyr and Ser residues. Upon integrin engagement with extracellular matrix, paxillin is phosphorylated at Tyr31, Tyr118, Ser188, and Ser190, activating numerous signaling cascades which promote cell migration, indicating that the regulation of adhesion dynamics is under the control of a complex display of signaling mechanisms. Among them, paxillin disassembly from focal adhesions induced by extracellular regulated kinase (ERK)-mediated phosphorylation of serines 106, 231, and 290 as well as the binding of the phosphatase PEST to paxillin have been shown to play a key role in cell migration. Paxillin also coordinates the spatiotemporal activation of signaling molecules, including Cdc42, Rac1, and RhoA GTPases, by recruiting GEFs, GAPs, and GITs to focal adhesions. As a major participant in the regulation of cell movement, paxillin plays distinct roles in specific tissues and developmental stages and is involved in immune response, epithelial morphogenesis, and embryonic development. Importantly, paxillin is also an essential player in pathological conditions including oxidative stress, inflammation, endothelial cell barrier dysfunction, and cancer development and metastasis.Electronic supplementary materialThe online version of this article (doi:10.1186/s13045-017-0418-y) contains supplementary material, which is available to authorized users.

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“…Hence, these results also suggest that other stimuli like direct fluid flow sensed by cells might be regulating osteoblast morphology. In addition, we can observe that the most important differences in cell morphology were observed when collagen gel was crosslinked, probably caused by the increment of the mechanical [70][71][72] and adhesion properties [43,73] induced by the inclusion of TG2.…”

Section: Discussionmentioning

confidence: 94%

Matrix architecture plays a pivotal role in 3D osteoblast migration: The effect of interstitial fluid flow

Amo

Olivares

Cóndor

et al. 2018

Journal of the Mechanical Behavior of Biomedical Materials

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Osteoblast migration is a crucial process in bone regeneration, which is strongly regulated by interstitial fluid flow. However, the exact role that such flow exerts on osteoblast migration is still unclear. To deepen the understanding of this phenomenon, we cultured human osteoblasts on 3D microfluidic devices under different fluid flow regimes. Our results show that a slow fluid flow rate by itself is not able to alter the 3D migratory patterns of osteoblasts in collagen-based gels but that at higher fluid flow rates (increased flow velocity) may indirectly influence cell movement by altering the collagen microstructure. In fact, we observed that high fluid flow rates (1 µl/min) are able to alter the collagen matrix architecture and to indirectly modulate the migration pattern. However, when these collagen scaffolds were crosslinked with a chemical crosslinker, specifically, transglutaminase II, we did not find significant alterations in the scaffold architecture or in osteoblast movement. Therefore, our data suggest that high interstitial fluid flow rates can regulate osteoblast migration by means of modifying the orientation of collagen fibers. Together, these results highlight the crucial role of the matrix architecture in 3D osteoblast migration. In addition, we show that interstitial fluid flow in conjunction with the matrix architecture regulates the osteoblast morphology in 3D.

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Transglutaminase-2 in cell adhesion

Cited by 9 publications

References 39 publications

Cell type specific adhesion to surfaces functionalised by amine plasma polymers

Cell type specific adhesion to surfaces functionalised by amine plasma polymers

Paxillin: a crossroad in pathological cell migration

Matrix architecture plays a pivotal role in 3D osteoblast migration: The effect of interstitial fluid flow

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