| Autor: |
Bauer TJ; Clinic for Plastic, Aesthetic and Hand Surgery, Otto-von-Guericke-University Magdeburg, D-39120 Magdeburg, Germany., Gombocz E; Melissa Informatics, 2550 Ninth Street, Suite 114, Berkeley, CA 94710, USA., Wehland M; Clinic for Plastic, Aesthetic and Hand Surgery, Otto-von-Guericke-University Magdeburg, D-39120 Magdeburg, Germany., Bauer J; Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany., Infanger M; Clinic for Plastic, Aesthetic and Hand Surgery, Otto-von-Guericke-University Magdeburg, D-39120 Magdeburg, Germany., Grimm D; Clinic for Plastic, Aesthetic and Hand Surgery, Otto-von-Guericke-University Magdeburg, D-39120 Magdeburg, Germany.; Department of Biomedicine, Aarhus University Hospital, DK-8000 Aarhus C, Denmark.; Department of Microgravity and Translational Regenerative Medicine, Otto von Guericke University, Pfälzer Platz, 39106 Magdeburg, Germany. |
| Abstrakt: |
The adhesion behavior of human tissue cells changes in vitro, when gravity forces affecting these cells are modified. To understand the mechanisms underlying these changes, proteins involved in cell-cell or cell-extracellular matrix adhesion, their expression, accumulation, localization, and posttranslational modification (PTM) regarding changes during exposure to microgravity were investigated. As the sialylation of adhesion proteins is influencing cell adhesion on Earth in vitro and in vivo, we analyzed the sialylation of cell adhesion molecules detected by omics studies on cells, which change their adhesion behavior when exposed to microgravity. Using a knowledge graph created from experimental omics data and semantic searches across several reference databases, we studied the sialylation of adhesion proteins glycosylated at their extracellular domains with regards to its sensitivity to microgravity. This way, experimental omics data networked with the current knowledge about the binding of sialic acids to cell adhesion proteins, its regulation, and interactions in between those proteins provided insights into the mechanisms behind our experimental findings, suggesting that balancing the sialylation against the de-sialylation of the terminal ends of the adhesion proteins' glycans influences their binding activity. This sheds light on the transition from two- to three-dimensional growth observed in microgravity, mirroring cell migration and cancer metastasis in vivo. |
