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Insight in Adhesion Protein Sialylation and Microgravity Dependent Cell Adhesion-An Omics Network Approach

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  • Thomas J Bauer, Otto von Guericke University Magdeburg
  • ,
  • Erich Gombocz, Melissa Informatics, 2550 Ninth Street, Suite 114, Berkeley, CA 94710, USA.
  • ,
  • Markus Wehland
  • Johann Bauer, f Max-Planck-Institute for Biochemistry , 82152 Martinsried , Germany.
  • ,
  • Manfred Infanger, Otto von Guericke University Magdeburg
  • ,
  • Daniela Grimm

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.

Original languageEnglish
Article number1749
JournalInternational Journal of Molecular Sciences
Number of pages23
Publication statusPublished - 2020

    Research areas

  • Cadherin, Graphical SPARQL, Integrin, Linked open database, Proteome, Semantic knowledgebase

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