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

Bauer, T. J., Gombocz, E., Wehland, M., Bauer, J., Infanger, M., & Grimm, D. (2020). Insight in Adhesion Protein Sialylation and Microgravity Dependent Cell Adhesion-An Omics Network Approach. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 21(5): 1749. doi:10.3390/ijms21051749.

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 Creators:
Bauer, Thomas J.1, Author
Gombocz, Erich1, Author
Wehland, Markus1, Author
Bauer, Johann2, Author           
Infanger, Manfred1, Author
Grimm, Daniela1, Author
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1external, ou_persistent22              
2Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565170              

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Free keywords: I-LIKE DOMAIN; BETA-GALACTOSIDE ALPHA-2,6-SIALYLTRANSFERASE; THYROID-CANCER CELLS; SIALIC ACIDS; N-GLYCANS; SPHEROID FORMATION; ENDOTHELIAL-CELLS; POLYSIALIC ACID; HOMOPHILIC INTERACTIONS; GENE-EXPRESSIONlinked open database; graphical SPARQL; semantic knowledgebase; proteome; integrin; cadherin;
 Abstract: 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.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published online
 Pages: 23
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000524908500200
DOI: 10.3390/ijms21051749
 Degree: -

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Title: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Source Genre: Journal
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Publ. Info: ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND : MDPI
Pages: - Volume / Issue: 21 (5) Sequence Number: 1749 Start / End Page: - Identifier: -