التفاصيل البيبلوغرافية
| العنوان: |
Identification of intracellular glycosaminoglycan-interacting proteins by affinity purification mass spectrometry |
| المؤلفون: |
Kristin Schubert, Sarah Vogel, Claudia Damaris Müller, Ute Hempel, Jan-Niklas Dürig, Sebastian Köhling, Martin von Bergen, Jörg Rademann, Stephanie Möller, Henning Großkopf, Matthias Schnabelrauch |
| بيانات النشر: |
Freie Universit��t Berlin, 2021. |
| سنة النشر: |
2021 |
| مصطلحات موضوعية: |
sulfated glycosaminoglycan derivatives, Clinical Biochemistry, Receptors, Cytoplasmic and Nuclear, Karyopherins, Endocytosis, Biochemistry, Exosome, Glycosaminoglycan, Extracellular matrix, Tandem Mass Spectrometry, Humans, LDL-Receptor Related Protein-Associated Protein, LC-MS/MS, Bone regeneration, hBMSC, Molecular Biology, Cells, Cultured, Glycosaminoglycans, Chemistry, GAG-biotin, Mesenchymal Stem Cells, Serine Protease HTRA1, High-Temperature Requirement A Serine Peptidase 1, pull-down approach, 500 Naturwissenschaften und Mathematik::570 Biowissenschaften, Biologie::570 Biowissenschaften, Biologie, Protein subcellular localization prediction, Cell biology, SaOS2/osteoblast cell line, Intracellular, Chromatography, Liquid |
| الوصف: |
Glycosaminoglycans (GAGs) are essential functional components of the extracellular matrix (ECM). Artificial GAGs like sulfated hyaluronan (sHA) exhibit pro-osteogenic properties and boost healing processes. Hence, they are of high interest for supporting bone regeneration and wound healing. Although sulfated GAGs (sGAGs) appear intracellularly, the knowledge about intracellular effects and putative interaction partners is scarce. Here we used an affinity-purification mass spectrometry-based (AP-MS) approach to identify novel and particularly intracellular sGAG-interacting proteins in human bone marrow stromal cells (hBMSC). Overall, 477 proteins were found interacting with at least one of four distinct sGAGs. Enrichment analysis for protein localization showed that mainly intracellular and cell-associated interacting proteins were identified. The interaction of sGAG with α2-macroglobulin receptor-associated protein (LRPAP1), exportin-1 (XPO1), and serine protease HTRA1 (HTRA1) was confirmed in reverse assays. Consecutive pathway and cluster analysis led to the identification of biological processes, namely processes involving binding and processing of nucleic acids, LRP1-dependent endocytosis, and exosome formation. Respecting the preferentially intracellular localization of sGAG in vesicle-like structures, also the interaction data indicate sGAG-specific modulation of vesicle-based transport processes. By identifying many sGAG-specific interacting proteins, our data provide a resource for upcoming studies aimed at molecular mechanisms and understanding of sGAG cellular effects. |
| DOI: |
10.17169/refubium-32793 |
| URL الوصول: |
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f605a24cf38b5bc4edb9762f50f30d2 |
| Rights: |
OPEN |
| رقم الانضمام: |
edsair.doi.dedup.....2f605a24cf38b5bc4edb9762f50f30d2 |
| قاعدة البيانات: |
OpenAIRE |