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Peer-reviewedCC BYBone reports

A proteomic roadmap of SaOS-2 osteoblast-to-osteocyte-like differentiation

  • Britta Eggers1
  • Sascha Roocke1
  • Svitlana Rozanova1
  • Karin Schork1
  • Maximilian Schütte1
  • Mira Struwe1
  • Paul Zandner1
  • Maximilian Hausherr1
  • Greta Domroese1
  • Morris Gellisch2
  • Martin Eisenacher1
  • Jacqueline Heinen-Weiler3
4 more authors
  • Carsten Theiss3
  • Annette Richter-Unruh4
  • Katalin Barkovits1
  • Katrin Marcus1
4 affiliations
  1. 1Medizinisches Proteom-Center, Medical Faculty, Ruhr University Bochum, Bochum, 44801, Germany
  2. 2Department of Anatomy and Molecular Embryology, Institute of Anatomy, Medical Faculty, Ruhr University Bochum
  3. 3Medical Imaging Center (MIC), Electron Microscopy Medical Analysis - Core Facility (EMMA ), Medical Faculty, Ruhr University Bochum, 44801, Bochum, Germany
  4. 4Clinic for Children and Adolescents, Pediatric Endocrinology, St. Josef-Hospital, Bochum, D-44791, Germany
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Abstract

Mineralized bone tissue is essential for skeletal integrity, mechanical stability, and mineral homeostasis. Osteocytes, the most abundant bone cell type, play central roles in bone remodeling and endocrine regulation but remain difficult to investigate because of their embedded localization within the mineralized matrix. Consequently, the molecular mechanisms underlying osteoblast-to-osteocyte differentiation remain incompletely understood.

Here, we performed a comprehensive quantitative proteomic analysis of the widely used human SaOS-2 cell line during osteoblast-to-osteocyte-like differentiation. More than 5000 proteins were quantified, providing a comprehensive proteomic roadmap of this differentiation process. Proteomic profiling demonstrated extensive molecular remodeling accompanied by extracellular matrix reorganization and dynamic changes in collagen abundance. Although differentiated SaOS-2 cells retained characteristics of late osteoblasts and did not fully recapitulate the phenotype of mature osteocytes, they acquired a distinct osteocyte-like proteomic signature. Furthermore, we identified and orthogonally validated several candidate protein markers associated with the osteoblast and osteocyte-like states.

Together, our study provides the first comprehensive protein-level characterization of SaOS-2 osteoblast-to-osteocyte-like differentiation. Beyond improving the molecular characterization of this widely used model, it provides a valuable resource for future studies investigating bone biology, extracellular matrix remodeling, and skeletal disease.

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Cite

BibTeXRIS
BibTeX
@article{eggers2026proteomic,
  title = {{A proteomic roadmap of SaOS-2 osteoblast-to-osteocyte-like differentiation}},
  author = {Britta Eggers and Sascha Roocke and Svitlana Rozanova and Karin Schork and Maximilian Schütte and Mira Struwe and Paul Zandner and Maximilian Hausherr and Greta Domroese and Morris Gellisch and Martin Eisenacher and Jacqueline Heinen-Weiler and Carsten Theiss and Annette Richter-Unruh and Katalin Barkovits and Katrin Marcus},
  journal = {Bone reports},
  year = {2026},
  month = oct,
  doi = {10.1016/j.bonr.2026.101961},
  url = {https://europepmc.org/article/PMC/PMC13722065},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - A proteomic roadmap of SaOS-2 osteoblast-to-osteocyte-like differentiation
AU  - Britta Eggers
AU  - Sascha Roocke
AU  - Svitlana Rozanova
AU  - Karin Schork
AU  - Maximilian Schütte
AU  - Mira Struwe
AU  - Paul Zandner
AU  - Maximilian Hausherr
AU  - Greta Domroese
AU  - Morris Gellisch
AU  - Martin Eisenacher
AU  - Jacqueline Heinen-Weiler
AU  - Carsten Theiss
AU  - Annette Richter-Unruh
AU  - Katalin Barkovits
AU  - Katrin Marcus
PY  - 2026
DA  - 2026/10/23
JO  - Bone reports
DO  - 10.1016/j.bonr.2026.101961
UR  - https://europepmc.org/article/PMC/PMC13722065
AB  - Mineralized bone tissue is essential for skeletal integrity, mechanical stability, and mineral homeostasis. Osteocytes, the most abundant bone cell type, play central roles in bone remodeling and endocrine regulation but remain difficult to investigate because of their embedded localization within the mineralized matrix. Consequently, the molecular mechanisms underlying osteoblast-to-osteocyte differentiation remain incompletely understood.  Here, we performed a comprehensive quantitative proteomic analysis of the widely used human SaOS-2 cell line during osteoblast-to-osteocyte-like differentiation. More than 5000 proteins were quantified, providing a comprehensive proteomic roadmap of this differentiation process. Proteomic profiling demonstrated extensive molecular remodeling accompanied by extracellular matrix reorganization and dynamic changes in collagen abundance. Although differentiated SaOS-2 cells retained characteristics of late osteoblasts and did not fully recapitulate the phenotype of mature osteocytes, they acquired a distinct osteocyte-like proteomic signature. Furthermore, we identified and orthogonally validated several candidate protein markers associated with the osteoblast and osteocyte-like states.  Together, our study provides the first comprehensive protein-level characterization of SaOS-2 osteoblast-to-osteocyte-like differentiation. Beyond improving the molecular characterization of this widely used model, it provides a valuable resource for future studies investigating bone biology, extracellular matrix remodeling, and skeletal disease.
SN  - 2352-1872
ER  -