Open AccessComparative proteomic analysis of osteogenic differentiated human adipose tissue and bone marrow‐derived stromal cells
Author(s) -
Dadras Mehran,
May Caroline,
Wagner Johannes Maximilian,
Wallner Christoph,
Becerikli Mustafa,
Dittfeld Stephanie,
Serschnitzki Bettina,
Schilde Lukas,
Guntermann Annika,
Sengstock Christina,
Köller Manfred,
Seybold Dominik,
Geßmann Jan,
Schildhauer Thomas Armin,
Lehnhardt Marcus,
Marcus Katrin,
Behr Björn
Publication year - 2020
Publication title -
journal of cellular and molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.44
H-Index - 130
eISSN - 1582-4934
pISSN - 1582-1838
DOI - 10.1111/jcmm.15797
Subject(s) - stromal cell , mesenchymal stem cell , bone marrow , integrin , microbiology and biotechnology , adipose tissue , cell , proteomics , stem cell , chemistry , biology , immunology , cancer research , biochemistry , gene
Mesenchymal stromal cells are promising candidates for regenerative applications upon treatment of bone defects. Bone marrow‐derived stromal cells (BMSCs) are limited by yield and donor morbidity but show superior osteogenic capacity compared to adipose‐derived stromal cells (ASCs), which are highly abundant and easy to harvest. The underlying reasons for this difference on a proteomic level have not been studied yet. Human ASCs and BMSCs were characterized by FACS analysis and tri‐lineage differentiation, followed by an intraindividual comparative proteomic analysis upon osteogenic differentiation. Results of the proteomic analysis were followed by functional pathway analysis. 29 patients were included with a total of 58 specimen analysed. In these, out of 5148 identified proteins 2095 could be quantified in >80% of samples of both cell types, 427 in >80% of ASCs only and 102 in >80% of BMSCs only. 281 proteins were differentially regulated with a fold change of >1.5 of which 204 were higher abundant in BMSCs and 77 in ASCs. Integrin cell surface interactions were the most overrepresented pathway with 5 integrins being among the proteins with highest fold change. Integrin 11a, a known key protein for osteogenesis, could be identified as strongly up‐regulated in BMSC confirmed by Western blotting. The integrin expression profile is one of the key distinctive features of osteogenic differentiated BMSCs and ASCs. Thus, they represent a promising target for modifications of ASCs aiming to improve their osteogenic capacity and approximate them to that of BMSCs.