Deubiquitinating Enzyme USP7 Is Required for Self-Renewal and Multipotency of Human Bone Marrow-Derived Mesenchymal Stromal Cells

Ubiquitin-specific protease 7 (USP7) is highly expressed in a variety of malignant tumors. However, the role of USP7 in regulating self-renewal and differentiation of human bone marrow derived mesenchymal stromal cells (hBMSCs) remains unknown. Herein, we report that USP7 regulates self-renewal of h...

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Bibliographic Details
Published in:International journal of molecular sciences 2022-08, Vol.23 (15), p.8674
Main Authors: Kim, You Ji, Park, Kwang Hwan, Lee, Kyoung-Mi, Chun, Yong-Min, Lee, Jin Woo
Format: Article
Language:English
Subjects:
Adipocytes
Biomedical materials
Bone marrow
Cell self-renewal
Cell therapy
Differentiation
Gene expression
Investigations
Mesenchyme
Oxidative stress
Proteins
Senescence
Stem cells
Stromal cells
Tumors
Ubiquitin
Ubiquitin-specific proteinase
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Summary:Ubiquitin-specific protease 7 (USP7) is highly expressed in a variety of malignant tumors. However, the role of USP7 in regulating self-renewal and differentiation of human bone marrow derived mesenchymal stromal cells (hBMSCs) remains unknown. Herein, we report that USP7 regulates self-renewal of hBMSCs and is required during the early stages of osteogenic, adipogenic, and chondrogenic differentiation of hBMSCs. USP7, a deubiquitinating enzyme (DUB), was found to be downregulated during hBMSC differentiation. Furthermore, USP7 is an upstream regulator of the self-renewal regulating proteins SOX2 and NANOG in hBMSCs. Moreover, we observed that SOX2 and NANOG are poly-ubiquitinated and their expression is downregulated in USP7-deficient hBMSCs. Overall, this study showed that USP7 is required for maintaining self-renewal and multipotency in cultured hBMSCs. Targeting USP7 might be a novel strategy to preserve the self-renewal capacity of hBMSCs intended for stem cell therapy.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms23158674