14-3-3γ Knockdown promotes matrix mineralization in human mesenchymal stromal cells.
Rivera L., Müller S., Uhart M., Bustos DM.
Laboratory Study, published in Cell Death Dis (2026) — summary generated from the PubMed abstract.
Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.
- Level A · Stronger Clinical Evidence
- Level B · Emerging clinical evidence with positive signals
- Level C · Early human research exploring benefits
- Level D · Scientific groundwork from lab and animal studies
- Emerging · Emerging topic under active research
This page is generated from the PubMed record. The Thai description is an automated summary of bibliographic fields and the abstract, not a full translation, and is not medical advice.
- Study type
- Laboratory Study
- Journal
- Cell Death Dis (2026)
- Country
- England
- Reported sample size
- —
- Source database
- PubMed
- PMID
- 41896518
- PMCID
- PMC13149861
- DOI
- 10.1038/s41419-026-08540-4
Abstract (original English)
The 14-3-3 proteins are emerging as important modulators of osteoblast differentiation and function. Recent studies highlight specific roles of 14-3-3 paralogs in bone physiology, with their dysregulation linked to impaired skeletal homeostasis and bone-related diseases. Among these, the 14-3-3γ paralog has been implicated in bone formation, though its precise role remains unclear.In this study, we investigated the function of 14-3-3γ in the osteogenic differentiation of human adipose-derived mesenchymal stem/stromal cells (hASCs). Using an adenoviral system, we knocked down 14-3-3γ and assessed osteogenic markers. Tissue-Nonspecific Alkaline Phosphatase (TNAP) activity, RUNX2 protein levels, and the expression of osteogenic genes (BGLAP, SPP1) were analyzed during matrix maturation and mineralization. Calcium and collagen deposition were evaluated via Alizarin Red S and Aniline Blue staining, respectively, and compared with cells overexpressing recombinant 14-3-3γ. Proteomic profiling via quantitative mass spectrometry was performed to identify protein changes after 14-3-3γ silencing. Subcellular localization of endogenous 14-3-3γ was also examined during differentiation. Knockdown of 14-3-3γ enhanced TNAP activity and increased matrix mineralization, while its overexpression suppressed these processes. Proteomic analysis revealed enrichment of proteins related to endoplasmic
What this study does not prove
- • This study does not prove SVF is an approved treatment or a replacement for standard care.
- • This is preclinical work; animal or laboratory results cannot be applied to humans.
Evidence level
Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.
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