Gene expression of Semaphorin 7A in human dental follicle cells

Takahashi, Kosuke; Ogura, Naomi; Kato, Ryo; Tomoki, Risa; Eda, Takashi; Okada, Hiroshi; Ito, Koichi; Kondoh, Toshirou

doi:10.1016/j.joms.2014.06.349

Cited by 1 publication

(1 citation statement)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Classic osteogenic factors observed in the hMSCs secretomes were also absent in FetMSCs secretome. Nevertheless, we observed some other proteins involved in osteogenic differentiation: COL6A1 [32], MMP2 [33], tenascin [34], semaphorin-7A [35], stanniocalcin-1 [36], exostosin-1 and Exostosin-2 [37]. On the other hand, inhibitors of osteogenic differentiation were also observed: gremlin-1 [38], insulin-like growth factor binding protein-3 [39] and twisted gastrulation protein homolog 1 [40].…”

Section: Discussionmentioning

confidence: 78%

Proteomic Profiling of the Human Fetal Multipotent Mesenchymal Stromal Cells Secretome

et al. 2020

View full text Add to dashboard Cite

Secretome of multipotent mesenchymal stromal cells (MSCs) is actively used in biomedical applications such as alveolar bone regeneration, treatment of cardiovascular disease, and neurodegenerative disorders. Nevertheless, hMSCs have low proliferative potential and production of the industrial quantity of their secretome might be challenging. Human fetal multipotent mesenchymal stromal cells (FetMSCs) isolated from early human embryo bone marrow are easy to expand and might be a potential source for pharmaceutical substances production based on their secretome. However, the secretome of FetMSCs was not previously analyzed. Here, we describe the secretome of FetMSCs using LC-MALDI shotgun proteomics. We identified 236 proteins. Functional annotation of the identified proteins revealed their involvement in angiogenesis, ossification, regulation of apoptosis, and immune response processes, which made it promising for biomedical applications. The proteins identified in the FetMSCs secretome are involved in the same biological processes as proteins from previously described adult hMSCs secretomes. Nevertheless, many of the common hMSCs secretome components (such as VEGF, FGF, Wnt and TGF-β) have not been identified in the FetMSCs secretome.

show abstract