Proteomic analysis of secreted proteins derived from amniotic fluid stem cells
5
Issued Date
2025-01-01
Resource Type
ISSN
0302766X
eISSN
14320878
Scopus ID
2-s2.0-105007315486
Journal Title
Cell and Tissue Research
Rights Holder(s)
SCOPUS
Bibliographic Citation
Cell and Tissue Research (2025)
Suggested Citation
Phermthai T., Chuaynarong P., Wichitwiengrat S., Phermthai K., Roytrakul S., Chitthira T., Thongbopit S. Proteomic analysis of secreted proteins derived from amniotic fluid stem cells. Cell and Tissue Research (2025). doi:10.1007/s00441-025-03984-0 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/110645
Title
Proteomic analysis of secreted proteins derived from amniotic fluid stem cells
Corresponding Author(s)
Other Contributor(s)
Abstract
Mesenchymal stem cells (MSCs) show promising therapeutic effects due to the proteins they secrete. However, MSCs from different sources exhibit only 60% similarity of proteins they secrete, suggesting that unique proteins may offer distinct therapeutic properties based on their origin. Amniotic fluid-derived MSCs (AFSCs) are promising for treating degenerative diseases and are unique in providing sufficient cells for fetal therapies. Nevertheless, their proteomic profiles remain largely undefined. This study investigated the proteomic profiles of bioactive molecules secreted by AFSCs (AFSC-se) using liquid chromatography and mass spectrometry, along with bioinformatics tools for protein function analysis. We identified over 2000 proteins in the AFSC-se that are involved in various mechanisms supporting organ development and function. The top three proteins identified were associated with organelle fusion, forebrain morphogenesis, and response to parathyroid hormone. Our findings indicate that AFSC-se has the ability to inhibit inflammation and apoptosis, which corresponds to 7.8% of the identified proteins involved in pathways related to these therapeutic effects. Furthermore, we discovered that 20% of identified proteins are associated with brain functions including synaptogenesis, neurogenesis, and neuroprotection. In conclusion, the proteomic profile of AFSC-se indicates its potential therapeutic effects. The significant presence of neuro-related proteins in AFSC-se suggests that AFSC-se may be a promising candidate for treating neurological diseases. Our work addresses existing knowledge gaps in this field.