KDP Poster session
Dr. Majer, Alíz
Institute of Translational Medicine, Semmelweis University, Budapest, Hungary
majer.aliz@med.semmelweis-univ.hu
Characterization of Native and Human Serum Albumin-bound Lysophosphatidic Acid Species and their Effect on the Viability of Mesenchymal Stem Cells in vitro
Aliz Majer1,2, Julianna Pesthy1, Balazs Besztercei1, Adel Hinsenkamp1, Laszlo Smeller3, Zsombor Lacza3,4, Zoltan Benyo1,5, Istvan Hornyak1,3 and Eva Ruisanchez1,5
1 Institute of Translational Medicine, Semmelweis University, Budapest, Hungary
2 Orthosera Medical Zrt., Budapest, Hungary
3 Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary
4 Institute for Sports and Health Sciences, University of Physical Education, Budapest, Hungary
5 Eötvös Loránd Research Network and Semmelweis University (ELKH-SE) Cerebrovascular and Neurocognitive Disorders Research Group, Budapest, Hungary
Szóbeli
KDP Poster session
Introduction: Scaffolds can provide a favorable environment for cell attachment, differentiation, proliferation, and migration in vitro and in vivo. In the serum, lysophosphatidic acid (LPA), a naturally occurring bioactive phospholipid binds primarily to albumin. Osteoblasts produce LPA, which is present in bone tissue, and during certain pathological conditions like fracture healing, bone cells are exposed to elevated levels of platelet-derived LPA. LPA affects proliferation, differentiation, survival, and migration in various bone cell types. The proliferation, migration, and differentiation of human bone marrow mesenchymal stem cells are crucial for the healing process.
Aims: This study aimed to examine the biocompatibility of LPA and determine the impact of different LPA species on the proliferation and migration of human bone marrow-derived mesenchymal stem cells (hBM-dMSCs) for LPA and human serum albumin (HSA) containing bone scaffold development.
Methods: Fourier-transform infrared (FTIR) spectroscopy was used to assess the formation of HSA-LPA complexes. XTT assay was conducted to evaluate the effect of various concentrations (0.1-0.3-1-3-10 µM) of 18:1, 18:2, or 16:0 LPA, alone or combined with 4% HSA, on cell viability and proliferation. Wound healing assay was performed to examine the impact of 1-3-10 µM concentrations of 18:1, 18:2, and 16:0 LPA on cell migration.
Results: The FTIR spectra of LPA-HSA compositions displayed distinct changes compared to HSA alone, indicating complex formation between the components. Concentrations of 18:1, 18:2, and 16:0 LPA up to 10 µM showed no cytotoxic effects. The different LPA species, when administered in the presence of HSA, increased the proliferation of hBM-dMSCs in a dose-dependent manner but had no effect on cell migration.
Conclusions: Our experimental results demonstrate that concentrations up to 10 µM of 18:1, 18:2, and 16:0 LPA species are non-cytotoxic. Furthermore, the different LPA species promote the proliferation of MSCs in a dose-dependent manner when combined with HSA. These findings hold promise for the potential in vivo application of LPA-HSA complexes in bone regeneration.
Fundation: EFOP-3.6.3-VEKOP-16-2017-00009, TKP2021-EGA-25, 2020-1.1.6-JÖVŐ-2021-00010, 2020-1.1.6-JÖVŐ-2021-00013, KDP-2020, OTKA K-125174, PD-132851, K-135683, K-139230, Biosafety H020-952520.
Semmelweis University, Doctoral School of Theoretical and Translational Medicine
Éva Ruisanchez and István Hornyák
Szabad
elfogadva
poszter
nem rendelkezett róla
4812
09:00
09:05
Aliz Majer1,2, Julianna Pesthy1, Balazs Besztercei1, Adel Hinsenkamp1, Laszlo Smeller3, Zsombor Lacza3,4, Zoltan Benyo1,5, Istvan Hornyak1,3 and Eva Ruisanchez1,5
1 Institute of Translational Medicine, Semmelweis University, Budapest, Hungary
2 Orthosera Medical Zrt., Budapest, Hungary
3 Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary
4 Institute for Sports and Health Sciences, University of Physical Education, Budapest, Hungary
5 Eötvös Loránd Research Network and Semmelweis University (ELKH-SE) Cerebrovascular and Neurocognitive Disorders Research Group, Budapest, Hungary