Background:
Laminin, a member of the Extracellular Matrix (ECM), is a glycoprotein
that is used as a factor that affects cell adhesion, proliferation, survival, and differentiation. Of
these, five globular domains (LG domains) of the alpha chain play an important role in influencing
the cell by binding to the integrin.
Objective:
This study aimed to evaluate the ability of globular domains 1-3 of laminin alpha2
(rhLAMA2LG1-3) in maintaining the pluripotency of human Mesenchymal Stem Cells (hMSCs),
which are widely used in regenerative medicine.
Methods:
hMSCs were grown in the medium supplemented with rhLAMA2LG1-3, then the effect of
the protein on hMSCs were confirmed through cell adhesion assay, proliferation assay and RTPCR.
Results:
rhLAMA2LG1-3 expressed in Escherichia coli has a molecular weight of 70 kDa, at 1 µg/ml
concentration of rhLAMA2LG1-3, the attachment and proliferation of hMSCs were approximately
3.18-fold and 1.67-fold, respectively, more efficient than those of untreated controls. In addition,
the undifferentiated state and degree of stemness of hMSCs were measured, on the basis of CD90
and CD105 levels. In the rhLAMA2LG1-3-treated hMSCs, the expression levels of CD90 and CD105
increased by 2.83-fold and 1.62-fold, respectively, compared to those in untreated controls.
Conclusion:
rhLAMA2LG1-3 can be potentially used in stem cell therapy to improve the viability
and maintain the undifferentiated state of hMSCs.
Protein Nanofibril Assemblies Templated by Graphene Oxide Nanosheets Accelerate Early Cell Adhesion and Induce Osteogenic Differentiation of Human Mesenchymal Stem Cells