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Isolation of Myeloid Dendritic Cells and Epithelial Cells from Human Thymus
Published on: September 20, 2013
Identification of a 16-kDa thymocyte membrane glycoprotein involved in the thymocyte/thymic medullary epithelial cell
J G Amarante-Mendes1, C Couture, E F Potworowski
1Institut Armand-Frappier, Laval, Québec, Canada.
Insights
Researchers identified a 16-kDa thymocyte glycoprotein involved in lymphoepithelial interactions. This molecule binds to epithelial cells and a specific adhesion molecule, suggesting its role in thymic cell binding.
Area of Science:
- Immunology
- Cell Biology
- Molecular Biology
Background:
- Lymphoepithelial interactions in the thymus are crucial for T-cell development.
- Previous studies identified CD4+ CD8+ thymocytes and a medullary epithelial cell line (E-5) involved in these interactions.
- The gp23/45 epithelial adhesion molecule and an unknown thymocyte receptor mediate this interaction.
Purpose of the Study:
- To identify the unknown thymocyte receptor involved in lymphoepithelial interactions.
- To characterize the molecular basis of binding between thymocytes and thymic epithelial cells.
Main Methods:
- Biochemical characterization of thymocyte surface glycoproteins.
- Binding assays using epithelial cells (E-5) and purified adhesion molecules (gp23/45).
- Analysis of thymic lymphoma cell lines (Ti-6) for surface glycoproteins.
Main Results:
- A 16-kDa thymocyte surface glycoprotein was identified.
- This 16-kDa glycoprotein binds to both E-5 epithelial cells and purified gp23/45.
- A thymic lymphoma cell line (Ti-6) that interacts with E-5 cells also expresses this 16-kDa glycoprotein.
Conclusions:
- The 16-kDa thymocyte surface glycoprotein is a key molecule mediating the interaction between thymocytes and thymic epithelium.
- This glycoprotein likely functions as the previously unknown thymocyte receptor for the gp23/45 adhesion molecule.
- The findings elucidate a critical molecular mechanism in thymic lymphocyte-epithelial cell adhesion.
Abstract:
We have previously described a type of lymphoepithelial interaction involving CD4+ CD8+ thymocytes and a medullary epithelial cell line (E-5). This interaction is mediated by the recently described gp23/45 epithelial adhesion molecule and an as yet unknown thymocyte receptor. The present work describes a thymocyte surface glycoprotein of 16 kDa which binds both to E-5 cells and to the purified gp23/45 adhesion molecule. In addition, a thymic lymphoma cell line (Ti-6), which interacts with the E-5 cells via the gp23/45 receptor, also present a 16-kDa glycoprotein on its surface. Taken together, the data suggest that the 16-kDa thymocyte surface glycoprotein participates in the binding between these cells and the thymic epithelium.
