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Updated: Aug 13, 2026
Isolation of Human Lymphatic Endothelial Cells by Multi-parameter Fluorescence-activated Cell Sorting
Published on: May 1, 2015
Interaction between endothelium and CD4+CD45RA+ lymphocytes. Role of the human CD38 molecule
U Dianzani1, A Funaro, D DiFranco
1Department of Medical Science, Torino University, Novara, Italy.
Insights
CD38, a lymphocyte marker, inhibits binding to endothelial cells, suggesting a role in lymphocyte migration. This function is distinct from T-cell activation, highlighting CD38
Area of Science:
- Immunology
- Cell Biology
Background:
- CD38 is a type II transmembrane glycoprotein used as a marker for lymphocytes and plasma cells.
- Its precise functional role and natural ligand remain unknown, though it transduces activation signals to lymphocytes.
Purpose of the Study:
- To investigate the functional role of CD38 in lymphocyte activation and migration.
- To determine if CD38 engagement affects the interaction between lymphocytes and endothelial cells.
Main Methods:
- Flow cytometry to analyze CD38 expression on CD4+CD45RA+ and CD4+CD45R0+ cells.
- Monoclonal antibody (mAb) cross-linking of CD38 to assess T-cell activation and endothelial cell binding.
- Inhibition assays using a hybrid cell line (CP410.A10) and its CD38- subclone (CP14).
- Binding assays between lymphocytes and endothelial cells under various conditions (temperature, rocking).
Main Results:
- CD38 is preferentially expressed on CD4+CD45RA+ (naive) cells, not CD4+CD45R0+ (memory) cells.
- CD38 engagement by mAb did not overcome the hyporesponsiveness of naive T cells to activation stimuli.
- CD38 engagement specifically inhibited binding of naive T cells to human vein endothelial cells.
- This inhibitory effect on cell binding was observed in a CD38+ hybrid cell line but not its CD38- counterpart.
- CD38-mediated inhibition of binding was apparent under conditions minimizing integrin function, suggesting a selectin-like mechanism.
- CD38 mediates weak cell binding to endothelium effective under dynamic conditions.
Conclusions:
- CD38 plays a role in lymphocyte migration, specifically by modulating their binding to endothelial cells.
- CD38's function in cell adhesion appears distinct from its role in T-cell activation.
- The mechanism of CD38-mediated adhesion resembles that of selectins, involved in leukocyte rolling and homing.
Abstract:
CD38 is a type II transmembrane glycoprotein, which is widely used as a marker for immature and activated lymphocytes, as well as plasma cells. Although its functional role and natural ligand are not known, CD38 has been shown to transduce activation signals to lymphocytes. Our work shows that CD38 is preferentially expressed by CD4+CD45RA+ cells, but not by CD4+CD45R0+ cells. CD4+CD45RA+ cells are reported to respond poorly to stimuli acting through the CD3/TCR in vitro and to display unique migration pathways in vivo. Cross-linking of CD38 by mAb did not overcome the hyporesponsiveness of CD4+ resting/naive cells to several activation stimuli; in contrast, CD38 engagement by mAb specifically inhibited their binding with human vein endothelial cells. These data suggest that CD38 may play a role in lymphocyte migration. The same inhibitory effect was detected on the (human x mouse) hybrid cell line CP410.A10, which expresses human CD38, but not on its CD38- subclone CP14. CD38 mAb did not inhibit the conventional binding assay between endothelium and several human CD38+ T and B cell lines. However, the inhibition was apparent when the binding assay was performed at 4 degrees C on a rocking shelf, conditions that minimized integrin function. These data suggest that CD38 mediates weak cell binding to endothelium, which is effective even in dynamic conditions. These features are reminiscent of those exerted by selectins, which are adhesion molecules that account for leukocyte rolling on vascular endothelial cells and play an important role in lymphocyte homing.
