Is signal peptide cleavage essential for surface expression of a regulatory T cell surface protein , leucine rich repeat containing 32 ( LRRC32 )?
A cleaved signal peptide site in LRRC32 is necessary for surface localization of native LRRC32 following activation of naturally-occurring freshly-isolated regulatory T cells. LRRC32 expression appears to alter the surface expression of activation markers of T cells such as CD62L. LRRC32 surface expression may be useful as a marker that selects for more potent T(reg) populations. In summary, understanding the processing and expression of LRRC32 may provide insight into the mechanism of action of T(regs) and the refinement of immunotherapeutic strategies aimed at targeting these cells.
In patients with single- or two-vessel territory perfusion abnormalities with similar size and severity of perfusion defects, the location of defect did not impact future cardiac events. Location of myocardial perfusion defect on SPECT imaging may not be helpful in clinical decision making.