|Detection of PD‑1 in Mouse Splenocytes by Flow Cytometry. Mouse splenocytes treated with 5 μg/mL PHA for 3 days were stained with Rat Anti-Mouse PD‑1 Monoclonal Antibody (Catalog # MAB7738, filled histogram) or isotype control antibody (Catalog # MAB006, open histogram), followed by Allophycocyanin-conjugated Anti-Rat IgG Secondary Antibody (Catalog # F0113).|
Programmed Death-1 (PD-1) is a type I transmembrane protein belonging to the CD28/CTLA-4 family of immunoreceptors that mediate signals for regulating immune responses (1). Other members of this family include CD28, CTLA-4, and ICOS (2-4). PD-1 is most closely related to CTLA-4 and shares approximately 24% amino acid (aa) sequence identity. The mouse PD-1 gene encodes a 288 aa protein with a putative 20 aa signal peptide, a 149 aa extracellular region with one immunoglobulin-like V-type domain, a 21 aa transmembrane domain, and a 98 aa cytoplasmic region. The cytoplasmic tail contains two tyrosine residues that form the immunoreceptor tyrosine-based inhibitory motif (ITIM) and immunoreceptor tyrosine-based switch motif (ITSM) that are important in mediating PD-1 signaling. Mouse and human PD-1 share approximately 69% aa sequence identity. Two B7 family proteins, PD-L1 (also called B7-H1) and PD-L2, have been identified as PD-1 ligands (5, 6). PD-1 is expressed on activated T cells, B cells, myeloid cells, and on a subset of thymocytes. PD-1 deficient mice have a defect in peripheral tolerance and spontaneously develop autoimmune diseases. Binding of PD-1 to PD-L1 or PD-L2 results in the inhibition of TCR-mediated proliferation and cytokine production as well as BCR-mediated signaling. PD-1 likely has an inhibitory role in regulating immune responses (1-4).
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