| 背景信息 |
C-type lectin domain family 12 member A (CLEC12A), also known as MICL or CLL-1, is a type II transmembrane glycoprotein and an inhibitory member of the C-type lectin-like receptor superfamily. Predominantly expressed on myeloid cells, it functions as a pattern recognition receptor that binds diverse ligands, including monosodium urate (MSU) crystals and mycobacterial mycolic acid. Upon ligand engagement, CLEC12A undergoes Src-dependent phosphorylation of its cytoplasmic immunoreceptor tyrosine-based inhibitory motif (ITIM), recruiting phosphatases SHP-1 and SHP-2 to dampen pro-inflammatory signaling. This mechanism suppresses neutrophil activation and cytokine release while facilitating antigen cross-presentation and antibacterial autophagy. Clinically, the downregulation of CLEC12A exacerbates inflammatory conditions such as gouty arthritis. Additionally, CLEC12A is a well-established cell surface marker for leukemic blasts in acute myeloid leukemia (AML). |