Human leukocyte antigen C alpha chain (HLA-C)

Human leukocyte antigen C alpha chain (HLA-C) is a glycoprotein encoded within the major histocompatibility complex (MHC) on chromosome 6[1][4][6][8]. It forms a cell surface heterodimer with beta-2 microglobulin and is expressed on nearly all nucleated cells[3][4][6]. HLA-C presents short intracellular peptides (typically 8–10 amino acids) to cytotoxic T lymphocytes, enabling immune recognition and destruction of infected or aberrant cells[4][5][8]. Its unique feature among HLA class I molecules is acting as a ligand for killer-cell immunoglobulin-like receptors (KIRs) on natural killer cells, critically regulating innate immunity and shaping tolerance or cytotoxic responses[1][2][8]. HLA-C exhibits notable polymorphism, affecting disease susceptibility, transplantation compatibility, and immune control of cancer and infections[1][8]. Its expression and peptide-binding properties are highly allele-specific and subject to epigenetic regulation, which can result in immune evasion by tumors or viruses, and influence therapeutic efficacy and safety[1][5][8].

Other names

HLA-CHLACHLA-CwHuman leukocyte antigen CD6S204HLA-JY3HLA class I histocompatibility antigen, C alpha chainHLA-C antigenMHC class I antigen heavy chain HLA-Chuman leukocyte antigen-C alpha chainmajor histocompatibility antigen HLA-CPSORS1

Immune modulation via alteration of HLA-C/KIR interactions, affecting NK cell activation or inhibition. Modulation of antigen presentation to cytotoxic T cells for immunotherapy or tolerance induction.