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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Truncated HLA-G isoforms are retained in the endoplasmic reticulum and insufficiently provide HLA-E ligands.
Hum. Immunol. 65, 200-208 (2004)
The preferential expression of the non-polymorphic human leukocyte antigen G (HLA-G) on invading extravillous cytotrophoblast cells that are, with the exception of HLA-C and -E, HLA class I negative led to the hypothesis that HLA-G plays a major role in controlling the effector functions of the large granular leukocytes (LGL), a specialized natural killer (NK) cell population present in large numbers in the decidua. Transcription of the HLA-G gene is characterized by extensive alternative splicing producing at least seven potentially membrane bound or secreted isoforms. Except for HLA-G1 and its soluble variant (HLA-G1s), there is still dispute as to whether any of the other isoforms displays a major immunological function. Here we describe that the membrane-bound isoforms HLA-G2, -G3, and G4 as well as the soluble variant of HLA-G2 (HLA-G2s) do not egress the endoplasmic reticulum as determined by Endo H sensitivity assays. Moreover these isoforms seem not to have a major immunological function with respect to NK cell inhibition by providing a ligand for HLA-E, which would allow the interaction of this molecule with the inhibitory CD94/NKG2A NK cell receptor.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
HLA-G; HLA-E; NK cells; antigen processing; MHC
ISSN (print) / ISBN
0198-8859
e-ISSN
0198-8859
Zeitschrift
Human Immunology
Quellenangaben
Band: 65,
Heft: 3,
Seiten: 200-208
Verlag
Elsevier
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Molecular Immunology (IMI)