In contrast to the classical HLA class Ia molecules, the nonclassical HLA-G primary transcript is alternatively spliced to generate several mRNAs that encode four membrane-bound and three soluble isoforms. This study demonstrated that the soluble form of HLA-G can also be generated by metalloproteinase-dependent shedding at post-translational level. These soluble HLA-G1 molecules generated by the cleavage of membrane-bound HLA-G1 associate with β2-microglobulin and contain bound peptides that are stable at physiological conditions. This report further showed that the soluble HLA-G1 is able to protect HLA class I-negative K562 cells from NK lysis, suggesting that soluble HLA-G could act as an immunoregulator in NK cell recognition and possibly in other immune responses.
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - 2004 Jan 16|
Bibliographical noteFunding Information:
The authors thank Drs. Daniel Geraghty and Michael McMaster for providing valuable reagents and the LG-Yeonam Cultural Foundation for the assistance. This work was supported by grants from the Molecular and Cellular BioDiscovery Research Program (M10106000054) and the Center for Functional Analysis of Human Genome (FG0003010011) of the Ministry of Science and Technology.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology