Soluble HLA-G generated by proteolytic shedding inhibits NK-mediated cell lysis

Gyu Man Park; Sunray Lee; Boyoun Park; Eunkyung Kim; Jinwook Shin; Kwangmin Cho; Kwangseog Ahn

doi:10.1016/j.bbrc.2003.11.153

Soluble HLA-G generated by proteolytic shedding inhibits NK-mediated cell lysis

Gyu Man Park, Sunray Lee, Boyoun Park, Eunkyung Kim, Jinwook Shin, Kwangmin Cho, Kwangseog Ahn

Research output: Contribution to journal › Article › peer-review

152 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	606-611
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	313
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2003.11.153
Publication status	Published - 2004 Jan 16

Bibliographical note

Funding 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

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2003.11.153

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title = "Soluble HLA-G generated by proteolytic shedding inhibits NK-mediated cell lysis",

abstract = "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.",

author = "Park, {Gyu Man} and Sunray Lee and Boyoun Park and Eunkyung Kim and Jinwook Shin and Kwangmin Cho and Kwangseog Ahn",

note = "Funding 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.",

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AU - Park, Gyu Man

AU - Lee, Sunray

AU - Park, Boyoun

AU - Kim, Eunkyung

AU - Shin, Jinwook

AU - Cho, Kwangmin

AU - Ahn, Kwangseog

N1 - Funding 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.

PY - 2004/1/16

Y1 - 2004/1/16

N2 - 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.

AB - 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.

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Soluble HLA-G generated by proteolytic shedding inhibits NK-mediated cell lysis

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

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