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

Korea University

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

156 Scopus citations

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
State	Published - 16 Jan 2004
Externally published	Yes

Keywords

Cytotoxicity
HLA-G
Immune evasion
MHC
NK cell
Proteolytic shedding
Quality control

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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.",

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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

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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.

KW - Cytotoxicity

KW - HLA-G

KW - Immune evasion

KW - MHC

KW - NK cell

KW - Proteolytic shedding

KW - Quality control

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

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