Soluble HLA proteins with bound peptides are released from the cell surface by the membrane metalloproteinase.

Abstract:

:The metalloproteinase (MPase)-mediated pathway of MHC class I processing is a distinct cellular mechanism that generates soluble HLA proteins. It has been implicated in modulation of immune responses induced during transplantation events. It is, therefore, important to define the characteristics of soluble HLA species produced by the MPase pathway. We have previously shown that some mutant peptide-conformed beta(2)-microglobulin (beta(2)m) free heavy chains (HC) with lower affinity for beta(2)m can be released into supernatants by the MPase. These soluble conformed beta(2)m-free HC intermediates can re-associate with beta(2)m in solution giving rise to beta(2)m-associated HC. We now demonstrate that also nonmutant soluble conformed beta(2)m-free HC can be detected in supernatants of activated cells. These soluble HC intermediates appear to have bound peptides and readily re-associate with exogenous beta(2)m producing beta(2)m-associated HC that are stable at physiologic temperature. Thus, generation of peptide-conformed beta(2)m-free HC intermediates is an important step, which precedes generation of both soluble beta(2)m-free and beta(2)m-associated HC by the MPase pathway operating in activated cells.

journal_name

Hum Immunol

journal_title

Human immunology

authors

Demaria S,Bushkin Y

doi

10.1016/s0198-8859(00)00213-5

subject

Has Abstract

pub_date

2000-12-01 00:00:00

pages

1332-8

issue

12

eissn

0198-8859

issn

1879-1166

pii

S0198885900002135

journal_volume

61

pub_type

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