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 Immunoljournal_title
Human immunologyauthors
Demaria S,Bushkin Ydoi
10.1016/s0198-8859(00)00213-5subject
Has Abstractpub_date
2000-12-01 00:00:00pages
1332-8issue
12eissn
0198-8859issn
1879-1166pii
S0198885900002135journal_volume
61pub_type
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