Changes in serum level and affinity for concanavalin A of human alpha 1-proteinase inhibitor in severe burn patients: relationship to natural killer cell activity.
In serum from five patients with severe burns, alpha 1-proteinase inhibitor (alpha 1-PI) was analyzed and then isolated by immunosorption chromatography. By Con A-Sepharose chromatography alpha 1-PI was separated into two types of fractions: the first containing the Con A-non-reactive isoforms and the second containing the Con A-reactive isoforms. The increase of alpha 1-PI serum level in burn patients is associated on the fifth day after the burn with a significant shift toward species enriched in bi-antennary oligosaccharides (Con A-reactive isoforms). This latter change passed very quickly and ten days after the burn, whereas the alpha 1-PI serum level was still high, the difference in proportions of Con A-reactive and non-reactive isoforms was not statistically significant. With respect to the difference in oligosaccharide structure, it appeared that the glycan moiety was involved in the inhibitory effect on natural killer cell activity. At the same concentration, purified alpha 1-PI and retained alpha 1-PI isoforms had an equal effect, whereas the non-retained alpha 1-PI isoforms were more efficient (P less than or equal to 0.01). Purified alpha 1-PI and its isoforms inhibited the natural killer cell activity in a dose-dependent manner.
Laboratoire de Chimie Biologique (Unité 38 INSERM), Faculté de Médecine, Hôpital Ste Marguerite, Marseille, France.
P J
PJ
Lejeune
B
B
Mallet
C
C
Farnarier
S
S
Kaplanski
D001798:Blood Proteins / Q000378:metabolism*; D002056:Burns / Q000097:blood* / Q000276:immunology; D003208:Concanavalin A / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D006031:Glycosylation; D006801:Humans; D007694:Killer Cells, Natural / Q000276:immunology*; D000515:alpha 1-Antitrypsin
D001798:Blood Proteins; D000515:alpha 1-Antitrypsin; D003208:Concanavalin A