Alpha 1-antitrypsin--complexation and inactivation in the uterine fluid of IUD-users.
Electrophoretic homogeneity of alpha 1-antitrypsin (alpha 1-AT) was studied in the uterine fluid from two groups of normal women; one group was comprised of IUD-users, the other non-users. Alpha 1-AT was found in its free and active form in non-users. In IUD-users, one fraction was complexed by granulocyte elastase and neutral proteinase. The other fraction had the same electrophoretic mobility as the native inhibitor, but was inactive, as determined from trypsin inhibition studies. This may explain the finding of elastase activity together with non-complexed alpha 1-AT in some samples from IUD-users. It is concluded that uterine fluid in IUD-users possess a minimal, if any, proteinase inhibiting potential. Non-inhibited activity of granulocyte proteinases in the uterine cavity may influence hemostasis of the endometrium.
D000293:Adolescent; D000328:Adult; D001826:Body Fluids / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D005260:Female; D006098:Granulocytes / Q000201:enzymology; D006801:Humans; D007123:Immunoelectrophoresis, Two-Dimensional; D007435:Intrauterine Devices, Copper; D014599:Uterus / Q000201:enzymology*; D000515:alpha 1-Antitrypsin / Q000378:metabolism*
D000515:alpha 1-Antitrypsin; D010450:Endopeptidases