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- Title
Intestinal Glycoprotein Activates the Alternative Complement Pathway by Reacting with Factor H.
- Authors
Winsnes, R.; Lachmann, P. J.
- Abstract
Previous observations indicating complement activation via the alternative pathway of chelated human serum by a rat intestinal glycoprotein fraction were substantiated by using C2-deficient serum. Some inactivation of C6 by the glycoprotein was observed both in normal and C2-deficient serum. As estimated by conglutination, the glycoprotein largely abolished the ability of serum to convert EAC3b to EAC3bi, indicating inhibition of the control factors H (β1H globulin) and I (C3bINA), or inhibition of C3b deposition on the cells. The glycoprotein caused no change in the electrophoretic mobility of factors H or I. By immunoelectrophoresis the glycoprotein interfered with the precipitation line of plasminogen and β-lipoprotein and some other serum proteins. The absence of plasminogen or β-lipoprotein in serum seemed unimportant for the C3 conversion by the glycoprotein. Factor H was retained when heat-inactivated serum, heat-inactivated serum depleted of 99% albumin or 85% IgG, or heat-inactivated hypogammaglobulinaemic serum was eluted through a column of the intestinal glycoprotein coupled to epoxy-activated Sepharose 6B. Presence of EDTA abolished factor H retention. Factor H from methylamine-treated serum was also adsorbed lo the glycoprotein. When serum depleted at 5°C of 31% of the factor H content was healed, the alternative pathway was activated spontaneously. Addition of some of the previously removed factor H reduced the C3 and factor B conversion rate.
- Subjects
GLYCOPROTEINS; GLYCOCONJUGATES; PLASMINOGEN; FIBRINOLYTIC agents; ELECTROPHORESIS; BLOOD proteins
- Publication
Scandinavian Journal of Immunology, 1982, Vol 15, Issue 4, p371
- ISSN
0300-9475
- Publication type
Article
- DOI
10.1111/j.1365-3083.1982.tb00661.x