Evaluation of a Hemolytic Assay of the Alternative Complement Pathway in Human Serum

1980 ◽  
Vol 74 (2) ◽  
pp. 167-173 ◽  
Author(s):  
J. Donald Coonrod ◽  
Susan D. Jenkins
2003 ◽  
Vol 10 (2) ◽  
pp. 216-220
Author(s):  
Marlene Pereira de Carvalho Florido ◽  
Patrícia Ferreira de Paula ◽  
Lourdes Isaac

ABSTRACT Due to the increasing numbers of reported clinical cases of complement deficiency in medical centers, clinicians are now more aware of the role of the complement system in the protection against infections caused by microorganisms. Therefore, clinical laboratories are now prepared to perform a number of diagnostic tests of the complement system other than the standard 50% hemolytic component assay. Deficiencies of alternative complement pathway proteins are related to severe and recurrent infections; and the application of easy, reliable, and low-cost methods for their detection and distinction are always welcome, notably in developing countries. When activation of the alternative complement pathway is evaluated in hemolytic agarose plates, some but not all human sera cross-react to form a late linear lysis. Since the formation of this linear lysis is dependent on C3 and factor B, it is possible to use late linear lysis to routinely screen for the presence of deficiencies of alternative human complement pathway proteins such as factor B. Furthermore, since linear lysis is observed between normal human serum and primary C3-deficient serum but not between normal human serum and secondary C3-deficient serum caused by the lack of factor H or factor I, this assay may also be used to discriminate between primary and secondary C3 deficiencies.


2001 ◽  
Vol 194 (11) ◽  
pp. 1609-1616 ◽  
Author(s):  
Haixiang Jiang ◽  
Eric Wagner ◽  
Huamei Zhang ◽  
Michael M. Frank

We studied complement 1 inhibitor (C1-INH) as an inhibitor of the alternative complement pathway. C1-INH prevented lysis, induced by the alternative complement pathway, of paroxysmal nocturnal hemoglobinuria (PNH) erythrocytes in human serum. It inhibited the binding of both factors B and C3 to PNH and rabbit erythrocytes and blocked the ability of factor B to restore alternative-pathway function in factor B–depleted serum. C1-INH did not bind to factors B or D but did bind to immobilized C3b and cobra venom factor (CVF), a C3b analogue. C1-INH prevented factor B from binding to CVF-coated beads and dissociated bound factor B from such beads. Factor B and C1-INH showed cross competition in binding to CVF-coated beads. Factor D cleaved factor B into Bb and Ba in the presence of C3b. Cleavage was markedly inhibited when C3b was preincubated with C1-INH. C1-INH inhibited the formation of CVFBb and decreased the C3 cleavage. Removal of C1-INH from serum, in the presence of Mg-EGTA with an anti–C1-INH immunoabsorbant, markedly increased alternative-pathway lysis. C1-INH interacts with C3b to inhibit binding of factor B to C3b. At physiologic concentrations, it is a downregulator of the alternative pathway convertase.


2014 ◽  
Vol 24 (5) ◽  
pp. 326-335 ◽  
Author(s):  
Scott P. Henry ◽  
Mark A. Jagels ◽  
Tony E. Hugli ◽  
Sheri Manalili ◽  
Richard S. Geary ◽  
...  

Biomaterials ◽  
1988 ◽  
Vol 9 (6) ◽  
pp. 514-518 ◽  
Author(s):  
Marie-Paule Carreno ◽  
Françoise Maillet ◽  
Denis Labarre ◽  
Marcel Jozefowicz ◽  
Michel D. Kazatchkine

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