Hemolysis by the complement of tanned erythrocytes coated with cobra venom factor: A sensitive method to detect the alternative complement pathway activity of serum

1981 ◽  
Vol 46 (1) ◽  
pp. 85-95 ◽  
Author(s):  
Hidechika Okada ◽  
Hiroko Tanaka
Keyword(s):  
Alternative Complement Pathway ◽  
Cobra Venom ◽  
Complement Pathway ◽  
Cobra Venom Factor ◽  
Pathway Activity ◽  
Alternative Complement ◽  
Sensitive Method

Familial deficiency of C5 in humans: Intact but deficient alternative complement pathway activity

1981 ◽  
Vol 21 (1) ◽  
pp. 62-76 ◽  
Author(s):  
Robert H. McLean ◽  
Georges Peter ◽  
Ronald Gold ◽  
Levi Guerra ◽  
Edmund J. Yunis ◽  
...  
Keyword(s):  
Alternative Complement Pathway ◽  
Complement Pathway ◽  
Pathway Activity ◽  
Alternative Complement

scholarly journals Deficient Alternative Complement Pathway Activity in Newborn Sera

1979 ◽  
Vol 13 (12) ◽  
pp. 1341-1344 ◽  
Author(s):  
Elaine L Mills ◽  
Bengt Björksten ◽  
Paul G Quie
Keyword(s):  
Alternative Complement Pathway ◽  
Complement Pathway ◽  
Pathway Activity ◽  
Alternative Complement

scholarly journals Complement 1 Inhibitor Is a Regulator of the Alternative Complement Pathway

2001 ◽  
Vol 194 (11) ◽  
pp. 1609-1616 ◽  
Author(s):  
Haixiang Jiang ◽  
Eric Wagner ◽  
Huamei Zhang ◽  
Michael M. Frank
Keyword(s):  
Human Serum ◽  
Paroxysmal Nocturnal Hemoglobinuria ◽  
Alternative Pathway ◽  
Alternative Complement Pathway ◽  
Complement Pathway ◽  
Cobra Venom Factor ◽  
Factor B ◽  
Alternative Complement ◽  
Pathway Function ◽  
Cross Competition

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.

Alternative complement pathway activity in cystic fibrosis

1977 ◽  
Vol 91 (4) ◽  
pp. 681-682 ◽  
Author(s):  
Raymond K. Lyrene ◽  
Rutherford B. Polhill ◽  
Linda A. Guthrie ◽  
Ralph E. Tiller
Keyword(s):  
Cystic Fibrosis ◽  
Alternative Complement Pathway ◽  
Complement Pathway ◽  
Pathway Activity ◽  
Alternative Complement

scholarly journals Titration of the alternative complement pathway activity of representative cultured fishes.

1988 ◽  
Vol 54 (6) ◽  
pp. 1049-1054 ◽  
Author(s):  
Tomoki Yano ◽  
Yukihiro Hatayama ◽  
Hiroko Matsuyama ◽  
Miki Nakao
Keyword(s):  
Alternative Complement Pathway ◽  
Complement Pathway ◽  
Pathway Activity ◽  
Alternative Complement

Alternative complement pathway: Activity levels in allogeneic pregnancy

1976 ◽  
Vol 32 (12) ◽  
pp. 1589-1591
Author(s):  
M. Brai ◽  
G. Tolone ◽  
A. Magro ◽  
H. Waks ◽  
Maria Brai
Keyword(s):  
Alternative Complement Pathway ◽  
Activity Levels ◽  
Complement Pathway ◽  
Pathway Activity ◽  
Alternative Complement
Sign in / Sign up

Export Citation Format

Share Document