The alternative complement pathway activation product Ba as a marker for transplant‐associated thrombotic microangiopathy

2019 ◽  
Vol 67 (3) ◽  
Author(s):  
Sarah Sartain ◽  
Stacey Shubert ◽  
Meng‐Fen Wu ◽  
Tao Wang ◽  
Caridad Martinez
Author(s):  
Juan M. Mejia-Vilet ◽  
Ismael A. Gómez-Ruiz ◽  
Cristino Cruz ◽  
R. Angélica Méndez-Pérez ◽  
Roque A. Comunidad-Bonilla ◽  
...  

1982 ◽  
Vol 155 (1) ◽  
pp. 231-247 ◽  
Author(s):  
G Pfaffenbach ◽  
M E Lamm ◽  
I Gigli

Activation of the complement system by IgA was investigated with immune complexes containing a mouse IgA myeloma protein with specificity for phosphorylcholine linked to bovine serum albumin (PC-BSA). These IgA anti-PC-BSA immune complexes activated the alternative complement pathway in mouse and guinea pig serum, while human complement was not affected. The activation proceeded with consumption of C3 but little or no consumption of C5. C3 did not bind to the IgA immune complexes during complement activation although it did bind covalently to IgG immune complexes. It is suggested that IgA immune complexes do not supply a suitable surface for C3 binding and effective alternative pathway convertase assembly; therefore, cleavage is limited and occurs primarily in the fluid phase. Without C3 binding, C5 cleavage does not occur nor can the alternative pathway activation proceed to the amplification step.


2019 ◽  
Vol 67 (3) ◽  
pp. 171-177
Author(s):  
Dorota Bartoszek ◽  
Oktawia Mazanowska ◽  
Katarzyna Kościelska-Kasprzak ◽  
Agnieszka Lepiesza ◽  
Marta Myszka ◽  
...  

1997 ◽  
Vol 326 (2) ◽  
pp. 377-383 ◽  
Author(s):  
Karim NABIL ◽  
Bertrand RIHN ◽  
Marie-Claude JAURAND ◽  
Jean-Michel VIGNAUD ◽  
Jean RIPOCHE ◽  
...  

We used chromatographic separation to purify to homogeneity a monomeric monocyte chemotactic protein of 150 kDa contained in mesothelioma pleural effusions. It was identified by N-terminal amino acid sequencing and immunoblotting as complement factor H, an inhibitor of the alternative complement pathway. Specific antibodies against factor H inhibited the monocyte chemotactic activity of the purified protein, which was most active at 10 nM. Factor H is a restrictive factor of alternative complement pathway activation. The new chemotactic function assigned to factor H in recruiting monocytes to the mesothelioma site might contribute to malignant cell phagocytosis via the iC3b/complement receptor type 3 pathway. These functions link the humoral and cellular immune systems.


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