Faculty Opinions recommendation of Inhibition of tumorigenesis driven by different Wnt proteins requires blockade of distinct ligand-binding regions by LRP6 antibodies.

Author(s):  
Thomas Pap ◽  
Marianne Heitzmann
2010 ◽  
Vol 107 (35) ◽  
pp. 15473-15478 ◽  
Author(s):  
S. A. Ettenberg ◽  
O. Charlat ◽  
M. P. Daley ◽  
S. Liu ◽  
K. J. Vincent ◽  
...  

2010 ◽  
Vol 12 (11) ◽  
pp. 2873-2884 ◽  
Author(s):  
Jesús Lacal ◽  
Cristina García-Fontana ◽  
Francisco Muñoz-Martínez ◽  
Juan-Luis Ramos ◽  
Tino Krell

2014 ◽  
Vol 452 (4) ◽  
pp. 980-985 ◽  
Author(s):  
Ken-ichi Aoyama ◽  
Yoshihide Ota ◽  
Kagemasa Kajiwara ◽  
Noriaki Hirayama ◽  
Minoru Kimura

Biochemistry ◽  
2004 ◽  
Vol 43 (41) ◽  
pp. 13193-13203 ◽  
Author(s):  
Cagdas D. Son ◽  
Hasmik Sargsyan ◽  
Fred Naider ◽  
Jeffrey M. Becker

2001 ◽  
Vol 276 (31) ◽  
pp. 28946-28953 ◽  
Author(s):  
Olin D. Liang ◽  
Triantafyllos Chavakis ◽  
Sandip M. Kanse ◽  
Klaus T. Preissner

2003 ◽  
Vol 198 (7) ◽  
pp. 1057-1068 ◽  
Author(s):  
Fredric Carlsson ◽  
Karin Berggård ◽  
Margaretha Stålhammar-Carlemalm ◽  
Gunnar Lindahl

The M protein of Streptococcus pyogenes is a major bacterial virulence factor that confers resistance to phagocytosis. To analyze how M protein allows evasion of phagocytosis, we used the M22 protein, which has features typical of many M proteins and has two well-characterized regions binding human plasma proteins: the hypervariable NH2-terminal region binds C4b-binding protein (C4BP), which inhibits the classical pathway of complement activation; and an adjacent semivariable region binds IgA-Fc. Characterization of chromosomal S. pyogenes mutants demonstrated that each of the ligand-binding regions contributed to phagocytosis resistance, which could be fully explained as cooperation between the two regions. Deposition of complement on S. pyogenes occurred almost exclusively via the classical pathway, even under nonimmune conditions, but was down-regulated by bacteria-bound C4BP, providing an explanation for the ability of bound C4BP to inhibit phagocytosis. Different opsonizing antisera shared the ability to block binding of both C4BP and IgA, suggesting that the two regions in M22 play important roles also under immune conditions, as targets for protective antibodies. These data indicate that M22 and similar M proteins confer resistance to phagocytosis through ability to bind two components of the human immune system.


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