Molecular and functional characteristics of the Fcα/μR, a novel Fc receptor for IgM and IgA

2006 ◽  
Vol 28 (4) ◽  
pp. 377-382 ◽  
Author(s):  
Akira Shibuya ◽  
Shin-ichiro Honda
1996 ◽  
Vol 40 (5) ◽  
pp. 389-395 ◽  
Author(s):  
Hajime Nagahata ◽  
Hidetoshi Higuchi ◽  
Noriko Goji ◽  
Hiroshi Noda ◽  
Mikinori Kuwabara

Author(s):  
Takeshi Baba ◽  
Nobuki Shiozawa ◽  
Masao Hotch ◽  
Shinichi Ohno

Endosomes are vesicular or tubular organelles that play important roles in transports of receptors and receptor―bound ligands during receptor-mediated endocytosis. The mechanisms of endocytic transports from clathrin-coated pits to lysosomes have been studied by many investigators. However, few studies were reported about the interactions between endosomes and cytoskeletons. In this study, Fc-receptor-mediated endocytosis in macrophages are investigated by quick-freezing and deep-etching (QF-DE) method combined with gold-labeled immune complex and “replica scraping method”.


1987 ◽  
Vol 57 (03) ◽  
pp. 298-301
Author(s):  
William F Clark ◽  
Gerald J M Tevaarwerk ◽  
Bruce D Reid ◽  
Suzanne Hall ◽  
Anita Caveney ◽  
...  

SummaryWe have described the calcium dependence of the IgG Fc receptor (Fc-R) on human platelets by analyzing the direct binding of radiolabelled Fc fragments, monomers and dimers of IgG. Specific binding to platelets was undetectable at 37° C in a calcium-free preparation but readily detected when calcium was restored. Scatchard analysis of the binding data for the calcium-restored platelets permitted calculation of the available Fc-R and the Ka of binding for the different IgG ligands. The mean Ka of binding for 12 normal subjects varied from 107 to 108 L/M, with an equal receptor number measured by Fc fragments and dimers of IgG, but a lesser amount for monomeric IgG. There was no apparent difference in Fc-R number for platelets from 6 normal male versus 6 normal female subjects.At 4° C binding was detectable for dimers and polymers of IgG in a calcium-free preparation and this was markedly increased with recalcification. Thus, our data are consistent with an Fc receptor population on human platelets whose avidity for binding is significantly enhanced in a calcium-restored medium.


Diabetes ◽  
1988 ◽  
Vol 37 (7) ◽  
pp. 916-919 ◽  
Author(s):  
D. L. Eizirik ◽  
E. Strandell ◽  
K. Bendtzen ◽  
S. Sandler

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