scholarly journals Induction of experimental allergic arthritis with outer surface proteins ofborrelia burgdorferi

1994 ◽  
Vol 37 (7) ◽  
pp. 1070-1077 ◽  
Author(s):  
Klaus B. Gondolf ◽  
Michael Mihatsch ◽  
Enrico Curschellas ◽  
John J. Dunn ◽  
Steven R. Batsford
2012 ◽  
Vol 66 (1) ◽  
pp. 1-19 ◽  
Author(s):  
Melisha R. Kenedy ◽  
Tiffany R. Lenhart ◽  
Darrin R. Akins

1995 ◽  
Vol 33 (7) ◽  
pp. 1867-1869 ◽  
Author(s):  
V Fingerle ◽  
U Hauser ◽  
G Liegl ◽  
B Petko ◽  
V Preac-Mursic ◽  
...  

1987 ◽  
Author(s):  
T M Chiang ◽  
R J H Wojcikiewicz ◽  
A H Kang ◽  
J N Fain

We have recently isolated and purified from human plasma two isomeric forms of protein kinase, both of which can phosphorylate the outer surface proteins of human platelets. One of the proteins phosphorylated is the platelet collagen receptor. The phosphorylation of the outer surface proteins of human platelets increased their functional responsiveness to collagen. Collagen-stimulated platelet aggregation, release of ATP and calcium translocation were all enhanced by pretreatment with plasma protein kinase in the presence of ATP. The mechanism by which phosphorylated platelets become hypersensitive to collagen is not established. In the present study, we have used [3H]myo-inositol-labeled human platelets to investigate the possible role of phosphoinositide metabolism in mediating this hypersensitivity. Formation of inositol mono-, bis-, and trisphosphate in response to collagen was more pronounced in phosphorylated platelets than controls. these results indicate that enhanced phosphoinositide hydrolysis in phosphorylated platelets correlate with the increased functional responses to collagen.


1997 ◽  
Vol 41 (9) ◽  
pp. 673-679 ◽  
Author(s):  
Jianhui Wang ◽  
Toshiyuki Masuzawa ◽  
Muqing Li ◽  
Yasutake Yanagihara

1994 ◽  
Vol 112 (3) ◽  
pp. 533-542 ◽  
Author(s):  
C. M. Hu ◽  
S. Leuba-Garcia ◽  
M. D. Kramer ◽  
A. Aeschlimann ◽  
L. Gern

SUMMARYBorrelia burgdorferiisolates were obtained fromIxodes ricinusfrom three sites in Switzerland. They were examined by SDS-PAGE and immunoblotting. The phenotypes, in respect of three outer surface proteins (Osp), differed between the sites of collection. In site 1, most isolates had an OspA of 31 kDa and an OspB of 34 kDa: in site 2, isolates presenting an OspA of 33 kDa dominated and in site 3, the isolates with an OspA of 32 kDa and an OspB of 35 kDa were most frequent. This distribution differed significantly. About half of the isolates from sites 1 and 3 reacted with anti-OspA monoclonal antibody H5332 compared to 29% from site 2. Site 1 isolates reacted significantly more frequently (81 %) with another anti-OspA monoclonal antibody LA-31 than isolates from site 3 (P< 0·0001). These findings have implications for the epidemiology of Lyme borreliosis, for the further development of serodiagnostic reagents and for the development of a vaccine.


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