Isolation and characterization of a neutrophil chemotactic factor fromTritrichomonas foetusorganisms

1994 ◽  
Vol 72 (3) ◽  
pp. 249-255 ◽  
Author(s):  
M. OWHASHI ◽  
F. TOMIYOSHI ◽  
H. HAYASHI
1990 ◽  
Vol 265 (14) ◽  
pp. 8311-8316
Author(s):  
P M Grob ◽  
E David ◽  
T C Warren ◽  
R P DeLeon ◽  
P R Farina ◽  
...  

1989 ◽  
Vol 106 (3) ◽  
pp. 436-441 ◽  
Author(s):  
Ryuji Furuta ◽  
Junichi Yamagishi ◽  
Hirotada Kotani ◽  
Fumiko Sakamoto ◽  
Toshikazu Fukui ◽  
...  

1995 ◽  
Vol 4 (4) ◽  
pp. 263-269 ◽  
Author(s):  
M. Dias-Baruffi ◽  
M. C. Roque-Barreira ◽  
F. Q. Cunha ◽  
S. H. Ferreira

We have recently described the purification of a 54 kDa acidic protein, identified as macrophage-derived neutrophil chemotactic factor (MNCF). This protein causesin vitrochemotaxis as well asin vivoneutrophil migration even in animals treated with dexamethasone. Thisin vivochemotactic activity of MNCF in animals pretreated with dexamethasone is an uncommon characteristic which discriminates MNCF from known chemotactic cytokines. MNCF is released in the supernatant by macrophage monolayers stimulated with lipopolysaccharide (LPS). In the present study, we describe some biological characteristics of homogenous purified MNCF. When assayedin vitro, MNCF gave a bell-shaped dose–response curve. Thisin vitroactivity was shown to be caused by haptotaxis. Unlike N-formyl-methionylleucyl- phenylalanine (FMLP) or interleukin 8 (IL-8), the chemotactic activity of MNCFin vivoandin vitro, was inhibited by preincubation with D-galactose but not with D-mannose. In contrast with IL-8, MNCF did not bind to heparin and antiserum against IL-8 was ineffective in inhibiting its chemotactic activity. These data indicate that MNCF induces neutrophil migration through a carbohydrate recognition property, but by a mechanism different from that of the known chemokines. It is suggested that MNCF may be an important mediator in the recruitment of neutrophils via the formation of a substrate bound chemotactic gradient (haptotaxis) in the inflamed tissues.


1993 ◽  
Vol 30 (14) ◽  
pp. 1315-1320 ◽  
Author(s):  
Owhashi Makoto ◽  
Futaki Shiroh ◽  
Kitagawa Kouki ◽  
Horii Yoichiro ◽  
Maruyama Haruhiko ◽  
...  

1995 ◽  
Vol 4 (4) ◽  
pp. 257-262 ◽  
Author(s):  
M. Dias-Baruffi ◽  
M. C. Roque-Barreira ◽  
F. Q. Cunha ◽  
S. H. Ferreira

Macrophages stimulated with lipopolysaccharide (LPS) release a factor (MNCF; macrophage-derived neutrophil chemotactic factor) which induces neutrophil migrationin vivoandin vitro. Thein vivochemotactic activity of crude MNCF is not affected by pretreating the animals with dexamethasone, an uncommon characteristic which discriminates MNCF from known chemotactic cytokines. We purified MNCF by affinity chromatography of the supernatant from LPS-stimulated macrophages on immobilized D-galactose, followed by gel filtration of the sugar-binding material on Superdex 75. The activity was eluted in the volume corresponding to a MW of 54 kDa. SDS–PAGE of this preparation revealed a single band, also corresponding to a 54 kDa protein. MNCF is an acidic protein (pI < 4) as shown by chromatofocussing. Like the crude MNCF, the homogeneous protein induced neutrophil migrationin vitroas well asin vivo. This was not modified by dexamethasone pretreatment.


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