نتایج جستجو برای: binding lectin gene

تعداد نتایج: 1441952  

Journal: :Journal of immunology 2006
Daisuke Iwaki Kazuko Kanno Minoru Takahashi Yuichi Endo Nicholas J Lynch Wilhelm J Schwaeble Misao Matsushita Masaru Okabe Teizo Fujita

Mannose-binding lectin (MBL) and ficolins are pattern recognition proteins acting in innate immunity, and they trigger the activation of the lectin complement pathway through MBL-associated serine proteases (MASPs). Upon activation of the lectin pathway, MASP-2 cleaves C4 and C2. A truncated form of MASP-2, named small MBL-associated protein (sMAP), is also associated with MBL/ficolin-MASP comp...

Journal: :The Journal of biological chemistry 1986
V Anantharam S R Patanjali M J Swamy A R Sanadi I J Goldstein A Surolia

A lectin specific for chito-oligosaccharides from the exudate of ridge gourd (Luffa acutangula) fruits has been purified to homogeneity by affinity chromatography. The lectin has a molecular weight of 48,000, an S(0)20,w of 4.06 S and a Stokes radius of 2.9 nm. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, a single band corresponding to Mr of 24,000 was observed both in the pr...

Journal: :The Biochemical journal 1999
T Aoyama T Sawamura Y Furutani R Matsuoka M C Yoshida H Fujiwara T Masaki

We have reported the cDNA cloning of a modified low-density-lipoprotein (LDL) receptor, designated lectin-like oxidized LDL receptor-1 (LOX-1), which is postulated to be involved in endothelial dysfunction and the pathogenesis of atherosclerosis. Here, we determined the organization of the human LOX-1 gene, including the 5'-regulatory region. The 5'-regulatory region contained several potential...

Journal: :The Journal of Cell Biology 1975
U Rutishauser L Sachs

The cell-to-cell binding induced by concanavalin A (Con A) and the lectins from wheatgerm, soybean, and waxbean has been analyzed by measuring the ability of single cells to bind to lectin-coated cells immobilized on nylon fibers. The cells used were lymphoma, myeloid leukemia, and normal fibroblast cells. With all lectins, cell-to-cell binding was inhibited if both cells were prefixed with glu...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1976
D M Dwyer K P Chang

Crithidia oncopelti, a parasitic trypanosomatid protozoan of insects, normally contains intracellular symbiotic bacteria. As shown earlier, the protozoa can be rid of their endosymbiotes by chloramphenicol, producing a symbiote-free cell line. Here surface-membrane carbohydrate ligands of the symbiote-containing and symbiote-free strains were compared by lectin-mediated agglutination, lectin-ul...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1995
A Aspberg C Binkert E Ruoslahti

The core proteins of large chondroitin sulfate proteoglycans contain a C-type lectin domain. The lectin domain of one of these proteoglycans, versican, was expressed as a recombinant 15-kDa protein and shown to bind to insolubilized fucose and GlcNAc. The lectin domain showed strong binding in a gel blotting assay to a glycoprotein doublet in rat brain extracts. The binding was calcium dependen...

Journal: :Blood 2011
Helen E Heslop

2017
Tianhua Liu Riqiang Liu Shu Zhang Kun Guo Qinle Zhang Wei Li Yinkun Liu

Sorafenib is a multikinase inhibitor and is effective in treating hepatocellular carcinoma (HCC). However, it remains unknown whether sorafenib induces the alteration of protein glycosylation. The present study treated HCC MHCC97L and MHCC97H cells with a 50% inhibitory concentration of sorafenib. Following this treatment, alteration of protein glycosylation was detected using a lectin microarr...

Journal: :Journal of nematology 1988
M A McClure B A Stynes

Lectin binding sites on the surface of Meloidogyne incognita Races 1, 2, 3, and 4; M. javanica; M. arenaria Races 1 and 2; and M. hapla Races A and B were determined with lectins conjugated to fluorescein isothiocyanate or colloidal gold. The amphidial exudate, which was demonstrated histochemically to contain carbohydrate, was the principal binding site. Some lectins also bound to the external...

2012
Mohamad Hamshou Els J. M. Van Damme Gianni Vandenborre Bart Ghesquière Geert Trooskens Kris Gevaert Guy Smagghe

Rhizoctonia solani agglutinin, further referred to as RSA, is a lectin isolated from the plant pathogenic fungus Rhizoctonia solani. Previously, we reported a high entomotoxic activity of RSA towards the cotton leafworm Spodoptera littoralis. To better understand the mechanism of action of RSA, Drosophila melanogaster Schneider S2 cells were treated with different concentrations of the lectin a...

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