Serum lectins

Hepatocellular carcinoma (HCC) develops in patients with chronic liver diseases associated with hepatitis B and hepatitis C vims infections with high incidences. Here, an acyclic retinoid has been shown to suppress the posttherapeutic recurrence after interferon-y or glycerrhicin treatment in cirrhotic patients who underwent curative treatment of preceding tumors. The retinoid induced the disappearance of serum lectin-reactive a-fetoprotein (AFP-L3), a tumor marker indicating the presence of unrecognizable tumors in the remnant liver, suggesting a deletion of such minute (pre)malignant clones (clonal deletion). As a molecular mechanism of the clonal deletion, a novel mechanism of... 

Serum lectin P35, huculin, EBP-35, ficolin 2 Eicolin 1, ficolin-alpha, ficolin-beta... 

Mannose binding proteins (MBPs) are C-type serum lectins in mammals. Lectins are widespread globular proteins, first identified from plants, which... 

Coles, J. G. Young, D. S. F. Brockhausen, 1. Human serum lectin-induced apoptosis and methods for detecting or inducing apoptosis. PCT Int. Appl. WO 9731107, 1997 Chem. Abstr. 1997, 127, 230947. 

GM-CSF is undetectable in the serum of normal humans, and no normal cells have been shown to express this protein constitutively. Some transformed cells may constitutively express GM-CSF, and it is actively synthesised and secreted by antigen- and lectin-stimulated T cells and by endothelial cells and fibroblasts exposed to TNF, IL-1 or endotoxin. Other sources of GM-CSF include stimulated B lymphocytes, macrophages, mast cells and osteoblasts, whilst TNF and IL-1 can stimulate its production by acute myeloid leukaemia cells. Some solid tumours and synovial cells from rheumatoid joints may also express GM-CSF and this may be important in disease pathology. 

Madera, M., Mechref, Y, Klouckova, I., and Novotny, M. V., Semiautomated high-sensitivity profiling of human blood serum glycoproteins through lectin preconcentration and multidimensional chromatography/tandem mass spectrometry. Journal of Proteome Research 5(9), 2348-2363, 2006. 

For the modification of the gold surface different chemical and biological substances (dodecanethiol, lectins, dextran sulfate DS, with the mass of 5 kDa and polyelectrolytes) were used. The mercaptane layer was formed in ethanol atlO" M concentration of thiol. Polyaniline hydrochloride (PAH), Aldrich , USA, was used to cover the transducer surface by a water insoluble polymer. Lectins from Phaseolus vulgaris (PLA), Solanum tuberosum (STA), Helix pomatia (HPA) and Tuberosum vulgaris (WGA) were immobilized on the surface pre-treated with dodecanethiol or PAH. These lectins were used for the immobilization of glycoproteins. Blocking of the free binding sites was carried out with 1% bovine serum albumin (BSA). 

Application of Lectins for the Detection of Ab to Viral Glycoproteins in the Blood Serum... 

Western blotting has become an important, modern technique for analysis and characterization of proteins. The procedure consists of, first, the electrophoretic transfer (blotting) of proteins from polyacrylamide gels to synthetic membranes. The transferred blots are then probed using immunological detection methods to identify proteins of specific structure and/or function. In this experiment, bovine serum will be fractionated by SDS-PAGE and the proteins blotted onto a nitrocellulose membrane. Serum glycoproteins will be identified by their specific interaction with the lectin concanavalin A. 

Pharmacotoxic and pharmacokinetic studies carried out for the new antitumor drug Aviscumine (rViscumin) were supported by a robust quantitative IPCR assay developed by Adler et al. [66, 85], The potency of this protein-based drug, derived from recombinant mistletoe lectine, required initial doses well below the quantification range accessible by conventional ELISA. An IPCR assay was adapted and validated for the quantification of rViscumin in standardized human serum [66, 85, 86] and subsequently... 

In Fig. 4, we show representative results. First, we detected an antibody reactivity specific for the carbohydrate moieties of an abundant human serum glycoprotein asialo-orosomucoid (ASOR) (Fig. 4B). Second, we found that lectin PHA-L (Phaseolus vulgaris L ) is specific for a defined complex carbohy-... 

In order to determine if lectins affect the reactions of complement mediated hemolysis subsequent to binding of antibody to the lymphocyte we have employed a synthetic particulate antigen. This was accomplished by testing the ability of lectin to inhibit the fixation of complement by the complex of anti-human serum albumin (HSA) and HSA-conjugated aminoethyl Biogel beads. The HSA-conjugated aminoethyl Biogel beads may be considered to be cell-like particles coated with a carbohydrate-free protein. 

Antiserum at 37°, 15 min Wash 0°. +Lectin 100-300 yg/ml at 0°, 30 min Wash, 0° Rabbit anti-lectin serum, 0°, 15 min Wash 0° Fluorescein labelled goat antirabbit IgG, 0°, 15 min Wash 0° View. FITC, Fluorescein isothiocyanate. TABLE II. Inhibition of Immunofluorescence ... 

In principle, the proportion of K-casein on the external surface can be studied by using cross-linked or immobilized enzymes, antibodies, lectins, or other specific functionalities. This approach is not without its problems, however. The rate of exchange of K-casein between the micelle and milk serum has not been established but may have a relaxation time of several hours, similar to that for p-casein (Creamer et al., 1977). If this rate is of the order of the time of the experiment, or faster, the proportion apparendy in the surface will be overestimated. Likewise, solubilization of micellar K-casein, e.g., by dissociation during the experiment, would lead to a similar error. 

Antibodies directed against recombinant erythropoietin have been obtained from rabbits immunized with the hormone and Freunds complete adjuvant [64], Two sets of antibodies are present in the serum of rabbits that have been immunized, Fig. (3C). The results of oxidation of the erythropoietin with periodate, Fig. (25A), reaction of the antibodies with lectins of known carbohydrate specificity, Fig. (25B) and inhibition of the antibodies with the structural monosaccharide residues of the hormone, Fig. (26), have established the types of antibodies to be anti-carbohydrate antibodies and the immunodeterminants for these antibodies are oligosaccharides with the following structure N-acetyl neuraminyl a(2->3)... 

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