Guinea pig peritoneal macrophages. Differential effects of lectins on interaction with IgG immunoglobulins. 1995

I Sokal, and A Kułacz, and W Gorczyca, and M Janusz, and J Lisowski
Department of Immunochemistry, Polish Academy of Sciences, Wrocław.

Guinea pig peritoneal macrophages have on their surface two receptors, one (Fc gamma 1/gamma 2 R) binding both guinea pig IgG1 and IgG2 and the second (Fc gamma 2R) binding only IgG2 immunoglobulins. We have previously shown that treatment of macrophages with neuraminidase or glycosylation inhibitors affects, in a different way, the binding of guinea pig IgG1, IgG2, and rabbit IgG. In the present study we have shown that pretreatment of guinea pig macrophages with lectins (Con A, WGA, and PNA) also has a different effect on the interaction of the cells with IgG. The lectins increased the binding of guinea pig IgG1, whereas rabbit IgG and guinea pig IgG2 were bound with a lower efficiency than in the case of control cells. Since sialic acid residues seem to modulate the activity of receptors and WGA interacts with sialylated oligosaccharides, we determined the IgG-binding characteristics for WGA-pretreated macrophages. We found that the increase in IgG1-binding ability was caused by an increase in the value of Kapp, but the number of IgG-binding sites was lower than in the control cells. In the case of rabbit IgG and guinea pig IgG2 we observed a decrease of both the value of Kapp and the number of IgG-binding sites. WGA did not interact directly with the Fc gamma receptor. The results of our former papers and the different effects of lectins of various specificities described in this paper suggest different positions of Fc gamma 1/gamma 2 and Fc gamma 2R in the plane of the macrophage membrane in respect to various membrane glycoconjugates.(ABSTRACT TRUNCATED AT 250 WORDS)

UI MeSH Term Description Entries
D007074 Immunoglobulin G The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B. Gamma Globulin, 7S,IgG,IgG Antibody,Allerglobuline,IgG(T),IgG1,IgG2,IgG2A,IgG2B,IgG3,IgG4,Immunoglobulin GT,Polyglobin,7S Gamma Globulin,Antibody, IgG,GT, Immunoglobulin
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D003208 Concanavalin A A MANNOSE/GLUCOSE binding lectin isolated from the jack bean (Canavalia ensiformis). It is a potent mitogen used to stimulate cell proliferation in lymphocytes, primarily T-lymphocyte, cultures.
D006031 Glycosylation The synthetic chemistry reaction or enzymatic reaction of adding carbohydrate or glycosyl groups. GLYCOSYLTRANSFERASES carry out the enzymatic glycosylation reactions. The spontaneous, non-enzymatic attachment of reducing sugars to free amino groups in proteins, lipids, or nucleic acids is called GLYCATION (see MAILLARD REACTION). Protein Glycosylation,Glycosylation, Protein
D006168 Guinea Pigs A common name used for the genus Cavia. The most common species is Cavia porcellus which is the domesticated guinea pig used for pets and biomedical research. Cavia,Cavia porcellus,Guinea Pig,Pig, Guinea,Pigs, Guinea
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012794 Sialic Acids A group of naturally occurring N-and O-acyl derivatives of the deoxyamino sugar neuraminic acid. They are ubiquitously distributed in many tissues. N-Acetylneuraminic Acids,Acids, N-Acetylneuraminic,Acids, Sialic,N Acetylneuraminic Acids
D014909 Wheat Germ Agglutinins Lectins purified from the germinating seeds of common wheat (Triticum vulgare); these bind to certain carbohydrate moieties on cell surface glycoproteins and are used to identify certain cell populations and inhibit or promote some immunological or physiological activities. There are at least two isoforms of this lectin. Agglutinins, Wheat Germ,Lectins, Triticum Vulgare,Lectins, Wheat Germ,Triticum Vulgare Lectin,Triticum Vulgare Lectins,Wheat Germ Agglutinin,Wheat Germ Lectin,Wheat Germ Lectins,Wheat Germ Agglutinin Isolectin 1,Wheat Germ Agglutinin Isolectin 2,Agglutinin, Wheat Germ,Germ Agglutinin, Wheat,Germ Lectin, Wheat,Lectin, Triticum Vulgare,Lectin, Wheat Germ,Vulgare Lectin, Triticum
D017452 Receptors, IgG Specific molecular sites on the surface of various cells, including B-lymphocytes and macrophages, that combine with IMMUNOGLOBULIN Gs. Three subclasses exist: Fc gamma RI (the CD64 antigen, a low affinity receptor), Fc gamma RII (the CD32 antigen, a high affinity receptor), and Fc gamma RIII (the CD16 antigen, a low affinity receptor). Antigens, CD16,Antigens, CD32,Antigens, CD64,CD16 Antigens,CD32 Antigens,CD64 Antigen,CD64 Antigens,Fc Gamma Receptor,Fc Receptors, gamma,Fc gamma Receptors,IgG Receptor,IgG Receptors,Leu-11 Antigen,Receptors, Fc gamma,gamma Fc Receptor,gamma Fc Receptors,CD 16 Antigens,CD 32 Antigens,CD 64 Antigens,CDw32 Antigens,Fc gamma RI,Fc gamma RII,Fc gamma RIII,Immunoglobulin G Receptor,Leu-11 Antigens,Antigen, CD64,Antigen, Leu-11,Antigens, CD 16,Antigens, CD 32,Antigens, CD 64,Antigens, CDw32,Antigens, Leu-11,Fc Receptor, gamma,Gamma Receptor, Fc,Leu 11 Antigen,Leu 11 Antigens,Receptor, Fc Gamma,Receptor, IgG,Receptor, Immunoglobulin G,Receptor, gamma Fc,Receptors, gamma Fc,gamma RI, Fc,gamma RII, Fc,gamma RIII, Fc,gamma Receptors, Fc

Related Publications

I Sokal, and A Kułacz, and W Gorczyca, and M Janusz, and J Lisowski
January 1972, Annales immunologiae Hungaricae,
I Sokal, and A Kułacz, and W Gorczyca, and M Janusz, and J Lisowski
August 1976, Infection and immunity,
I Sokal, and A Kułacz, and W Gorczyca, and M Janusz, and J Lisowski
May 1976, Experimental cell research,
I Sokal, and A Kułacz, and W Gorczyca, and M Janusz, and J Lisowski
November 1971, Journal of immunology (Baltimore, Md. : 1950),
I Sokal, and A Kułacz, and W Gorczyca, and M Janusz, and J Lisowski
February 1984, Shigaku = Odontology; journal of Nihon Dental College,
I Sokal, and A Kułacz, and W Gorczyca, and M Janusz, and J Lisowski
December 1998, The international journal of biochemistry & cell biology,
I Sokal, and A Kułacz, and W Gorczyca, and M Janusz, and J Lisowski
January 1982, Archives roumaines de pathologie experimentales et de microbiologie,
I Sokal, and A Kułacz, and W Gorczyca, and M Janusz, and J Lisowski
October 1976, Infection and immunity,
I Sokal, and A Kułacz, and W Gorczyca, and M Janusz, and J Lisowski
January 1971, Journal of immunology (Baltimore, Md. : 1950),
I Sokal, and A Kułacz, and W Gorczyca, and M Janusz, and J Lisowski
January 1977, Preparative biochemistry,
Copied contents to your clipboard!