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Mouse chondrolectin (chodl) was isolated out of the tail tip of fourday old 129/SvJ mice as a by-product of a PCR-based subtractive cDNA library screening. The gene is predominantly expressed in adult skeletal muscle, heart, testes and lungs and in embryonic stadia. Chodl is the mouse homologue of human chondrolectin (CHODL), a gene that encodes for a type Ia transmembrane protein and that is expressed in human testis, prostate, heart and skeletal muscle tissue. CHODL-splice variants (CHODLf, CHODLfΔE, CHODLΔE) are detected in human leukocytes. The proteins of the chondrolectin family belong to the family of C-type lectins. As the members of this protein family are important for a wide array of biological processes, the function of chodl was investigated by searching for its protein interaction partners. The β-subunit of Rab geranylgeranyl transferase (Rabggtb) was isolated 8 times after a complete Sos recruitment system (SRS) screen with the cytoplasmic domain of chodl. The interaction was confirmed with in vitro transcription/translation and co-immunoprecipitation (co-IP) experiments
CA-125 (coelomic epithelium-related antigen) forms the extracellular portion of transmembrane mucin 16 (MUC16). It is shed after proteolytic degradation. Due to structural heterogeneity, CA-125 ligand capacity and biological roles are not yet understood. In this study, we assessed CA-125 as a ligand for dendritic cell-specific ICAM-3-grabbing non-integrin (DC-SIGN), which is a C-type lectin showing specificity for mannosylated and fucosylated structures. It plays a role as a pattern recognition molecule for viral and bacterial glycans or as an adhesion receptor. We probed a human DC-SIGN-Fc chimera with CA-125 of fetal or cancer origin using solid- or fluid-phase binding and inhibition assays. The results showed that DC-SIGN binds to CA-125 of fetal origin and that this interaction is carbohydrate-dependent. By contrast, cancerderived CA-125 displayed negligible binding. Inhibition assays indicated differences in the potency of CA-125 to interfere with DC-SIGN binding to pathogen-related glycoconjugates, such as mannan and Helicobacter pylori antigens. The differences in ligand properties between CA-125 of fetal and cancer origin may be due to specificities of glycosylation. This might influence various functions of dendritic cells based on their subset diversity and maturation-related functional capacity.
Conglutinin, collectin-43 (CL-43) and collectin-46 (CL-46) are serum proteins characteristic for Bovidae. They belong to collectins - family of oligomeric proteins composed of trimeric subunits containing collagen-like sequences joined to C-type lectin domains. The genes encoding conglutinin, CL-43 and CL-46 are located on the bovine chromosome 28, and phylogenetic analysis indicates their common origin - from the lung surfactant protein D gene. Northern blot or immunocytochemical analysis confirm biosynthesis of bovine collectins mainly in the liver (conglutinin, CL-43) and in the thymus (CL-46). The level of conglutinin in the serum of dairy cows depends on many factors such as breeding, the season of the year, the stage of the reproductive cycle and infection. The collectins are involved in the innate immune defense. They bind to microbial surface carbohydrates inducing aggregation and, thereby, impeding infectivity. On the other hand the destruction of pathogens occurs due to stimulation of effector cells. CL-43 as well as conglutinin, binds to the collectin receptor (ClqR) localized on many types of cells identified as a surface variant of calreticulin. Conglutinin and CL-43 show antiviral activities towards influenza A virus and rotaviruses. Conglutinin also displays protective activity against bacterial infections.
Galectin-3 is a 31 kDa member of a growing family of b-galactosidebinding animal lectins. This protein is expressed in a variety of tissues and cell types and is mainly found in the cytoplasm, although, depending on cell type and proliferative state, a significant amount of this lectin can also be detected in the nucleus, on the cell surface or in the extracellular environment. Galectin-3 is secreted from cells by a novel and incompletely understood mechanism that is independent of the classical secretory pathway through the endoplasmic reticulum/Golgi network. Galectin-3 exhibits pleiotropic biological function, playing a key role in many physiological and pathological processes.
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