Galectin

About: Galectin is a research topic. Over the lifetime, 2076 publications have been published within this topic receiving 103409 citations. The topic is also known as: IPR001079 & Galectin.

Novel hybrid galactoside inhibitor of galectins

Abstract: The present invention relates to a compound of the general formula (1). The compound of formula (1) is suitable for use in a method for treating a disorder relating to the binding of a galectin, such as galectin-3 to a ligand in a mammal, such as a human. Furthermore the present invention concerns a method for treatment of a disorder relating to the binding of a galectin, such as galectin-3 to a ligand in a mammal, such as a human.

Binding Properties and Applications of Aplysia Gonad Lectin

Abstract: Adult Aplysia gonad contains high levels of a galactophilic lectin (MW around 65 kDa; composed of 2 subunits of apparent single species). It binds galactose and various a/s-galactosides (but not N-acetylgalactosamine), in addition to an outstanding high affinity for galacturonic acid. This lectin is relatively resistant to heating up to 70°C and to alkaline pH, but sensitive to proteolysis and low pH. It resembles galectins in binding to poly LacNAc (preferentially branched) complexes at low temperatures (0°-4°C) more avidly than at room temperature or at 37°C, but differs from them in being Ca2+-dependent. It agglutinates papain/sialidase-treated erythrocytes more strongly than untreated cells and stimulates mitosis in peripheral human lymphocytes (inducing IL-2 formation). This lectin also enhances neurite outgrowth and increases their viability, while suppressing cell tumorigenicity. It is useful for histochemical/ cytochemical studies of galacturonic acid in plant tissues and fungi and for the study of cell surface composition of various prokaryotic (including halophilic Archaea) and eukaryotic cells and for their typing. It is useful as a reagent for I-antigen detection in adult human erythrocytes (anti-I), exhibiting strongest agglutination of 0(h) Bombay-type erythrocytes and also exhibits sensitivity to the T antigen. It binds galactosylated molecules in human body fluids (shown by hemagglutination - inhibition tests), including saliva, seminal fluid and milk (detecting individual divergence) and in fowl egg albumens (exhibiting highest affinity for that of pigeon). Therefore, it might be valuable as a probe and fishhook for fishing compounds exhibiting anti-bacterial/neoplastic cell adhesion activities.

Galectin 9-inducing factor

Abstract: It has been disclosed that Galectin 9, which is a physiologically active substance acting as a lectin, is expressed in various cells and a correlationship is observed between the expression level of galectin 9 and the metastatic ability of tumors. Therefore, it is presumed that galectin 9 would relate to various physiological phenomena. Thus, a substance allowing the control of galectin 9 production and release is expected as exerting an activity of inducing antitumor and/or anti-inflammatory actions, etc. Therefore, it is required to reveal the same. It has been found that a factor inducing the production and release of galectin 9, "galectin 9-inducing factor", is contained in a certain solubilized tumor cell membrane fraction. This factor can be obtained as a concanavalin A-adsorbed fraction and as a concentrated active fraction by fractionation with an ion exchange column packed with Resource Q@, a hydroxyapatite column, etc. Assay reagents, drugs, assays, etc. can be developed by using the galectin 9-inducing activity of this factor.

Induction of Mac-2BP by nerve growth factor is regulated by the PI3K/Akt/NF-κB-dependent pathway in the HEK293 cell line

Abstract: Mac-2BP is a ligand of the galectin family that has been suggested to affect tumor proliferation and metastasis formation. We as- sessed Mac-2BP expression at the transcriptional and transla- tional levels to evaluate nerve growth factor (NGF)-induced Mac-2BP expression. A time kinetic analysis using reverse tran- scription-polymerase chain reaction showed that NGF-induced Mac-2BP transcript levels were 4-5 times higher than in controls. Mac-2BP enzyme-linked immunosorbent assay and immuno- fluorescence staining showed a 2-3-fold increase in intracellular and secreted Mac-2BP as a result of NGF stimulation. This in- crease was regulated by Akt activation and NF-κB binding. p65 and p50-NF-κB are major transcriptional factors in the Mac-2BP promoter region, and were shown to be regulated in accordance with the Akt activation states. Collectively, these results suggest that NGF induces Mac-2BP expression via the PI3K/Akt/NF-κB pathway. (BMB reports 2008; 41(11): 784-789)

Alkylation of galectin-1 with iodoacetamide and mass spectrometric mapping of the sites of incorporation.

Abstract: Galectins can display unique sensitivity to oxidative changes that result in significant conformational alterations that prevent carbohydrate recognition. While a variety of approaches can be utilized to prevent galectin oxidation, several of these require inclusion of reducing agents that not only prevent galectins from undergoing oxidative inactivation, but can also interfere with normal redox potentials required for fundamental cellular processes. To overcome limitations associated with placing cells in an artificial reducing environment, cysteine residues on galectins can be directly alkylated with iodoacetamide to form a stable thioether adduct that is resistant to further modification. Iodoacetamide alkylated galectin remains stable over prolonged periods of time and retains the carbohydrate binding and biological activities of the native protein. As a result, this approach allows examination of the biological roles of a stabilized form of galectin-1 without introducing the confounding variables that can occur when typical soluble reducing agents are employed.