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.

Carbohydrate-binding protein 35: identification of the galactose-specific lectin in various tissues of mice.

Abstract: In previous studies, a lectin designated as carbohydrate-binding protein 35 (CBP35) has been isolated from cultured mouse 3T3 fibroblasts. In this study, antibodies directed against CBP35 were used to screen for cross-reactive proteins in various cultured cells and in various organs and tissues of mice. Cross-reactive proteins of the same molecular weight (Mr, 35,000) were found in human, mouse, and chicken fibroblasts and in a macrophage-like cell line, P388D1. Similarly, cross-reactive proteins were also found in the embryonic liver, lung, spleen, thymus, skin, and muscle tissue and in the lung, artery, thymus, and spleen of the adult mouse. Fractionation of extracts of mouse lung on affinity columns of asialofetuin-Sepharose yielded a protein whose molecular weight, carbohydrate-binding specificity, and immunological properties suggest that it is CBP35 derived from the lung, hereafter designated CBP35 (lung). The binding of 125I-labeled CBP35 (lung) to rabbit erythrocytes was quantitated in the presence and absence of various carbohydrates. It was found that only carbohydrates containing galactose were inhibitors of the binding; the disaccharide lactose was 100-fold more potent as an inhibitor than was the monosaccharide galactose. When extracts of the adult mouse liver were fractionated by asialofetuin-Sepharose chromatography, only a protein corresponding to CBP16 was isolated; no CBP35 was found. These results corroborate the immunoblotting data, which indicated that CBP35 was not detectable in the adult mouse liver.

Inhibition and detection of galectins

Abstract: More and more studies report on the roles that galectins play in numerous types of cancer. These roles can be varied, as has been shown particularly for galectin-3. These studies have created the need for inhibitors that can block unwanted effects, and the need to detect galectins in tissues, in order to better understand their role, and aid in diagnosis and prognosis. Since galectins bind beta-galactosides, monovalent galactose-derived inhibitors have been prepared but also peptidic ones have appeared. Since galectins often induce crosslinking and partake in aggregation phenomena, multivalency has been a successful design element in inhibitor development. Currently, there are no cheap and convenient solutions available for the detection of, ideally multiple, galectins in tissue samples, although antibody-based methods such as ELISA and Western blot analysis are being used. Besides these, a chemical probe-based method also shows potential as an alternative.

Galectins structure and function--a synopsis

Abstract: The 20 or so galectins expected to be found in man, and their many possible functional effects promise a rich and fruitful research field in the future. At present, the biomedically most promising areas for use of galectins or their ligands are in inflammation, immunity, and cancer. Many good stories can be formulated, but the field lacks the cohesion of knowing basic galectin function. The only basic common denominators among galectins are beta-galactoside binding, and the unusual combination of intra- and extracellular expression with non-classical secretion in between. Maybe that is all there is, and nature has used these properties for multiple, otherwise unrelated functions. Then again, maybe there is some deeper common function that has so far been overlooked. If it exists, this probably lies somewhere in the detailed integration of galectin activity in the complexities of cell physiology.