A class of animal lectins that bind specifically to beta-galactoside in a calcium-independent manner. Members of this class are distiguished from other lectins by the presence of a conserved carbohydrate recognition domain. The majority of proteins in this class bind to sugar molecules in a sulfhydryl-dependent manner and are often referred to as S-type lectins, however this property is not required for membership in this class.
A galectin found abundantly in smooth muscle (MUSCLE, SMOOTH) and SKELETAL MUSCLE and many other tissues. It occurs as a homodimer with two 14-kDa subunits.
A galectin found preferentially expressed in the gastrointestinal tract. The protein occurs as a homodimer with two 14-kDa subunits.
A multifunctional galactin initially discovered as a macrophage antigen that binds to IMMUNOGLOBULIN E, and as 29-35-kDa lectin that binds LAMININ. It is involved in a variety of biological events including interactions with galactose-containing glycoconjugates, cell proliferation, CELL DIFFERENTIATION, and APOPTOSIS.
Agents that cause agglutination of red blood cells. They include antibodies, blood group antigens, lectins, autoimmune factors, bacterial, viral, or parasitic blood agglutinins, etc.
Glycosides formed by the reaction of the hydroxyl group on the anomeric carbon atom of galactose with an alcohol to form an acetal. They include both alpha- and beta-galactosides.
A galectin found in the small and large intestine and the stomach. It occurs as a homodimer with two 36-kDa subunits and is localized to sites of cell adhesion where it may play role in assembly of ADHERENS JUNCTIONS.
Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.
A genus of black-spored basidiomycetous fungi of the family Coprinaceae, order Agaricales; some species are edible.
Carbohydrates covalently linked to a nonsugar moiety (lipids or proteins). The major glycoconjugates are glycoproteins, glycopeptides, peptidoglycans, glycolipids, and lipopolysaccharides. (From Biochemical Nomenclature and Related Documents, 2d ed; From Principles of Biochemistry, 2d ed)
Common name for an order (Anguilliformes) of voracious, elongate, snakelike teleost fishes.
Physiological mechanisms that sustain the state of PREGNANCY.
Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.
Polysaccharides are complex carbohydrates consisting of long, often branched chains of repeating monosaccharide units joined together by glycosidic bonds, which serve as energy storage molecules (e.g., glycogen), structural components (e.g., cellulose), and molecular recognition sites in various biological systems.
Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.
A family of calcium-binding alpha-globulins that are synthesized in the LIVER and play an essential role in maintaining the solubility of CALCIUM in the BLOOD. In addition the fetuins contain aminoterminal cystatin domains and are classified as type 3 cystatins.
Antigens expressed primarily on the membranes of living cells during sequential stages of maturation and differentiation. As immunologic markers they have high organ and tissue specificity and are useful as probes in studies of normal cell development as well as neoplastic transformation.
A disaccharide of GLUCOSE and GALACTOSE in human and cow milk. It is used in pharmacy for tablets, in medicine as a nutrient, and in industry.
The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.

Endogenous galectins and effect of galectin hapten inhibitors on the differentiation of the chick mesonephros. (1/501)

Galectins are galactoside-binding lectins. In the mesonephros of the chick embryo, the 16-kDa galectin is abundant in the glomerular and tubular basement membranes where it colocalizes with fibronectin and laminin. To test whether galectin-glycoprotein interactions could play a role in mesonephric development, the effects of the galectin hapten inhibitors thiodigalactoside (TDG) and lactose on the differentiation of the cultured mesonephros were investigated. When compared to control saccharide-free or maltose-treated cultures, mesonephroi cultured in the presence of TDG and lactose exhibited defects in tissue organization. These included a distorted tubule shape, pseudo-stratification of the tubular epithelium, and detachment of glomerular podocytes from the basement membrane. The presence of molecular differentiation markers in the developing mesonephros was investigated. In vivo, expression of the epithelial-specific cell adhesion molecule E-cadherin is restricted to differentiated tubular epithelial cells, whereas the intermediate filament protein vimentin is present in mesonephrogenic mesenchyme and is undetectable in tubular epithelial cells. In mesonephroi cultured in the absence of sugars or in the presence of maltose, the expression pattern of these two marker molecules resembles that found in the mesonephros in vivo. In contrast, in the mesonephroi cultured in the presence of TDG and lactose, the epithelial tubular cells expressing E-cadherin also express vimentin. Re-expression of vimentin in the tubular epithelial cells could indicate a partial reversal to a mesenchymal phenotype. Results suggest that galectin-glycoprotein interactions in the basement membrane are important in the maintenance of the renal epithelial phenotype. Dev Dyn 1999;215:248-263.  (+info)

Expression of galectin-7 during epithelial development coincides with the onset of stratification. (2/501)

Galectin-7 is a 14 KDa member of the galectin family that we have cloned from human, rat and mouse. Our previous studies have shown that in the adult, galectin-7 is expressed in all cell layers of epidermis and of other stratified epithelia such asthe cornea and the lining of the oesophagus. This suggested that galectin-7 expression might be induced at a particular stage in the embryonic development of stratified epithelia. In the present study we have investigated this hypothesis by in situ hybridization of galectin-7 mRNA in mouse embryos. Starting from E13.5, weak expression of galectin-7 was detected in bilayered ectoderm, and stronger expression was found in areas of embryonic epidermis where stratification was more advanced. Galectin-7 expression was maintained in all living layers after epidermal development was completed. Galectin-7 was also strongly and specifically expressed in stratified regions of ectodermally-derived non-epidermal epithelia such as the lining of the buccal cavity, the oesophagus and the ano-rectal region. In contrast, no expression of galectin-7 was found in epithelia derived from endoderm, such as lining of the intestine, kidney and lung. Our results demonstrate that galectin-7 is expressed in all stratified epithelia examined so far, and that the onset of its expression coincides with the first visible signs of stratification. These results establish galectin-7 as the first region-independent marker of epithelial stratification.  (+info)

Cloning of a galactose-binding lectin from the venom of Trimeresurus stejnegeri. (3/501)

A galactose-binding lectin isolated from the venom of Trimeresurus stejnegeri is a homodimer C-type lectin. The cloned cDNA encoding the monomer of Trimeresurus stejnegeri lectin (TSL) was sequenced and found to contain a 5'-end non-coding region, a sequence which encodes 135 amino acids, including a typical 23 amino acid signal peptide followed by the mature protein sequence, a 3'-end non-coding region, a polyadenylation signal, and a poly(A) region. To completely characterize the deduced amino acid sequence, on-line HPLC-MS and tandem MS were used to analyse the intact monomer and its proteolytic peptides. A modified peptide fragment was also putatively identified by HPLC-MS analysis. The deduced amino acid sequence was found to contain a carbohydrate-recognition domain homologous with those of some known C-type animal lectins. Thus TSL belongs to group VII of the C-type animal lectins as classified by Drickamer [(1993) Prog. Nucleic Acid Res. Mol. Biol. 45, 207-232]. At present, a number of C-type lectins have been purified from snake venom, but most of them have been characterized only at the protein level. To our knowledge, this is the first known cDNA sequence of a true C-type lectin from snake venom.  (+info)

Galectins: an evolutionarily conserved family of animal lectins with multifunctional properties; a trip from the gene to clinical therapy. (4/501)

Galectins constitute a family of evolutionarily conserved animal lectins, which are defined by their affinity for poly-N-acetyllactosamine-enriched glycoconjugates and sequence similarities in the carbohydrate recognition domain. During the past decade, attempts to dissect the functional role for galectins in vivo have been unsuccessful in comparison to the overwhelming information reached at the biochemical and molecular levels. The present review deals with the latest advances in galectin research and is aimed at validating the functional significance of these carbohydrate-binding proteins. Novel implications of galectins in cell adhesion, cell growth regulation, immunomodulation, apoptosis, inflammation, embryogenesis, metastasis and pre-mRNA splicing will be particularly discussed in a trip from the gene to the clinical therapy. Elucidation of the molecular mechanisms involved in galectin functions will certainly open new avenues not only in biomedical research, but also at the level of disease diagnosis and clinical intervention, attempting to delineate new therapeutic strategies in autoimmune diseases, inflammatory processes, allergic reactions and tumor spreading.  (+info)

Accelerated evolution in the protein-coding region of galectin cDNAs, congerin I and congerin II, from skin mucus of conger eel (Conger myriaster). (5/501)

Two cDNAs encoding galectins named congerins I and II from the skin mucus of conger eel (Conger myriaster) were isolated and sequenced. Comparison of the nucleotide sequences of congerins I and II showed that the sequence similarities of the 5' and 3' untranslated regions (86 and 88%, respectively) were much higher than those of the protein-coding region (73%). The numbers of nucleotide substitutions per site (KN) for the untranslated regions are smaller than the numbers of nucleotide substitutions per synonymous site (KS) for the protein coding region. Furthermore, nonsynonymous nucleotide substitutions have accelerated more frequently than synonymous nucleotide substitutions in the protein coding region (KA/KS = 2.57). These results suggest that accelerated substitutions have occurred in the protein-coding regions of galectin genes to generate diverse galectins with different molecular properties. Northern blot analysis showed that both congerins were expressed not only in the skin tissues but also in the stomach of conger eel.  (+info)

Galectin-7 overexpression is associated with the apoptotic process in UVB-induced sunburn keratinocytes. (6/501)

Galectin-7 is a beta-galactoside binding protein specifically expressed in stratified epithelia and notably in epidermis, but barely detectable in epidermal tumors and absent from squamous carcinoma cell lines. Galectin-7 gene is an early transcriptional target of the tumor suppressor protein P53 [Polyak, K., Xia, Y., Zweier, J., Kinzler, K. & Vogelstein, B. (1997) Nature (London) 389, 300-305]. Because p53 transcriptional activity is increased by genotoxic stresses we have examined the possible effects of ultraviolet radiations (UVB) on galectin-7 expression in epidermal keratinocytes. The amounts of galectin-7 mRNA and protein are increased rapidly after UVB irradiation of epidermal keratinocytes. The increase of galectin-7 is parallel to P53 stabilization. UVB irradiation of skin reconstructed in vitro and of human skin ex vivo demonstrates that galectin-7 overexpression is associated with sunburn/apoptotic keratinocytes. Transfection of a galectin-7 expression vector results in a significant increase in terminal deoxynucleotidyltransferase-mediated UTP end labeling-positive keratinocytes. The present findings demonstrate a keratinocyte-specific protein involved in the UV-induced apoptosis, an essential process in the maintenance of epidermal homeostasis.  (+info)

High-resolution structure of the conger eel galectin, congerin I, in lactose-liganded and ligand-free forms: emergence of a new structure class by accelerated evolution. (7/501)

BACKGROUND: Congerin I is a member of the galectin (animal beta-galactoside-binding lectin) family and is found in the skin mucus of conger eel. The galectin family proteins perform a variety of biological activities. Because of its histological localization and activity against marine bacteria and starfish embryos, congerin I is thought to take part in the eels' biological defense system against parasites. RESULTS: The crystal structure of congerin I has been determined in both lactose-liganded and ligand-free forms to 1. 5 A and 1.6 A resolution, respectively. The protein is a homodimer of 15 kDa subunits. Congerin I has a beta-sheet topology that is markedly different from those of known relatives. One of the beta-strands is exchanged between two identical subunits. This strand swap might increase the dimer stability. Of the known galectin complexes, congerin I forms the most extensive interaction with lactose molecules. Most of these interactions are substituted by similar interactions with water molecules, including a pi-electron hydrogen bond, in the ligand-free form. This observation indicates an increased affinity of congerin I for the ligand. CONCLUSIONS: The genes for congerin I and an isoform, congerin II, are known to have evolved under positive selection pressure. The strand swap and the modification in the carbohydrate-binding site might enhance the cross-linking activity, and should be the most apparent consequence of positive selection. The protein has been adapted to functioning in skin mucus that is in direct contact with surrounding environments by an enhancement in cross-linking activity. The structure of congerin I demonstrates the emergence of a new structure class by accelerated evolution under selection pressure.  (+info)

Immunocytochemical study of the distribution of a 16-kDa galectin in the chicken retina. (8/501)

PURPOSE: To compare the distribution of a developmentally regulated 16-kDa galectin in the chicken retina at two different developmental stages: embryonic day 13 (ED13) and postnatal day 10 (PD10) retinas, by immunocytochemical analysis using light and transmission electron microscopy. METHODS: Semi-thin and thin sections from ED13 and PD10 retinas were incubated with the IgG fraction purified from a rabbit antiserum raised against the 16-kDa chicken galectin. After incubation with colloidal gold particle-labeled goat anti-rabbit IgGs, tissue sections were analyzed by light and transmission electron microscopy. To improve the observation by light microscopy, semi-thin immunostained sections were intensified by silver enhancement. RESULTS: In ED13 retinas a specific galectin labeling was detected in the region corresponding to the outer limiting membrane by light microscopy. This labeling seemed to be associated with the apical villi of Muller glial cells and their specialized junctions, as judged by transmission electron microscopy. In PD10 retinas, the more relevant finding revealed by light microscopy was the detection of a widespread immunostaining at the level of all retinal layers. The ultrastructural analysis indicated that the galectin labeling was detected at the cytoplasmic and nuclear compartments of Muller cells throughout the different retinal layers. Moreover, the labeling was detected in the inner limiting membrane in structures that resemble the end feet of Muller cells. The apical villi, and the specialized junctions of these glial cells, appeared more strongly stained in PD10 retinas than in ED13 retinas. Finally, highly intense labeling in a group of mitochondria localized in the inner segments of cone cells was observed. CONCLUSIONS: The present study clearly supports the idea that the subcellular distribution of the 16-kDa galectin changes during the development of the chicken retina. Morphologic changes associated with developmentally regulated expression and subcellular compartmentalization of the retinal galectin suggest that this lectin may be involved in the modulation of several processes in the visual system. Its presence in the apical villi of Miller cells may be related by modulatory functions between retina and pigment epithelium, but its presence in the cytoplasm and nucleus of these glial cells suggests a potential immunomodulatory role and its involvement in different metabolic processes between Muller and the other retinal cells. Finally, although the presence of galectins inside mitochondria has not been described before, this localization gives rise to the idea that this lectin may be involved in the modulation of mitochondrial processes.  (+info)

Galectins are a family of animal lectins (carbohydrate-binding proteins) that bind specifically to beta-galactosides. They play important roles in various biological processes, including inflammation, immune response, cancer progression, and development. Galectins are widely distributed in various tissues and organ systems, and they can be found both intracellularly and extracellularly.

There are 15 known mammalian galectins, which are classified into three groups based on their structure: prototype (Gal-1, -2, -5, -7, -10, -13, -14, and -16), chimera-type (Gal-3), and tandem-repeat type (Gal-4, -6, -8, -9, and -12). Each galectin has a unique set of functions, but they often work together to regulate cellular processes.

Abnormal expression or function of galectins has been implicated in various diseases, including cancer, fibrosis, and autoimmune disorders. Therefore, galectins are considered potential targets for the development of new therapeutic strategies.

Galectin-1 is a protein that belongs to the galectin family, which are carbohydrate-binding proteins with diverse functions in various biological processes. Galectin-1 is found in both intracellular and extracellular environments and has been implicated in several physiological and pathological conditions.

Galectin-1 is a homodimeric protein composed of two identical subunits, each containing a carbohydrate recognition domain (CRD) that binds to beta-galactoside sugars found on glycoproteins and glycolipids. The CRDs are connected by a linker peptide, which allows the protein to adopt different conformations and interact with various ligands.

Galectin-1 has been shown to regulate cell adhesion, migration, proliferation, apoptosis, and immune responses. In the immune system, Galectin-1 can modulate T-cell activation and differentiation, promote regulatory T-cell function, and induce apoptosis of activated T cells. These properties make Galectin-1 a potential target for immunotherapy in cancer and autoimmune diseases.

In summary, Galectin-1 is a multifunctional protein involved in various biological processes, including immune regulation, cell adhesion, and migration. Its role in disease pathogenesis and potential therapeutic applications are currently under investigation.

Galectin-2 is a protein that belongs to the galectin family, which are carbohydrate-binding proteins with diverse functions in various biological processes. Specifically, Galectin-2 is a 14 kDa S-type lectin that contains one carbohydrate recognition domain (CRD) and forms homodimers.

Galectin-2 is primarily expressed in hematopoietic cells, including T lymphocytes, natural killer cells, and dendritic cells. It has been implicated in several immune functions, such as T cell activation, proliferation, and apoptosis. Galectin-2 can also modulate the adhesion and migration of immune cells by interacting with various glycoproteins on the cell surface.

In addition to its role in the immune system, Galectin-2 has been associated with several pathological conditions, including cancer, inflammation, and autoimmune diseases. However, further research is needed to fully understand the molecular mechanisms underlying these associations and to explore the potential therapeutic implications of targeting Galectin-2.

Galectin-3 is a type of protein belonging to the galectin family, which binds to carbohydrates (sugars) and plays a role in various biological processes such as inflammation, immune response, and cancer. It is also known as Mac-2 binding protein or LGALS3.

Galectin-3 is unique among galectins because it can form oligomers (complexes of multiple subunits) and has a wide range of functions in the body. It is involved in cell adhesion, proliferation, differentiation, apoptosis (programmed cell death), and angiogenesis (formation of new blood vessels).

In the context of disease, Galectin-3 has been implicated in several pathological conditions such as fibrosis, heart failure, and cancer. High levels of Galectin-3 have been associated with poor prognosis in patients with heart failure, and it is considered a potential biomarker for this condition. In addition, Galectin-3 has been shown to promote tumor growth, angiogenesis, and metastasis, making it a target for cancer therapy.

Hemagglutinins are proteins found on the surface of some viruses, including influenza viruses. They have the ability to bind to specific receptors on the surface of red blood cells, causing them to clump together (a process known as hemagglutination). This property is what allows certain viruses to infect host cells and cause disease. Hemagglutinins play a crucial role in the infection process of influenza viruses, as they facilitate the virus's entry into host cells by binding to sialic acid receptors on the surface of respiratory epithelial cells. There are 18 different subtypes of hemagglutinin (H1-H18) found in various influenza A viruses, and they are a major target of the immune response to influenza infection. Vaccines against influenza contain hemagglutinins from the specific strains of virus that are predicted to be most prevalent in a given season, and induce immunity by stimulating the production of antibodies that can neutralize the virus.

Galactosides are compounds that contain a galactose molecule. Galactose is a monosaccharide, or simple sugar, that is similar in structure to glucose but has a different chemical formula (C~6~H~10~O~5~). It is found in nature and is a component of lactose, the primary sugar in milk.

Galactosides are formed when a galactose molecule is linked to another molecule through a glycosidic bond. This type of bond is formed between a hydroxyl group (-OH) on the galactose molecule and a functional group on the other molecule. Galactosides can be found in various substances, including some plants and microorganisms, as well as in certain medications and medical supplements.

One common example of a galactoside is lactose, which is a disaccharide consisting of a glucose molecule linked to a galactose molecule through a glycosidic bond. Lactose is the primary sugar found in milk and dairy products, and it is broken down into its component monosaccharides (glucose and galactose) by an enzyme called lactase during digestion.

Other examples of galactosides include various glycoproteins, which are proteins that have one or more galactose molecules attached to them. These types of compounds play important roles in the body, including in cell-cell recognition and communication, as well as in the immune response.

Galectin-4 is a type of galectin, which is a group of proteins that bind to carbohydrates (sugars) and play roles in various biological processes. Galectin-4 is primarily found in the gastrointestinal tract, where it is involved in maintaining the integrity of the intestinal barrier and modulating inflammation. It has been implicated in several physiological and pathological conditions, including gut homeostasis, inflammatory bowel disease, and cancer.

Galectin-4 binds to specific carbohydrate structures, such as those found on the surface of intestinal epithelial cells and immune cells. This binding can influence cellular behavior, including cell adhesion, proliferation, differentiation, and apoptosis (programmed cell death). In the context of gut homeostasis, galectin-4 helps maintain a healthy balance between the intestinal epithelium and the gut microbiota.

Inflammatory bowel disease (IBD) is characterized by chronic inflammation in the gastrointestinal tract. Galectin-4 has been shown to have both protective and pathogenic roles in IBD, depending on the context. On one hand, it can help maintain intestinal barrier function and reduce inflammation. On the other hand, overexpression of galectin-4 may contribute to the development of IBD by promoting immune cell activation and tissue damage.

In cancer, galectin-4 has been implicated in tumor progression and metastasis. It can promote cancer cell survival, proliferation, and migration, as well as modulate the interactions between cancer cells and their microenvironment. However, its precise role in cancer is complex and may depend on the specific type of cancer and the context in which it is expressed.

In summary, Galectin-4 is a protein involved in various biological processes, particularly in the gastrointestinal tract. Its roles include maintaining intestinal barrier function, modulating inflammation, and influencing cellular behavior. However, its precise functions can vary depending on the context, and it has been implicated in both protective and pathogenic processes in conditions such as IBD and cancer.

Lectins are a type of proteins that bind specifically to carbohydrates and have been found in various plant and animal sources. They play important roles in biological recognition events, such as cell-cell adhesion, and can also be involved in the immune response. Some lectins can agglutinate certain types of cells or precipitate glycoproteins, while others may have a more direct effect on cellular processes. In some cases, lectins from plants can cause adverse effects in humans if ingested, such as digestive discomfort or allergic reactions.

"Coprinus" is a genus of fungi in the family Agaricaceae. It includes several species commonly known as "ink caps" or "shaggy manes." These mushrooms are characterized by their slimy, shaggy caps and the dark ink-like liquid that oozes from the gills when they mature. Some species of Coprinus are edible and considered delicacies, while others can cause adverse reactions if consumed with alcohol. It's important to note that proper identification is necessary before consuming any wild mushrooms.

Glycoconjugates are a type of complex molecule that form when a carbohydrate (sugar) becomes chemically linked to a protein or lipid (fat) molecule. This linkage, known as a glycosidic bond, results in the formation of a new molecule that combines the properties and functions of both the carbohydrate and the protein or lipid component.

Glycoconjugates can be classified into several categories based on the type of linkage and the nature of the components involved. For example, glycoproteins are glycoconjugates that consist of a protein backbone with one or more carbohydrate chains attached to it. Similarly, glycolipids are molecules that contain a lipid anchor linked to one or more carbohydrate residues.

Glycoconjugates play important roles in various biological processes, including cell recognition, signaling, and communication. They are also involved in the immune response, inflammation, and the development of certain diseases such as cancer and infectious disorders. As a result, understanding the structure and function of glycoconjugates is an active area of research in biochemistry, cell biology, and medical science.

"Eels" is not a term that has a medical definition. It refers to a type of long, snake-like fish that belong to the order Anguilliformes. There are several species of eels found in fresh and saltwater environments around the world. While there may be some references to "eels" in a medical context, such as in the name of certain medical conditions or procedures, these would be specific and unrelated to the fish themselves.

Pregnancy maintenance refers to the ongoing process and care required to support and sustain a healthy pregnancy until childbirth. This includes regular prenatal check-ups to monitor the health of both the mother and the developing fetus, proper nutrition, regular exercise, and avoiding harmful behaviors such as smoking or consuming alcohol. In some cases, pregnancy maintenance may also include medical interventions such as hormone treatments or bed rest. The goal of pregnancy maintenance is to ensure the best possible outcome for both the mother and the baby.

Carbohydrate metabolism is the process by which the body breaks down carbohydrates into glucose, which is then used for energy or stored in the liver and muscles as glycogen. This process involves several enzymes and chemical reactions that convert carbohydrates from food into glucose, fructose, or galactose, which are then absorbed into the bloodstream and transported to cells throughout the body.

The hormones insulin and glucagon regulate carbohydrate metabolism by controlling the uptake and storage of glucose in cells. Insulin is released from the pancreas when blood sugar levels are high, such as after a meal, and promotes the uptake and storage of glucose in cells. Glucagon, on the other hand, is released when blood sugar levels are low and signals the liver to convert stored glycogen back into glucose and release it into the bloodstream.

Disorders of carbohydrate metabolism can result from genetic defects or acquired conditions that affect the enzymes or hormones involved in this process. Examples include diabetes, hypoglycemia, and galactosemia. Proper management of these disorders typically involves dietary modifications, medication, and regular monitoring of blood sugar levels.

Polysaccharides are complex carbohydrates consisting of long chains of monosaccharide units (simple sugars) bonded together by glycosidic linkages. They can be classified based on the type of monosaccharides and the nature of the bonds that connect them.

Polysaccharides have various functions in living organisms. For example, starch and glycogen serve as energy storage molecules in plants and animals, respectively. Cellulose provides structural support in plants, while chitin is a key component of fungal cell walls and arthropod exoskeletons.

Some polysaccharides also have important roles in the human body, such as being part of the extracellular matrix (e.g., hyaluronic acid) or acting as blood group antigens (e.g., ABO blood group substances).

Oligosaccharides are complex carbohydrates composed of relatively small numbers (3-10) of monosaccharide units joined together by glycosidic linkages. They occur naturally in foods such as milk, fruits, vegetables, and legumes. In the body, oligosaccharides play important roles in various biological processes, including cell recognition, signaling, and protection against pathogens.

There are several types of oligosaccharides, classified based on their structures and functions. Some common examples include:

1. Disaccharides: These consist of two monosaccharide units, such as sucrose (glucose + fructose), lactose (glucose + galactose), and maltose (glucose + glucose).
2. Trisaccharides: These contain three monosaccharide units, like maltotriose (glucose + glucose + glucose) and raffinose (galactose + glucose + fructose).
3. Oligosaccharides found in human milk: Human milk contains unique oligosaccharides that serve as prebiotics, promoting the growth of beneficial bacteria in the gut. These oligosaccharides also help protect infants from pathogens by acting as decoy receptors and inhibiting bacterial adhesion to intestinal cells.
4. N-linked and O-linked glycans: These are oligosaccharides attached to proteins in the body, playing crucial roles in protein folding, stability, and function.
5. Plant-derived oligosaccharides: Fructooligosaccharides (FOS) and galactooligosaccharides (GOS) are examples of plant-derived oligosaccharides that serve as prebiotics, promoting the growth of beneficial gut bacteria.

Overall, oligosaccharides have significant impacts on human health and disease, particularly in relation to gastrointestinal function, immunity, and inflammation.

Fetuins are a group of proteins that are produced by the liver and found in circulation in the blood. The most well-known fetuin, fetuin-A, is a 64 kDa glycoprotein that is synthesized in the liver and secreted into the bloodstream. Fetuin-A plays a role in several physiological processes, including inhibition of tissue calcification, regulation of insulin sensitivity, and modulation of immune responses.

Fetuin-B is another member of the fetuin family that shares some structural similarities with fetuin-A but has distinct functions. Fetuin-B is also produced by the liver and secreted into the bloodstream, where it plays a role in regulating lipid metabolism and insulin sensitivity.

It's worth noting that while both fetuins have been studied for their roles in various physiological processes, there is still much to be learned about their functions and regulation.

Antigens are substances (usually proteins) on the surface of cells, viruses, fungi, or bacteria that can be recognized by the immune system and provoke an immune response. In the context of differentiation, antigens refer to specific markers that identify the developmental stage or lineage of a cell.

Differentiation antigens are proteins or carbohydrates expressed on the surface of cells during various stages of differentiation, which can be used to distinguish between cells at different maturation stages or of different cell types. These antigens play an essential role in the immune system's ability to recognize and respond to abnormal or infected cells while sparing healthy cells.

Examples of differentiation antigens include:

1. CD (cluster of differentiation) molecules: A group of membrane proteins used to identify and define various cell types, such as T cells, B cells, natural killer cells, monocytes, and granulocytes.
2. Lineage-specific antigens: Antigens that are specific to certain cell lineages, such as CD3 for T cells or CD19 for B cells.
3. Maturation markers: Antigens that indicate the maturation stage of a cell, like CD34 and CD38 on hematopoietic stem cells.

Understanding differentiation antigens is crucial in immunology, cancer research, transplantation medicine, and vaccine development.

Lactose is a disaccharide, a type of sugar, that is naturally found in milk and dairy products. It is made up of two simple sugars, glucose and galactose, linked together. In order for the body to absorb and use lactose, it must be broken down into these simpler sugars by an enzyme called lactase, which is produced in the lining of the small intestine.

People who have a deficiency of lactase are unable to fully digest lactose, leading to symptoms such as bloating, diarrhea, and abdominal cramps, a condition known as lactose intolerance.

A "carbohydrate sequence" refers to the specific arrangement or order of monosaccharides (simple sugars) that make up a carbohydrate molecule, such as a polysaccharide or an oligosaccharide. Carbohydrates are often composed of repeating units of monosaccharides, and the sequence in which these units are arranged can have important implications for the function and properties of the carbohydrate.

For example, in glycoproteins (proteins that contain carbohydrate chains), the specific carbohydrate sequence can affect how the protein is processed and targeted within the cell, as well as its stability and activity. Similarly, in complex carbohydrates like starch or cellulose, the sequence of glucose units can determine whether the molecule is branched or unbranched, which can have implications for its digestibility and other properties.

Therefore, understanding the carbohydrate sequence is an important aspect of studying carbohydrate structure and function in biology and medicine.

Tandem galectins include galectin-4, -6, -8, -9 and -12. The final galectin is galectin-3 which is the only galectin found in ... The best understood galectin in terms of cancer is galectin-3. Evidence suggests that galectin-3 plays a considerable part in ... Galectin-3, galectin 8 and galectin-9 have been shown to play additional roles in autophagy both through control of mTOR ( ... Galectin-12 expression induces apoptosis of adipocytes. Galectin-3 has been shown to be the only galectin with anti-apoptotic ...
... was first isolated from mouse embryonic kidney in 1997 as a 36 kDa beta-galactoside lectin protein. Human galectin-9 ... Galectin-9, through its regulation of AMPK, a kinase that negatively regulates mTOR, cooperates with Galectin-8-based effects ... Galectin-9 is one of the most studied ligands for HAVCR2 (TIM-3) and is expressed on various tumor cells. However, it can also ... Zhang ZY, Dong JH, Chen YW, Wang XQ, Li CH, Wang J, Wang GQ, Li HL, Wang XD (2012). "Galectin-9 acts as a prognostic factor ...
... is a protein of the galectin family that in humans is encoded by the LGALS8 gene. This gene encodes a member of the ... Galectin-8, interacts with the mTOR regulatory system composed of SLC38A9, Ragulator, RagAB, RagCD. Galectin-8 controls mTOR ... Hadari YR, Paz K, Dekel R, Mestrovic T, Accili D, Zick Y (February 1995). "Galectin-8. A new rat lectin, related to galectin-4 ... Galectins are beta-galactoside-binding animal lectins with conserved carbohydrate recognition domains. The galectins have been ...
... is a protein that in humans is encoded by the LGALS7 gene. The galectins are a family of beta-galactoside-binding ... 2006). "Galectin 7 (p53-induced gene 1): a new prognostic predictor of recurrence and survival in stage IV hypopharyngeal ... 2003). "Galectin-7 as a potential mediator of corneal epithelial cell migration". Arch. Ophthalmol. 121 (1): 82-6. doi:10.1001/ ... 2003). "Homodimeric galectin-7 (p53-induced gene 1) is a negative growth regulator for human neuroblastoma cells". Oncogene. 22 ...
The roles of galectins and galectin-3, in particular, in cancer have been heavily investigated. Of note, galectin-3 has been ... Galectin-3 is a member of the lectin family, of which 14 mammalian galectins have been identified. Galectin-3 is approximately ... Companies have developed galectin modulators that block the binding of galectins to carbohydrate structures. The galectin-3 ... Galectin-3 is encoded by a single gene, LGALS3, located on chromosome 14, locus q21-q22. Galectin-3 is expressed in the nucleus ...
... is a protein that in humans is encoded by the LGALS2 gene. The protein encoded by this gene is a soluble beta- ... 2006). "Genotype of galectin 2 (LGALS2) is associated with insulin-glucose profile in the British Women's Heart and Health ... 2007). "Human galectin-1, -2, and -4 induce surface exposure of phosphatidylserine in activated human neutrophils but not in ... Sturm A, Lensch M, Andre S, Kaltner H, Wiedenmann B, Rosewicz S, Dignass AU, Gabius HJ (Sep 2004). "Human galectin-2: novel ...
... is a protein that in humans is encoded by the LGALS4 gene. The galectins are a family of beta-galactoside-binding ... Gal 4 belongs to the family of galectin. Among various structure of galectins like dimeric, tandem or chimera, Gal-4 is tandem ... Circulating levels of galectin-1/-3/-4 in CRC patients were importantly higher compared to those in controls. Gal-1 and gal-4 ... Recommended name:Galectin-4, Short name: Gal-4 Alternative name(s): Antigen NY-CO-27 L-36 lactose-binding protein, Short name: ...
... is a protein that in humans is encoded by the LGALS1 gene. LGALS1 contains four exons. The galectin-1 protein is 135 ... Galectin-1 is thought to play a role in creating immune tolerance in pregnancy. Galectin-1 is expressed by the endometrial ... Galectin-1 may act as an autocrine negative growth factor that regulates cell proliferation. Galectin-1 expression in Hodgkin ... Park JW, Voss PG, Grabski S, Wang JL, Patterson RJ (September 2001). "Association of galectin-1 and galectin-3 with Gemin4 in ...
"Galectin Therapeutics Advisory Board". Archived from the original on 2014-11-21. Retrieved 16 October 2014. "Russians catch the ... 2008). Galectins. John Wiley & Sons. ISBN 9780470377789. Klyosov, A. A., ed. (2012). Glycobiology and Drug Design. ACS ... 2013). Galectins and Disease Implications for Targeted Therapeutics. ACS symposium series (Vol 1115). Washington DC: American ... The company was renamed as Galectin Therapeutics in May 2011. He then became a member of the company's scientific advisory ...
E.g. Interleukin, Galectin. The process by which such secretory proteins gain access to the cell exterior is termed ...
In 2018, he continued to look at galectin-driven regulation and how galectin-glycan interactions play a role in autoimmune ... They found that galectin-glycan interactions are crucial to immune response to reduce inflammation while also preventing ... In 2004, Rabinovich and his colleagues further researched the galectin-1 gene and found that if this gene is inhibited in vivo ... As of March 2020, Rabinovich and his colleagues published a patent for their invention of kits and methods which use galectin-1 ...
"Galecto develops galectin modulators , Case Study". Edinburgh Bioquarter. 3 December 2020. Retrieved 26 July 2022. "Edinburgh ...
"TRIMs and Galectins Globally Cooperate and TRIM16 and Galectin-3 Co-direct Autophagy in Endomembrane Damage Homeostasis". ... "TRIMs and Galectins Globally Cooperate and TRIM16 and Galectin-3 Co-direct Autophagy in Endomembrane Damage Homeostasis". ... In a paper in Molecular Cell, this group has shown that a novel system termed GALTOR, based on Galectin-8, interacts with the ... This occurs by Galectin-9-dependent activation of the ubiquitination systems on damaged lysosomes resulting in K63- ...
Under homeostatic conditions, Galectin-8 associates with active mTOR. Following membrane damage galectin-8 no longer interacts ... April 2018). "Galectins Control mTOR in Response to Endomembrane Damage". Molecular Cell. 70 (1): 120-135.e8. doi:10.1016/j. ... GALTOR contains galectin-8, a cytosolic lectin, which recognizes damaged lysosomal membranes by binding to the exposed ...
At the heart of GALTOR is galectin-8, a member of β-galactoside binding superfamily of cytosolic lectins termed galectins, ... At this stage another galectin, galectin-3, interacts with TRIM16 to guide selective autophagy of damaged lysosomes. TRIM16 ... "TRIMs and Galectins Globally Cooperate and TRIM16 and Galectin-3 Co-direct Autophagy in Endomembrane Damage Homeostasis". ... Following membrane damage, galectin-8, which normally associates with mTOR under homeostatic conditions, no longer interacts ...
Gordon-Alonso M, Bruger AM, van der Bruggen P (August 2018). "Extracellular galectins as controllers of cytokines in ... Interleukin-6 has been shown to interact with interleukin-6 receptor, glycoprotein 130, and Galectin-3. There is considerable ...
Galectin-related protein, also known as HSPC159, is a human gene. GRCh38: Ensembl release 89: ENSG00000119862 - Ensembl, May ... "Entrez Gene: HSPC159 galectin-related protein". Ahmed H, Vasta GR (2007). "Unlike mammalian GRIFIN, the zebrafish homologue ( ... DrGRIFIN) represents a functional carbohydrate-binding galectin". Biochem. Biophys. Res. Commun. 371 (3): 350-5. doi:10.1016/j. ...
Su J, Wang Y, Si Y, Gao J, Song C, Cui L, Wu R, Tai G, Zhou Y (January 2018). "Galectin-13, a different prototype galectin, ... It is a galectin-like protein. The ligand of this protein is still unknown. PP13 levels that are low in the first trimester of ...
Also known as galectin-3 (Gal3), LGALS3 participates in various cellular functions including apoptosis, innate immunity, cell ... "LGALS3 galectin 3 [ Homo sapiens (human) ]". NCBI (National Center for Biotechnology Information) Gene. Graham RL, Sims AC, ...
Galectin Therapeutics Inc. (2018-09-20). "Positive Preliminary Results from Phase 1b Clinical Trial of GR-MD-02 and KEYTRUDA® ... There is promising evidence for inhibiting Galectin-3 as a therapeutic target to reduce MDSCs. In a Phase 1b clinical trial of ... Wang T, Chu Z, Lin H, Jiang J, Zhou X, Liang X (June 2014). "Galectin-3 contributes to cisplatin-induced myeloid derived ... "Re-wiring regulatory cell networks in immunity by galectin-glycan interactions". FEBS Letters. 589 (22): 3407-18. doi:10.1016/j ...
BCoV S1-NTD does not recognize galactose as galectins do. Instead, it recognizes 5-N-acetyl-9-O-acetylneuraminic acid (Neu5, ...
Galectin-10 is an enzyme that in humans is encoded by the CLC gene. Lysophospholipases are enzymes that act on biological ... "CLC Charcot-Leyden crystal galectin [ Homo sapiens (human) ]". Human CLC genome location and CLC gene details page in the UCSC ... It is both structurally and functionally related to the galectin family of beta-galactoside binding proteins. It may be ... 2003). "Potential roles of galectins in myeloid differentiation into three different lineages". J. Leukoc. Biol. 73 (5): 650-6 ...
Yu F, Finley RL, Raz A, Kim HR (2002). "Galectin-3 translocates to the perinuclear membranes and inhibits cytochrome c release ... A role for synexin in galectin-3 translocation". J. Biol. Chem. 277 (18): 15819-27. doi:10.1074/jbc.M200154200. PMID 11839755. ...
In addition to galectin-9, several ligands have been identified, such as phosphatidylserine (PtdSer), High Mobility Group ... HAVCR2 is primarily activated by soluble galectin-9. The engagement leads to stimulation of an influx of calcium to ... December 2005). "The Tim-3 ligand galectin-9 negatively regulates T helper type 1 immunity". Nature Immunology. 6 (12): 1245- ... Wada J, Kanwar YS (February 1997). "Identification and characterization of galectin-9, a novel beta-galactoside-binding ...
Galectin-3-binding protein is a protein that in humans is encoded by the LGALS3BP gene. The galectins are a family of beta- ... 2001). "Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation". Int. J. Cancer. ... "Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation". Int. J. Cancer. 91 (2): ... The native protein binds specifically to a human macrophage-associated lectin known as Mac-2 and also binds to galectin 1. ...
Rabinovich, G. A., Baum, L. G., Tinari, N., Paganelli, R., Natoli, C., Liu, F. T., & Iacobelli, S. (2002). Galectins and their ... In collaboration with GA Rabinovich, he investigated the extracellular and intracellular functions of galectins and provided ... "Galectins and their ligands: amplifiers, silencers or tuners of the inflammatory response?". Trends in Immunology. 23 (6): 313- ...
2007 and is the first bivalve PGRP to be cloned.: 47 AiGal1 is a galectin discovered by Song et al. 2010,: 49 CfToll-1 is a ...
Galectin-3 drives glycosphingolipid-dependent biogenesis of clathrin-independent carriers. Nat Cell Biol 16: 595-606. Comments ... "Galectin-3 drives glycosphingolipid-dependent biogenesis of clathrin-independent carriers". Nature Cell Biology. 16 (6): 592- ...
Galectin-specific mechanisms of the tumor microenvironment are under study. Gastrointestinal cancer Pancreatic Cancer Action ...
Because the galectin-8 pathway detects membrane damage rather than the invading pathogen per se, its importance likely reaches ... He discovered a new pathway of cell-autonomous defence relying on galectin-8 as the receptor for membrane-damage caused by ... Thurston TL, Wandel MP, von Muhlinen N, Foeglein A, Randow F (January 2012). "Galectin 8 targets damaged vesicles for autophagy ... Falcon B, Noad J, McMahon H, Randow F, Goedert M (February 2018). "Galectin-8-mediated selective autophagy protects against ...

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