Swainsonine
Alkaloids
Plant Poisoning
Indolizines
alpha-Mannosidase
1-Deoxynojirimycin
Oligosaccharides
Ipomoea
Tunicamycin
Bentonite
Rhizoctonia
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
alpha-Mannosidosis
Mannose
Receptors, Concanavalin A
Sarcoma 180
Glycoproteins
Hexosaminidases
Binding partners for the myelin-associated glycoprotein of N2A neuroblastoma cells. (1/194)
The myelin-associated glycoprotein (MAG) has been proposed to be important for the integrity of myelinated axons. For a better understanding of the interactions involved in the binding of MAG to neuronal axons, we performed this study to identify the binding partners for MAG on neuronal cells. Experiments with glycosylation inhibitors revealed that sialylated N-glycans of glycoproteins represent the major binding sites for MAG on the neuroblastoma cell line N2A. From extracts of [3H]glucosamine-labelled N2A cells several glycoproteins with molecular weights between 20 and 230 kDa were affinity-precipitated using immobilised MAG. The interactions of these proteins with MAG were sialic acid-dependent and specific for MAG. (+info)A lysosomal storage disease induced by Ipomoea carnea in goats in Mozambique. (2/194)
A novel plant-induced lysosomal storage disease was observed in goats from a village in Mozambique. Affected animals were ataxic, with head tremors and nystagmus. Because of a lack of suitable feed, the animals consumed an exotic hedge plant growing in the village that was identified as Ipomoea carnea (shrubby morning glory, Convolvulaceae). The toxicosis was reproduced by feeding I. carnea plant material to goats. In acute cases, histologic changes in the brain and spinal cord comprised widespread cytoplasmic vacuolation of neurons and glial cells in association with axonal spheroid formation. Ultrastructurally, cytoplasmic storage vacuoles in neurons were membrane bound and consistent with lysosomes. Cytoplasmic vacuolation was also found in neurons in the submucosal and mesenteric plexuses in the small intestine, in renal tubular epithelial cells, and in macrophage-phagocytic cells in the spleen and lymph nodes in acute cases. Residual alterations in the brain in chronic cases revealed predominantly cerebellar lesions characterized by loss of Purkinje neurons and gliosis of the Purkinje cell layer. Analysis of I. carnea plant material by gas chromatography-mass spectrometry established the presence of the mannosidase inhibitor swainsonine and 2 glycosidase inhibitors, calystegine B2 and calystegine C1, consistent with a plant-induced alpha-mannosidosis in the goats. The described storage disorder is analogous to the lysosomal storage diseases induced by ingestion of locoweeds (Astragalus and Oxytropis) and poison peas (Swainsona). (+info)Use of inhibitors to characterize intermediates in the processing of N-glycans synthesized by insect cells: a metabolic study with Sf9 cell line. (3/194)
The most frequent type of N-glycan synthesized by lepidopteran Sf9 cells appears to be fucosylated Man3GlcNAc2,and this has been a limitation for a large scale production and utilization of therapeutic glycoproteins in cultured insect cells. The current knowledge of the protein glycosylation pathway derived from structural studies on recombinant glyco-proteins expressed by using baculovirus vectors. In this work we provide more direct evidence for the sequential events occurring in the processing of endogenous N-glycoproteins of noninfected Sf9 cells. By metabolic labeling with radioactive mannose, we characterized the glycan structures which accumulated in the presence of processing inhibitors (castanospermine and swainsonine) and in the presence of an intracellular trafficking inhibitor (monensin). We thus demonstrated that from the glycan precursor Glc3Man9GlcNAc2 to GlcNAcMan5(Fuc)GlcNAc2 intermediate, the processing pathway in Sf9 cells paralleled the one demonstrated in mammalian cells. By using monensin, we demonstrated the formation of Man3(Fuc)GlcNAc2 from GlcNAcMan3(Fuc)GlcNAc2, a reaction which has not been described in mammalian cells. Our results support the idea that the hexosaminidase activity is of physiological relevance to the glycosylation pathway and is Golgi located. (+info)Temporal association of the N- and O-linked glycosylation events and their implication in the polarized sorting of intestinal brush border sucrase-isomaltase, aminopeptidase N, and dipeptidyl peptidase IV. (4/194)
The temporal association between O-glycosylation and processing of N-linked glycans in the Golgi apparatus as well as the implication of these events in the polarized sorting of three brush border proteins has been the subject of the current investigation. O-Glycosylation of pro-sucrase-isomaltase (pro-SI), aminopeptidase N (ApN), and dipeptidyl peptidase IV (DPPIV) is drastically reduced when processing of the mannose-rich N-linked glycans is blocked by deoxymannojirimycin, an inhibitor of the Golgi-located mannosidase I. By contrast, O-glycosylation is not affected in the presence of swainsonine, an inhibitor of Golgi mannosidase II. The results indicate that removal of the outermost mannose residues by mannosidase I from the mannose-rich N-linked glycans is required before O-glycosylation can ensue. On the other hand, subsequent mannose residues in the core chain impose no sterical constraints on the progression of O-glycosylation. Reduction or modification of N- and O-glycosylation do not affect the transport of pro-SI, ApN, or DPPIV to the cell surface per se. However, the polarized sorting of two of these proteins, pro-SI and DPPIV, to the apical membrane is substantially altered when O-glycans are not completely processed, while the sorting of ApN is not affected. The processing of N-linked glycans, on the other hand, has no influence on sorting of all three proteins. The results indicate that O-linked carbohydrates are at least a part of the sorting mechanism of pro-SI and DPPIV. The sorting of ApN implicates neither O-linked nor N-linked glycans and is driven most likely by carbohydrate-independent mechanisms. (+info)Swainsonine protects both murine and human haematopoietic systems from chemotherapeutic toxicity. (5/194)
The haematopoietic system is sensitive to cytotoxic damage and is often the site of dose-limiting toxicity. We previously reported that swainsonine, an inhibitor of protein glycosylation, reduced the bone marrow toxicity resulting from a single dose of anticancer drugs in otherwise healthy mice. However, more important questions are (1) can swainsonine protect tumour-bearing mice without interfering with the anti-tumour effects of the drugs, and (2) can swainsonine stimulate haematopoietic activity of human, as well as murine, bone marrow. We demonstrate here that swainsonine protects C57BL/6 mice bearing melanoma-derived tumours from cyclophosphamide-induced toxicity without interfering with the drug's ability to inhibit tumour growth. Similar results were obtained in vivo with 3'-azido-3'-deoxythymidine (AZT), a myelosuppressive agent often used in therapy for acquired immune deficiency syndrome. Swainsonine increased both total bone marrow cellularity and the number of circulating white blood cells in mice treated with doses of AZT that typically lead to severe myelosuppression. Swainsonine also increased the number of erythroid and myeloid colony forming cells (CFCs) in short-term cultures of murine bone marrow, restoring the number of progenitor cells to the control level in the presence of AZT doses that reduced CFCs by 80%. With respect to the sensitivity of human haematopoietic cells to swainsonine, we show that swainsonine protected human myeloid progenitor cells from AZT toxicity in vitro. These results suggest that swainsonine may be useful as an adjuvant in several types of human chemotherapy. (+info)High-mannose type oligosaccharide-dependent apoptosis in U937 cells induced by pradimicin, a mannose-binding antibiotic. (6/194)
Cell surface oligosaccharides play a role in a variety of biological events such as cell adhesion and signal transduction. We have shown that BMY-28864, a semi-synthetic analog of pradimicin, induced apoptosis of U937 cells which had been incubated with 1-deoxymannojirimycin, an inhibitor of mannosidase I. BMY-28864 was not cytotoxic to the cells which had been cultivated with other glycosidase inhibitors such as castanospermine and swainsonine. We thus propose that BMY-28864 induces apoptosis by acting on a specific mannose-rich oligosaccharide, presumably (Man)9(GlcNAc)2+. (+info)The Drosophila GMII gene encodes a Golgi alpha-mannosidase II. (7/194)
In this paper we show the organisation of the Drosophila gene encoding a Golgi alpha-mannosidase II. We demonstrate that it encodes a functional homologue of the mouse Golgi alpha-mannosidase II. The Drosophila and mouse cDNA sequences translate into amino acid sequences which show 41% identity and 61% similarity. Expression of the Drosophila GMII sequence in CHOP cells produces an enzyme which has mannosidase activity and is inhibited by swainsonine and by CuSO(4.) In cultured Drosophila cells and in Drosophila embryos, antibodies raised against a C-terminal peptide localise this product mainly to the Golgi apparatus as identified by cryo-immuno electron microscopy studies and by antibodies raised against known mammalian Golgi proteins. We discuss these results in terms of the possible use of dGMII as a Drosophila Golgi marker. (+info)N-Linked oligosaccharides on the meprin A metalloprotease are important for secretion and enzymatic activity, but not for apical targeting. (8/194)
The alpha and beta subunits of meprins, mammalian zinc metalloendopeptidases, are extensively glycosylated; approximately 25% of the total molecular mass of the subunits is carbohydrate. The aim of this study was to investigate the roles of the N-linked oligosaccharides on the secreted form of mouse meprin A. Recombinant meprin alpha and mutants in which one of the 10 potential Asn glycosylation sites was mutated to Gln were all secreted and sorted exclusively into the apical medium of polarized Madin-Darby canine kidney cells, indicating that no specific N-linked oligosaccharide acts as a determinant for apical targeting of meprin alpha. Several of the mutant proteins had decreased enzymatic activity using a bradykinin analog as substrate, and deglycosylation of the wild-type protein resulted in loss of 75-100% activity. Some of the mutants were also more sensitive to heat inactivation. In studies with agents that inhibit glycosylation processes in vivo, tunicamycin markedly decreased secretion of meprin, whereas castanospermine and swainsonine had little effect on secretion, sorting, or enzymatic properties of meprin. When all the potential glycosylation sites on a truncated form of meprin alpha (alpha-(1-445)) were mutated, the protein was not secreted into the medium, but was retained within the cells even after 10 h. These results indicate that there is no one specific glycosylation site or type of oligosaccharide (high mannose- or complex-type) that determines apical sorting, but that core N-linked carbohydrates are required for optimal enzymatic activity and for secretion of meprin alpha. (+info)Swainsonine is not a medical condition or disease, but rather a toxin that can cause a medical condition known as "locoism" in animals. Swainsonine is produced by certain plants, including some species of the genera Swainsona and Astragalus, which are commonly known as locoweeds.
Swainsonine inhibits an enzyme called alpha-mannosidase, leading to abnormal accumulation of mannose-rich oligosaccharides in various tissues and organs. This can result in a range of clinical signs, including neurological symptoms such as tremors, ataxia (loss of coordination), and behavioral changes; gastrointestinal symptoms such as diarrhea, weight loss, and decreased appetite; and reproductive problems.
Locoism is most commonly seen in grazing animals such as cattle, sheep, and horses that consume large quantities of locoweeds over an extended period. It can be difficult to diagnose and treat, and prevention through management practices such as rotational grazing and avoiding the introduction of toxic plants into pastures is often the best approach.
Oxytropis is a genus of flowering plants in the legume family, Fabaceae. It is native to temperate regions of the Northern Hemisphere, primarily in North America and Asia. Some common names for Oxytropis include locoweeds and wild peas.
In a medical context, Oxytropis species are most well-known for containing toxic alkaloids that can cause serious poisoning in livestock, particularly cattle, sheep, and goats. The toxins, including swainsonine and other indolizidine alkaloids, can affect the nervous system and cause symptoms such as weakness, tremors, blindness, and ultimately death.
While Oxytropis poisoning is not a direct concern for human health, it is important for medical professionals to be aware of its potential impact on animal health in rural and agricultural communities.
Alkaloids are a type of naturally occurring organic compounds that contain mostly basic nitrogen atoms. They are often found in plants, and are known for their complex ring structures and diverse pharmacological activities. Many alkaloids have been used in medicine for their analgesic, anti-inflammatory, and therapeutic properties. Examples of alkaloids include morphine, quinine, nicotine, and caffeine.
Plant poisoning is a form of poisoning that occurs when someone ingests, inhales, or comes into contact with any part of a plant that contains toxic substances. These toxins can cause a range of symptoms, depending on the type and amount of plant consumed or exposed to, as well as the individual's age, health status, and sensitivity to the toxin.
Symptoms of plant poisoning may include nausea, vomiting, diarrhea, abdominal pain, difficulty breathing, skin rashes, seizures, or in severe cases, even death. Some common plants that can cause poisoning include poison ivy, poison oak, foxglove, oleander, and hemlock, among many others.
If you suspect plant poisoning, it is important to seek medical attention immediately and bring a sample of the plant or information about its identity if possible. This will help healthcare providers diagnose and treat the poisoning more effectively.
Mannosidases are a group of enzymes that catalyze the hydrolysis of mannose residues from glycoproteins, oligosaccharides, and glycolipids. These enzymes play a crucial role in the processing and degradation of N-linked glycans, which are carbohydrate structures attached to proteins in eukaryotic cells.
There are several types of mannosidases, including alpha-mannosidase and beta-mannosidase, which differ in their specificity for the type of linkage they cleave. Alpha-mannosidases hydrolyze alpha-1,2-, alpha-1,3-, alpha-1,6-mannosidic bonds, while beta-mannosidases hydrolyze beta-1,4-mannosidic bonds.
Deficiencies in mannosidase activity can lead to various genetic disorders, such as alpha-mannosidosis and beta-mannosidosis, which are characterized by the accumulation of unprocessed glycoproteins and subsequent cellular dysfunction.
I'm sorry for any confusion, but "Indolizines" is not a medical term. It is a chemical term that refers to a class of heterocyclic organic compounds which contain a seven-membered ring with two nitrogen atoms and a carbon-carbon double bond. They are used in the synthesis of various pharmaceuticals and natural products, but they are not a medical condition or diagnosis.
Alpha-Mannosidase is an enzyme that belongs to the glycoside hydrolase family 47. It is responsible for cleaving alpha-1,3-, alpha-1,6-mannosidic linkages in N-linked oligosaccharides during the process of glycoprotein degradation. A deficiency or malfunction of this enzyme can lead to a lysosomal storage disorder known as alpha-Mannosidosis.
1-Deoxynojirimycin (DNJ) is an antagonist of the enzyme alpha-glucosidase, which is involved in the digestion of carbohydrates. DNJ is a naturally occurring compound found in some plants, including mulberry leaves and the roots of the African plant Moringa oleifera. It works by binding to the active site of alpha-glucosidase and inhibiting its activity, which can help to slow down the digestion and absorption of carbohydrates in the small intestine. This can help to reduce postprandial glucose levels (the spike in blood sugar that occurs after a meal) and may have potential benefits for the management of diabetes and other metabolic disorders. DNJ is also being studied for its potential anti-cancer effects.
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.
"Ipomoea" is a botanical term that refers to a genus of plants in the morning glory family, Convolvulaceae. These plants are primarily found in tropical and warm temperate regions around the world. Some species of Ipomoea have medicinal uses, but it's important to note that 'Ipomoea' itself is not a medical term or concept.
For instance, one species, Ipomoea batatas, commonly known as sweet potato, has been used in traditional medicine for various purposes, such as treating wounds and gastrointestinal disorders. However, any medicinal use would refer to the specific plant or extract, not simply the genus name 'Ipomoea'.
As always, if you're considering using any plant or herb for medicinal purposes, it's crucial to consult with a healthcare provider first to ensure safety and efficacy.
Tunicamycin is not a medical condition or disease, but rather a bacterial antibiotic and a research tool used in biochemistry and cell biology. It is produced by certain species of bacteria, including Streptomyces lysosuperificus and Streptomyces chartreusis.
Tunicamycin works by inhibiting the enzyme that catalyzes the first step in the biosynthesis of N-linked glycoproteins, which are complex carbohydrates that are attached to proteins during their synthesis. This leads to the accumulation of misfolded proteins and endoplasmic reticulum (ER) stress, which can ultimately result in cell death.
In medical research, tunicamycin is often used to study the role of N-linked glycoproteins in various biological processes, including protein folding, quality control, and trafficking. It has also been explored as a potential therapeutic agent for cancer and other diseases, although its use as a drug is limited by its toxicity to normal cells.
Bentonite is not a medical term, but a geological one. It refers to a type of clay that is composed primarily of montmorillonite, a soft phyllosilicate mineral. Bentonite has a wide range of uses, including as a binding agent in the manufacture of medicines, as an absorbent in cat litter and personal care products, and as a component in drilling muds and cement mixtures.
In medical contexts, bentonite is sometimes used as a bulk-forming laxative to treat constipation or irregularity. It works by absorbing water and increasing the size and weight of stool, which stimulates bowel movements. However, it's important to note that bentonite should only be used under the guidance of a healthcare professional, as it can interfere with the absorption of certain medications and may cause side effects such as bloating, gas, and diarrhea.
Rhizoctonia is a genus of saprophytic and facultative parasitic fungi that belong to the order Corticiales. It is widely distributed in soil and on plant debris, and can cause various plant diseases known as "rhizoctonioses." The most common species associated with plant pathogenicity is Rhizoctonia solani. These fungi infect a wide range of plants, including crops, turfgrass, and ornamentals, causing symptoms such as root rot, stem canker, damping-off, and wirestem blight. The fungus can also form sclerotia, which are compact masses of hardened fungal mycelium that can survive in the soil for many years, serving as a source of infection for future plant growth.
I'm happy to help, but I want to clarify that the term "sheep diseases" refers to a wide range of health issues that can affect sheep populations. It's not a single medical condition with a specific definition. Here are some examples of common diseases that can affect sheep:
1. Ovine Johne's Disease (OJD): A chronic, infectious disease caused by the bacterium Mycobacterium avium subspecies paratuberculosis. It affects the intestines and can cause weight loss, diarrhea, and death.
2. Footrot: A highly contagious bacterial infection that affects the feet of sheep, causing lameness, swelling, and pain. It's caused by the bacteria Dichelobacter nodosus.
3. Caseous Lymphadenitis (CL): A chronic infectious disease caused by the bacterium Corynebacterium pseudotuberculosis. It affects the lymph nodes and can cause abscesses, weight loss, and death.
4. Contagious Ecthyma (Orf): A highly contagious viral infection that affects the skin and mucous membranes of sheep, causing sores and lesions.
5. Mastitis: An inflammation of the mammary gland in sheep, usually caused by a bacterial infection. It can cause decreased milk production, fever, and loss of appetite.
6. Pneumonia: A respiratory infection that can affect sheep, causing coughing, difficulty breathing, and fever. It can be caused by various bacteria or viruses.
7. Enterotoxemia: A potentially fatal disease caused by the overproduction of toxins in the intestines of sheep, usually due to a bacterial infection with Clostridium perfringens.
8. Polioencephalomalacia (PEM): A neurological disorder that affects the brain of sheep, causing symptoms such as blindness, circling, and seizures. It's often caused by a thiamine deficiency or excessive sulfur intake.
9. Toxoplasmosis: A parasitic infection that can affect sheep, causing abortion, stillbirth, and neurological symptoms.
10. Blue tongue: A viral disease that affects sheep, causing fever, respiratory distress, and mouth ulcers. It's transmitted by insect vectors and is often associated with climate change.
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase (MGNAG) is an enzyme that is involved in the breakdown and recycling of glycoproteins, which are proteins that contain oligosaccharide chains attached to them. The enzyme's primary function is to cleave the beta-N-acetylglucosaminyl linkages in the chitobiose core of N-linked glycans, which are complex carbohydrates that are attached to many proteins in eukaryotic cells.
MGNAG is a lysosomal enzyme, meaning it is located within the lysosomes, which are membrane-bound organelles found in the cytoplasm of eukaryotic cells. Lysosomes contain hydrolytic enzymes that break down various biomolecules, including glycoproteins, lipids, and nucleic acids, into their constituent parts for recycling or disposal.
Deficiency in MGNAG activity can lead to a rare genetic disorder known as alpha-mannosidosis, which is characterized by the accumulation of mannose-rich oligosaccharides in various tissues and organs throughout the body. This condition can result in a range of symptoms, including developmental delays, intellectual disability, coarse facial features, skeletal abnormalities, hearing loss, and immune dysfunction.
Alpha-mannosidosis is a rare inherited metabolic disorder caused by the deficiency of the enzyme alpha-mannosidase. This enzyme is responsible for breaking down complex sugar molecules called mannose-rich oligosaccharides, which are found on the surface of many different types of cells in the body.
When the alpha-mannosidase enzyme is deficient or not working properly, these sugar molecules accumulate inside the lysosomes (the recycling centers of the cell) and cause damage to various tissues and organs, leading to a range of symptoms.
The severity of the disease can vary widely, depending on the amount of functional alpha-mannosidase enzyme activity present in an individual's cells. Three main types of alpha-mannosidosis have been described: mild, moderate, and severe. The severe form is usually diagnosed in infancy or early childhood and is characterized by developmental delay, intellectual disability, coarse facial features, skeletal abnormalities, hearing loss, and recurrent respiratory infections.
The moderate form of the disease may not be diagnosed until later in childhood or even adulthood, and it is generally milder than the severe form. Symptoms can include mild to moderate intellectual disability, skeletal abnormalities, hearing loss, and speech difficulties. The mild form of alpha-mannosidosis may not cause any noticeable symptoms until much later in life, and some individuals with this form of the disease may never experience any significant health problems.
Currently, there is no cure for alpha-mannosidosis, and treatment is focused on managing the symptoms of the disease. Enzyme replacement therapy (ERT) has shown promise in treating some forms of the disorder, but it is not yet widely available. Bone marrow transplantation has also been used to treat alpha-mannosidosis, with varying degrees of success.
Mannose is a simple sugar (monosaccharide) that is similar in structure to glucose. It is a hexose, meaning it contains six carbon atoms. Mannose is a stereoisomer of glucose, meaning it has the same chemical formula but a different structural arrangement of its atoms.
Mannose is not as commonly found in foods as other simple sugars, but it can be found in some fruits, such as cranberries, blueberries, and peaches, as well as in certain vegetables, like sweet potatoes and turnips. It is also found in some dietary fibers, such as those found in beans and whole grains.
In the body, mannose can be metabolized and used for energy, but it is also an important component of various glycoproteins and glycolipids, which are molecules that play critical roles in many biological processes, including cell recognition, signaling, and adhesion.
Mannose has been studied as a potential therapeutic agent for various medical conditions, including urinary tract infections (UTIs), because it can inhibit the attachment of certain bacteria to the cells lining the urinary tract. Additionally, mannose-binding lectins have been investigated for their potential role in the immune response to viral and bacterial infections.
Imino furanoses are not a recognized medical term, but they may be referred to in the field of biochemistry and carbohydrate research. In this context, imino furanoses are a type of sugar ring structure that contains an imine group (-C=N-) instead of the usual oxygen atom in the furanose form of sugars. Imino furanoses can be formed under certain conditions during chemical reactions involving carbohydrates, but they are not typically found in biological systems.
Concanavalin A (Con A) receptors are not a medical term per se, but rather a term used in the field of immunology and cell biology. Concanavalin A is a type of lectin, a protein that can bind to specific sugars found on the surface of cells. Con A receptors refer to the specific binding sites or proteins on the surface of certain types of cells, such as immune cells, that can recognize and bind to Concanavalin A.
When Con A binds to its receptors, it can activate various cellular responses, including changes in cell shape, movement, and metabolism. In research settings, Con A is often used as a tool to study the behavior of immune cells and other cell types that express Con A receptors. However, it's worth noting that Concanavalin A is not typically used in medical treatments or diagnoses.
I'm sorry for any confusion, but "Sarcoma 180" is not a recognized medical term or an official classification of sarcomas in humans. It appears to be a term used primarily in research involving mice. Sarcoma 180 is a transplantable tumor that was first isolated from a mouse and has been used as a model for cancer research, particularly in studies involving immunotherapy and cancer treatment.
In general, sarcomas are cancers that develop from connective tissues such as bones, muscles, tendons, cartilages, nerves, and blood vessels. They can be further classified into various subtypes based on the specific type of tissue they originate from and their genetic characteristics. If you have any concerns about a specific medical condition or term, I would recommend consulting with a healthcare professional for accurate information.
Carbohydrate conformation refers to the three-dimensional shape and structure of a carbohydrate molecule. Carbohydrates, also known as sugars, can exist in various conformational states, which are determined by the rotation of their component bonds and the spatial arrangement of their functional groups.
The conformation of a carbohydrate molecule can have significant implications for its biological activity and recognition by other molecules, such as enzymes or antibodies. Factors that can influence carbohydrate conformation include the presence of intramolecular hydrogen bonds, steric effects, and intermolecular interactions with solvent molecules or other solutes.
In some cases, the conformation of a carbohydrate may be stabilized by the formation of cyclic structures, in which the hydroxyl group at one end of the molecule forms a covalent bond with the carbonyl carbon at the other end, creating a ring structure. The most common cyclic carbohydrates are monosaccharides, such as glucose and fructose, which can exist in various conformational isomers known as anomers.
Understanding the conformation of carbohydrate molecules is important for elucidating their biological functions and developing strategies for targeting them with drugs or other therapeutic agents.
Glycoproteins are complex proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. These glycans are linked to the protein through asparagine residues (N-linked) or serine/threonine residues (O-linked). Glycoproteins play crucial roles in various biological processes, including cell recognition, cell-cell interactions, cell adhesion, and signal transduction. They are widely distributed in nature and can be found on the outer surface of cell membranes, in extracellular fluids, and as components of the extracellular matrix. The structure and composition of glycoproteins can vary significantly depending on their function and location within an organism.
Hexosaminidases are a group of enzymes that play a crucial role in the breakdown of complex carbohydrates, specifically glycoproteins and glycolipids, in the human body. These enzymes are responsible for cleaving the terminal N-acetyl-D-glucosamine (GlcNAc) residues from these molecules during the process of glycosidase digestion.
There are several types of hexosaminidases, including Hexosaminidase A and Hexosaminidase B, which are encoded by different genes and have distinct functions. Deficiencies in these enzymes can lead to serious genetic disorders, such as Tay-Sachs disease and Sandhoff disease, respectively. These conditions are characterized by the accumulation of undigested glycolipids and glycoproteins in various tissues, leading to progressive neurological deterioration and other symptoms.
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.
Swainsonine