Concanavalin A
Receptors, Concanavalin A
Methylmannosides
Lectins
Mannosides
Plant Lectins
Lymphocyte Activation
Lymphocytes
Mitogens
T-Lymphocytes
Wheat Germ Agglutinins
Chromatography, Affinity
Phytohemagglutinins
Carbohydrates
Immunologic Capping
Mannose
Glycoproteins
Cells, Cultured
Cell Membrane
Pokeweed Mitogens
Glycopeptides
Receptors, Mitogen
Receptors, Drug
Colchicine
Interleukin-2
Sepharose
Electrophoresis, Polyacrylamide Gel
Mice, Inbred BALB C
Oligosaccharides
Canavalia
Macrophage-Activating Factors
Chromatography, Gel
Hemagglutination
Methylglucosides
Methylglycosides
Peanut Agglutinin
Nucleotidases
Mice, Inbred Strains
Binding Sites
Drug-Induced Liver Injury
Glucosamine
Thymus Gland
Monosaccharides
Lymphokines
Thymidine
Immunity, Cellular
Carbohydrate Sequence
Cell Division
Glycosylation
3,3'-Diaminobenzidine
Fluorimetric multiparameter cell assay at the single cell level fabricated by optical tweezers. (1/3415)
A fluorimetric multi-parameter cell sensor at the single cell level is presented which makes it possible to observe the physiological behavior of different cell lines, different physiological parameters, and statistical data at the same time. Different cell types were immobilized at predefined positions with high accuracy using optical tweezers and adhesion promoting surface layers. The process is applicable to both adherent and non-adherent cells. Coating of the immobilization area with mussel adhesive protein was shown to be essential for the process. Intracellular proton and calcium concentrations in different cell classes were simultaneously imaged and the specific activation of T lymphocytes was demonstrated. This method should be especially useful for drug screening due to the small sample volume and high information density. (+info)Hydrophobic interaction of human, mouse, and rabbit interferons with immobilized hydrocarbons. (2/3415)
Interferons of human, mouse, and rabbit origin bind to straight chain hydrocarbons immobilized on agarose. The hydrophobic nature of binding is established by the following observations: (a) a positive correlation between the length of hydrocarbon ligand and the strength of interaction; (b) a stronger interaction with hydrocarbon ligands terminated with apolar rather than polar head groups; (c) a lack of dependence of binding on ionic strength and pH of the solvent; (d) a reversal of binding by ethylene glycol, a hydrophobic solute; (e) an increasing eluting efficacy of tetraalkylammonium ions with the length of their alkyl substituents. The hydrophobic interactions of human interferon underlie the efficiency of two-step chromatographic procedures. For example, human embryo kidney interferon can be purified about 3,600-fold by sequential chromatography on (a) concanavalin A-agarose, (b) octyl-agarose. Another two-step procedure: (a) concanavalin A-agarose, (b) L-tryptophan-agarose, gives about 10,000-fold purification. The overall recovery of interferon in both cases in close to 90%. (+info)Lectin receptor sites on rat liver cell nuclear membranes. (3/3415)
The presence and localization of lectin receptor sites on rat liver cell nuclear and other endomembranes was studied by light and electron microscopy using fluorescein and ferritin-coupled lectin conjugates. Isolated nuclei labelled with fluorescein-conjugated Concanavalin A (Con A) or wheat germ agglutinin (WGA) often showed membrane staining, which sometimes was especially bright on small stretches of the nuclear surface. Unlabelled nuclei and nuclei with a complete ring fluorescence were also seen. The nuclear fluorescence corresponded in intensity to that seen on the surface of isolated rat liver cells. Con A-ferritin particles were seldom detected on the cytoplasmic surface of the intact nuclear envelope. However, at places where the 2 leaflets of the envelope were widely separated or where the outer nuclear membrane was partly torn away, heavy labelling was seen on the cisternal surface of both the inner and outer nuclear membranes. Labelling with Con A-ferritin was also found on the cisternal side of rough endoplasmic reticulum present in the specimens. No labelling was seen on the cytoplasmic surface of mitochondrial outer membrane. The results demonstrate the presence of binding sites for Con A and WGA in nuclei and an asymmetric localization of these sites on the cisternal side of ribosome-carrying endomembranes in rat liver cells. (+info)Analysis of the stimulation-inhibition paradox exhibited by lymphocytes exposed to concanavalin A. (4/3415)
High doses of Concanavalin A (Con A), which normally inhibit T-lymphocyte stimulation as measured by increases in DNA synthesis, cause these lymphocytes to become committed to mitogenesis while also generating a dominant but reversible negative growth signal. The observed response to the stimulatory signal as measured by the rate of commitment to enter the S phase (i.e., the rate at which the stimulation becomes lectin independent) increases with lectin concentration even in the inhibitory range. The generation of this positive signal is prevented by treating the cells with colchicine. Cells that have become committed but are also simultaneously blocked from entering the S phase by the high doses of Con A can begin synthesizing DNA if the lectin is released by adding a competitive inhibitor of binding. Experiments done in agarose cultures in which lymphocytes are kept from contact with each other suggest that the reversible inhibitory signal is mediated by structures in the individual cells rather than as a result of agglutination. Continuously dividing cells of the lymphoid line P388 are also individually and reversibly inhibited by Con A. These findings are considered in terms of the relation of the inhibitory signal to the microtubular components of cell surface modulating assemblies made up of submembranous arrays of microtubules, microfilaments, and associated proteins. (+info)5'-Nucleotidase activity of mouse peritoneal macrophages. II. Cellular distribution and effects of endocytosis. (5/3415)
The diazonium salt of sulfanilic acid (DASA) can inactivate about 80% of the total 5'-nucleotidase of viable macrophages. The remaining 20% can be inactivated if the cells are first lysed in detergent, and presumably represents an intracellular pool of 5'-nucleotidase. The bulk of this pool may represent cytoplasmic vesicles derived from plasma membrane by endocytosis. This internal compartment is expanded up to threefold immediately after the cells have ingested a large latex load. This is consistent with previous observations on the internalization of 5'-nucleotidase in latex phagosomes. In latex-filled cells this intracellular pool of enzyme is inactivated over a few hours, and the cells then slowly increase their enzyme activity to nearly normal levels. However, 24 h after latex ingestion the metabolism of 5'-nucleotidase in these recovered cells is abnormal, as the rate of enzyme degradation is about twice the normal rate, and the DASA-insensitive enzyme pool in these cells is strikingly diminished. This may reflect effects of the accumulated indigestible particles on the fate of incoming pinocytic vesicles or on newly synthesized plasma membrane precursor. Another endocytic stimulus, concanavalin A, also reduces the total cell 5'-nucleotidase activity. This effect, which is time and temperature dependent, can be prevented by the competitive sugar alpha-methyl mannose. The concanavalin A inhibition can be reversed in the absence of new protein synthesis or in cells cultivated in serum-free conditions. It is not known whether the effect of concanavalin A on 5'-nucleotidase depends upon the interiorizaiton of plasma membrane or is strictly associated with events at the cell surface. (+info)Effect of sodium butyrate on lymphocyte activation. (6/3415)
Butyrate, in relatively low concentrations, has been shown to induce synthesis of enzymes, cause changes in cell morphology, and inhibit growth of a variety of mammalian cells in tissue culture (reviewed in [1]). In this communication, we report our observations on the effect of butyrate on lymphocyte activation. Butyrate completely and reversibly inhibits mitogen-induced blast formation. We present evidence that it does not interfere with the binding of mitogens, that it does not inhibit a number of the "early" reactions involved in activation, and that it does not affect ongoing DNA synthesis for an extended period of time. However, butyrate rapidly inhibits any increase in the rate of DNA synthesis. (+info)Concanavalin A-mediated binding and sphering of human red blood cells by homologous monocytes. (7/3415)
Human red blood cells sensitized with concanavalin A became bound to homologous peripheral blood monocytes. Binding occured at a concentration of 10(5) molecules of tetrameric Con A per red blood cell (RBC) and increased with additional Con A. RBC binding began within 5 min and was maximal at 90 min. Phagocytosis of sensitized RBCs was minimal. RBC attachment was prevented by 0.01 M alpha-methyl-D-mannopyranoside, and, once the RBC-monocyte rosette was established, bound RBCs were largely removed with this specific saccharide inhibitor of Con A. RBCs attached to monocytes became spherocytic and osmotically fragile. The recognition of concanavalin A (Con A)-coated RBCs was not mediated through the monocyte IgG-Fc receptor. These studies demonstrate that, like IgG and C3b, Con A is capable of mediating the binding of human RBCs to human monocytes. Red cells so bound are damaged at the monocyte surface. (+info)Binding partners for the myelin-associated glycoprotein of N2A neuroblastoma cells. (8/3415)
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)Concanavalin A (Con A) is a type of protein known as a lectin, which is found in the seeds of the plant Canavalia ensiformis, also known as jack bean. It is often used in laboratory settings as a tool to study various biological processes, such as cell division and the immune response, due to its ability to bind specifically to certain sugars on the surface of cells. Con A has been extensively studied for its potential applications in medicine, including as a possible treatment for cancer and viral infections. However, more research is needed before these potential uses can be realized.
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.
Methylmannosides are not a recognized medical term or a specific medical condition. However, in biochemistry, methylmannosides refer to a type of glycosylation pattern where a methyl group (-CH3) is attached to a mannose sugar molecule. Mannose is a type of monosaccharide or simple sugar that is commonly found in various glycoproteins and glycolipids in the human body.
Methylmannosides can be formed through the enzymatic transfer of a methyl group from a donor molecule, such as S-adenosylmethionine (SAM), to the mannose sugar by methyltransferase enzymes. These modifications can play important roles in various biological processes, including protein folding, trafficking, and quality control, as well as cell-cell recognition and signaling.
It's worth noting that while methylmannosides have significant biochemical importance, they are not typically referred to in medical contexts unless discussing specific biochemical or molecular research studies.
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.
Mannosides are glycosylated compounds that consist of a mannose sugar molecule (a type of monosaccharide) linked to another compound, often a protein or lipid. They are formed when an enzyme called a glycosyltransferase transfers a mannose molecule from a donor substrate, such as a nucleotide sugar (like GDP-mannose), to an acceptor molecule.
Mannosides can be found on the surface of many types of cells and play important roles in various biological processes, including cell recognition, signaling, and protein folding. They are also involved in the immune response and have been studied as potential therapeutic targets for a variety of diseases, including infectious diseases and cancer.
It's worth noting that mannosides can be further classified based on the specific linkage between the mannose molecule and the acceptor compound. For example, an N-linked mannoside is one in which the mannose is linked to a nitrogen atom on the acceptor protein, while an O-linked mannoside is one in which the mannose is linked to an oxygen atom on the acceptor protein.
Agglutination is a medical term that refers to the clumping together of particles, such as cells, bacteria, or precipitates, in a liquid medium. It most commonly occurs due to the presence of antibodies in the fluid that bind to specific antigens on the surface of the particles, causing them to adhere to one another and form visible clumps.
In clinical laboratory testing, agglutination is often used as a diagnostic tool to identify the presence of certain antibodies or antigens in a patient's sample. For example, a common application of agglutination is in blood typing, where the presence of specific antigens on the surface of red blood cells causes them to clump together when mixed with corresponding antibodies.
Agglutination can also occur in response to certain infectious agents, such as bacteria or viruses, that display antigens on their surface. In these cases, the agglutination reaction can help diagnose an infection and guide appropriate treatment.
Plant lectins are proteins or glycoproteins that are abundantly found in various plant parts such as seeds, leaves, stems, and roots. They have the ability to bind specifically to carbohydrate structures present on cell membranes, known as glycoconjugates. This binding property of lectins is reversible and non-catalytic, meaning it does not involve any enzymatic activity.
Lectins play several roles in plants, including defense against predators, pathogens, and herbivores. They can agglutinate red blood cells, stimulate the immune system, and have been implicated in various biological processes such as cell growth, differentiation, and apoptosis (programmed cell death). Some lectins also exhibit mitogenic activity, which means they can stimulate the proliferation of certain types of cells.
In the medical field, plant lectins have gained attention due to their potential therapeutic applications. For instance, some lectins have been shown to possess anti-cancer properties and are being investigated as potential cancer treatments. However, it is important to note that some lectins can be toxic or allergenic to humans and animals, so they must be used with caution.
Lymphocyte activation is the process by which B-cells and T-cells (types of lymphocytes) become activated to perform effector functions in an immune response. This process involves the recognition of specific antigens presented on the surface of antigen-presenting cells, such as dendritic cells or macrophages.
The activation of B-cells leads to their differentiation into plasma cells that produce antibodies, while the activation of T-cells results in the production of cytotoxic T-cells (CD8+ T-cells) that can directly kill infected cells or helper T-cells (CD4+ T-cells) that assist other immune cells.
Lymphocyte activation involves a series of intracellular signaling events, including the binding of co-stimulatory molecules and the release of cytokines, which ultimately result in the expression of genes involved in cell proliferation, differentiation, and effector functions. The activation process is tightly regulated to prevent excessive or inappropriate immune responses that can lead to autoimmunity or chronic inflammation.
Lymphocytes are a type of white blood cell that is an essential part of the immune system. They are responsible for recognizing and responding to potentially harmful substances such as viruses, bacteria, and other foreign invaders. There are two main types of lymphocytes: B-lymphocytes (B-cells) and T-lymphocytes (T-cells).
B-lymphocytes produce antibodies, which are proteins that help to neutralize or destroy foreign substances. When a B-cell encounters a foreign substance, it becomes activated and begins to divide and differentiate into plasma cells, which produce and secrete large amounts of antibodies. These antibodies bind to the foreign substance, marking it for destruction by other immune cells.
T-lymphocytes, on the other hand, are involved in cell-mediated immunity. They directly attack and destroy infected cells or cancerous cells. T-cells can also help to regulate the immune response by producing chemical signals that activate or inhibit other immune cells.
Lymphocytes are produced in the bone marrow and mature in either the bone marrow (B-cells) or the thymus gland (T-cells). They circulate throughout the body in the blood and lymphatic system, where they can be found in high concentrations in lymph nodes, the spleen, and other lymphoid organs.
Abnormalities in the number or function of lymphocytes can lead to a variety of immune-related disorders, including immunodeficiency diseases, autoimmune disorders, and cancer.
Mitogens are substances that stimulate mitosis, or cell division, in particular, the proliferation of cells derived from the immune system. They are often proteins or glycoproteins found on the surface of certain bacteria, viruses, and other cells, which can bind to receptors on the surface of immune cells and trigger a signal transduction pathway that leads to cell division.
Mitogens are commonly used in laboratory research to study the growth and behavior of immune cells, as well as to assess the function of the immune system. For example, mitogens can be added to cultures of lymphocytes (a type of white blood cell) to stimulate their proliferation and measure their response to various stimuli.
Examples of mitogens include phytohemagglutinin (PHA), concanavalin A (ConA), and pokeweed mitogen (PWM). It's important to note that while mitogens can be useful tools in research, they can also have harmful effects if they are introduced into the body in large quantities or inappropriately, as they can stimulate an overactive immune response.
The spleen is an organ in the upper left side of the abdomen, next to the stomach and behind the ribs. It plays multiple supporting roles in the body:
1. It fights infection by acting as a filter for the blood. Old red blood cells are recycled in the spleen, and platelets and white blood cells are stored there.
2. The spleen also helps to control the amount of blood in the body by removing excess red blood cells and storing platelets.
3. It has an important role in immune function, producing antibodies and removing microorganisms and damaged red blood cells from the bloodstream.
The spleen can be removed without causing any significant problems, as other organs take over its functions. This is known as a splenectomy and may be necessary if the spleen is damaged or diseased.
T-lymphocytes, also known as T-cells, are a type of white blood cell that plays a key role in the adaptive immune system's response to infection. They are produced in the bone marrow and mature in the thymus gland. There are several different types of T-cells, including CD4+ helper T-cells, CD8+ cytotoxic T-cells, and regulatory T-cells (Tregs).
CD4+ helper T-cells assist in activating other immune cells, such as B-lymphocytes and macrophages. They also produce cytokines, which are signaling molecules that help coordinate the immune response. CD8+ cytotoxic T-cells directly kill infected cells by releasing toxic substances. Regulatory T-cells help maintain immune tolerance and prevent autoimmune diseases by suppressing the activity of other immune cells.
T-lymphocytes are important in the immune response to viral infections, cancer, and other diseases. Dysfunction or depletion of T-cells can lead to immunodeficiency and increased susceptibility to infections. On the other hand, an overactive T-cell response can contribute to autoimmune diseases and chronic inflammation.
Wheat germ agglutinins (WGA) are proteins found in wheat germ that have the ability to bind to specific carbohydrate structures, such as N-acetylglucosamine and sialic acid, which are present on the surface of many cells in the human body. WGA is a type of lectin, a group of proteins that can agglutinate, or clump together, red blood cells and bind to specific sugars on cell membranes.
WGA has been studied for its potential effects on various biological processes, including inflammation, immune response, and gut barrier function. Some research suggests that WGA may interact with the gut epithelium and affect intestinal permeability, potentially contributing to the development of gastrointestinal symptoms in some individuals. However, more research is needed to fully understand the clinical significance of these findings.
It's worth noting that while WGA has been studied for its potential biological effects, it is not currently recognized as a major allergen or toxic component of wheat. However, some people may still choose to avoid foods containing WGA due to personal dietary preferences or sensitivities.
Affinity chromatography is a type of chromatography technique used in biochemistry and molecular biology to separate and purify proteins based on their biological characteristics, such as their ability to bind specifically to certain ligands or molecules. This method utilizes a stationary phase that is coated with a specific ligand (e.g., an antibody, antigen, receptor, or enzyme) that selectively interacts with the target protein in a sample.
The process typically involves the following steps:
1. Preparation of the affinity chromatography column: The stationary phase, usually a solid matrix such as agarose beads or magnetic beads, is modified by covalently attaching the ligand to its surface.
2. Application of the sample: The protein mixture is applied to the top of the affinity chromatography column, allowing it to flow through the stationary phase under gravity or pressure.
3. Binding and washing: As the sample flows through the column, the target protein selectively binds to the ligand on the stationary phase, while other proteins and impurities pass through. The column is then washed with a suitable buffer to remove any unbound proteins and contaminants.
4. Elution of the bound protein: The target protein can be eluted from the column using various methods, such as changing the pH, ionic strength, or polarity of the buffer, or by introducing a competitive ligand that displaces the bound protein.
5. Collection and analysis: The eluted protein fraction is collected and analyzed for purity and identity, often through techniques like SDS-PAGE or mass spectrometry.
Affinity chromatography is a powerful tool in biochemistry and molecular biology due to its high selectivity and specificity, enabling the efficient isolation of target proteins from complex mixtures. However, it requires careful consideration of the binding affinity between the ligand and the protein, as well as optimization of the elution conditions to minimize potential damage or denaturation of the purified protein.
Phytohemagglutinins (PHA) are a type of lectin, specifically a mitogen, found in certain plants such as red kidney beans, white kidney beans, and butter beans. They have the ability to agglutinate erythrocytes (red blood cells) and stimulate the proliferation of lymphocytes (a type of white blood cell). PHA is often used in medical research and diagnostics as a means to study immune system function, particularly the activation and proliferation of T-cells. It's also used in some immunological assays. However, it should be noted that ingesting large amounts of raw or undercooked beans containing high levels of PHA can cause adverse gastrointestinal symptoms due to their ability to interact with the cells lining the digestive tract.
Carbohydrates are a major nutrient class consisting of organic compounds that primarily contain carbon, hydrogen, and oxygen atoms. They are classified as saccharides, which include monosaccharides (simple sugars), disaccharides (double sugars), oligosaccharides (short-chain sugars), and polysaccharides (complex carbohydrates).
Monosaccharides, such as glucose, fructose, and galactose, are the simplest form of carbohydrates. They consist of a single sugar molecule that cannot be broken down further by hydrolysis. Disaccharides, like sucrose (table sugar), lactose (milk sugar), and maltose (malt sugar), are formed from two monosaccharide units joined together.
Oligosaccharides contain a small number of monosaccharide units, typically less than 20, while polysaccharides consist of long chains of hundreds to thousands of monosaccharide units. Polysaccharides can be further classified into starch (found in plants), glycogen (found in animals), and non-starchy polysaccharides like cellulose, chitin, and pectin.
Carbohydrates play a crucial role in providing energy to the body, with glucose being the primary source of energy for most cells. They also serve as structural components in plants (cellulose) and animals (chitin), participate in various metabolic processes, and contribute to the taste, texture, and preservation of foods.
Immunologic capping is a biological process that occurs in immune cells, particularly B lymphocytes and neutrophils. It refers to the redistribution and clustering of immunoglobulin receptors or antibodies on the cell surface upon engagement with their specific antigens. This phenomenon leads to the formation of a cap-like structure at one pole of the cell, which is then internalized by endocytosis, followed by the degradation of the antigen-antibody complex in lysosomes. Immunologic capping helps regulate immune responses and contributes to the elimination of antigens from the cell surface.
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.
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.
Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.
"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.
Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.
It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.
A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.
I'm sorry for any confusion, but "Animal Hepatitis" is not a medical term used to describe a specific disease. Hepatitis refers to inflammation of the liver, and it can be caused by various factors, including viruses, alcohol, drugs, and certain medical conditions.
However, there are several viral hepatitis types that can infect animals, such as Hepatitis A, B, and C, which primarily affect humans. But there are also other hepatitis viruses that are species-specific and primarily infect animals, such as:
1. Canine Hepatitis (Adenovirus Type 1): This is a viral infection that affects dogs and causes liver damage, respiratory signs, and occasionally death.
2. Feline Infectious Peritonitis (FIP) Virus: While not strictly a hepatitis virus, this feline coronavirus can cause severe inflammation of the liver and other organs in cats.
3. Equine Infectious Anemia Virus (EIAV): This retrovirus affects horses and causes cyclic fever, anemia, and occasionally liver disease.
4. Avian Hepatitis E Virus: A recently discovered virus that infects birds and can cause hepatitis and other systemic signs in chickens and other avian species.
If you're looking for information on a specific animal hepatitis virus or a different medical term, please provide more context so I can give you a more accurate answer.
Pokeweed mitogens are substances derived from the pokeweed plant (Phytolacca americana) that have the ability to stimulate the production and proliferation of various types of cells, particularly white blood cells (lymphocytes). They are often used in laboratory settings as tools for studying the immune system and cell biology.
Pokeweed mitogens are typically extracted from the roots or leaves of the pokeweed plant and purified for use in research and diagnostic applications. When introduced to cells, they bind to specific receptors on the surface of lymphocytes and trigger a series of intracellular signaling events that lead to cell division and growth.
These mitogens are commonly used in immunological assays to measure immune function, such as assessing the proliferative response of lymphocytes to mitogenic stimulation. They can also be used to study the mechanisms of signal transduction and gene regulation in lymphocytes and other cell types.
It is important to note that pokeweed mitogens should only be handled by trained professionals in a controlled laboratory setting, as they can cause adverse reactions if improperly administered or ingested.
Glycopeptides are a class of antibiotics that are characterized by their complex chemical structure, which includes both peptide and carbohydrate components. These antibiotics are produced naturally by certain types of bacteria and are effective against a range of Gram-positive bacterial infections, including methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant Enterococci (VRE).
The glycopeptide antibiotics work by binding to the bacterial cell wall precursor, preventing the cross-linking of peptidoglycan chains that is necessary for the formation of a strong and rigid cell wall. This leads to the death of the bacteria.
Examples of glycopeptides include vancomycin, teicoplanin, and dalbavancin. While these antibiotics have been used successfully for many years, their use is often limited due to concerns about the emergence of resistance and potential toxicity.
Mitogen receptors are a type of cell surface receptor that become activated in response to the binding of mitogens, which are substances that stimulate mitosis (cell division) and therefore promote growth and proliferation of cells. The activation of mitogen receptors triggers a series of intracellular signaling events that ultimately lead to the transcription of genes involved in cell cycle progression and cell division.
Mitogen receptors include receptor tyrosine kinases (RTKs), G protein-coupled receptors (GPCRs), and cytokine receptors, among others. RTKs are transmembrane proteins that have an intracellular tyrosine kinase domain, which becomes activated upon ligand binding and phosphorylates downstream signaling molecules. GPCRs are seven-transmembrane domain proteins that activate heterotrimeric G proteins upon ligand binding, leading to the activation of various intracellular signaling pathways. Cytokine receptors are typically composed of multiple subunits and activate Janus kinases (JAKs) and signal transducer and activator of transcription (STAT) proteins upon ligand binding.
Abnormal activation of mitogen receptors has been implicated in the development and progression of various diseases, including cancer, autoimmune disorders, and inflammatory conditions. Therefore, understanding the mechanisms underlying mitogen receptor signaling is crucial for the development of targeted therapies for these diseases.
Drug receptors are specific protein molecules found on the surface of cells, to which drugs can bind. These receptors are part of the cell's communication system and are responsible for responding to neurotransmitters, hormones, and other signaling molecules in the body. When a drug binds to its corresponding receptor, it can alter the receptor's function and trigger a cascade of intracellular events that ultimately lead to a biological response.
Drug receptors can be classified into several types based on their function, including:
1. G protein-coupled receptors (GPCRs): These are the largest family of drug receptors and are involved in various physiological processes such as vision, olfaction, neurotransmission, and hormone signaling. They activate intracellular signaling pathways through heterotrimeric G proteins.
2. Ion channel receptors: These receptors form ion channels that allow the flow of ions across the cell membrane when activated. They are involved in rapid signal transduction and can be directly gated by ligands or indirectly through G protein-coupled receptors.
3. Enzyme-linked receptors: These receptors have an intracellular domain that functions as an enzyme, activating intracellular signaling pathways when bound to a ligand. Examples include receptor tyrosine kinases and receptor serine/threonine kinases.
4. Nuclear receptors: These receptors are located in the nucleus and function as transcription factors, regulating gene expression upon binding to their ligands.
Understanding drug receptors is crucial for developing new drugs and predicting their potential therapeutic and adverse effects. By targeting specific receptors, drugs can modulate cellular responses and produce desired pharmacological actions.
Colchicine is a medication that is primarily used to treat gout, a type of arthritis characterized by sudden and severe attacks of pain, swelling, redness, and tenderness in the joints. It works by reducing inflammation and preventing the formation of uric acid crystals that cause gout symptoms.
Colchicine is also used to treat familial Mediterranean fever (FMF), a genetic disorder that causes recurrent fevers and inflammation in the abdomen, chest, and joints. It can help prevent FMF attacks and reduce their severity.
The medication comes in the form of tablets or capsules that are taken by mouth. Common side effects of colchicine include diarrhea, nausea, vomiting, and abdominal pain. In rare cases, it can cause more serious side effects such as muscle weakness, nerve damage, and bone marrow suppression.
It is important to follow the dosage instructions carefully when taking colchicine, as taking too much of the medication can be toxic. People with certain health conditions, such as liver or kidney disease, may need to take a lower dose or avoid using colchicine altogether.
Interleukin-2 (IL-2) is a type of cytokine, which are signaling molecules that mediate and regulate immunity, inflammation, and hematopoiesis. Specifically, IL-2 is a growth factor for T cells, a type of white blood cell that plays a central role in the immune response. It is primarily produced by CD4+ T cells (also known as T helper cells) and stimulates the proliferation and differentiation of activated T cells, including effector T cells and regulatory T cells. IL-2 also has roles in the activation and function of other immune cells, such as B cells, natural killer cells, and dendritic cells. Dysregulation of IL-2 production or signaling can contribute to various pathological conditions, including autoimmune diseases, chronic infections, and cancer.
In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."
1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.
2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.
3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.
4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).
Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.
Sepharose is not a medical term itself, but it is a trade name for a type of gel that is often used in medical and laboratory settings. Sepharose is a type of cross-linked agarose gel, which is derived from seaweed. It is commonly used in chromatography, a technique used to separate and purify different components of a mixture based on their physical or chemical properties.
Sepharose gels are available in various forms, including beads and sheets, and they come in different sizes and degrees of cross-linking. These variations allow for the separation and purification of molecules with different sizes, charges, and other properties. Sepharose is known for its high porosity, mechanical stability, and low non-specific binding, making it a popular choice for many laboratory applications.
Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.
In this process:
1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.
EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.
BALB/c is an inbred strain of laboratory mouse that is widely used in biomedical research. The strain was developed at the Institute of Cancer Research in London by Henry Baldwin and his colleagues in the 1920s, and it has since become one of the most commonly used inbred strains in the world.
BALB/c mice are characterized by their black coat color, which is determined by a recessive allele at the tyrosinase locus. They are also known for their docile and friendly temperament, making them easy to handle and work with in the laboratory.
One of the key features of BALB/c mice that makes them useful for research is their susceptibility to certain types of tumors and immune responses. For example, they are highly susceptible to developing mammary tumors, which can be induced by chemical carcinogens or viral infection. They also have a strong Th2-biased immune response, which makes them useful models for studying allergic diseases and asthma.
BALB/c mice are also commonly used in studies of genetics, neuroscience, behavior, and infectious diseases. Because they are an inbred strain, they have a uniform genetic background, which makes it easier to control for genetic factors in experiments. Additionally, because they have been bred in the laboratory for many generations, they are highly standardized and reproducible, making them ideal subjects for scientific research.
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.
Periodic acid is not a medical term per se, but it is a chemical reagent that is used in some laboratory tests and staining procedures in the field of pathology, which is a medical specialty.
Periodic acid is an oxidizing agent with the chemical formula HIO4 or H5IO6. It is often used in histology (the study of the microscopic structure of tissues) to perform a special staining technique called the periodic acid-Schiff (PAS) reaction. This reaction is used to identify certain types of carbohydrates, such as glycogen and some types of mucins, in tissues.
The periodic acid first oxidizes the carbohydrate molecules, creating aldehydes. These aldehydes then react with a Schiff reagent, which results in a pink or magenta color. This reaction can help pathologists identify and diagnose various medical conditions, such as cancer, infection, and inflammation.
'Canavalia' is a genus of herbaceous plants in the legume family, also known as jackbeans or horse eye beans. While the plant itself has some medicinal uses, such as being used as a traditional remedy for skin conditions and inflammation, it is not typically the subject of medical definition.
However, a compound called canavalia ensiformis agglutinin (Con A) can be extracted from the seeds of Canavalia ensiformis (also known as jackbean). Con A is a type of lectin, which is a protein that binds to carbohydrates and has various biological effects.
Con A has been studied for its potential medical applications, such as in cancer research. It can bind to specific structures on the surface of cancer cells and induce cell death, making it a subject of interest in immunotherapy and other cancer treatments. However, more research is needed before Con A can be used as a standard treatment for cancer or any other medical condition.
Macrophage-activating factors (MAFs) are substances that stimulate the activation and function of macrophages, which are a type of white blood cell involved in the immune response. These factors can be produced by various cells, including T lymphocytes, and can enhance the ability of macrophages to phagocytize (ingest and destroy) foreign substances, such as bacteria and viruses, and to produce cytokines, which are signaling molecules that mediate and regulate the immune response.
MAFs can be classified into two main groups: endogenous and exogenous. Endogenous MAFs are produced by cells of the body in response to various stimuli, such as infection or inflammation. Examples of endogenous MAFs include interferon-gamma (IFN-γ), granulocyte-macrophage colony-stimulating factor (GM-CSF), and tumor necrosis factor-alpha (TNF-α). Exogenous MAFs, on the other hand, are substances that are introduced into the body from outside sources, such as bacterial toxins or synthetic compounds, and can also activate macrophages.
MAFs play an important role in the immune response by helping to coordinate the activities of different types of immune cells and regulate the intensity and duration of the immune response. Dysregulation of MAF production or activity has been implicated in various diseases, including autoimmune disorders, chronic infections, and cancer.
Gel chromatography is a type of liquid chromatography that separates molecules based on their size or molecular weight. It uses a stationary phase that consists of a gel matrix made up of cross-linked polymers, such as dextran, agarose, or polyacrylamide. The gel matrix contains pores of various sizes, which allow smaller molecules to penetrate deeper into the matrix while larger molecules are excluded.
In gel chromatography, a mixture of molecules is loaded onto the top of the gel column and eluted with a solvent that moves down the column by gravity or pressure. As the sample components move down the column, they interact with the gel matrix and get separated based on their size. Smaller molecules can enter the pores of the gel and take longer to elute, while larger molecules are excluded from the pores and elute more quickly.
Gel chromatography is commonly used to separate and purify proteins, nucleic acids, and other biomolecules based on their size and molecular weight. It is also used in the analysis of polymers, colloids, and other materials with a wide range of applications in chemistry, biology, and medicine.
Hemagglutination is a medical term that refers to the agglutination or clumping together of red blood cells (RBCs) in the presence of an agglutinin, which is typically a protein or a polysaccharide found on the surface of certain viruses, bacteria, or incompatible blood types.
In simpler terms, hemagglutination occurs when the agglutinin binds to specific antigens on the surface of RBCs, causing them to clump together and form visible clumps or aggregates. This reaction is often used in diagnostic tests to identify the presence of certain viruses or bacteria, such as influenza or HIV, by mixing a sample of blood or other bodily fluid with a known agglutinin and observing whether hemagglutination occurs.
Hemagglutination inhibition (HI) assays are also commonly used to measure the titer or concentration of antibodies in a serum sample, by adding serial dilutions of the serum to a fixed amount of agglutinin and observing the highest dilution that still prevents hemagglutination. This can help determine whether a person has been previously exposed to a particular pathogen and has developed immunity to it.
Methylglucosides are not a medical term, but rather a chemical term referring to a type of compound known as glycosides, where a methanol molecule is linked to a glucose molecule. They do not have a specific medical relevance, but they can be used in various industrial and laboratory applications, including as sweetening agents or intermediates in chemical reactions.
However, if you meant "Methylglucamine," it is a related term that has medical significance. Methylglucamine is an organic compound used as an excipient (an inactive substance that serves as a vehicle or medium for a drug) in some pharmaceutical formulations. It is often used as a solubilizing agent to improve the solubility and absorption of certain drugs, particularly those that are poorly soluble in water. Methylglucamine is generally considered safe and non-toxic, although it can cause gastrointestinal symptoms such as diarrhea or nausea in some individuals if taken in large amounts.
A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.
Methylglycosides are not a recognized medical term or concept. However, in chemistry, methylglycosides refer to glycosidic compounds in which the glycosidic linkage is formed between a hemiacetal or hemiketal of a monosaccharide and a methanol molecule. These compounds are not typically associated with medical definitions or applications, but rather fall under the broader categories of organic chemistry or biochemistry.
Peanut agglutinin (PNA) is a lectin, a type of carbohydrate-binding protein, found in peanuts. It is known to bind specifically to Galβ1-3GalNAc, a disaccharide present on glycoproteins and glycolipids of various cells. PNA has been used in research as a tool for identifying and isolating specific cell types, such as immature red blood cells (reticulocytes) and certain types of cancer cells, due to its affinity for these structures. However, it's important to note that peanut agglutinin may also have potential implications in the development of allergies to peanuts.
Nucleotidases are a class of enzymes that catalyze the hydrolysis of nucleotides into nucleosides and phosphate groups. Nucleotidases play important roles in various biological processes, including the regulation of nucleotide concentrations within cells, the salvage pathways for nucleotide synthesis, and the breakdown of nucleic acids during programmed cell death (apoptosis).
There are several types of nucleotidases that differ in their substrate specificity and subcellular localization. These include:
1. Nucleoside monophosphatases (NMPs): These enzymes hydrolyze nucleoside monophosphates (NMPs) into nucleosides and inorganic phosphate.
2. Nucleoside diphosphatases (NDPs): These enzymes hydrolyze nucleoside diphosphates (NDPs) into nucleoside monophosphates (NMPs) and inorganic phosphate.
3. Nucleoside triphosphatases (NTPs): These enzymes hydrolyze nucleoside triphosphates (NTPs) into nucleoside diphosphates (NDPs) and inorganic phosphate.
4. 5'-Nucleotidase: This enzyme specifically hydrolyzes the phosphate group from the 5' position of nucleoside monophosphates, producing nucleosides.
5. Pyrophosphatases: These enzymes hydrolyze pyrophosphates into two phosphate groups and play a role in regulating nucleotide metabolism.
Nucleotidases are widely distributed in nature and can be found in various tissues, organs, and biological fluids, including blood, urine, and cerebrospinal fluid. Dysregulation of nucleotidase activity has been implicated in several diseases, such as cancer, neurodegenerative disorders, and infectious diseases.
Inbred strains of mice are defined as lines of mice that have been brother-sister mated for at least 20 consecutive generations. This results in a high degree of homozygosity, where the mice of an inbred strain are genetically identical to one another, with the exception of spontaneous mutations.
Inbred strains of mice are widely used in biomedical research due to their genetic uniformity and stability, which makes them useful for studying the genetic basis of various traits, diseases, and biological processes. They also provide a consistent and reproducible experimental system, as compared to outbred or genetically heterogeneous populations.
Some commonly used inbred strains of mice include C57BL/6J, BALB/cByJ, DBA/2J, and 129SvEv. Each strain has its own unique genetic background and phenotypic characteristics, which can influence the results of experiments. Therefore, it is important to choose the appropriate inbred strain for a given research question.
In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.
The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.
In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.
Drug-Induced Liver Injury (DILI) is a medical term that refers to liver damage or injury caused by the use of medications or drugs. This condition can vary in severity, from mild abnormalities in liver function tests to severe liver failure, which may require a liver transplant.
The exact mechanism of DILI can differ depending on the drug involved, but it generally occurs when the liver metabolizes the drug into toxic compounds that damage liver cells. This can happen through various pathways, including direct toxicity to liver cells, immune-mediated reactions, or metabolic idiosyncrasies.
Symptoms of DILI may include jaundice (yellowing of the skin and eyes), fatigue, abdominal pain, nausea, vomiting, loss of appetite, and dark urine. In severe cases, it can lead to complications such as ascites, encephalopathy, and bleeding disorders.
The diagnosis of DILI is often challenging because it requires the exclusion of other potential causes of liver injury. Liver function tests, imaging studies, and sometimes liver biopsies may be necessary to confirm the diagnosis. Treatment typically involves discontinuing the offending drug and providing supportive care until the liver recovers. In some cases, medications that protect the liver or promote its healing may be used.
Cytochalasin B is a fungal metabolite that inhibits actin polymerization in cells, which can disrupt the cytoskeleton and affect various cellular processes such as cell division and motility. It is often used in research to study actin dynamics and cell shape.
Glucosamine is a natural compound found in the body, primarily in the fluid around joints. It is a building block of cartilage, which is the tissue that cushions bones and allows for smooth joint movement. Glucosamine can also be produced in a laboratory and is commonly sold as a dietary supplement.
Medical definitions of glucosamine describe it as a type of amino sugar that plays a crucial role in the formation and maintenance of cartilage, ligaments, tendons, and other connective tissues. It is often used as a supplement to help manage osteoarthritis symptoms, such as pain, stiffness, and swelling in the joints, by potentially reducing inflammation and promoting cartilage repair.
There are different forms of glucosamine available, including glucosamine sulfate, glucosamine hydrochloride, and N-acetyl glucosamine. Glucosamine sulfate is the most commonly used form in supplements and has been studied more extensively than other forms. While some research suggests that glucosamine may provide modest benefits for osteoarthritis symptoms, its effectiveness remains a topic of ongoing debate among medical professionals.
The thymus gland is an essential organ of the immune system, located in the upper chest, behind the sternum and surrounding the heart. It's primarily active until puberty and begins to shrink in size and activity thereafter. The main function of the thymus gland is the production and maturation of T-lymphocytes (T-cells), which are crucial for cell-mediated immunity, helping to protect the body from infection and cancer.
The thymus gland provides a protected environment where immune cells called pre-T cells develop into mature T cells. During this process, they learn to recognize and respond appropriately to foreign substances while remaining tolerant to self-tissues, which is crucial for preventing autoimmune diseases.
Additionally, the thymus gland produces hormones like thymosin that regulate immune cell activities and contribute to the overall immune response.
Monosaccharides are simple sugars that cannot be broken down into simpler units by hydrolysis. They are the most basic unit of carbohydrates and are often referred to as "simple sugars." Monosaccharides typically contain three to seven atoms of carbon, but the most common monosaccharides contain five or six carbon atoms.
The general formula for a monosaccharide is (CH2O)n, where n is the number of carbon atoms in the molecule. The majority of monosaccharides have a carbonyl group (aldehyde or ketone) and multiple hydroxyl groups. These functional groups give monosaccharides their characteristic sweet taste and chemical properties.
The most common monosaccharides include glucose, fructose, and galactose, all of which contain six carbon atoms and are known as hexoses. Other important monosaccharides include pentoses (five-carbon sugars) such as ribose and deoxyribose, which play crucial roles in the structure and function of nucleic acids (DNA and RNA).
Monosaccharides can exist in various forms, including linear and cyclic structures. In aqueous solutions, monosaccharides often form cyclic structures through a reaction between the carbonyl group and a hydroxyl group, creating a hemiacetal or hemiketal linkage. These cyclic structures can adopt different conformations, known as anomers, depending on the orientation of the hydroxyl group attached to the anomeric carbon atom.
Monosaccharides serve as essential building blocks for complex carbohydrates, such as disaccharides (e.g., sucrose, lactose, and maltose) and polysaccharides (e.g., starch, cellulose, and glycogen). They also participate in various biological processes, including energy metabolism, cell recognition, and protein glycosylation.
Lymphokines are a type of cytokines that are produced and released by activated lymphocytes, a type of white blood cell, in response to an antigenic stimulation. They play a crucial role in the regulation of immune responses and inflammation. Lymphokines can mediate various biological activities such as chemotaxis, activation, proliferation, and differentiation of different immune cells including lymphocytes, monocytes, macrophages, and eosinophils. Examples of lymphokines include interleukins (ILs), interferons (IFNs), tumor necrosis factor (TNF), and colony-stimulating factors (CSFs).
Thymidine is a pyrimidine nucleoside that consists of a thymine base linked to a deoxyribose sugar by a β-N1-glycosidic bond. It plays a crucial role in DNA replication and repair processes as one of the four nucleosides in DNA, along with adenosine, guanosine, and cytidine. Thymidine is also used in research and clinical settings for various purposes, such as studying DNA synthesis or as a component of antiviral and anticancer therapies.
Cellular immunity, also known as cell-mediated immunity, is a type of immune response that involves the activation of immune cells, such as T lymphocytes (T cells), to protect the body against infected or damaged cells. This form of immunity is important for fighting off infections caused by viruses and intracellular bacteria, as well as for recognizing and destroying cancer cells.
Cellular immunity involves a complex series of interactions between various immune cells and molecules. When a pathogen infects a cell, the infected cell displays pieces of the pathogen on its surface in a process called antigen presentation. This attracts T cells, which recognize the antigens and become activated. Activated T cells then release cytokines, chemicals that help coordinate the immune response, and can directly attack and kill infected cells or help activate other immune cells to do so.
Cellular immunity is an important component of the adaptive immune system, which is able to learn and remember specific pathogens in order to mount a faster and more effective response upon subsequent exposure. This form of immunity is also critical for the rejection of transplanted organs, as the immune system recognizes the transplanted tissue as foreign and attacks it.
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.
Cell division is the process by which a single eukaryotic cell (a cell with a true nucleus) divides into two identical daughter cells. This complex process involves several stages, including replication of DNA, separation of chromosomes, and division of the cytoplasm. There are two main types of cell division: mitosis and meiosis.
Mitosis is the type of cell division that results in two genetically identical daughter cells. It is a fundamental process for growth, development, and tissue repair in multicellular organisms. The stages of mitosis include prophase, prometaphase, metaphase, anaphase, and telophase, followed by cytokinesis, which divides the cytoplasm.
Meiosis, on the other hand, is a type of cell division that occurs in the gonads (ovaries and testes) during the production of gametes (sex cells). Meiosis results in four genetically unique daughter cells, each with half the number of chromosomes as the parent cell. This process is essential for sexual reproduction and genetic diversity. The stages of meiosis include meiosis I and meiosis II, which are further divided into prophase, prometaphase, metaphase, anaphase, and telophase.
In summary, cell division is the process by which a single cell divides into two daughter cells, either through mitosis or meiosis. This process is critical for growth, development, tissue repair, and sexual reproduction in multicellular organisms.
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.
Glycosylation is the enzymatic process of adding a sugar group, or glycan, to a protein, lipid, or other organic molecule. This post-translational modification plays a crucial role in modulating various biological functions, such as protein stability, trafficking, and ligand binding. The structure and composition of the attached glycans can significantly influence the functional properties of the modified molecule, contributing to cell-cell recognition, signal transduction, and immune response regulation. Abnormal glycosylation patterns have been implicated in several disease states, including cancer, diabetes, and neurodegenerative disorders.
3,3'-Diaminobenzidine (DAB) is a chemical compound that is commonly used as a chromogen in histological and immunohistochemical staining techniques. It is a type of polymerization substrate that reacts with horseradish peroxidase (HRP) to produce an insoluble, dark-brown precipitate at the site of the antigen-antibody reaction. This allows for the visualization and localization of specific proteins or other antigens within tissue sections.
The chemical formula for DAB is C12H12N2O2, and it is a light-sensitive compound that should be handled and stored in a dark environment to prevent unwanted photochemical reactions. It is important to note that DAB is considered a potential carcinogen and should be handled with appropriate safety precautions, including the use of gloves, lab coats, and eye protection.
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.
Regulatory T-lymphocytes (Tregs), also known as suppressor T cells, are a subpopulation of T-cells that play a critical role in maintaining immune tolerance and preventing autoimmune diseases. They function to suppress the activation and proliferation of other immune cells, thereby regulating the immune response and preventing it from attacking the body's own tissues.
Tregs constitutively express the surface markers CD4 and CD25, as well as the transcription factor Foxp3, which is essential for their development and function. They can be further divided into subsets based on their expression of other markers, such as CD127 and CD45RA.
Tregs are critical for maintaining self-tolerance by suppressing the activation of self-reactive T cells that have escaped negative selection in the thymus. They also play a role in regulating immune responses to foreign antigens, such as those encountered during infection or cancer, and can contribute to the immunosuppressive microenvironment found in tumors.
Dysregulation of Tregs has been implicated in various autoimmune diseases, including type 1 diabetes, rheumatoid arthritis, and multiple sclerosis, as well as in cancer and infectious diseases. Therefore, understanding the mechanisms that regulate Treg function is an important area of research with potential therapeutic implications.
Concanavalin A
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ITIH2
ITIH1
William Lipscomb
James Naismith (chemist)
Canavalin
Circular permutation in proteins
Mildred Gordon (biologist)
Leguminous lectin family
Gelonin
Glutathione reductase
Tetrandrine
JacSue Kehoe
Ahmad Salahuddin
Cytochalasin B
MPZL1
Methanosarcinales S-layer Tile Protein
Dynamic combinatorial chemistry
Beth Mallard
BanLec
Fluorescent glucose biosensor
Proliferative vitreoretinopathy
Model lipid bilayer
Lectin
Bafilomycin
Canavalia ensiformis
Phosphatidylserine
Blood glucose monitoring
Concanavalin A - Wikipedia
Lectins: Concanavalin A (Con A), Biotinylated
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Concanavalin A Cona
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Lectin10
- Concanavalin A (ConA) is a lectin (carbohydrate-binding protein) originally extracted from the jack-bean (Canavalia ensiformis). (wikipedia.org)
- Biotinylated Concanavalin A has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin. (vectorlabs.com)
- Concanavalin A is a lectin found in Canavelia that exhibits immunostimulatory, pro-fibrotic, and anticancer chemotherapeutic activities. (lktlabs.com)
- Lectin of Concanavalin A as an anti-hepatoma therapeutic agent. (lktlabs.com)
- Noonan KD, Burger MM. The relationship of concanavalin A binding to lectin-initiated cell agglutination. (lktlabs.com)
- Metabolic labeling of immature jackbean cotyledons with 14C-amino acids was used to determine the processing steps involved in the assembly of concanavalin A. Pulse-chase experiments and analyses of immunoprecipitated lectin forms indicated a complex series of events involving seven distinct species. (rupress.org)
- NH2-terminal sequencing of the abundant precursors confirmed that the intact subunit of concanavalin A was formed by the reannealing of two fragments, since the alignment of residues 1-118 and 119-237 was reversed in the final form of the lectin identified in the chase and the precursor first labeled. (rupress.org)
- Concanavalin A is a unique lectin purified from the jack bean, C. ensiformis, that selectively cross-links cell-surface glycoproteins and affects the initiation of cell agglutination, mitogenesis, and apoptosis. (bertin-bioreagent.com)
- Concanavalin A (Con A) completely inhibits IgG-dependent adhesion of human neutrophils, demonstrating lectin-dependent modulation of cell receptor functions. (consensus.app)
- The liver injury was induced by injection of concanavalin A (con-A), a lectin derived from jack beans. (biomedcentral.com)
Hepatitis6
- Inhibitory effect of liposomal quercetin on acute hepatitis and hepatic fibrosis induced by concanavalin A. Braz J Med Biol Res. (lktlabs.com)
- 23897,8536} At 20 mg/kg concanavalin A is also used to induce liver injury in experimental mouse models of autoimmune hepatitis in order to study immune regulation by macrophages and T cells. (bertin-bioreagent.com)
- Curcumin inhibits HMGB1 releasing and attenuates concanavalin A-induced hepatitis in mice. (greenmedinfo.com)
- Oral administration of ovalbumin protects mice from concanavalin A-induced hepatitis through suppression of interferon-gamma responses. (bvsalud.org)
- Oral administration of OVA at high doses inhibited the development of OVA -specific and concanavalin A (Con A)-induced hepatitis in DO11.10 mice , and these effects were associated with the downregulation of Th1 responses. (bvsalud.org)
- Increase in hepatic NKT cells in leukocyte cell-derived chemotaxin 2-deficient mice contributes to severe concanavalin A-induced hepatitis. (ox.ac.uk)
Mannose3
- Concanavalin A interacts with diverse receptors containing mannose carbohydrates, notably rhodopsin, blood group markers, insulin-receptor the Immunoglobulins and the carcino-embryonary antigen (CEA). (wikipedia.org)
- 23899} Concanavalin A specifically binds to α-mannose and α-galactose structures found in sugars, glycoproteins, and glycolipids and has been used in affinity chromatography purifications of various glycoproteins and cellular structures. (bertin-bioreagent.com)
- Affinity chromatography was employed to separate any mixture of compounds based on their affinity towards Concanavalin A, a mannose specific protein. (montana.edu)
Lectins2
- The distinctive saccharide-binding properties of plant lectins, resembling Concanavalin A (Con A) have made them helpful for the labeling and isolation of glycanpresenting cells and glycoproteins in serum and cell lysate. (gentaurpriceonline.com)
- Concanavalin A-like lectins/glucanases superfamily assignments to Clostridium botulinum A str. (cam.ac.uk)
Affinity chromatography1
- Concanavalin A (Con A) affinity chromatography is the standard procedure to separate cholesterol nucleating biliary proteins from lipids and pigment. (wustl.edu)
Protein3
- 7: Marks A, Labourdette G. Succinyl concanavalin A stimulates and antimicrotubular drugs inhibit the synthesis of a brain-specific protein in rat glial cells Proc Natl Acad Sci U S A. 1977 Sep;74(9):3855-8. (moleculardepot.com)
- Involvement of water in carbohydrate-protein binding: concanavalin A revisited. (expasy.org)
- I am working on concanavalin A protein. (bio.net)
Liver injury2
- Curcumin attenuates Concanavalin A-induced liver injury in mice. (greenmedinfo.com)
- This research is undertaken to evaluate the effect of MSC-derived exosome on concanavalin-A (con-A)-induced liver injury. (biomedcentral.com)
Mice1
- In addition, the inflammatory response to concanavalin A was assessed in mice. (news-medical.net)
Glucose1
- Labib, M., Hedström, M. , Amin, M., Mattiasson, B. A novel competitive capacitive glucose biosensor based on concanavalin A-labeled nano-gold colloids assembled on a polytyramine-modified gold electrode. (lu.se)
Membranes1
- The concanavalin A receptor from human erythrocytes in lipid bilayer membranes. (moleculardepot.com)
Differential1
- Differential effects of concanavalin A and succinyl concanavalin A on the macromolecular events of platelet activation Biochim Biophys Acta. (moleculardepot.com)
Vivo1
- In vivo, concanavalin A induces fibrosis. (lktlabs.com)
Partially purified2
- To investigate the functional capabilities of Thy-1 + dEC in vitro, cell suspensions prepared from trypsin-disaggregated sheets of mouse body wall epidermis were first enriched to 8 to 20% Ia + and 20 to 40% Thy-1 + cells by centrifugation over Isolymph and then were cultured for 2 to 10 days with Concanavalin A (Con A) and/or partially purified rat IL 2. (elsevierpure.com)
- T cell growth factor (TCGF) resulting from the incubation of murine splenocytes with concanavalin A (Con A) has been partially purified and separated from Con A. Sequential application of 50-70% saturated ammonium sulfate precipitation and G-100 gel filtration chromatography has resulted in a 300-fold purification of TCGF with a 60% yield. (johnshopkins.edu)
Cells5
- We have identified two populations of human lymphocytes differing in responsiveness to the plant mitogen concanavalin A (Con-A). When peripheral blood lymphocytes are passed through a nylon column a population of lymphocytes highly responsive to Con-A adheres to the fibers while a second population of cells relatively unresponsive to Con-A emerges from the column. (jci.org)
- Dwyer JM, Johnson C. The use of concanavalin A to study the immunoregulation of human T cells. (lktlabs.com)
- Quantitative studies on concanavalin A-induced, TCGF-reactive T cells. (elsevierpure.com)
- Dive into the research topics of 'Quantitative studies on concanavalin A-induced, TCGF-reactive T cells. (elsevierpure.com)
- Polyploidization and fusion of insect cells exposed to concanavalin A]. Dokl Akad Nauk SSSR . (medscape.com)
Receptors1
- Regulation of insulin receptors in frog erythrocytes by insulin and concanavalin A. Evidence for discrete classes of insulin binding sites. (aspetjournals.org)
Stimulation1
- In 72 hr cultures the lowest supraoptimal dose of Concanavalin (Con A) showing no stimulation of rat thymocytes above background was 160 μg/ml. (usuhs.edu)
Glycoprotein2
- Concanavalin A (Con A) is covalently connected to functionalized BioMag Plus particles to be used in glycoprotein isolations from serum and mobile extracts. (gentaurpriceonline.com)
- Concanavalin A Column for Analysis of Glycoprotein. (analyteguru.com)
ChIP1
- BioMag Concanavalin A has additionally been used for CUT&RUN, a chromatin profiling protocol that has a number of key benefits over ChIP. (gentaurpriceonline.com)
Tumor2
- In animal models of hepatoma, concanavalin A induces autophagy and cell death and decreases tumor nodule formation. (lktlabs.com)
- 23900,23898} Concanavalin A is toxic to several tumor cell lines and has been reported to induce programmed cell death of cortical neurons by a mechanism similar to that of the amyloid β peptide. (bertin-bioreagent.com)
Biochemistry1
- 10: Mandal DK, Brewer CF. Differences in the binding affinities of dimeric concanavalin A (including acetyl and succinyl derivatives) and tetrameric concanavalin A with large oligomannose-type glycopeptides Biochemistry. (moleculardepot.com)
Chains1
- 9: Kido N, Ohta M, Kato N. Inhibition by succinyl concanavalin A of strong adjuvant activity of lipopolysaccharides which possess mannans as the O-specific polysaccharide chains Cell Immunol. (moleculardepot.com)
Cell4
- A concanavalin-A-induced suppressor cell assay was carried out in 10 patients with chronic filarial disease, 13 asymptomatic microfilaria carriers and 7 healthy subjects. (karger.com)
- Concanavalin A is used in research to study cell adhesion. (lktlabs.com)
- Effects of bovine serum albumin on the interaction of concanavalin A and succinyl-concanavalin A with phospholipid bilayers Can J Biochem Cell Biol. (moleculardepot.com)
- Electrokinetic response of granulocytes to concanavalin A and succinyl-concanavalin A Cell Biophys. (moleculardepot.com)
Journal1
- Behenic Acid Monolayer and Bilayer Assemblies- A Study of Concanavalin A (Con A) Adsorption and its Interaction with Dextran Using Surface Plasmon Resonance Spectroscopy and Microscopy', Iranian Journal of Chemistry and Chemical Engineering , 12(1), pp. 22-31. (ac.ir)
Product2
- Cross selling for this product : Concanavalin A There are 3 products. (bertin-bioreagent.com)
- Succinyl-Concanavalin A is a high quality Succinyl-Concanavalin A. This product has been used as molecular tool for various biochemical applications. (moleculardepot.com)
Analysis1
- Capillary electrophoresis analysis of concanavalin A and its succinyl derivative J Pharm Biomed Anal. (moleculardepot.com)
Effect1
- 2: Grail A, Norval M. Effect of concanavalin A and succinyl concanavalin A on cytomegalovirus replication in fibroblasts Arch Virol. (moleculardepot.com)