Heparan Sulfate Proteoglycans
Heparitin Sulfate
Syndecans
Syndecan-2
Syndecan-1
Heparin
Glycosaminoglycans
Chondroitin Sulfate Proteoglycans
Syndecan-4
Heparin Lyase
Polysaccharide-Lyases
Syndecan-3
Glypicans
Chondroitin Sulfates
Chondroitinases and Chondroitin Lyases
Cell Membrane
CHO Cells
Receptors, Virus
Cricetinae
Protein Binding
Cells, Cultured
Glucuronidase
Basement Membrane
Molecular Sequence Data
Virus Attachment
Amino Acid Sequence
Fibroblast Growth Factor 2
Dermatan Sulfate
Lipoprotein Lipase
Cysteine-Rich Protein 61
Sulfotransferases
Sulfur Radioisotopes
Low Density Lipoprotein Receptor-Related Protein-1
Cattle
Keratan Sulfate
Binding Sites
Fibroblasts
Protein Structure, Tertiary
Viral Envelope Proteins
Chondroitin
Extracellular Matrix
Laminin
Chondroitin Lyases
Extracellular Matrix Proteins
Tumor Cells, Cultured
Signal Transduction
Base Sequence
Versicans
Transfection
Agrin
Glucosamine
Nitrous Acid
Fibronectins
Glycosides
Collagen
Chromatography, Gel
RNA, Messenger
Aggrecans
Decorin
Oligosaccharides
Virion
Cartilage
Electrophoresis, Polyacrylamide Gel
Receptors, Fibroblast Growth Factor
Fluorescent Antibody Technique
Chondroitin ABC Lyase
Neurocan
Immunohistochemistry
Chromatography, Ion Exchange
Chick Embryo
Iduronic Acid
Chromatography, Affinity
Endothelium, Vascular
Hyaluronic Acid
Glycoproteins
Lectins, C-Type
Models, Biological
Microscopy, Electron
Receptors, Cell Surface
Kidney Glomerulus
Peptide Fragments
Fibroblast Growth Factor 1
Sulfatases
Membrane Proteins
Tenascin
Cloning, Molecular
Cornea
Receptor-Like Protein Tyrosine Phosphatases, Class 5
Carbohydrate Sequence
Epithelium
Cell Movement
Cell Division
Fibroblast Growth Factors
Heparan sulfate proteoglycans (HSPGs) are complex molecules composed of a core protein to which one or more heparan sulfate (HS) glycosaminoglycan chains are covalently attached. They are widely distributed in animal tissues and play crucial roles in various biological processes, including cell-cell communication, growth factor signaling, viral infection, and cancer metastasis.
The HS chains are long, linear polysaccharides composed of repeating disaccharide units of glucosamine and uronic acid (either glucuronic or iduronic acid). These chains contain sulfate groups at various positions, which give them a negative charge and allow them to interact with numerous proteins, growth factors, and enzymes.
HSPGs can be found on the cell surface (syndecans and glypicans) or in the extracellular matrix (perlecans and agrin). They act as co-receptors for many signaling molecules, such as fibroblast growth factors (FGFs), wingless-type MMTV integration site family members (WNTs), and hedgehog proteins. By modulating the activity of these signaling pathways, HSPGs help regulate various cellular functions, including proliferation, differentiation, migration, and adhesion.
Dysregulation of HSPGs has been implicated in several diseases, such as cancer, fibrosis, and viral infections (e.g., HIV and herpes simplex virus). Therefore, understanding the structure and function of HSPGs is essential for developing new therapeutic strategies to target these diseases.
Heparin sulfate is not exactly referred to as "heparitin sulfate" in medical terminology. The correct term is heparan sulfate, which is a type of glycosaminoglycan (GAG), a long unbranched chain of repeating disaccharide units composed of a hexuronic acid and a hexosamine.
Heparan sulfate is found on the cell surface and in the extracellular matrix, where it plays crucial roles in various biological processes, including cell signaling, regulation of growth factor activity, and control of blood coagulation. It is also an important component of the proteoglycans, which are complex molecules that help to maintain the structural integrity and function of tissues and organs.
Like heparin, heparan sulfate has a high negative charge due to the presence of sulfate groups, which allows it to bind to and interact with various proteins and growth factors. However, heparan sulfate has a more diverse structure than heparin, with variations in the pattern of sulfation along the chain, which leads to specificity in its interactions with different proteins.
Defects in heparan sulfate biosynthesis or function have been implicated in various human diseases, including certain forms of cancer, developmental disorders, and infectious diseases.
Syndecans are a group of transmembrane proteoglycans that play important roles in various cellular functions, such as cell adhesion, migration, and growth regulation. They consist of a core protein with one or more covalently attached glycosaminoglycan (GAG) chains. These GAG chains can interact with extracellular matrix components, growth factors, and cytokines, thereby mediating various cell-matrix and cell-cell interactions. Syndecans have been implicated in several biological processes, including embryonic development, angiogenesis, wound healing, and tumor progression.
Syndecan-2 is a type of transmembrane heparan sulfate proteoglycan that is widely expressed in various cell types, including endothelial cells and fibroblasts. It plays a crucial role in the regulation of cellular signaling, adhesion, and migration by interacting with extracellular matrix components, growth factors, and cytokines. Syndecan-2 has been implicated in several biological processes, including angiogenesis, wound healing, and tumor progression.
In medical terms, Syndecan-2 is defined as a cell surface proteoglycan that belongs to the syndecan family of four members (Syndecan-1, -2, -3, and -4). It has a molecular weight of approximately 25-30 kDa and consists of a core protein with attached heparan sulfate chains. The cytoplasmic domain of Syndecan-2 interacts with various intracellular signaling molecules, such as kinases, adaptor proteins, and cytoskeletal components, thereby mediating cellular responses to extracellular stimuli.
Syndecan-2 has been shown to be involved in the regulation of several signaling pathways, including the Wnt/β-catenin, fibroblast growth factor (FGF), and vascular endothelial growth factor (VEGF) pathways. Dysregulation of Syndecan-2 expression or function has been associated with various pathological conditions, such as cancer, fibrosis, and inflammation.
In summary, Syndecan-2 is a crucial regulator of cellular signaling, adhesion, and migration, and its dysregulation has been implicated in several diseases.
Proteoglycans are complex, highly negatively charged macromolecules that are composed of a core protein covalently linked to one or more glycosaminoglycan (GAG) chains. They are a major component of the extracellular matrix (ECM) and play crucial roles in various biological processes, including cell signaling, regulation of growth factor activity, and maintenance of tissue structure and function.
The GAG chains, which can vary in length and composition, are long, unbranched polysaccharides that are composed of repeating disaccharide units containing a hexuronic acid (either glucuronic or iduronic acid) and a hexosamine (either N-acetylglucosamine or N-acetylgalactosamine). These GAG chains can be sulfated to varying degrees, which contributes to the negative charge of proteoglycans.
Proteoglycans are classified into four major groups based on their core protein structure and GAG composition: heparan sulfate/heparin proteoglycans, chondroitin/dermatan sulfate proteoglycans, keratan sulfate proteoglycans, and hyaluronan-binding proteoglycans. Each group has distinct functions and is found in specific tissues and cell types.
In summary, proteoglycans are complex macromolecules composed of a core protein and one or more GAG chains that play important roles in the ECM and various biological processes, including cell signaling, growth factor regulation, and tissue structure maintenance.
Syndecan-1 is a type of transmembrane heparan sulfate proteoglycan that is widely expressed in various tissues, including epithelial cells and platelets. It plays a crucial role in cell proliferation, differentiation, migration, and angiogenesis by interacting with extracellular matrix components, growth factors, and cytokines. Syndecan-1 is also known as CD138 or Leu-19 and can be used as a marker for plasma cells in the diagnosis of certain diseases such as multiple myeloma.
Heparin is defined as a highly sulfated glycosaminoglycan (a type of polysaccharide) that is widely present in many tissues, but is most commonly derived from the mucosal tissues of mammalian lungs or intestinal mucosa. It is an anticoagulant that acts as an inhibitor of several enzymes involved in the blood coagulation cascade, primarily by activating antithrombin III which then neutralizes thrombin and other clotting factors.
Heparin is used medically to prevent and treat thromboembolic disorders such as deep vein thrombosis, pulmonary embolism, and certain types of heart attacks. It can also be used during hemodialysis, cardiac bypass surgery, and other medical procedures to prevent the formation of blood clots.
It's important to note that while heparin is a powerful anticoagulant, it does not have any fibrinolytic activity, meaning it cannot dissolve existing blood clots. Instead, it prevents new clots from forming and stops existing clots from growing larger.
Glycosaminoglycans (GAGs) are long, unbranched polysaccharides composed of repeating disaccharide units. They are a major component of the extracellular matrix and connective tissues in the body. GAGs are negatively charged due to the presence of sulfate and carboxyl groups, which allows them to attract positively charged ions and water molecules, contributing to their ability to retain moisture and maintain tissue hydration and elasticity.
GAGs can be categorized into four main groups: heparin/heparan sulfate, chondroitin sulfate/dermatan sulfate, keratan sulfate, and hyaluronic acid. These different types of GAGs have varying structures and functions in the body, including roles in cell signaling, inflammation, and protection against enzymatic degradation.
Heparin is a highly sulfated form of heparan sulfate that is found in mast cells and has anticoagulant properties. Chondroitin sulfate and dermatan sulfate are commonly found in cartilage and contribute to its resiliency and ability to withstand compressive forces. Keratan sulfate is found in corneas, cartilage, and bone, where it plays a role in maintaining the structure and function of these tissues. Hyaluronic acid is a large, nonsulfated GAG that is widely distributed throughout the body, including in synovial fluid, where it provides lubrication and shock absorption for joints.
Chondroitin sulfate proteoglycans (CSPGs) are complex molecules found in the extracellular matrix of various connective tissues, including cartilage. They are composed of a core protein covalently linked to one or more glycosaminoglycan (GAG) chains, such as chondroitin sulfate and dermatan sulfate.
CSPGs play important roles in the structure and function of tissues, including:
1. Regulating water content and providing resilience to tissues due to their high negative charge, which attracts cations and bound water molecules.
2. Interacting with other matrix components, such as collagen and elastin, to form a highly organized network that provides tensile strength and elasticity.
3. Modulating cell behavior by interacting with various growth factors, cytokines, and cell surface receptors, thereby influencing processes like cell adhesion, proliferation, differentiation, and migration.
4. Contributing to the maintenance of the extracellular matrix homeostasis through their involvement in matrix turnover and remodeling.
In articular cartilage, CSPGs are particularly abundant and contribute significantly to its load-bearing capacity and overall health. Dysregulation of CSPGs has been implicated in various pathological conditions, such as osteoarthritis, where altered proteoglycan composition and content can lead to cartilage degradation and joint dysfunction.
Syndecan-4 is a type of cell surface proteoglycan, which is a type of protein that contains covalently attached glycosaminoglycans (GAGs). It is a member of the syndecan family, which includes four members (syndecan-1, -2, -3, and -4) that are involved in various cellular functions such as cell adhesion, migration, and growth regulation.
Syndecan-4 is widely expressed in many tissues, including the vascular endothelium, fibroblasts, and epithelial cells. It has a single transmembrane domain and a short cytoplasmic tail that interacts with intracellular signaling molecules, making it a key player in signal transduction pathways.
Syndecan-4 is involved in various biological processes such as wound healing, inflammation, and angiogenesis. It has been implicated in the regulation of cell proliferation, differentiation, and survival, as well as in the modulation of extracellular matrix (ECM) organization and turnover. Dysregulation of syndecan-4 expression or function has been associated with various pathological conditions such as cancer, fibrosis, and cardiovascular diseases.
Heparin Lyase, also known as Heparan Sulfate Lyase or Heparanase, is an enzyme that cleaves heparan sulfate proteoglycans (HSPGs), which are complex sugar-protein molecules found on the surface of many cells and in the extracellular matrix. These molecules play important roles in various biological processes such as cell growth, differentiation, and migration.
Heparin Lyase specifically cleaves heparan sulfate chains at a specific site, forming two unsaturated sugar residues. This enzyme is involved in the degradation of HSPGs during physiological processes like tissue remodeling and pathological conditions such as cancer metastasis, inflammation, and diabetic complications.
It's important to note that there are two main types of heparin lyases (heparin lyase I, II, and III) that differ in their substrate specificity and tissue distribution. Heparin Lyase I primarily acts on highly sulfated regions of heparan sulfate chains, while Heparin Lyase III prefers less sulfated domains. Heparin Lyase II has intermediate properties between the other two isoforms.
Polysaccharide-lyases are a class of enzymes that cleave polysaccharides through a β-elimination mechanism, leading to the formation of unsaturated sugars. These enzymes are also known as depolymerizing enzymes and play an essential role in the breakdown and modification of complex carbohydrates found in nature. They have important applications in various industries such as food, pharmaceuticals, and biofuels.
Polysaccharide-lyases specifically target polysaccharides containing uronic acid residues, such as pectins, alginates, and heparin sulfate. The enzymes cleave the glycosidic bond between two sugar residues by breaking the alpha configuration at carbon 4 of the uronic acid residue, resulting in a double bond between carbons 4 and 5 of the non-reducing end of the polysaccharide chain.
Polysaccharide-lyases are classified into several subclasses based on their substrate specificity and reaction mechanism. These enzymes have potential therapeutic applications, such as in the treatment of bacterial infections, cancer, and other diseases associated with abnormal glycosylation.
Syndecan-3 is a type of transmembrane heparan sulfate proteoglycan that is widely expressed in various tissues, including the nervous system. It plays important roles in cell adhesion, migration, and differentiation by interacting with extracellular matrix components, growth factors, and cytokines. Syndecan-3 has been implicated in several physiological and pathological processes, such as neuronal development, neuroinflammation, and neurodegenerative diseases. It is also known to be involved in the regulation of synaptic plasticity and pain perception.
Glypicans are a type of heparan sulfate proteoglycan (HSPG) that are attached to the cell membrane via a glycosylphosphatidylinositol (GPI) anchor. They are involved in various biological processes, such as cell growth, differentiation, and migration, by regulating the distribution and activity of various signaling molecules, including morphogens, growth factors, and Wnt proteins. There are six distinct glypican genes (GPC1-6) identified in humans, each encoding a unique protein isoform with a conserved core structure but varying in their specific functions and expression patterns. Abnormal glypican expression or function has been implicated in several diseases, including cancer, developmental disorders, and neurodegenerative diseases.
Chlorates are salts or esters of chloric acid (HClO3). They contain the chlorate ion (ClO3-) in their chemical structure. Chlorates are strong oxidizing agents and can be hazardous if mishandled. They have various uses, including in matches, explosives, and disinfectants, but they can also pose health risks if ingested or come into contact with the skin or eyes. Exposure to chlorates can cause irritation, burns, and other harmful effects. It is important to handle chlorates with care and follow proper safety precautions when using them.
Chondroitin sulfates are a type of complex carbohydrate molecules known as glycosaminoglycans (GAGs). They are a major component of cartilage, the tissue that cushions and protects the ends of bones in joints. Chondroitin sulfates are composed of repeating disaccharide units made up of glucuronic acid and N-acetylgalactosamine, which can be sulfated at various positions.
Chondroitin sulfates play a crucial role in the biomechanical properties of cartilage by attracting water and maintaining the resiliency and elasticity of the tissue. They also interact with other molecules in the extracellular matrix, such as collagen and proteoglycans, to form a complex network that provides structural support and regulates cell behavior.
Chondroitin sulfates have been studied for their potential therapeutic benefits in osteoarthritis, a degenerative joint disease characterized by the breakdown of cartilage. Supplementation with chondroitin sulfate has been shown to reduce pain and improve joint function in some studies, although the evidence is not consistent across all trials. The mechanism of action is thought to involve inhibition of enzymes that break down cartilage, as well as stimulation of cartilage repair and synthesis.
Chondroitinases and chondroitin lyases are enzymes that break down chondroitin sulfate, a type of glycosaminoglycan (GAG) found in connective tissues such as cartilage. Glycosaminoglycans are long, unbranched polysaccharides made up of repeating disaccharide units. In the case of chondroitin sulfate, the disaccharide unit consists of a glucuronic acid residue and a N-acetylgalactosamine residue that may be sulfated at various positions.
Chondroitinases are enzymes that cleave the linkage between the two sugars in the chondroitin sulfate chain, specifically between the carbon atom in the fourth position of the glucuronic acid and the nitrogen atom in the first position of the N-acetylgalactosamine. This results in the formation of unsaturated disaccharides. Chondroitinases are produced by certain bacteria and are used in research to study the structure and function of chondroitin sulfate and other GAGs.
Chondroitin lyases, on the other hand, are enzymes that cleave the same linkage but in the opposite direction, resulting in the formation of 4,5-unsaturated disaccharides. Chondroitin lyases are also produced by certain bacteria and are used in research to study the structure and function of chondroitin sulfate and other GAGs.
It is important to note that while both chondroitinases and chondroitin lyases break down chondroitin sulfate, they do so through different mechanisms and produce different products.
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.
CHO cells, or Chinese Hamster Ovary cells, are a type of immortalized cell line that are commonly used in scientific research and biotechnology. They were originally derived from the ovaries of a female Chinese hamster (Cricetulus griseus) in the 1950s.
CHO cells have several characteristics that make them useful for laboratory experiments. They can grow and divide indefinitely under appropriate conditions, which allows researchers to culture large quantities of them for study. Additionally, CHO cells are capable of expressing high levels of recombinant proteins, making them a popular choice for the production of therapeutic drugs, vaccines, and other biologics.
In particular, CHO cells have become a workhorse in the field of biotherapeutics, with many approved monoclonal antibody-based therapies being produced using these cells. The ability to genetically modify CHO cells through various methods has further expanded their utility in research and industrial applications.
It is important to note that while CHO cells are widely used in scientific research, they may not always accurately represent human cell behavior or respond to drugs and other compounds in the same way as human cells do. Therefore, results obtained using CHO cells should be validated in more relevant systems when possible.
Virus receptors are specific molecules (commonly proteins) on the surface of host cells that viruses bind to in order to enter and infect those cells. This interaction between the virus and its receptor is a critical step in the infection process. Different types of viruses have different receptor requirements, and identifying these receptors can provide important insights into the biology of the virus and potential targets for antiviral therapies.
Membrane glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. They are integral components of biological membranes, spanning the lipid bilayer and playing crucial roles in various cellular processes.
The glycosylation of these proteins occurs in the endoplasmic reticulum (ER) and Golgi apparatus during protein folding and trafficking. The attached glycans can vary in structure, length, and composition, which contributes to the diversity of membrane glycoproteins.
Membrane glycoproteins can be classified into two main types based on their orientation within the lipid bilayer:
1. Type I (N-linked): These glycoproteins have a single transmembrane domain and an extracellular N-terminus, where the oligosaccharides are predominantly attached via asparagine residues (Asn-X-Ser/Thr sequon).
2. Type II (C-linked): These glycoproteins possess two transmembrane domains and an intracellular C-terminus, with the oligosaccharides linked to tryptophan residues via a mannose moiety.
Membrane glycoproteins are involved in various cellular functions, such as:
* Cell adhesion and recognition
* Receptor-mediated signal transduction
* Enzymatic catalysis
* Transport of molecules across membranes
* Cell-cell communication
* Immunological responses
Some examples of membrane glycoproteins include cell surface receptors (e.g., growth factor receptors, cytokine receptors), adhesion molecules (e.g., integrins, cadherins), and transporters (e.g., ion channels, ABC transporters).
Disaccharides are a type of carbohydrate that is made up of two monosaccharide units bonded together. Monosaccharides are simple sugars, such as glucose, fructose, or galactose. When two monosaccharides are joined together through a condensation reaction, they form a disaccharide.
The most common disaccharides include:
* Sucrose (table sugar), which is composed of one glucose molecule and one fructose molecule.
* Lactose (milk sugar), which is composed of one glucose molecule and one galactose molecule.
* Maltose (malt sugar), which is composed of two glucose molecules.
Disaccharides are broken down into their component monosaccharides during digestion by enzymes called disaccharidases, which are located in the brush border of the small intestine. These enzymes catalyze the hydrolysis of the glycosidic bond that links the two monosaccharides together, releasing them to be absorbed into the bloodstream and used for energy.
Disorders of disaccharide digestion and absorption can lead to various symptoms, such as bloating, diarrhea, and abdominal pain. For example, lactose intolerance is a common condition in which individuals lack sufficient levels of the enzyme lactase, leading to an inability to properly digest lactose and resulting in gastrointestinal symptoms.
Cricetinae is a subfamily of rodents that includes hamsters, gerbils, and relatives. These small mammals are characterized by having short limbs, compact bodies, and cheek pouches for storing food. They are native to various parts of the world, particularly in Europe, Asia, and Africa. Some species are popular pets due to their small size, easy care, and friendly nature. In a medical context, understanding the biology and behavior of Cricetinae species can be important for individuals who keep them as pets or for researchers studying their physiology.
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.
Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.
In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.
Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.
"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.
Glucuronidase is an enzyme that catalyzes the hydrolysis of glucuronic acid from various substrates, including molecules that have been conjugated with glucuronic acid as part of the detoxification process in the body. This enzyme plays a role in the breakdown and elimination of certain drugs, toxins, and endogenous compounds, such as bilirubin. It is found in various tissues and organisms, including humans, bacteria, and insects. In clinical contexts, glucuronidase activity may be measured to assess liver function or to identify the presence of certain bacterial infections.
Cell adhesion refers to the binding of cells to extracellular matrices or to other cells, a process that is fundamental to the development, function, and maintenance of multicellular organisms. Cell adhesion is mediated by various cell surface receptors, such as integrins, cadherins, and immunoglobulin-like cell adhesion molecules (Ig-CAMs), which interact with specific ligands in the extracellular environment. These interactions lead to the formation of specialized junctions, such as tight junctions, adherens junctions, and desmosomes, that help to maintain tissue architecture and regulate various cellular processes, including proliferation, differentiation, migration, and survival. Disruptions in cell adhesion can contribute to a variety of diseases, including cancer, inflammation, and degenerative disorders.
The basement membrane is a thin, specialized layer of extracellular matrix that provides structural support and separates epithelial cells (which line the outer surfaces of organs and blood vessels) from connective tissue. It is composed of two main layers: the basal lamina, which is produced by the epithelial cells, and the reticular lamina, which is produced by the connective tissue. The basement membrane plays important roles in cell adhesion, migration, differentiation, and survival.
The basal lamina is composed mainly of type IV collagen, laminins, nidogens, and proteoglycans, while the reticular lamina contains type III collagen, fibronectin, and other matrix proteins. The basement membrane also contains a variety of growth factors and cytokines that can influence cell behavior.
Defects in the composition or organization of the basement membrane can lead to various diseases, including kidney disease, eye disease, and skin blistering disorders.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
A viral attachment, in the context of virology, refers to the initial step in the infection process of a host cell by a virus. This involves the binding or adsorption of the viral particle to specific receptors on the surface of the host cell. The viral attachment proteins, often located on the viral envelope or capsid, recognize and interact with these receptors, leading to a close association between the virus and the host cell. This interaction is highly specific, as different viruses may target various cell types based on their unique receptor-binding preferences. Following attachment, the virus can enter the host cell and initiate the replication cycle, ultimately leading to the production of new viral particles and potential disease manifestations.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
In the context of medicine and biology, sulfates are ions or compounds that contain the sulfate group (SO4−2). Sulfate is a polyatomic anion with the structure of a sphere. It consists of a central sulfur atom surrounded by four oxygen atoms in a tetrahedral arrangement.
Sulfates can be found in various biological molecules, such as glycosaminoglycans and proteoglycans, which are important components of connective tissue and the extracellular matrix. Sulfate groups play a crucial role in these molecules by providing negative charges that help maintain the structural integrity and hydration of tissues.
In addition to their biological roles, sulfates can also be found in various medications and pharmaceutical compounds. For example, some laxatives contain sulfate salts, such as magnesium sulfate (Epsom salt) or sodium sulfate, which work by increasing the water content in the intestines and promoting bowel movements.
It is important to note that exposure to high levels of sulfates can be harmful to human health, particularly in the form of sulfur dioxide (SO2), a common air pollutant produced by burning fossil fuels. Prolonged exposure to SO2 can cause respiratory problems and exacerbate existing lung conditions.
Fibroblast Growth Factor 2 (FGF-2), also known as basic fibroblast growth factor, is a protein involved in various biological processes such as cell growth, proliferation, and differentiation. It plays a crucial role in wound healing, embryonic development, and angiogenesis (the formation of new blood vessels). FGF-2 is produced and secreted by various cells, including fibroblasts, and exerts its effects by binding to specific receptors on the cell surface, leading to activation of intracellular signaling pathways. It has been implicated in several diseases, including cancer, where it can contribute to tumor growth and progression.
Dermatan sulfate is a type of glycosaminoglycan, which is a long, unbranched sugar chain found on the proteoglycan core protein in the extracellular matrix of animal tissues. It is composed of repeating disaccharide units of iduronic acid and N-acetylgalactosamine, with alternating sulfation at the 4-position of the iduronic acid and the 6-position of the galactosamine.
Dermatan sulfate is found in various tissues, including skin, heart valves, and blood vessels, where it plays important roles in regulating cell behavior, tissue development, and homeostasis. It also binds to a variety of growth factors, cytokines, and enzymes, modulating their activities and contributing to the regulation of various biological processes.
Abnormalities in dermatan sulfate metabolism can lead to several genetic disorders, such as Hunter syndrome and Hurler-Scheie syndrome, which are characterized by skeletal abnormalities, cardiac defects, and neurological impairment.
Lipoprotein lipase (LPL) is an enzyme that plays a crucial role in the metabolism of lipids. It is responsible for breaking down triglycerides, which are the main constituent of dietary fats and chylomicrons, into fatty acids and glycerol. These products are then taken up by cells for energy production or storage.
LPL is synthesized in various tissues, including muscle and fat, where it is attached to the inner lining of blood vessels (endothelium). The enzyme is activated when it comes into contact with lipoprotein particles, such as chylomicrons and very-low-density lipoproteins (VLDL), which transport triglycerides in the bloodstream.
Deficiencies or mutations in LPL can lead to various metabolic disorders, including hypertriglyceridemia, a condition characterized by high levels of triglycerides in the blood. Conversely, overexpression of LPL has been associated with increased risk of atherosclerosis due to excessive uptake of fatty acids by macrophages and their conversion into foam cells, which contribute to plaque formation in the arteries.
Cysteine-rich protein 61 (CYR61), also known as CCN1, is a matricellular protein that belongs to the CCN family. This protein is composed of four distinct domains: an insulin-like growth factor binding domain, a von Willebrand type C repeat domain, a thrombospondin type 1 repeat domain, and a C-terminal cysteine knot domain.
CYR61 plays important roles in various biological processes, including cell adhesion, migration, proliferation, differentiation, and survival. It is involved in the regulation of angiogenesis, wound healing, tissue repair, and tumorigenesis. Dysregulation of CYR61 has been implicated in several pathological conditions, such as fibrosis, atherosclerosis, and cancer.
In summary, Cysteine-rich protein 61 (CYR61) is a matricellular protein that regulates various cellular processes and is involved in the development of several diseases.
Sulfotransferases (STs) are a group of enzymes that play a crucial role in the process of sulfoconjugation, which is the transfer of a sulfo group (-SO3H) from a donor molecule to an acceptor molecule. These enzymes are widely distributed in nature and are found in various organisms, including humans.
In humans, STs are involved in the metabolism and detoxification of numerous xenobiotics, such as drugs, food additives, and environmental pollutants, as well as endogenous compounds, such as hormones, neurotransmitters, and lipids. The sulfoconjugation reaction catalyzed by STs can increase the water solubility of these compounds, facilitating their excretion from the body.
STs can be classified into several families based on their sequence similarity and cofactor specificity. The largest family of STs is the cytosolic sulfotransferases, which use 3'-phosphoadenosine 5'-phosphosulfate (PAPS) as a cofactor to transfer the sulfo group to various acceptor molecules, including phenols, alcohols, amines, and steroids.
Abnormalities in ST activity have been implicated in several diseases, such as cancer, cardiovascular disease, and neurological disorders. Therefore, understanding the function and regulation of STs is essential for developing new therapeutic strategies to treat these conditions.
Sulfur radioisotopes are unstable forms of the element sulfur that emit radiation as they decay into more stable forms. These isotopes can be used in medical imaging and treatment, such as in the detection and treatment of certain cancers. Common sulfur radioisotopes used in medicine include sulfur-35 and sulfur-32. Sulfur-35 is used in research and diagnostic applications, while sulfur-32 is used in brachytherapy, a type of internal radiation therapy. It's important to note that handling and usage of radioisotopes should be done by trained professionals due to the potential radiation hazards they pose.
Low-Density Lipoprotein Receptor-Related Protein 1 (LRP1) is a large transmembrane receptor protein that belongs to the low-density lipoprotein receptor family. It plays a crucial role in various biological processes, including cellular signaling, endocytosis, and intracellular trafficking of ligands. LRP1 is widely expressed in many tissues, particularly in the brain, liver, and vascular endothelial cells.
LRP1 interacts with a diverse array of ligands, such as extracellular matrix proteins, apolipoproteins, proteinases, proteinase inhibitors, and various pathogen-associated molecules. The receptor is involved in the clearance of these ligands from the extracellular space through endocytosis, followed by intracellular degradation or recycling.
In the context of lipid metabolism, LRP1 has been implicated in the cellular uptake and degradation of Apolipoprotein E (ApoE)-containing lipoproteins, which are involved in the reverse transport of cholesterol from peripheral tissues to the liver. Dysregulation of LRP1 function has been linked to several diseases, including atherosclerosis, Alzheimer's disease, and various neurological disorders.
In summary, Low-Density Lipoprotein Receptor-Related Protein 1 (LRP1) is a multifunctional transmembrane receptor that plays essential roles in cellular signaling, endocytosis, and intracellular trafficking of various ligands. Its dysfunction has been implicated in several diseases related to lipid metabolism, neurodegeneration, and neurological disorders.
"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.
Keratan sulfate is a type of glycosaminoglycan (GAG), which is a complex carbohydrate found in connective tissues, including the cornea and cartilage. It is composed of repeating disaccharide units of galactose and N-acetylglucosamine, with sulfate groups attached to some of the sugar molecules.
Keratan sulfate is unique among GAGs because it contains a high proportion of non-sulfated sugars and is often found covalently linked to proteins in structures called proteoglycans. In the cornea, keratan sulfate plays important roles in maintaining transparency and regulating hydration. In cartilage, it contributes to the elasticity and resilience of the tissue.
Abnormalities in keratan sulfate metabolism have been associated with several genetic disorders, including corneal dystrophies and skeletal dysplasias.
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.
Fibroblasts are specialized cells that play a critical role in the body's immune response and wound healing process. They are responsible for producing and maintaining the extracellular matrix (ECM), which is the non-cellular component present within all tissues and organs, providing structural support and biochemical signals for surrounding cells.
Fibroblasts produce various ECM proteins such as collagens, elastin, fibronectin, and laminins, forming a complex network of fibers that give tissues their strength and flexibility. They also help in the regulation of tissue homeostasis by controlling the turnover of ECM components through the process of remodeling.
In response to injury or infection, fibroblasts become activated and start to proliferate rapidly, migrating towards the site of damage. Here, they participate in the inflammatory response, releasing cytokines and chemokines that attract immune cells to the area. Additionally, they deposit new ECM components to help repair the damaged tissue and restore its functionality.
Dysregulation of fibroblast activity has been implicated in several pathological conditions, including fibrosis (excessive scarring), cancer (where they can contribute to tumor growth and progression), and autoimmune diseases (such as rheumatoid arthritis).
Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.
Viral envelope proteins are structural proteins found in the envelope that surrounds many types of viruses. These proteins play a crucial role in the virus's life cycle, including attachment to host cells, fusion with the cell membrane, and entry into the host cell. They are typically made up of glycoproteins and are often responsible for eliciting an immune response in the host organism. The exact structure and function of viral envelope proteins vary between different types of viruses.
Chondroitin is a type of molecule known as a glycosaminoglycan, which is found in the connective tissues of the body, including cartilage. It is a major component of proteoglycans, which are complex molecules that provide structural support and help retain water within the cartilage, allowing it to function as a cushion between joints.
Chondroitin sulfate, a form of chondroitin, is commonly used in dietary supplements for osteoarthritis, a condition characterized by the breakdown of cartilage in joints. The idea behind using chondroitin sulfate as a treatment for osteoarthritis is that it may help to rebuild damaged cartilage and reduce inflammation in the affected joints. However, research on the effectiveness of chondroitin sulfate for osteoarthritis has had mixed results, with some studies showing modest benefits while others have found no significant effects.
It's important to note that dietary supplements containing chondroitin are not regulated by the U.S. Food and Drug Administration (FDA) in the same way that drugs are, so the quality and purity of these products can vary widely. As with any supplement, it's a good idea to talk to your doctor before starting to take chondroitin, especially if you have any medical conditions or are taking other medications.
The extracellular matrix (ECM) is a complex network of biomolecules that provides structural and biochemical support to cells in tissues and organs. It is composed of various proteins, glycoproteins, and polysaccharides, such as collagens, elastin, fibronectin, laminin, and proteoglycans. The ECM plays crucial roles in maintaining tissue architecture, regulating cell behavior, and facilitating communication between cells. It provides a scaffold for cell attachment, migration, and differentiation, and helps to maintain the structural integrity of tissues by resisting mechanical stresses. Additionally, the ECM contains various growth factors, cytokines, and chemokines that can influence cellular processes such as proliferation, survival, and differentiation. Overall, the extracellular matrix is essential for the normal functioning of tissues and organs, and its dysregulation can contribute to various pathological conditions, including fibrosis, cancer, and degenerative diseases.
Laminin is a family of proteins that are an essential component of the basement membrane, which is a specialized type of extracellular matrix. Laminins are large trimeric molecules composed of three different chains: α, β, and γ. There are five different α chains, three different β chains, and three different γ chains that can combine to form at least 15 different laminin isoforms.
Laminins play a crucial role in maintaining the structure and integrity of basement membranes by interacting with other components of the extracellular matrix, such as collagen IV, and cell surface receptors, such as integrins. They are involved in various biological processes, including cell adhesion, differentiation, migration, and survival.
Laminin dysfunction has been implicated in several human diseases, including cancer, diabetic nephropathy, and muscular dystrophy.
Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.
Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.
The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.
Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.
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.
Chondroitin lyases are a group of enzymes that breakdown chondroitin, which is a type of proteoglycan found in connective tissues such as cartilage. These enzymes cleave chondroitin at specific points by removing certain sugar units, thereby breaking down the large, complex molecule into smaller fragments. Chondroitin lyases are classified based on their site of action and the type of fragment they produce. They play important roles in various biological processes, including tissue remodeling, growth, and development. In some cases, chondroitin lyases may also be used in research and medical settings to study the structure and function of proteoglycans or for the production of smaller chondroitin fragments with therapeutic potential.
Extracellular matrix (ECM) proteins are a group of structural and functional molecules that provide support, organization, and regulation to the cells in tissues and organs. The ECM is composed of a complex network of proteins, glycoproteins, and carbohydrates that are secreted by the cells and deposited outside of them.
ECM proteins can be classified into several categories based on their structure and function, including:
1. Collagens: These are the most abundant ECM proteins and provide strength and stability to tissues. They form fibrils that can withstand high tensile forces.
2. Proteoglycans: These are complex molecules made up of a core protein and one or more glycosaminoglycan (GAG) chains. The GAG chains attract water, making proteoglycans important for maintaining tissue hydration and resilience.
3. Elastin: This is an elastic protein that allows tissues to stretch and recoil, such as in the lungs and blood vessels.
4. Fibronectins: These are large glycoproteins that bind to cells and ECM components, providing adhesion, migration, and signaling functions.
5. Laminins: These are large proteins found in basement membranes, which provide structural support for epithelial and endothelial cells.
6. Tenascins: These are large glycoproteins that modulate cell adhesion and migration, and regulate ECM assembly and remodeling.
Together, these ECM proteins create a microenvironment that influences cell behavior, differentiation, and function. Dysregulation of ECM proteins has been implicated in various diseases, including fibrosis, cancer, and degenerative disorders.
'Tumor cells, cultured' refers to the process of removing cancerous cells from a tumor and growing them in controlled laboratory conditions. This is typically done by isolating the tumor cells from a patient's tissue sample, then placing them in a nutrient-rich environment that promotes their growth and multiplication.
The resulting cultured tumor cells can be used for various research purposes, including the study of cancer biology, drug development, and toxicity testing. They provide a valuable tool for researchers to better understand the behavior and characteristics of cancer cells outside of the human body, which can lead to the development of more effective cancer treatments.
It is important to note that cultured tumor cells may not always behave exactly the same way as they do in the human body, so findings from cell culture studies must be validated through further research, such as animal models or clinical trials.
Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.
The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.
Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.
A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.
Versican is a type of proteoglycan, which is a complex protein molecule that contains one or more long sugar chains (glycosaminoglycans) attached to it. Proteoglycans are important components of the extracellular matrix (the material that provides structural support and regulates cell behavior in tissues and organs).
Versican is primarily found in the extracellular matrix of connective tissues, including skin, tendons, ligaments, and blood vessels. It plays a role in regulating cell adhesion, migration, and proliferation, as well as in maintaining the structural integrity of tissues. Versican has been implicated in various physiological and pathological processes, such as embryonic development, wound healing, inflammation, and cancer progression.
There are several isoforms of versican (V0, V1, V2, and V3) that differ in their structure and function, depending on the specific glycosaminoglycan chains attached to them. Abnormal expression or regulation of versican has been associated with various diseases, including cancer, fibrosis, and inflammatory disorders.
Transfection is a term used in molecular biology that refers to the process of deliberately introducing foreign genetic material (DNA, RNA or artificial gene constructs) into cells. This is typically done using chemical or physical methods, such as lipofection or electroporation. Transfection is widely used in research and medical settings for various purposes, including studying gene function, producing proteins, developing gene therapies, and creating genetically modified organisms. It's important to note that transfection is different from transduction, which is the process of introducing genetic material into cells using viruses as vectors.
Agrin is a protein that plays a crucial role in the formation and maintenance of the neuromuscular junction, which is the specialized synapse between motor neurons and muscle fibers. It is produced by the motor neuron and released into the synaptic cleft, where it helps to cluster acetylcholine receptors on the muscle fiber membrane. This clustering of receptors is essential for efficient neuromuscular transmission and normal muscle function.
Agrin is a large heparan sulfate proteoglycan that contains a number of functional domains, including a unique alternatively spliced region that determines its activity in acetylcholine receptor clustering. Mutations in the gene encoding agrin have been associated with certain forms of congenital myasthenic syndrome, a group of inherited disorders characterized by muscle weakness and fatigability.
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.
I'm sorry for any confusion, but "Nitrous Acid" is not a term used in medical definitions. Nitrous acid is a chemical compound with the formula HNO2. It is a weak acid and a powerful oxidizing agent. It is used as a reducing agent in organic synthesis and as a laboratory reagent to produce nitric oxide.
If you have any questions related to medical terminology or health concerns, I would be happy to help with those!
Fibronectin is a high molecular weight glycoprotein that is found in many tissues and body fluids, including plasma, connective tissue, and the extracellular matrix. It is composed of two similar subunits that are held together by disulfide bonds. Fibronectin plays an important role in cell adhesion, migration, and differentiation by binding to various cell surface receptors, such as integrins, and other extracellular matrix components, such as collagen and heparan sulfate proteoglycans.
Fibronectin has several isoforms that are produced by alternative splicing of a single gene transcript. These isoforms differ in their biological activities and can be found in different tissues and developmental stages. Fibronectin is involved in various physiological processes, such as wound healing, tissue repair, and embryonic development, and has been implicated in several pathological conditions, including fibrosis, tumor metastasis, and thrombosis.
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.
Glycosides are organic compounds that consist of a glycone (a sugar component) linked to a non-sugar component, known as an aglycone, via a glycosidic bond. They can be found in various plants, microorganisms, and some animals. Depending on the nature of the aglycone, glycosides can be classified into different types, such as anthraquinone glycosides, cardiac glycosides, and saponin glycosides.
These compounds have diverse biological activities and pharmacological effects. For instance:
* Cardiac glycosides, like digoxin and digitoxin, are used in the treatment of heart failure and certain cardiac arrhythmias due to their positive inotropic (contractility-enhancing) and negative chronotropic (heart rate-slowing) effects on the heart.
* Saponin glycosides have potent detergent properties and can cause hemolysis (rupture of red blood cells). They are used in various industries, including cosmetics and food processing, and have potential applications in drug delivery systems.
* Some glycosides, like amygdalin found in apricot kernels and bitter almonds, can release cyanide upon hydrolysis, making them potentially toxic.
It is important to note that while some glycosides have therapeutic uses, others can be harmful or even lethal if ingested or otherwise introduced into the body in large quantities.
Collagen is the most abundant protein in the human body, and it is a major component of connective tissues such as tendons, ligaments, skin, and bones. Collagen provides structure and strength to these tissues and helps them to withstand stretching and tension. It is made up of long chains of amino acids, primarily glycine, proline, and hydroxyproline, which are arranged in a triple helix structure. There are at least 16 different types of collagen found in the body, each with slightly different structures and functions. Collagen is important for maintaining the integrity and health of tissues throughout the body, and it has been studied for its potential therapeutic uses in various medical conditions.
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.
Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.
Aggrecan is a large, complex proteoglycan molecule found in the extracellular matrix of articular cartilage and other connective tissues. It is a key component of the structural framework of these tissues, helping to provide resiliency, cushioning, and protection to the cells within. Aggrecan contains numerous glycosaminoglycan (GAG) chains, which are negatively charged molecules that attract water and ions, creating a swelling pressure that contributes to the tissue's load-bearing capacity.
The medical definition of 'Aggrecans' can be described as:
1. A large proteoglycan molecule found in articular cartilage and other connective tissues.
2. Composed of a core protein with attached glycosaminoglycan (GAG) chains, primarily chondroitin sulfate and keratan sulfate.
3. Plays a crucial role in the biomechanical properties of articular cartilage by attracting water and ions, creating a swelling pressure that contributes to the tissue's load-bearing capacity.
4. Aggrecan degradation or loss is associated with various joint diseases, such as osteoarthritis, due to reduced structural integrity and shock-absorbing capabilities of articular cartilage.
Decorin is a small proteoglycan, a type of protein with a attached sugar chain, that is found in the extracellular matrix of connective tissues in the body. It is composed of a core protein and one or more glycosaminoglycan (GAG) chains, specifically dermatan sulfate. Decorin plays important roles in the organization and biomechanical properties of collagen fibrils, regulation of cell proliferation and migration, and modulation of growth factor activity. It has been studied for its potential role in various physiological and pathological processes, including wound healing, fibrosis, and cancer.
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.
A virion is the complete, infectious form of a virus outside its host cell. It consists of the viral genome (DNA or RNA) enclosed within a protein coat called the capsid, which is often surrounded by a lipid membrane called the envelope. The envelope may contain viral proteins and glycoproteins that aid in attachment to and entry into host cells during infection. The term "virion" emphasizes the infectious nature of the virus particle, as opposed to non-infectious components like individual capsid proteins or naked viral genome.
Cartilage is a type of connective tissue that is found throughout the body in various forms. It is made up of specialized cells called chondrocytes, which are embedded in a firm, flexible matrix composed of collagen fibers and proteoglycans. This unique structure gives cartilage its characteristic properties of being both strong and flexible.
There are three main types of cartilage in the human body: hyaline cartilage, elastic cartilage, and fibrocartilage.
1. Hyaline cartilage is the most common type and is found in areas such as the articular surfaces of bones (where they meet to form joints), the nose, trachea, and larynx. It has a smooth, glassy appearance and provides a smooth, lubricated surface for joint movement.
2. Elastic cartilage contains more elastin fibers than hyaline cartilage, which gives it greater flexibility and resilience. It is found in structures such as the external ear and parts of the larynx and epiglottis.
3. Fibrocartilage has a higher proportion of collagen fibers and fewer chondrocytes than hyaline or elastic cartilage. It is found in areas that require high tensile strength, such as the intervertebral discs, menisci (found in joints like the knee), and the pubic symphysis.
Cartilage plays a crucial role in supporting and protecting various structures within the body, allowing for smooth movement and providing a cushion between bones to absorb shock and prevent wear and tear. However, cartilage has limited capacity for self-repair and regeneration, making damage or degeneration of cartilage tissue a significant concern in conditions such as osteoarthritis.
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.
Fibroblast growth factor (FGF) receptors are a group of cell surface tyrosine kinase receptors that play crucial roles in various biological processes, including embryonic development, tissue repair, and tumor growth. There are four high-affinity FGF receptors (FGFR1-4) in humans, which share a similar structure, consisting of an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyrosine kinase domain.
These receptors bind to FGFs with different specificities and affinities, triggering a cascade of intracellular signaling events that regulate cell proliferation, differentiation, migration, and survival. Aberrant FGFR signaling has been implicated in several diseases, such as cancer, developmental disorders, and fibrotic conditions. Dysregulation of FGFRs can occur through various mechanisms, including genetic mutations, amplifications, or aberrant expression, leading to uncontrolled cell growth and malignant transformation. Therefore, FGFRs are considered promising targets for therapeutic intervention in several diseases.
The Fluorescent Antibody Technique (FAT) is a type of immunofluorescence assay used in laboratory medicine and pathology for the detection and localization of specific antigens or antibodies in tissues, cells, or microorganisms. In this technique, a fluorescein-labeled antibody is used to selectively bind to the target antigen or antibody, forming an immune complex. When excited by light of a specific wavelength, the fluorescein label emits light at a longer wavelength, typically visualized as green fluorescence under a fluorescence microscope.
The FAT is widely used in diagnostic microbiology for the identification and characterization of various bacteria, viruses, fungi, and parasites. It has also been applied in the diagnosis of autoimmune diseases and certain cancers by detecting specific antibodies or antigens in patient samples. The main advantage of FAT is its high sensitivity and specificity, allowing for accurate detection and differentiation of various pathogens and disease markers. However, it requires specialized equipment and trained personnel to perform and interpret the results.
Chondroitin ABC lyase, also known as chondroitinase ABC or chondroitin sulfate eliminase, is an enzyme that breaks down chondroitin sulfate proteoglycans (CSPGs), which are major components of the extracellular matrix in various tissues including cartilage. CSPGs contain chondroitin sulfate chains, which are long, negatively charged polysaccharides composed of alternating sugars (N-acetylgalactosamine and glucuronic acid) with sulfate groups attached at specific positions.
Chondroitin ABC lyase cleaves chondroitin sulfate chains by removing a disaccharide unit from the polymer, resulting in the formation of unsaturated bonds between the remaining sugars. This enzymatic activity has been used in research to study the structure and function of CSPGs and their role in various biological processes, such as cell migration, tissue repair, and neural plasticity. Additionally, chondroitin ABC lyase has potential therapeutic applications for treating conditions associated with excessive accumulation of CSPGs, such as fibrosis and some neurological disorders.
Neurocan is defined as a type of proteoglycan, which is a complex protein molecule that contains one or more polysaccharide (carbohydrate) chains called glycosaminoglycans (GAGs). It is primarily found in the extracellular matrix of the central nervous system (CNS), including the brain and spinal cord.
Neurocan plays a crucial role in the development and functioning of the CNS by helping to regulate cell-to-cell interactions, providing structural support, and modulating signaling pathways involved in neuronal growth, differentiation, and survival. It is also involved in the process of synaptic plasticity, which is important for learning and memory.
Abnormalities in Neurocan expression or function have been implicated in various neurological disorders, including Alzheimer's disease, schizophrenia, and brain tumors.
Immunohistochemistry (IHC) is a technique used in pathology and laboratory medicine to identify specific proteins or antigens in tissue sections. It combines the principles of immunology and histology to detect the presence and location of these target molecules within cells and tissues. This technique utilizes antibodies that are specific to the protein or antigen of interest, which are then tagged with a detection system such as a chromogen or fluorophore. The stained tissue sections can be examined under a microscope, allowing for the visualization and analysis of the distribution and expression patterns of the target molecule in the context of the tissue architecture. Immunohistochemistry is widely used in diagnostic pathology to help identify various diseases, including cancer, infectious diseases, and immune-mediated disorders.
Ion exchange chromatography is a type of chromatography technique used to separate and analyze charged molecules (ions) based on their ability to exchange bound ions in a solid resin or gel with ions of similar charge in the mobile phase. The stationary phase, often called an ion exchanger, contains fixed ated functional groups that can attract counter-ions of opposite charge from the sample mixture.
In this technique, the sample is loaded onto an ion exchange column containing the charged resin or gel. As the sample moves through the column, ions in the sample compete for binding sites on the stationary phase with ions already present in the column. The ions that bind most strongly to the stationary phase will elute (come off) slower than those that bind more weakly.
Ion exchange chromatography can be performed using either cation exchangers, which exchange positive ions (cations), or anion exchangers, which exchange negative ions (anions). The pH and ionic strength of the mobile phase can be adjusted to control the binding and elution of specific ions.
Ion exchange chromatography is widely used in various applications such as water treatment, protein purification, and chemical analysis.
A chick embryo refers to the developing organism that arises from a fertilized chicken egg. It is often used as a model system in biological research, particularly during the stages of development when many of its organs and systems are forming and can be easily observed and manipulated. The study of chick embryos has contributed significantly to our understanding of various aspects of developmental biology, including gastrulation, neurulation, organogenesis, and pattern formation. Researchers may use various techniques to observe and manipulate the chick embryo, such as surgical alterations, cell labeling, and exposure to drugs or other agents.
Iduronic acid is a type of uronic acid, which is a derivative of glucose. It is a component of certain complex carbohydrates known as glycosaminoglycans (GAGs) or mucopolysaccharides, which are found in the extracellular matrix and on the surface of cells in the body. Specifically, iduronic acid is a component of dermatan sulfate and heparan sulfate, two types of GAGs that play important roles in various biological processes such as cell signaling, growth factor regulation, and blood clotting.
Iduronic acid has an unusual structure compared to other sugars because it contains a five-membered ring instead of the more common six-membered ring found in most other sugars. This unique structure allows iduronic acid to form complex structures with other sugar molecules, which is important for the biological activity of GAGs.
Abnormalities in the metabolism of iduronic acid and other GAG components can lead to various genetic disorders known as mucopolysaccharidoses (MPS), which are characterized by a range of symptoms including developmental delays, coarse facial features, skeletal abnormalities, and cardiac problems.
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.
The endothelium is a thin layer of simple squamous epithelial cells that lines the interior surface of blood vessels, lymphatic vessels, and heart chambers. The vascular endothelium, specifically, refers to the endothelial cells that line the blood vessels. These cells play a crucial role in maintaining vascular homeostasis by regulating vasomotor tone, coagulation, platelet activation, inflammation, and permeability of the vessel wall. They also contribute to the growth and repair of the vascular system and are involved in various pathological processes such as atherosclerosis, hypertension, and diabetes.
Hyaluronic acid is a glycosaminoglycan, a type of complex carbohydrate, that is naturally found in the human body. It is most abundant in the extracellular matrix of soft connective tissues, including the skin, eyes, and joints. Hyaluronic acid is known for its remarkable capacity to retain water, which helps maintain tissue hydration, lubrication, and elasticity. Its functions include providing structural support, promoting wound healing, and regulating cell growth and differentiation. In the medical field, hyaluronic acid is often used in various forms as a therapeutic agent for conditions like osteoarthritis, dry eye syndrome, and skin rejuvenation.
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.
C-type lectins are a family of proteins that contain one or more carbohydrate recognition domains (CRDs) with a characteristic pattern of conserved sequence motifs. These proteins are capable of binding to specific carbohydrate structures in a calcium-dependent manner, making them important in various biological processes such as cell adhesion, immune recognition, and initiation of inflammatory responses.
C-type lectins can be further classified into several subfamilies based on their structure and function, including selectins, collectins, and immunoglobulin-like receptors. They play a crucial role in the immune system by recognizing and binding to carbohydrate structures on the surface of pathogens, facilitating their clearance by phagocytic cells. Additionally, C-type lectins are involved in various physiological processes such as cell development, tissue repair, and cancer progression.
It is important to note that some C-type lectins can also bind to self-antigens and contribute to autoimmune diseases. Therefore, understanding the structure and function of these proteins has important implications for developing new therapeutic strategies for various diseases.
Biological models, also known as physiological models or organismal models, are simplified representations of biological systems, processes, or mechanisms that are used to understand and explain the underlying principles and relationships. These models can be theoretical (conceptual or mathematical) or physical (such as anatomical models, cell cultures, or animal models). They are widely used in biomedical research to study various phenomena, including disease pathophysiology, drug action, and therapeutic interventions.
Examples of biological models include:
1. Mathematical models: These use mathematical equations and formulas to describe complex biological systems or processes, such as population dynamics, metabolic pathways, or gene regulation networks. They can help predict the behavior of these systems under different conditions and test hypotheses about their underlying mechanisms.
2. Cell cultures: These are collections of cells grown in a controlled environment, typically in a laboratory dish or flask. They can be used to study cellular processes, such as signal transduction, gene expression, or metabolism, and to test the effects of drugs or other treatments on these processes.
3. Animal models: These are living organisms, usually vertebrates like mice, rats, or non-human primates, that are used to study various aspects of human biology and disease. They can provide valuable insights into the pathophysiology of diseases, the mechanisms of drug action, and the safety and efficacy of new therapies.
4. Anatomical models: These are physical representations of biological structures or systems, such as plastic models of organs or tissues, that can be used for educational purposes or to plan surgical procedures. They can also serve as a basis for developing more sophisticated models, such as computer simulations or 3D-printed replicas.
Overall, biological models play a crucial role in advancing our understanding of biology and medicine, helping to identify new targets for therapeutic intervention, develop novel drugs and treatments, and improve human health.
Electron microscopy (EM) is a type of microscopy that uses a beam of electrons to create an image of the sample being examined, resulting in much higher magnification and resolution than light microscopy. There are several types of electron microscopy, including transmission electron microscopy (TEM), scanning electron microscopy (SEM), and reflection electron microscopy (REM).
In TEM, a beam of electrons is transmitted through a thin slice of the sample, and the electrons that pass through the sample are focused to form an image. This technique can provide detailed information about the internal structure of cells, viruses, and other biological specimens, as well as the composition and structure of materials at the atomic level.
In SEM, a beam of electrons is scanned across the surface of the sample, and the electrons that are scattered back from the surface are detected to create an image. This technique can provide information about the topography and composition of surfaces, as well as the structure of materials at the microscopic level.
REM is a variation of SEM in which the beam of electrons is reflected off the surface of the sample, rather than scattered back from it. This technique can provide information about the surface chemistry and composition of materials.
Electron microscopy has a wide range of applications in biology, medicine, and materials science, including the study of cellular structure and function, disease diagnosis, and the development of new materials and technologies.
Cell surface receptors, also known as membrane receptors, are proteins located on the cell membrane that bind to specific molecules outside the cell, known as ligands. These receptors play a crucial role in signal transduction, which is the process of converting an extracellular signal into an intracellular response.
Cell surface receptors can be classified into several categories based on their structure and mechanism of action, including:
1. Ion channel receptors: These receptors contain a pore that opens to allow ions to flow across the cell membrane when they bind to their ligands. This ion flux can directly activate or inhibit various cellular processes.
2. G protein-coupled receptors (GPCRs): These receptors consist of seven transmembrane domains and are associated with heterotrimeric G proteins that modulate intracellular signaling pathways upon ligand binding.
3. Enzyme-linked receptors: These receptors possess an intrinsic enzymatic activity or are linked to an enzyme, which becomes activated when the receptor binds to its ligand. This activation can lead to the initiation of various signaling cascades within the cell.
4. Receptor tyrosine kinases (RTKs): These receptors contain intracellular tyrosine kinase domains that become activated upon ligand binding, leading to the phosphorylation and activation of downstream signaling molecules.
5. Integrins: These receptors are transmembrane proteins that mediate cell-cell or cell-matrix interactions by binding to extracellular matrix proteins or counter-receptors on adjacent cells. They play essential roles in cell adhesion, migration, and survival.
Cell surface receptors are involved in various physiological processes, including neurotransmission, hormone signaling, immune response, and cell growth and differentiation. Dysregulation of these receptors can contribute to the development of numerous diseases, such as cancer, diabetes, and neurological disorders.
A kidney glomerulus is a functional unit in the nephron of the kidney. It is a tuft of capillaries enclosed within a structure called Bowman's capsule, which filters waste and excess fluids from the blood. The glomerulus receives blood from an afferent arteriole and drains into an efferent arteriole.
The process of filtration in the glomerulus is called ultrafiltration, where the pressure within the glomerular capillaries drives plasma fluid and small molecules (such as ions, glucose, amino acids, and waste products) through the filtration membrane into the Bowman's space. Larger molecules, like proteins and blood cells, are retained in the blood due to their larger size. The filtrate then continues down the nephron for further processing, eventually forming urine.
A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.
Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.
Fibroblast Growth Factor 1 (FGF-1), also known as acidic fibroblast growth factor, is defined medically as a protein with mitogenic and chemotactic properties that play an essential role in various biological processes such as embryonic development, wound healing, tissue repair, and angiogenesis. It is produced by many cell types, including fibroblasts, endothelial cells, and macrophages. FGF-1 binds to specific tyrosine kinase receptors (FGFRs) on the cell surface, leading to intracellular signaling cascades that regulate cell proliferation, differentiation, and survival. It is involved in several diseases, including cancer, fibrotic disorders, and neurological conditions.
Monoclonal antibodies are a type of antibody that are identical because they are produced by a single clone of cells. They are laboratory-produced molecules that act like human antibodies in the immune system. They can be designed to attach to specific proteins found on the surface of cancer cells, making them useful for targeting and treating cancer. Monoclonal antibodies can also be used as a therapy for other diseases, such as autoimmune disorders and inflammatory conditions.
Monoclonal antibodies are produced by fusing a single type of immune cell, called a B cell, with a tumor cell to create a hybrid cell, or hybridoma. This hybrid cell is then able to replicate indefinitely, producing a large number of identical copies of the original antibody. These antibodies can be further modified and engineered to enhance their ability to bind to specific targets, increase their stability, and improve their effectiveness as therapeutic agents.
Monoclonal antibodies have several mechanisms of action in cancer therapy. They can directly kill cancer cells by binding to them and triggering an immune response. They can also block the signals that promote cancer growth and survival. Additionally, monoclonal antibodies can be used to deliver drugs or radiation directly to cancer cells, increasing the effectiveness of these treatments while minimizing their side effects on healthy tissues.
Monoclonal antibodies have become an important tool in modern medicine, with several approved for use in cancer therapy and other diseases. They are continuing to be studied and developed as a promising approach to treating a wide range of medical conditions.
Sulfatases are a group of enzymes that play a crucial role in the metabolism of sulfated steroids, glycosaminoglycans (GAGs), and other sulfated molecules. These enzymes catalyze the hydrolysis of sulfate groups from these substrates, converting them into their respective unsulfated forms.
The human genome encodes for several different sulfatases, each with specificity towards particular types of sulfated substrates. For instance, some sulfatases are responsible for removing sulfate groups from steroid hormones and neurotransmitters, while others target GAGs like heparan sulfate, dermatan sulfate, and keratan sulfate.
Defects in sulfatase enzymes can lead to various genetic disorders, such as multiple sulfatase deficiency (MSD), X-linked ichthyosis, and mucopolysaccharidosis (MPS) type IIIC (Sanfilippo syndrome type C). These conditions are characterized by the accumulation of sulfated molecules in different tissues, resulting in progressive damage to multiple organs and systems.
Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:
1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction
Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:
1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.
Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).
Tenascin is a large extracellular matrix protein that is involved in various biological processes, including cell adhesion, migration, and differentiation. It is found in high concentrations during embryonic development, tissue repair, and inflammation. Tenascin has a modular structure, consisting of multiple domains that can interact with various cell surface receptors and other extracellular matrix components. Its expression is regulated by a variety of growth factors, cytokines, and mechanical signals, making it an important player in the dynamic regulation of tissue architecture and function. In pathological conditions, abnormal tenascin expression has been implicated in various diseases, such as fibrosis, cancer, and autoimmune disorders.
Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:
1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.
Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.
The cornea is the clear, dome-shaped surface at the front of the eye. It plays a crucial role in focusing vision. The cornea protects the eye from harmful particles and microorganisms, and it also serves as a barrier against UV light. Its transparency allows light to pass through and get focused onto the retina. The cornea does not contain blood vessels, so it relies on tears and the fluid inside the eye (aqueous humor) for nutrition and oxygen. Any damage or disease that affects its clarity and shape can significantly impact vision and potentially lead to blindness if left untreated.
Receptor-like protein tyrosine phosphatases, class 5 (RPTPs-Class 5), also known as R7 family or PTP receptor type R, are a subfamily of receptor-like protein tyrosine phosphatases (RPTPs) that play crucial roles in various cellular processes, including cell growth, differentiation, and migration. These transmembrane enzymes are characterized by the presence of two extracellular carbonic anhydrase-like domains (CA domains), a single membrane-spanning region, and one intracellular protein tyrosine phosphatase domain.
The RPTPs-Class 5 includes four members in humans: PTPRF (also known as LAR), PTPRF-B (or LAR2), PTPRJ (or PTP receptor type J), and PTPRK (or PTP receptor type K). These phosphatases have the ability to dephosphorylate tyrosine residues on their target proteins, thereby regulating various signaling pathways. Dysregulation of RPTPs-Class 5 has been implicated in several diseases, including cancer and neurological disorders.
In summary, Receptor-like protein tyrosine phosphatases, class 5 are a group of transmembrane enzymes that regulate cellular processes by dephosphorylating tyrosine residues on target proteins, playing essential roles in maintaining proper cell function and homeostasis.
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.
Epithelium is the tissue that covers the outer surface of the body, lines the internal cavities and organs, and forms various glands. It is composed of one or more layers of tightly packed cells that have a uniform shape and size, and rest on a basement membrane. Epithelial tissues are avascular, meaning they do not contain blood vessels, and are supplied with nutrients by diffusion from the underlying connective tissue.
Epithelial cells perform a variety of functions, including protection, secretion, absorption, excretion, and sensation. They can be classified based on their shape and the number of cell layers they contain. The main types of epithelium are:
1. Squamous epithelium: composed of flat, scalelike cells that fit together like tiles on a roof. It forms the lining of blood vessels, air sacs in the lungs, and the outermost layer of the skin.
2. Cuboidal epithelium: composed of cube-shaped cells with equal height and width. It is found in glands, tubules, and ducts.
3. Columnar epithelium: composed of tall, rectangular cells that are taller than they are wide. It lines the respiratory, digestive, and reproductive tracts.
4. Pseudostratified epithelium: appears stratified or layered but is actually made up of a single layer of cells that vary in height. The nuclei of these cells appear at different levels, giving the tissue a stratified appearance. It lines the respiratory and reproductive tracts.
5. Transitional epithelium: composed of several layers of cells that can stretch and change shape to accommodate changes in volume. It is found in the urinary bladder and ureters.
Epithelial tissue provides a barrier between the internal and external environments, protecting the body from physical, chemical, and biological damage. It also plays a crucial role in maintaining homeostasis by regulating the exchange of substances between the body and its environment.
Cell movement, also known as cell motility, refers to the ability of cells to move independently and change their location within tissue or inside the body. This process is essential for various biological functions, including embryonic development, wound healing, immune responses, and cancer metastasis.
There are several types of cell movement, including:
1. **Crawling or mesenchymal migration:** Cells move by extending and retracting protrusions called pseudopodia or filopodia, which contain actin filaments. This type of movement is common in fibroblasts, immune cells, and cancer cells during tissue invasion and metastasis.
2. **Amoeboid migration:** Cells move by changing their shape and squeezing through tight spaces without forming protrusions. This type of movement is often observed in white blood cells (leukocytes) as they migrate through the body to fight infections.
3. **Pseudopodial extension:** Cells extend pseudopodia, which are temporary cytoplasmic projections containing actin filaments. These protrusions help the cell explore its environment and move forward.
4. **Bacterial flagellar motion:** Bacteria use a whip-like structure called a flagellum to propel themselves through their environment. The rotation of the flagellum is driven by a molecular motor in the bacterial cell membrane.
5. **Ciliary and ependymal movement:** Ciliated cells, such as those lining the respiratory tract and fallopian tubes, have hair-like structures called cilia that beat in coordinated waves to move fluids or mucus across the cell surface.
Cell movement is regulated by a complex interplay of signaling pathways, cytoskeletal rearrangements, and adhesion molecules, which enable cells to respond to environmental cues and navigate through tissues.
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.
Fibroblast Growth Factors (FGFs) are a family of growth factors that play crucial roles in various biological processes, including cell survival, proliferation, migration, and differentiation. They bind to specific tyrosine kinase receptors (FGFRs) on the cell surface, leading to intracellular signaling cascades that regulate gene expression and downstream cellular responses. FGFs are involved in embryonic development, tissue repair, and angiogenesis (the formation of new blood vessels). There are at least 22 distinct FGFs identified in humans, each with unique functions and patterns of expression. Some FGFs, like FGF1 and FGF2, have mitogenic effects on fibroblasts and other cell types, while others, such as FGF7 and FGF10, are essential for epithelial-mesenchymal interactions during organ development. Dysregulation of FGF signaling has been implicated in various pathological conditions, including cancer, fibrosis, and developmental disorders.
Heparanase
Lacritin
Syndecan 1
Syndecan-2
Syndecan-4
Syndecan
Syndecan-3
CYR61
SULF1
Glycocalyx
Carbohydrate sulfotransferase
Plasma cell
CASK
Thrombospondin 1
Fibronectin
Heparan sulfate
Envelope glycoprotein GP120
Glypican
Slit-Robo
Perlecan
Proteins20
- 5′-aza-dC and/or Trichostatin A resulted in transcriptional upregulation of the genes, suggesting that low expression of ECM components, proteoglycan core proteins and HS biosynthetic system is due to epigenetic suppression in type I cells. (oncotarget.com)
- Syndecans are transmembrane proteins, whereas glypicans are attached to the cell surface via a GPI anchor. (leonieclaire.com)
- It is a glycosaminoglycan that is covalently attached to core proteins to form proteoglycans. (leonieclaire.com)
- HS is covalently attached to core proteins to form HS-proteoglycans. (leonieclaire.com)
- Syndecans are transmembrane proteins with an N-terminal signal sequence and an ectodomain-containing consensus sequences for heparin-binding extracellular ligands including growth factors, extracellular matrix proteins, cell adhesion molecules, among others. (leonieclaire.com)
- More specifically, these core proteins carry three to five heparan sulfate and chondroitin sulfate chains, i.e. they are proteoglycans, which allow for interaction with a large variety of ligands including fibroblast growth factors, vascular endothelial growth factor, transforming growth factor -beta, fibronectin and antithrombin -1. (leonieclaire.com)
- The GCX, which is major constituent of the ESL, forms a luminal mesh that provides endothelial cells with a framework to bind plasma proteins and soluble GAGs. (biomedcentral.com)
- Principal functions of the syndecan core proteins are to target the heparan sulphate chains to the appropriate plasma-membrane compartment and to interact with components of the actin-based cytoskeleton. (scienceopen.com)
- Interactions of heparin/heparan sulfate with proteins: appraisal of structural factors and experimental approaches. (research.com)
- By interaction with extracellular matrix components, growth factors, enzymes, and their inhibitors, they regulate and influence tissue distribution of the cells and biological activities of the proteins. (exbio.cz)
- Since the last overview of sPLA 2 -binding proteins (sPLA 2 -BPs) 10 years ago, several important discoveries have occurred in this area. (ijbs.com)
- We provide a novel strategy for global profiling of surface proteins as targets for immunotherapies directly in patient tissue and experimental 3D glioma models. (lu.se)
- As demonstrated on LF fibroblasts, the resistance to trypsin was similar in serum-supplemented and serum-free media, i.e., medium without cell adhesion-mediating proteins. (nature.com)
- Based on all the results, the increased resistance to trypsinization of C2C12, LF, HaCaT, and VSMC cells on amine PPs can be explained most probably by a non-specific cell adhesion such as electrostatic interaction between the cells and amine groups on the material surface, rather than by the receptor-mediated adhesion through serum-derived proteins adsorbed on the PPs. (nature.com)
- Each of the syndecan core proteins has a short cytoplasmic domain that binds cytosolic regulatory factors. (embrapa.br)
- A constitutive expression of both mRNAs and proteins was detected in undifferentiated U-937 cells. (shengsci.com)
- Sulfate is essential in forming the mucin proteins which line the gut walls. (simplymimi.net)
- Mucin proteins, which line the gastrointestinal tract, are sulfated glyco-proteins which control adhesion/lubrication of gut contents and absorption of nutrients (2). (simplymimi.net)
- This reduced sulfation of mucin proteins may underlie the relatively common finding of Candida infections in the gut, since the slight negative charges on Candida cells would lead to their repulsion by the negatively charged sulfate groups on normal mucins. (simplymimi.net)
- Soluble components are also embedded in the glycocalyx such as proteins and soluble proteoglycans and are important in preserving the charge of the layer and play critical roles in functionality. (pulmccm.org)
Family of heparan sulfa1
- The syndecans comprise a family of heparan sulfate bearing transmembrane proteoglycans that arise from four distinct genes within mammals. (archive.org)
Chondroitin sulfate5
- hyaluronan (HA), chondroitin sulfate (CS) and dermatan sulfate (DS), heparin and heparan sulphate (HS), and keratan sulfate (KS). (hindawi.com)
- We have previously demonstrated that chondroitin sulfate glycosaminoglycans (CS-GAGs) on breast cancer cells function as P-selectin ligands. (biomedcentral.com)
- Transient transfection of the human breast cancer cell line MDA-MB-231 with the siRNAs for carbohydrate (chondroitin 4) sulfotransferase-11 ( CHST11 ) and chondroitin sulfate proteoglycan 4 ( CSPG4 ) was used to investigate the involvement of these genes in expression of surface P-selectin ligands. (biomedcentral.com)
- Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix. (cusabio.com)
- Glycosaminoglycans (linear disaccharide polymers of a uronic acid and a hexosamine) are predominantly heparan sulfate (50-90%), then dermatan sulfate, chondroitin sulfate, keratan sulfate and hyaluronan (or hyaluronic acid). (pulmccm.org)
Chains18
- HSPGs interact with growth factors and receptors through heparan sulfate (HS) chains. (scielo.br)
- The sulfation pattern of heparan sulfate chains influences signaling events mediated by heparan sulfate proteoglycans located on the cell surface. (scielo.br)
- SULF1 and SULF2 are two endo-sulfatases that can cleave specific 6-O-sulfate groups within the heparan chains. (scielo.br)
- HA is synthesized in the absence of a protein core at the inner face of the plasma membrane and consequently found in the form of free chains whereas other GAG types are covalently bound into protein cores to form proteoglycans (PGs). (hindawi.com)
- PGs, molecules which consist of a protein core that is covalently modified with GAG chains, are distributed both to the ECM "proper" associated with the cell membrane as well as located to intracellular compartment. (hindawi.com)
- Syndecan-1, via its heparan sulfate chains, binds to a variety of extracellular matrix macromolecules including collagens, fibronectin, thrombospondin, and tenascin etc. (archive.org)
- It has been shown that PGs and their polysaccharide chains (especially heparan sulfates, HS) play an important role in the immune system participating in leukocyte development and migration, immune activation and inflammatory processes as well as in lymphoma development [ 3 ]. (oncotarget.com)
- Tightly regulated HSPGs expression is a requirement for normal B cell maturation, differentiation and function [ 4 ] and the conformation of their HS polysaccharide chains is crucial for recruitment of factors that control plasma cell survival [ 5 ]. (oncotarget.com)
- Recently, advanced microscopy techniques have enabled direct visualization of the GCX in vivo, most of which use fluorescent-labeled lectins that bind to specific disaccharide moieties of glycosaminoglycan (GAG) chains. (biomedcentral.com)
- Syndecans bind a variety of extracellular ligands via their covalently attached heparan sulphate chains. (scienceopen.com)
- Proteoglycan (PG) coreceptors carry heparan sulfate (HS) chains that mediate interactions with growth factors, morphogens, and receptors. (silverchair.com)
- The heparan sulfate chains of the syndecan-Fc crossbreed molecule are necessary for HIV-1 neutralization absolutely. (biotech-angels.com)
- HIV-1 binds syndecans via a 6-O sulfation (11) within the HS chains demonstrating that this binding is not the result of random interactions between basic residues and negative charges but the result of specific contacts between gp120 and a well-defined sulfation in syndecans. (biotech-angels.com)
- The syndecans, heparan sulfate proteoglycans, are abundant molecules associated with the cell surface and extracellular matrix and consist of a protein core to which heparan sulfate chains are covalently attached. (embrapa.br)
- Several antigens have been used as targets for CAR-T cell therapy against MM, including B cell maturation antigen (BCMA), CD19, CD138, signaling lymphocytic activation molecule 7 (SLAM7), and immunoglobulin light chains. (biomedcentral.com)
- Before birth, the functional units of the brain, 'neurons', are laid down on a scaffolding network of sulfated carbohydrate chains. (simplymimi.net)
- Surprisingly, the regulatory activity of glypicans in the Wnt, Hedgehog and BMP signaling pathways is only partially dependent on the heparan sulfate chains. (biomedcentral.com)
- Proteoglycans (protein core with chains of glycosaminoglycans) are the "backbone" of the glycocalyx, and consist of syndecans, glipicans, mimecan, perlecans and biglycans. (pulmccm.org)
Transmembrane heparan2
- This review will summarize our current state of knowledge of the structure, biochemical properties and functions of syndecans, a family of transmembrane heparan sulphate proteoglycans. (scienceopen.com)
- Syndecan-2 is a member of the Syndecans family comprised of type I transmembrane heparan sulfate proteoglycans (HSPG) that are involved in the regulation of many cellular processes. (joplink.net)
HSPGs3
- APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (PubMed:12970454, PubMed:12356718, PubMed:12913001, PubMed:28404852, PubMed:22767607). (proteopedia.org)
- Heparan sulfate proteoglycans (HSPGs) are present on the cell surface and in the extracellular matrix in all metazoans. (scielo.br)
- Syndecan is the family name of membrane-intercalated HSPGs. (leonieclaire.com)
Protein26
- The protein is originally synthesised in an inactive 65 kDa proheparanase form in the golgi apparatus and transferred to late endosomes/lysosomes for transport to the cell-surface. (wikipedia.org)
- C-type lectin (CTL) is a protein that binds to saccharides and plays an important role in parasite adhesion, host cell invasion and immune evasion. (bvsalud.org)
- Trichinella spiralis dipeptidyl peptidase 1 (TsDPP1), or cysteine cathepsin C, is a secretory protein that is highly expressed during the infective larvae and adult worm stages in the intestines. (bvsalud.org)
- Proteoglycans (PGs) are complex macromolecules composed of a core protein and covalently linked polysaccharide chain(s) which play a critical role in cell-cell and cell-matrix interactions. (oncotarget.com)
- Proteolysis of insulin-like growth factor binding protein-1 (IGFBP 1) in pregnancy.J Perinat Med. (mdx.ac.uk)
- This review summarizes recent biochemical and genetic information that sheds new light on the nature of HS-protein binding. (silverchair.com)
- The sulfated saccharide domains provide numerous docking sites for protein ligands and are abundantly expressed at cell surfaces and in the extracellular matrix as part of proteoglycans (PGs). (silverchair.com)
- Interactions with HS contribute to or modify the various protein functions, which are of particular interest in relation to growth factor/morphogen translocation and signaling ( Fig. 1 ). (silverchair.com)
- In addition, the influences of aberrant expressed SDC-1 in Janus kinase 1 (JAK1)/signal transducer and activator of transcription 3 (STAT3) and rat sarcoma virus (Ras)/rapidly accelerated fibrosarcoma (Raf)/mitogen-activated protein kinase (MEK)/extracellular signal-regulated kinase (ERK) pathways were detected by western blot analysis. (biomedcentral.com)
- SDC-1 mRNA and protein levels were down-regulated in human colorectal carcinoma tissues. (biomedcentral.com)
- Additionally, SDC-1 overexpression restrained cell migration via inhibiting the protein expression of matrix metallopeptidase 9 (MMP-9), and elicited cell adhesion through increasing intercellular cell adhesion molecule-1 (ICAM-1). (biomedcentral.com)
- Furthermore, SDC-1 overexpression suppressed JAK1/STAT3 and Ras/Raf/MEK/ERK-related protein levels. (biomedcentral.com)
- In this paper, we verified the mRNA and protein expression of SDC-1 in human colorectal carcinoma tissues and focused on the biological cellular effects of SDC-1 on human colorectal carcinoma cell lines (SW620, SW480 and LOVO), by evaluating cell viability, apoptosis, migration and adhesion. (biomedcentral.com)
- Korábbi cirkuláris dikroizmus (CD) spektroszkópiai vizsgálataink feltárták, hogy magasabb rendű növények és több algacsalád kloroplasztiszainak tilakoidmembránjaiban a pigment-protein komplexek kiterjedt, magasan szervezett királis makrodoméneket alkotnak, melynek köszönhetően a CD spektrumokban nagy erősségű, úgynevezett psi-típusú sávok jelennek meg (1. (brc.hu)
- These protein domains locate the syndecan on cell surface sites during development and tumor formation where they interact with other receptors to regulate signaling and cytoskeletal organization. (embrapa.br)
- METHODS: ESG was immunolabeled with anti-heparan sulfate (HS), followed by an ATTO488 conjugated goat anti-mouse IgG, and with biotinylated hyaluronic … acid (HA) binding protein, followed by an AF647 conjugated anti-biotin. (semcs.net)
- Chimeric antigen receptor (CAR) T cell therapy has emerged as a novel immunotherapy which modifies T cells with CAR, an artificial fusion protein that incorporates an extracellular antigen recognition domain, a transmembrane domain, and an intracellular domain including costimulation and signaling components [ 4 , 5 ]. (biomedcentral.com)
- The effect of dexamethasone on mRNA and protein synthesis of lipocortins (LCT) 1, 2 and 5 has been investigated in U-937 cells. (shengsci.com)
- Lipopolysaccharide-binding protein mediates CD14-independent intercalation of lipopolysaccharide into phospholipid membranes. (shengsci.com)
- Sequence-specific binding property of Arabidopsis thaliana telomeric DNA binding protein 1 (AtTBP1). (shengsci.com)
- We have identified an Arabidopsis thaliana cDNA, designated as AtTBP1, encoding a protein with a predicted size of 70.6 kDa that specifically binds to the plant telomeric repeat sequence TTTAGGG. (shengsci.com)
- Removal of the sulfate residues leads to a protein which has a more globular structure and provides less protection for the tissues from the intestinal contents. (simplymimi.net)
- On the other hand, GPC3 has recently been reported to inhibit Hedgehog protein signaling during development by competing with Patched, the Hedgehog receptor, for Hedgehog binding. (biomedcentral.com)
- Dally, an ortholog of the mammalian glypican 3/5 subfamily, and Dally-like protein, an ortholog of the glypican 1/2/4/6 subfamily. (biomedcentral.com)
- The CCR5 co-receptor also binds with chemokines produced by CD8+ T cells, including RANTES (CCL5), and MIP (macrophage inflammatory protein) 1α (CCL3) and 1β (CCL4). (biomedcentral.com)
- Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets and binds with high affinity to heparin. (wikidoc.org)
Receptors10
- Free glycosaminoglycans (GAGs) and proteoglycan- (PG-) containing GAGs, key effectors of cell surface, pericellular and extracellular microenvironments, perform multiple functions in cancer by virtue of their coded structure and their ability to interact with both ligands and receptors that regulate cancer growth [ 1 - 4 ]. (hindawi.com)
- Syndecans are thought to function predominantly as coreceptors for other receptors such as integrins, members of the fibroblast growth factor family, vascular endothelial cell growth factor, and transforming growth factor β, which need heparin sulfate for signaling. (leonieclaire.com)
- Syndecans: multifunctional cell-surface co-receptors. (scienceopen.com)
- The main function of syndecans appears to be to modulate the ligand-dependent activation of primary signalling receptors at the cell surface. (scienceopen.com)
- The dominating cell surface area heparan sulfate proteoglycans (HSPG) (25 29 30 33 are syndecans that are transmembrane receptors extremely indicated on adherent cells (macrophages and epithelial and endothelial cells) but badly expressed on suspension system cells (T cells) (2 3 4 10 35 Their ectodomain bears three linear heparan sulfate (HS) stores which are comprised of the repetition of the sulfated disaccharide theme (1). (biotech-angels.com)
- HSPG including syndecans serve as receptors for human being NMS-873 deficiency disease type-1 (HIV-1) (16) herpes virus (HSV) (7) human being papillomavirus (HPV) (13 37 and Tmem140 human being T-lymphotropic disease type 1 (HTLV-1) (19 20 Pretreatment of focus on cells such as for example macrophages with heparinase an enzyme that gets rid of HS moieties from syndecans considerably decreases HIV-1 infectivity (35). (biotech-angels.com)
- Although syndecans usually do not relieve the necessity for Compact disc4 and chemokine receptors for viral admittance (35) these in connection receptors amplify HIV-1 disease by advertising viral adsorption to the top of permissive cells. (biotech-angels.com)
- Syndecans also serve as in receptors for HIV-1 (2 16 HIV-1 binds syndecans richly indicated for the endothelium and continues to be infectious for weekly whereas cell-free disease manages to lose its infectivity after an individual day (2). (biotech-angels.com)
- The finding that CCR5 and syndecans are exploited by HIV-1 via a single determinant echoes the mechanisms by which chemokines utilize these two disparate receptors and suggests that the gp120/chemokine mimicry may represent a common strategy in microbial pathogenesis. (biotech-angels.com)
- The heparan Golgi-resident selenide receptors in interconnectivity a state of interactions that are to mitochondrial influx membrane used by the irreversible expression( HA) response, and the sustained polypeptide of the archival distinct knot km2 into the tail of the complex dementia. (evakoch.com)
Members of the syndecan family4
- In contrast, the transmembrane and cytoplasmic domains are highly conversed both as members of the syndecan family and among different species. (archive.org)
- The authors of this paper have shown the first evidence that syndecan-1 or other members of the syndecan family can mediate cell-cell adhesion. (archive.org)
- All members of the syndecan family have 5 exons. (leonieclaire.com)
- What are the members of the syndecan family? (leonieclaire.com)
Membrane10
- The enzyme degrades the heparan sulfate scaffold of the basement membrane and extracellular matrix. (wikipedia.org)
- Diffusion of the complex E1/E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (PubMed:12970454, PubMed:24038151, PubMed:12913001, PubMed:20375010, PubMed:19182773) (By similarity). (proteopedia.org)
- IFA results show that rTsCTL and SDC-1 co-localized on Caco-2 cell membrane. (bvsalud.org)
- The results of the immunofluorescence test (IFT) and confocal microscopy showed that rTsDPP1 specifically bound to macrophages, and the binding site was localized on the cell membrane. (bvsalud.org)
- GAGs bound into PGs are located to the extracellular matrix, basal membrane, and cell surface [ 7 ]. (hindawi.com)
- How do Syndecan and Glypican attach to the membrane? (leonieclaire.com)
- The endothelial glycocalyx is a network of membrane-bound proteoglycans and glycoproteins, covering the endothelium luminally. (scienceopen.com)
- Syndecan-1 (SDC-1) is a crucial membrane proteoglycan, which is confirmed to participate in several tumor cell biological processes. (biomedcentral.com)
- N-sulfated heparan sulfate proteoglycans are located in specific microdomains in the plasma membrane, independent on those formed around N-acetyl-rich heparan sulfate, and play different role in the cell signaling. (exbio.cz)
- Glypicans are heparan sulfate proteoglycans that are bound to the outer surface of the plasma membrane by a glycosyl-phosphatidylinositol anchor. (biomedcentral.com)
Adhesion13
- Thus, syndecans participate in cell matrix adhesion. (archive.org)
- In addition, it has been widely speculated that syndecans participate in cell-cell adhesion. (archive.org)
- However, there has been no direct evidence demonstrating that syndecans can mediate cell-cell adhesion. (archive.org)
- CD138 is a heparin sulphate proteoglycan that controls tumor cell survival, growth, adhesion and bone cell differentiation in MM (2). (leonieclaire.com)
- At each point, blood was collected for hyaluronan, syndecan-1, vascular cell adhesion molecule (VCAM-1), and von Willebrand factor (vWF), and a PBR measurement was performed. (scienceopen.com)
- Syndecans have been proposed to play a role in a variety of cellular functions, including cell proliferation and cell-matrix and cell-cell adhesion. (scienceopen.com)
- Tumor-associated glycans play a significant role in promoting aggressive and metastatic behavior of malignant cells [ 1 - 5 ], participating in cell-cell and cell-extracellular matrix interactions that promote tumor cell adhesion and migration. (biomedcentral.com)
- In previous studies we found that CS/DS-GAGs are expressed on the cell surface of murine and human breast cancer cell lines with high metastatic capacity and that they play a major role in P-selectin binding and P-selectin-mediated adhesion of cancer cells to platelets and endothelial cells [ 24 ]. (biomedcentral.com)
- Next, SW480, SW620 and LOVO cell viability, apoptosis, migration and adhesion were assessed to explore the effects of exogenous overexpressed SDC-1 on colorectal carcinoma. (biomedcentral.com)
- Functional analyses indicated that some of the genes induced by dragonfly larvae caused an increase in laminins necessary for cell adhesion in the extracellular matrix. (biomedcentral.com)
- Our previously-obtained impressive results of highly increased C2C12 mouse myoblast adhesion to amine plasma polymers (PPs) motivated current detailed studies of cell resistance to trypsinization, cell proliferation, motility, and the rate of attachment carried out for fibroblasts (LF), keratinocytes (HaCaT), rat vascular smooth muscle cells (VSMC), and endothelial cells (HUVEC, HSVEC, and CPAE) on three different amine PPs. (nature.com)
- The increased cell adhesion was also confirmed for LF cells by an independent technique, single-cell force spectroscopy. (nature.com)
- Glycoproteins are also part of the "backbone" structure and the main types are the endothelial cell adhesion molecules ( -cams, which are selectins, integrins and immunoglobulins) and components of the fibrin/coagulation system. (pulmccm.org)
Biosynthesis2
- Interacting polymer-modification enzymes in heparan sulfate biosynthesis. (uu.se)
- Carriers of the rs8069770 variant allele were associated with a lower risk of HIV MTCT (odds ratio = 0.27, 95% confidence interval = 0.14, 0.51), where rs8069770 is located within HS3ST3A1 , a gene involved in heparan sulfate biosynthesis. (biomedcentral.com)
Glycoproteins1
- Its is essentially a meshwork of glycoproteins and proteoglycans, anchored to the epithelial cells, in which many soluble molecules are enmeshed. (pulmccm.org)
Molecules8
- Heparanase, also known as HPSE, is an enzyme that acts both at the cell-surface and within the extracellular matrix to degrade polymeric heparan sulfate molecules into shorter chain length oligosaccharides. (wikipedia.org)
- Crystal structures of both proheparanase and mature heparanase are available, showing that the linker peptide forms a large helical domain which blocks heparan sulfate molecules from interacting with heparanase. (wikipedia.org)
- Heparanase has endoglycosidase activity and cleaves polymeric heparan sulfate molecules at sites which are internal within the polymeric chain. (wikipedia.org)
- Cell type and tissue specific alterations in fine GAG structure, which are strictly predetermined [ 8 - 10 ], allow these molecules to modulate with high specificity different cellular processes [ 7 ]. (hindawi.com)
- The term "oncotarget" encompasses all molecules, pathways, cellular functions, cell types, and even tissues that can be viewed as targets relevant to cancer as well as other diseases. (oncotarget.com)
- Low-molecular weight sulfated marine polysaccharides: Promising molecules to prevent neurodegeneration in mucopolysaccharidosis IIIA? (uu.se)
- Trefoil factor family (TFF)-domain peptides 1-3 are mucin-associated molecules, largely found in epithelia of gastrointestinal tissues. (shengsci.com)
- Its major physiologic role appears to be neutralization of heparin-like molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. (wikidoc.org)
Glycosaminoglycans6
- Importantly, cell-associated and tumor microenvironment glycosaminoglycans (GAGs)/proteoglycan (PG) content and distribution are markedly altered during tumor pathogenesis and progression. (hindawi.com)
- Glycosaminoglycans (GAGs) comprise a class of linear, negatively charged polysaccharides composed of repeating disaccharide units of acetylated hexosamines (N-acetyl-galactosamine in the case of chondroitin sulphate and dermatan sulfate or N-acetyl-glucosamine in the case of heparin sulphate and heparin) and mainly of uronic acids (d-glucuronic acid or l-iduronic acid) being sulfated at various positions. (hindawi.com)
- Subsequent studies replicated these results and led to the concept that this layer was composed of proteoglycans (PGs) and glycosaminoglycans (GAGs) with a thickness of several tens of nanometers, as has been previously reviewed [ 5 , 6 ]. (biomedcentral.com)
- Among glycans that play a critical role in stromal tumor cell interactions are glycosaminoglycans (GAGs) attached to proteoglycans (PGs). (biomedcentral.com)
- Currently, he is research interests include investigating the role of glycosaminoglycans and proteoglycans on the development of placental pathology and breast cancer. (mdx.ac.uk)
- Placental syndecan-1 and sulphated glycosaminoglycans are decreased in preeclampsia. (mdx.ac.uk)
Ligands3
- Syndecan-1 (SDC-1) is a member of the heparan sulfate proteoglycan family which is mainly expressed on the surface of IEC and in extracellular matrices where they interact with a plethora of ligands. (bvsalud.org)
- What kind of ligands does a syndecan carry? (leonieclaire.com)
- Genes that regulate ligands for chemokine receptor genes have been associated with the risk of HIV infection, a notable example existing for chemokine (C-C motif) ligand 3-like 1 ( CCL3L1 ). (biomedcentral.com)
Specificity1
- The sulfation design of HSs dictates the ligand specificity of syndecans (1). (biotech-angels.com)
Disaccharide2
- Heparan sulfate (HS) is a linear polysaccharide composed of 50-200 glucosamine and uronic acid (glucuronic acid or iduronic acid) disaccharide repeats with epimerization and various sulfation modifications. (leonieclaire.com)
- Antia IU, Yagnik DR, Pantoja Munoz L, Shah AJ, Hills FA (2017).Heparan sulfate disaccharide measurement from biological samples using pre-column derivatization, UPLC-MS and single ion monitoring. (mdx.ac.uk)
Fibroblast1
- Identification of the basic fibroblast growth factor binding sequence in fibroblast heparan sulfate. (research.com)
Antigen5
- Antigen-presenting cells (APCs) produce and release a broad spectrum of EVs involved in the pathogenesis of atherosclerosis. (bmrat.org)
- They are secreted by a wide array of cells, including cardiac myocytes, mature and progenitor endothelial cells, mesenchymal stem cells, immune cells like antigen-presenting cells (APCs), and malignant cells 5 , 6 . (bmrat.org)
- The mouse monoclonal antibody HepSS-1 (also known as HepSS1) recognizes N-sulfated heparan sulfate (extracellular antigen) present in many species. (exbio.cz)
- There is an unmet need to develop novel therapies for refractory/relapsed MM. In the past few years, chimeric antigen receptor (CAR)-modified T cell therapy for MM has shown promising efficacy in preclinical and clinical studies. (biomedcentral.com)
- Two main advantages of BCMA as an antigen for CAR-T therapy are the potential reduction of on-target/off-tumor toxicity and the lack of antigen-dependent reduction in CAR-T cell expansion [ 16 ]. (biomedcentral.com)
Hyaluronan1
- Fragments of the GCX, such as syndecan-1 and/or hyaluronan (HA), have been examined, and their validity is now being examined. (biomedcentral.com)
SDC12
- During normal B-cell development, cells acquire expression of CD138, also known as syndecan-1 (SDC1), a marker highly specific for terminally differentiated normal plasma cells (1). (leonieclaire.com)
- our findings revealed that SDC1 suppressed EMT via the modulation of the ERK signaling pathway that, in turn, negatively affected the invasiveness of human oral cancer cells. (cusabio.com)
Tissues5
- To determine their possible roles in tissues and satellite cells in vitro, their expression pattern was examined in tissues from 40-day-old chickens and in satellite cells from the breast muscles of 1-week-old and 2-week-old chickens using RT-PCR and immunocytochemistry analyses. (scielo.br)
- In tissues, syndecan-1 localizes to the basolateral surface of simple epithelia and during B cell differentiation, syndecan-1 is expressed only at times when B cells associate with the extracellular matrix. (archive.org)
- Regulation of Syndecan Expression Syndecan-1 is expressed predominantly in epithelial and mesenchymal tissues, syndecan-2 in cells of mesenchymal origin and neuronal and epithelial cells, and syndecan-3 almost exclusively in neuronal and musculoskeletal tissue, whereas syndecan-4 is found in virtually every cell type. (leonieclaire.com)
- Expression of SDC-1 in colorectal carcinoma tissues was evaluated by Reverse transcription-quantitative real-time PCR (RT-qPCR) and western blot. (biomedcentral.com)
- BCMA is not present in other hematological cells like hematopoietic stem cells or other tissues. (biomedcentral.com)
Tumor cell2
- Specifically, these extracellular matrix (ECM) components critically modulate the tumor cell "motile phenotype" affecting their adhesive/migratory abilities which are directly correlated to the metastatic cascade [ 5 , 6 ]. (hindawi.com)
- Enzymatic removal of tumor-cell surface CS-GAGs significantly inhibited lung colonization of the 4T1 murine mammary cell line ( P = 0.0002). (biomedcentral.com)
Proliferation5
- Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (PubMed:11086025, PubMed:17881511). (proteopedia.org)
- The proliferation and differentiation of satellite cells are regulated by a number of extracellular signals ( Wang & Rudnicki, 2012 Wang YX, Rudnicki MA. (scielo.br)
- SDC-1 overexpression inhibited cell proliferation via suppressing CyclinD1 and c-Myc expression, meanwhile stimulated cell apoptosis via increasing the expression levels of B-cell lymphoma-2-associated x (Bax) and Cleaved-Caspase-3. (biomedcentral.com)
- Dysregulated cell proliferation underlies all forms of oncogenesis. (wisc.edu)
- Multiple myeloma (MM) is a hematological malignancy characterized by the proliferation of transformed monoclonal plasma cells in the bone marrow (BM) [ 1 ]. (biomedcentral.com)
Target for inhibition2
CD1384
- I went through the 2004 study, which reported that "highly clonogenic cells from both human MM cell lines and primary patient samples do not express CD138, but rather markers that are characteristic of B cells. (healthblogs.org)
- Also known as syndecan-1, CD138 "is "a heparan sulfate proteoglycan expressed on the surface of, and actively shed by, myeloma cells. (healthblogs.org)
- CD138 "is the most specific marker for normal and MM plasma cells. (healthblogs.org)
- However, normal CD138 + plasma cells appear to be terminally differentiated and unable to proliferate, and there have been few studies using this marker to study the proliferative capacity of MM cells. (healthblogs.org)
Differentiation3
- The possible role of PGs has so far been largely neglected, both during B-cell differentiation and as a factor in EBV-driven lymphomagenesis [ 1 , 2 ]. (oncotarget.com)
- It is involved in cell death, growth, and differentiation as well as tissue repair by tissue remodeling/wound healing and ECM assembly [ 5 ] . (encyclopedia.pub)
- Moreover, BCMA plays an essential role in regulating B cell maturation and differentiation into plasma cells. (biomedcentral.com)
Polysaccharide1
- The HS polysaccharide is composed of alternating hexuronic acid and d -glucosamine units and is substituted with sulfate groups in various positions. (silverchair.com)
Fibroglycan1
- This PG family consists of four members: syndecan-1,44 syndecan-2/fibroglycan, 45 syndecan-3/N-syndecan, 46 and syndecan-4/amphiglycan/ryudocan, 47,48 all of which are expressed in the CNS. (leonieclaire.com)
Interactions7
- The consecutive stages of cancer growth and dissemination are obligatorily perpetrated through specific interactions of the tumor cells with their microenvironment. (hindawi.com)
- The consecutive steps of tumor growth, local invasion, intravasation, extravasation, and invasion of anatomically distant sites are obligatorily perpetrated through specific interactions of the tumor cells with their microenvironment. (hindawi.com)
- The involvement of proteoglycans (PGs) in EBV-host interactions and lymphomagenesis remains poorly investigated. (oncotarget.com)
- Disruptions of such interactions might affect B cell interaction with surrounding stroma and may thus perturb the cell phenotypes. (oncotarget.com)
- Over the past decade, insight has been gained into the role of the glycocalyx in vascular physiology and pathology, including mechanotransduction, hemostasis, signaling, and blood cell-vessel wall interactions. (scienceopen.com)
- Inhibition of Tumor-Host Cell Interactions Using Synthetic Heparin Mimetics. (uu.se)
- Our studies integrate molecular genetics, genomics, biochemistry and cell biology to address fundamental questions in virus replication and virus-cell interactions. (wisc.edu)
Regulatory2
- The review focuses on the role of APC-derived EVs in regulating the transformation of macrophage phenotype, shaping foam cells, driving autophagy and/or inhibiting apoptosis of Th4 + cells, T regulatory cells, endothelial and smooth muscle cells (SMCs), as well as in facilitating oxidative stress in vasculature. (bmrat.org)
- our results identify the CD63-syntenin-1-ALIX complex as a key regulatory component in post-endocytic HPV trafficking. (cusabio.com)
Signal transduction2
Multifunctional1
- Heparan sulfate: decoding a dynamic multifunctional cell regulator. (research.com)
20171
- 2017 Dec 7;8(1):1973. (exbio.cz)
Glycosaminoglycan3
- Except for the glycosaminoglycan attachment sites, the extracellular domains of the syndecans are highly divergent. (archive.org)
- Kure S, Yoshie O: A syngeneic monoclonal antibody to murine Meth-A sarcoma (HepSS-1) recognizes heparan sulfate glycosaminoglycan (HS-GAG): cell density and transformation dependent alteration in cell surface HS-GAG defined by HepSS-1. (exbio.cz)
- Kure S, Yoshie O, Aso H: Metastatic potential of murine B16 melanoma correlates with reduced surface heparan sulfate glycosaminoglycan. (exbio.cz)
Distinct5
- Heparin is distinct from HS in that it is produced primarily by mast cells, whereas, HS is produced by all cell types. (leonieclaire.com)
- GRP75-driven, cell-cycle-dependent macropinocytosis of Tat/pDNA-Ca2+ nanoparticles underlies distinct gene therapy effect in ovarian cancer. (uu.se)
- Chung JS, Shiue LH, Duvic M, Pandya A, Cruz PD Jr, Ariizumi K: Sézary syndrome cells overexpress syndecan-4 bearing distinct heparan sulfate moieties that suppress T-cell activation by binding DC-HIL and trapping TGF-beta on the cell surface. (exbio.cz)
- To date, it has remained unclear whether these clonogenic cells are distinct from the plasma cells that constitute the majority of tumor cells. (healthblogs.org)
- The 2004 study also suggested that, like chronic myeloid leukaemia or CML, "MM is another example in which cancer stem cells are a rare cell population that is distinct from the differentiated cells that comprise the bulk of the disease. (healthblogs.org)
Microvascular endothelial cells2
- Furthermore syndecans on NMS-873 microvascular endothelial cells perform a NMS-873 significant part in cell-free HIV-1 transmigration through the blood-brain hurdle (3). (biotech-angels.com)
- OBJECTIVES: To investigate the ESG components and their organization on bEnd3 (mouse brain microvascular endothelial cells) monolayer. (semcs.net)
Sulfation5
- Quantitative real-time PCR (qRT-PCR) and flow cytometry assays were used to detect the expression of genes involved in the sulfation and presentation of chondroitin in several human breast cancer cell lines. (biomedcentral.com)
- Supporting this hypothesis the 6-O sulfation recognized by HIV-1 on syndecans mimics the sulfated tyrosines recognized by HIV-1 in the N terminus of CCR5 (11). (biotech-angels.com)
- The process of sulfation involves adding on a sulfate residue, which has two negative charges, to a biological molecule. (simplymimi.net)
- Sulfation can activate or inactivate a wide range of biological compounds and any aberration in the supply of sulfate can have potentially serious consequences. (simplymimi.net)
- Principally, sulfation is a major inactivation pathway for catecholamines such as the neurotransmitter dopamine, about 80% of which is sulfated in man (1). (simplymimi.net)
Growth factor r1
- E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (PubMed:22855500). (proteopedia.org)
Soluble1
- The positive correlation between soluble Syndecan-1 levels and breast cancer tumor size in the present study highlights the importance of this molecule in the breast tumor progression and their significance as tumor biomarkers. (cusabio.com)
Regulation5
- Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). (proteopedia.org)
- Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NF-kappa-B activation, and activates AP-1 (By similarity). (proteopedia.org)
- Lymphoblastoid EBV+ B cell lines (LCLs) showed specific PG expression with down-regulation of CD44 and ECM components and up-regulation of serglycin and perlecan/HSPG2. (oncotarget.com)
- Glypican-3 (GPC3) is upregulated in A2780cis cells in response to LMWH treatment, probably as counter-regulation to sustain the high Wnt activity against LMWH. (oncotarget.com)
- The higher expression of gremlin 1 and HIF1a genes after exposure to dragonfly larvae indicated an in vivo hypoxic reaction, while down-regulation of syndecan-2 may indicate impairment of angiogenesis. (biomedcentral.com)
Endothelial cell2
- The successful penetration of the endothelial cell layer that lines the interior surface of blood vessels is an important process in the formation of blood borne tumour metastases. (wikipedia.org)
- The increased resistance observed for the non-endothelial cell types was accompanied by an increased rate of cellular attachment, even though spontaneous migration was comparable to the control, i.e., to the standard cultivation surface. (nature.com)
Metastases1
- CTCs are tumor cells originating from primary sites or metastases that circulate in the patients' bloodstream and are very rarely found in healthy individuals ( 9 , 10 ) ( Figure 1 ). (iiarjournals.org)
Endothelium5
- The GCX is a major constituent of the endothelial surface layer (ESL), which covers most of the surface of the endothelial cells and reduces the access of cellular and macromolecular components of the blood to the surface of the endothelium. (biomedcentral.com)
- About 20 years later, Copley [ 3 ] reported the endothelium-plasma interface and developed a concept in which the endothelial surface was covered by a thin molecular layer and an immobile sheet of plasma. (biomedcentral.com)
- The ESL is composed of a layer of PGs and GAGs lining the luminal surface of the endothelium. (biomedcentral.com)
- Furthermore HIV-1 attached onto the endothelium via syndecans represents an in way to obtain disease for circulating T cells (2). (biotech-angels.com)
- Its role with cellular elements is interesting, as it contains key elements for interaction (CAMs) but at the same time physically prevents direct interaction between cells (WBC, RBC, plt) and the endothelium. (pulmccm.org)
Uronic acid1
- The exception constitutes keratan sulphate whose uronic acid is substituted by galactose. (hindawi.com)
Enzyme5
- Removal of the linker reveals an extended cleft on the enzyme surface, which contains the heparanase active site. (wikipedia.org)
- It is interesting that Helicobacter pylori, which can colonise the stomach, only does so when it has produced a sulfatase enzyme to de-sulphate the gastric mucins (6). (simplymimi.net)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Horse Transforming Growth Factor Beta 1 (TGFb1) in serum, platelet-poor plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids. (stemcellcharter.org)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Horse Transforming Growth Factor Beta 1 (TGFb1) in samples from serum, platelet-poor plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids with no significant corss-reactivity with analogues from other species. (stemcellcharter.org)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Branched Chain Alpha-Ketoacid Dehydrogenase Kinase (BCKDK) in Tissue homogenates, cell lysates and other biological fluids. (chemcarbindia.com)
Biological8
- Analysis of procainamide-derived heparan sulphate disaccharides in biological samples using hydrophilic interaction liquid chromatography mass spectrometry. (mdx.ac.uk)
- However, the biological significance of SDC-1 in colorectal carcinoma is not yet clear. (biomedcentral.com)
- Thanks to its multiple roles, TG2 exerts various biological functions depending on the stimulus, leading to cell death or survival and tissue repair. (encyclopedia.pub)
- Sulfate is essential for many biological processes. (simplymimi.net)
- Description: A sandwich ELISA kit for detection of Transforming Growth Factor Beta 3 from Horse in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (stemcellcharter.org)
- Description: A sandwich ELISA kit for detection of Trefoil Factor 2 from Mouse in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (envite.org)
- Description: A sandwich quantitative ELISA assay kit for detection of Rat Trefoil Factor 2 (TFF2) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids. (envite.org)
- Description: tissue homogenates, cell lysates and other biological fluids. (chemcarbindia.com)
Tissue8
- In this article, we focus on the role of TG2 in cell death, macrophage activation, and tissue repair processes, which are involved in several pathogeneses, including tissue injury, inflammation, and fibrosis. (encyclopedia.pub)
- This review aims to summarize the recent knowledge on the mechanisms activated by TG2 to regulate cell death/survival and fibrosis in the tissue repair process. (encyclopedia.pub)
- Therefore, many laboratories try with great effort to develop resorbable tissue scaffolds that could support the patient´s cells. (nature.com)
- In orthopaedic non‐load bearing devices or dental implants, the preferred materials can be resorbable ceramics chemically similar to the inorganic component of the bone tissue, such as hydroxyapatite 1 , 2 . (nature.com)
- ECM provides mechanical support for cells and also determines the shape of tissue 9 . (nature.com)
- Manuscripts should report original theoretical and/or experimental research promoting the scientific and technological advances in a broad field that ranges from the rheology of macromolecules and macromolecular arrays to cell, tissue and organ rheology. (semcs.net)
- Sulfate is necessary for formation of brain tissue. (simplymimi.net)
- Tissue factor (TF) is the initiator of the coagulation cascade, constitutively expressed in subendothelial cells such as vascular smooth muscle cells and initiating rapid coagulation when the vascular vessel is damaged. (go.jp)
Roles2
- Mii Y, Yamamoto T, Takada R, Mizumoto S, Matsuyama M, Yamada S, Takada S, Taira M: Roles of two types of heparan sulfate clusters in Wnt distribution and signaling in Xenopus. (exbio.cz)
- BACKGROUND: In order to play different roles in vascular functions as a mechanosensor to blood flows and as a barrier to transvascular exchange, the endothelial surface glycocalyx (ESG) should have an organized structure. (semcs.net)
Extracellular domains1
- The syndecans also contain highly conserved transmembrane domains and extracellular domains for which important activities are becoming known. (embrapa.br)
Antibody2
- Separation of EA.hy926 cells (red-filled) from EA.hy926 cells treated with heparinase (1 hour, 1 UI per ml of cell suspension) stained using anti-N-sulfated heparan sulfate (HepSS-1) PE antibody (concentration in sample 10 μg/ml). (exbio.cz)
- In the past several decades, numerous studies have been conducted to understand the pathogenesis of IF/TA and multiple factors and mechanisms have been demonstrated to be involved in the progress of the IF/TA, including immunosuppressive drug toxicity, antibody-mediated injury, and epithelial-mesenchymal transition (EMT) (Figure 1 ). (biomedcentral.com)
Peptides3
- Crim RL, Audet SA, Feldman SA, Mostowski HS, Beeler JA: Identification of linear heparin-binding peptides derived from human respiratory syncytial virus fusion glycoprotein that inhibit infectivity. (exbio.cz)
- Rolling in the clover: trefoil factor family (TFF)-domain peptides, cell migration and cancer. (shengsci.com)
- These amino acid sequences are glycosylated with a range of sugars and both these carbohydrate residues and the peptides themselves are sulfated. (simplymimi.net)
Gene5
- This study was performed to identify the carrier proteoglycan (PG) and the sulfotransferase gene involved in synthesis of the surface P-selectin-reactive CS-GAGs in human breast cancer cells with high metastatic capacity, as well as to determine a direct role for CS-GAGs in metastatic spread. (biomedcentral.com)
- The CHST11 gene was highly expressed in aggressive breast cancer cells but significantly less so in less aggressive breast cancer cell lines. (biomedcentral.com)
- Cell surface P-selectin binding depends on CHST11 gene expression. (biomedcentral.com)
- In his research, Jeremy E. Turnbull performs multidisciplinary study on Cell biology and Gene. (research.com)
- Gene and Cell biology are two areas of study in which he engages in interdisciplinary work. (research.com)
Regulate1
- Using phosphoproteomic approaches, they are mapping downstream effectors of TFG-NTRK1 and TFG-ALK that simultaneously drive cell transformation and regulate vesicle secretion. (wisc.edu)
Modulate1
- W e for the first time show that stress conditions modulate surfaceome turnover in cancer cells, providing opportunities for tumor specific drug delivery. (lu.se)
Dendritic cells1
- HIV-1 transmission includes transmigration of HIV-1 through the genital epithelium and subsequent capture and transfer of infectious particles from dendritic cells (DC) and/or Langerhans cells (LC) to T cells (31 34 38 Importantly human cervical and vaginal mucosal epithelia richly express syndecans (4). (biotech-angels.com)
Glypicans4
- Glypicans can be released from the cell surface by a lipase called Notum, and most of them are subjected to endoproteolytic cleavage by furin-like convertases. (biomedcentral.com)
- The mouse genome also has six glypicans, which are identified by the same nomenclature (Table 1 ). (biomedcentral.com)
- Glypicans fall into two broad subfamilies: glypicans 1/2/4/6 and glypicans 3/5 (Figure 1 ), with approximately 25% amino-acid identity between groups. (biomedcentral.com)
- Within the first subfamily, glypicans 4 and 6 are relatively closely related (64% identity) and glypicans 1 and 2 form a more divergent clade. (biomedcentral.com)
Significantly inhibited1
- ß-Xyloside (a syndecan-1 synthesis inhibitor) and Stattic (a STAT3 inhibitor) significantly inhibited rTsCTL binding to syndecan-1 in Caco-2 cells and activation of the STAT3 pathway, abrogated the effects of rTsCTL on the expression of gut tight junctions, and impeded larval invasion. (bvsalud.org)
Malignant3
- Malignant tumor diseases induce an upregulation of blood coagulation by a functional interlinkage that has first been described more than 150 years ago, referred to as Trousseau syndrome [ 1 ]. (oncotarget.com)
- With growing new cases being diagnosed all around the world every year, colorectal carcinoma is known to be one of the most critical popular diseases, accompanying by a high malignant degree and mortality [ 1 ]. (biomedcentral.com)
- BCMA, a member of the tumor necrosis factor (TNF) superfamily, is exclusively expressed in a subpopulation of B cells, normal plasma cells, and malignant plasma cells. (biomedcentral.com)