Chondroitin Sulfate Proteoglycans
Chondroitin ABC Lyase
Heparan Sulfate Proteoglycans
Chondroitinases and Chondroitin Lyases
Receptor-Like Protein Tyrosine Phosphatases, Class 5
Extracellular Matrix Proteins
Spinal Cord Injuries
Chromatography, Ion Exchange
Nerve Tissue Proteins
Molecular Sequence Data
Fluorescent Antibody Technique
Amino Acid Sequence
Electrophoresis, Polyacrylamide Gel
Fibroblast Growth Factor 2
Disease Models, Animal
Chromatography, High Pressure Liquid
Identification of the human melanoma-associated chondroitin sulfate proteoglycan antigen epitope recognized by the antitumor monoclonal antibody 763.74 from a peptide phage library. (1/1155)To identify the epitope of the melanoma-associated chondroitin sulfate proteoglycan (MCSP) recognized by the monoclonal antibody (mAb) 763.74, we first expressed random DNA fragments obtained from the complete coding sequence of the MCSP core glycoproteins in phages and selected without success for binders to the murine mAb 763.74. We then used a library of random heptapeptides displayed at the surface of the filamentous M13 phage as fusion protein to the NH2-terminal portion of the minor coat protein III. After three rounds of selection on the bound mAb, several phages displaying related binding peptides were identified, yielding the consensus sequence Val-His-Leu-Asn-Tyr-Glu-His. Competitive ELISA experiments showed that this peptide can be specifically prevented from binding to mAb 763.74 by an anti-idiotypic MK2-23 mouse:human chimeric mAb and by A375 melanoma cells expressing the antigen MCSP. We screened the amino acid sequence of the MCSP molecule for a region of homology to the consensus sequence and found that the amino acid sequence Val-His-Ile-Asn-Ala-His spanning positions 289 and 294 has high homology. Synthetic linear peptides corresponding to the consensus sequence as well as to the MCSP-derived epitope inhibit the binding of mAb 763.74 to the phages displaying the consensus amino acid sequence. Finally, the biotinylated consensus peptide absorbed to streptavidin-microtiter plates can be used for the detection of mAb 763.74 in human serum. These results show clearly that the MCSP epitope defined by mAb 763.74 has been identified. (+info)
Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon. (2/1155)Fibromodulin is a member of a family of connective tissue glycoproteins/proteoglycans containing leucine-rich repeat motifs. Several members of this gene family bind to fibrillar collagens and are believed to function in the assembly of the collagen network in connective tissues. Here we show that mice lacking a functional fibromodulin gene exhibit an altered morphological phenotype in tail tendon with fewer and abnormal collagen fiber bundles. In fibromodulin-null animals virtually all collagen fiber bundles are disorganized and have an abnormal morphology. Also 10-20% of the bundles in heterozygous mice are similar to the abnormal bundles in fibromodulin-null tail tendon. Ultrastructural analysis of Achilles tendon from fibromodulin-null mice show collagen fibrils with irregular and rough outlines in cross-section. Morphometric analysis show that fibromodulin-null mice have on the average thinner fibrils than wild type animals as a result of a larger preponderance of very thin fibrils in an overall similar range of fibril diameters. Protein and RNA analyses show an approximately 4-fold increase in the content of lumican in fibromodulin-null as compared with wild type tail tendon, despite a decrease in lumican mRNA. These results demonstrate a role for fibromodulin in collagen fibrillogenesis and suggest that the orchestrated action of several leucine-rich repeat glycoproteins/proteoglycans influence the architecture of collagen matrices. (+info)
Formation of hyaluronan- and versican-rich pericellular matrix is required for proliferation and migration of vascular smooth muscle cells. (3/1155)The accumulation of hyaluronan (HA) and the HA-binding proteoglycan versican around smooth muscle cells in lesions of atherosclerosis suggests that together these molecules play an important role in the events of atherogenesis. In this study we have examined the formation of HA- and versican-rich pericellular matrices by human aortic smooth muscle cells in vitro, using a particle-exclusion assay, and the role of the pericellular matrix in cell proliferation and migration. The structural dependence of the pericellular matrix on HA can be demonstrated by the complete removal of the matrix with Streptomyces hyaluronidase. The presence of versican in the pericellular matrix was confirmed immunocytochemically. By electron microscopy, the cell coat was seen as a tangled network of hyaluronidase-sensitive filaments decorated with ruthenium red-positive proteoglycan granules. Ninety percent of migrating cells in wounded cultures, and virtually all mitotic cells, displayed abundant HA- and versican-rich coats. Time-lapse video imaging revealed that HA- and versican-rich pericellular matrix formation is dynamic and rapid, and coordinated specifically with cell detachment and mitotic cell rounding. HA oligosaccharides, which inhibit the binding of HA to the cell surface and prevent pericellular matrix formation, significantly reduced proliferation and migration in response to platelet-derived growth factor, whereas larger HA fragments and high molecular weight HA had no effect. Treatment with HA oligosaccharides also led to changes in cell shape from a typical fusiform morphology to a more spread and flattened appearance. These data suggest that organization of HA- and versican-rich pericellular matrices may facilitate migration and mitosis by diminishing cell surface adhesivity and affecting cell shape through steric exclusion and the viscous properties of HA proteoglycan gels. (+info)
The proteoglycan lectin domain binds sulfated cell surface glycolipids and promotes cell adhesion. (4/1155)The lecticans are a group of chondroitin sulfate proteoglycans characterized by the presence of C-type lectin domains. Despite the suggestion that their lectin domains interact with carbohydrate ligands, the identity of such ligands has not been elucidated. We previously showed that brevican, a nervous system-specific lectican, binds the surface of B28 glial cells (Yamada, H., Fredette, B., Shitara, K., Hagihara, K., Miura, R., Ranscht, B., Stallcup, W. B., and Yamaguchi, Y. (1997) J. Neurosci. 17, 7784-7795). In this paper, we demonstrate that two classes of sulfated glycolipids, sulfatides and HNK-1-reactive sulfoglucuronylglycolipids (SGGLs), act as cell surface receptors for brevican. The lectin domain of brevican binds sulfatides and SGGLs in a calcium-dependent manner as expected of a C-type lectin domain. Intact, full-length brevican also binds both sulfatides and SGGLs. The lectin domain immobilized as a substrate supports adhesion of cells expressing SGGLs or sulfatides, which was inhibited by monoclonal antibodies against these glycolipids or by treatment of the substrate with SGGLs or sulfatides. Our findings demonstrate that the interaction between the lectin domains of lecticans and sulfated glycolipids comprises a novel cell substrate recognition system, and suggest that lecticans in extracellular matrices serve as substrate for adhesion and migration of cells expressing these glycolipids in vivo. (+info)
Resistance of small leucine-rich repeat proteoglycans to proteolytic degradation during interleukin-1-stimulated cartilage catabolism. (5/1155)A bovine nasal-cartilage culture system has been utilized to analyse the catabolic events occurring in response to interleukin-1beta over a 14-day period. An early event following the start of interleukin-1 treatment was the release of glycosaminoglycan into the culture medium. This release was accompanied by the appearance in the tissue, and shortly thereafter also in the culture media, of a globular domain (G1)-containing aggrecan degradation product generated by the action of aggrecanase. Link protein was also released from the cartilage with a similar timeframe to that of the G1 fragment, although there was no evidence of its proteolytic degradation. By comparison with aggrecan, the small leucine-rich repeat proteoglycans decorin, biglycan and lumican showed a resistance to both proteolytic cleavage and release throughout the culture period. In contrast, fibromodulin exhibited a marked decrease in size after day 4, presumably due to proteolytic modification, but the major degradation product was retained throughout the culture period. Also in contrast with the early changes in the components of the proteoglycan aggregate, type II collagen did not display signs of extensive degradation until much later in the culture period. Collagen degradation products compatible with collagenase action first appeared in the medium by day 10 and increased thereafter. These data demonstrate that the leucine-rich repeat proteoglycans are resistant to proteolytic action during interleukin-1-stimulated cartilage catabolism, compared with aggrecan. This resistance and continued interaction with the surface of the collagen fibrils may help to stabilize the collagen fibrillar network and protect it from extensive proteolytic attack during the early phases of cartilage degeneration. (+info)
Identification and characterization of ligands for L-selectin in the kidney. I. Versican, a large chondroitin sulfate proteoglycan, is a ligand for L-selectin. (6/1155)Ligands for a leukocyte adhesion molecule, L-selectin, are expressed not only in the specific vascular endothelium in lymph nodes and Peyer's patches but also in the extravascular tissues such as the brain white matter, choroid plexus and the kidney distal straight tubuli. However, the biological significance of these extravascular ligands is currently unknown. We now report the purification and characterization of a novel extravascular ligand for L-selectin in the kidney using a tubule-derived cell line, ACHN. Binding of L-selectin-IgG chimera (LEC-IgG) to the isolated ligand was specifically blocked with either (i) anti-L-selectin mAb, (ii) EDTA, (iii) fucoidan, (iv) chondroitin sulfate (CS) B or CS E, or (v) treatment with chondroitinases. Partial amino acid sequencing, Western blotting and immunoprecipitation analyses showed that a major ligand for L-selectin in ACHN cells is versican of 1600 kDa. Histochemical as well as biochemical analyses verified that a versican subspecies in the kidney was indeed reactive with L-selectin. Studies with cell lines including those derived from the kidney indicated that a certain glycoform and/or splice form of versican is reactive with L-selectin. Under pathological conditions such as those induced by unilateral ureteral obstruction, versican was shed from the distal straight tubuli and became localized in the adjacent vascular bundles around which a substantial leukocyte infiltration was concomitantly observed. Possible involvement of versican in leukocyte trafficking into the kidney under diseased conditions is discussed. (+info)
Dermatopontin expression is decreased in hypertrophic scar and systemic sclerosis skin fibroblasts and is regulated by transforming growth factor-beta1, interleukin-4, and matrix collagen. (7/1155)Dermatopontin is a recently discovered extracellular matrix protein with proteoglycan and cell-binding properties and is assumed to play important roles in cell-matrix interactions and matrix assembly. In this study we examined the expression of dermatopontin mRNA and protein in skin fibroblast cultures from patients with hypertrophic scar and patients with systemic sclerosis. Dermatopontin mRNA and protein levels were reduced in fibroblast cultures from hypertrophic scar lesional skin compared with fibroblasts from normal skin of the same hypertrophic scar patient. Fibroblast cultures from systemic sclerosis patient involved skin also showed significantly reduced expression of dermatopontin compared with normal skin fibroblasts from healthy individuals. We also investigated the effects of cytokines and matrix collagen on dermatopontin expression in normal cultured fibroblasts. Transforming growth factor-beta1 increased dermatopontin mRNA and protein levels, while interleukin-4 reduced dermatopontin expression. Substrate coated with type I collagen reduced dermatopontin mRNA levels, the reduction being more prominent in three-dimensional collagen matrices. Our results suggest that the decreased expression of dermatopontin is associated with the pathogenesis of fibrosis in hypertrophic scar and systemic sclerosis, and that the effect of the cytokines and matrix collagen on dermatopontin may have important implications for skin fibrosis. (+info)
DSD-1-proteoglycan is the mouse homolog of phosphacan and displays opposing effects on neurite outgrowth dependent on neuronal lineage. (8/1155)DSD-1-PG is a chondroitin sulfate proteoglycan (CSPG) expressed by glial cells that can promote neurite outgrowth from rat embryonic mesencephalic (E14) and hippocampal (E18) neurons, an activity that is associated with the CS glycosaminoglycans (GAGs). Further characterization of DSD-1-PG has included sequencing of peptides from the core protein and the cloning of the corresponding cDNA using polyclonal antisera against DSD-1-PG to screen phage expression libraries. On the basis of these studies we have identified DSD-1-PG as the mouse homolog of phosphacan, a neural rat CSPG. Monoclonal antibodies 3H1 and 3F8 against carbohydrate residues on rat phosphacan recognize these epitopes on DSD-1-PG. The epitopes of the antibodies, L2/HNK-1 and L5/Lewis-X, which have been implicated in functional interactions, are also found on DSD-1-PG. Although DSD-1-PG has previously been shown to promote neurite outgrowth, its upregulation after stab wounding of the CNS and its localization in regions that are considered boundaries to axonal extension suggested that it may also have inhibitory functions. Neonatal dorsal root ganglion (DRG) explants grown on a rich supportive substrate (laminin) with and without DSD-1-PG were strikingly inhibited by the proteoglycan. The inhibitory effects of DSD-1-PG on the DRG explants were not relieved by removal of the CS GAGs, indicating that this activity is associated with the core glycoprotein. The neurite outgrowth from embryonic hippocampal neurons on laminin was not affected by the addition of DSD-1-PG. This indicates that DSD-1-PG/mouse phosphacan can have opposing effects on the process of neurite outgrowth dependent on neuronal lineage. (+info)
Chondroitin sulfate proteoglycans (CSPGs) are a type of proteoglycan found in the extracellular matrix of connective tissues, including cartilage, bone, and the central nervous system. They are composed of a core protein to which multiple chains of chondroitin sulfate glycosaminoglycans (GAGs) are attached. CSPGs play important roles in various biological processes, including cell adhesion, migration, and differentiation, as well as in the development and maintenance of tissue structure and function. In the medical field, CSPGs are of interest for their potential roles in various diseases and conditions, including osteoarthritis, spinal cord injury, and cancer.
Chondroitin sulfates are a group of complex carbohydrates that are found in the extracellular matrix of connective tissues, including cartilage, bone, and blood vessels. They are composed of repeating disaccharide units of glucuronic acid and galactosamine, which are linked by a sulfate group. In the medical field, chondroitin sulfates are often used as dietary supplements to support joint health and reduce the symptoms of osteoarthritis. They are thought to work by inhibiting the activity of enzymes that break down cartilage, promoting the production of proteoglycans, and reducing inflammation in the joints. Chondroitin sulfates are also used in some medical treatments, such as the treatment of certain types of cancer and the prevention of blood clots. However, their effectiveness and safety in these applications are still being studied, and more research is needed to fully understand their potential benefits and risks.
Chondroitin ABC Lyase (CABCyL) is an enzyme that breaks down chondroitin sulfate, a complex carbohydrate found in cartilage, tendons, and other connective tissues. It is involved in the degradation of proteoglycans, which are large molecules composed of proteins and carbohydrates, and plays a role in the turnover of extracellular matrix in tissues. In the medical field, CABCyL has been studied for its potential therapeutic applications in various conditions, including osteoarthritis, a degenerative joint disease characterized by the breakdown of cartilage and the development of bone spurs. CABCyL has been shown to increase the turnover of cartilage matrix and promote the synthesis of new cartilage, which may help to slow down the progression of osteoarthritis. It has also been studied for its potential use in the treatment of other connective tissue disorders, such as intervertebral disc degeneration and fibrosis.
Proteoglycans are complex macromolecules that consist of a core protein to which one or more glycosaminoglycan chains are covalently attached. They are found in the extracellular matrix of connective tissues, including cartilage, bone, skin, and blood vessels, and play important roles in various biological processes, such as cell signaling, tissue development, and wound healing. Proteoglycans are involved in the regulation of cell growth and differentiation, as well as in the maintenance of tissue homeostasis. They also play a crucial role in the formation and function of the extracellular matrix, which provides structural support and helps to maintain tissue integrity. In the medical field, proteoglycans are of interest because they are involved in a number of diseases and disorders, including osteoarthritis, cancer, and cardiovascular disease. For example, changes in the composition and distribution of proteoglycans in the cartilage matrix have been implicated in the development of osteoarthritis, a degenerative joint disease characterized by the breakdown of cartilage and bone. Similarly, alterations in proteoglycan expression and function have been observed in various types of cancer, including breast, prostate, and colon cancer.
Heparan sulfate proteoglycans (HSPGs) are a family of complex molecules that are found in the extracellular matrix of many tissues in the human body. They are composed of a core protein, which is modified with heparan sulfate chains. HSPGs play important roles in a variety of biological processes, including cell signaling, cell adhesion, and the regulation of growth and development. They are also involved in the formation and function of blood vessels, and have been implicated in a number of diseases, including cancer, cardiovascular disease, and neurological disorders.
Chondroitin is a complex polysaccharide that is found in the extracellular matrix of connective tissues, particularly in cartilage. It is composed of repeating disaccharide units of glucuronic acid and N-acetylglucosamine, and it plays an important role in maintaining the structure and function of cartilage. In the medical field, chondroitin is often used as a dietary supplement to support joint health and reduce the symptoms of osteoarthritis. It is thought to work by inhibiting the activity of enzymes that break down cartilage, thereby slowing down the progression of joint damage. Chondroitin supplements are also sometimes used to treat other conditions, such as interstitial cystitis and high blood pressure. However, the effectiveness of chondroitin supplements for these conditions is not well-established, and more research is needed to confirm their benefits. Additionally, some studies have suggested that high doses of chondroitin may increase the risk of bleeding, so it is important to use caution when taking this supplement and to consult with a healthcare provider before starting any new supplement regimen.
Chondroitinases and chondroitin lyases are enzymes that break down chondroitin sulfate, a complex carbohydrate found in cartilage. These enzymes are used in medical research and treatment of various conditions, including osteoarthritis, spinal cord injury, and multiple sclerosis. Chondroitinases are a type of lyase that specifically cleave the glycosidic bond between the disaccharide units of chondroitin sulfate. This results in the release of smaller chondroitin sulfate fragments, which can be used for various purposes, such as studying the structure and function of cartilage, or developing new treatments for diseases that affect cartilage. Chondroitin lyases, on the other hand, are a broader category of enzymes that can cleave various types of glycosaminoglycans, including chondroitin sulfate, heparan sulfate, and dermatan sulfate. These enzymes are used in research to study the structure and function of glycosaminoglycans, and in clinical settings to treat conditions such as osteoarthritis and spinal cord injury. Overall, chondroitinases and chondroitin lyases play important roles in the medical field by providing tools for studying cartilage and developing new treatments for diseases that affect this tissue.
Glycosaminoglycans (GAGs) are a group of complex carbohydrates that are found in the extracellular matrix of connective tissues in the human body. They are composed of repeating disaccharide units of a sugar called glucose and another sugar called uronic acid, which are linked together by glycosidic bonds. GAGs play important roles in various biological processes, including cell signaling, tissue development, and wound healing. They are also involved in the regulation of inflammation, blood clotting, and the immune response. In the medical field, GAGs are often studied in relation to various diseases and conditions, such as osteoarthritis, rheumatoid arthritis, and cancer. They are also used as diagnostic markers and therapeutic targets in the treatment of these conditions. Additionally, GAGs are used in various medical applications, such as wound dressings, tissue engineering, and drug delivery systems.
I'm sorry, but I couldn't find any information on a medical term called "Brevican." It's possible that you may have misspelled the term or that it is not a recognized medical term. If you have any additional information or context, please let me know and I'll do my best to assist you.
Heparitin Sulfate is a naturally occurring glycosaminoglycan found in the extracellular matrix of connective tissue. It is a linear polysaccharide composed of repeating disaccharide units of glucuronic acid and N-sulfated glucosamine. Heparitin Sulfate is known for its ability to bind and modulate the activity of various growth factors, cytokines, and other signaling molecules, making it an important component of the body's regulatory network. In the medical field, Heparitin Sulfate is used as a medication to treat a variety of conditions, including thrombosis, inflammation, and cancer. It is also used in research as a tool to study the interactions between proteins and carbohydrates.
In the medical field, "versican" refers to a large chondroitin sulfate proteoglycan that is expressed in various tissues, including cartilage, bone, and the central nervous system. Versican is a member of the aggrecan family of proteoglycans, which play important roles in the maintenance of tissue structure and function. In cartilage, versican is primarily found in the extracellular matrix and is involved in the regulation of cell behavior and matrix organization. In bone, versican is expressed by osteoblasts and is thought to play a role in bone formation and remodeling. In the central nervous system, versican is expressed by astrocytes and is involved in the regulation of cell migration and axon guidance. Abnormal expression or function of versican has been implicated in a number of diseases, including osteoarthritis, multiple sclerosis, and glioblastoma.
Chondroitin lyases are a group of enzymes that break down chondroitin sulfate, a complex carbohydrate found in cartilage and other connective tissues. These enzymes are important in the process of cartilage turnover and repair, as they help to break down old or damaged cartilage and replace it with new tissue. There are several different types of chondroitin lyases, each with a slightly different mechanism of action. Some chondroitin lyases are able to cleave the glycosidic bonds between the sugar molecules that make up chondroitin sulfate, while others are able to remove specific sulfate groups from the molecule. Chondroitin lyases have been the subject of extensive research in the medical field, as they have potential applications in the treatment of a variety of conditions that affect cartilage, including osteoarthritis, rheumatoid arthritis, and other forms of joint disease. Some studies have suggested that chondroitin lyases may be able to help stimulate the production of new cartilage tissue, or to reduce the inflammation and pain associated with joint disease. However, more research is needed to fully understand the potential therapeutic applications of chondroitin lyases, and to determine the most effective ways to use these enzymes in the treatment of cartilage-related conditions.
Receptor-like protein tyrosine phosphatases, class 5 (PTPRC5) are a group of proteins that are involved in cell signaling and communication. They are characterized by the presence of a tyrosine phosphatase domain, which is responsible for removing phosphate groups from tyrosine residues on other proteins. This activity can regulate the activity of these proteins and alter their function. PTPRC5 proteins are expressed in a variety of tissues and cell types, and they have been implicated in a number of biological processes, including cell adhesion, migration, and differentiation. Some members of this family have also been associated with diseases, such as cancer and autoimmune disorders. In the medical field, PTPRC5 proteins are of interest as potential therapeutic targets for the treatment of various conditions. For example, they may be targeted to modulate the activity of proteins involved in cell signaling pathways that are dysregulated in certain diseases. Additionally, PTPRC5 proteins may be used as diagnostic markers to identify individuals who are at risk for certain diseases or to monitor the progression of these diseases.
Aggrecans are a type of proteoglycan that are found in the extracellular matrix of connective tissues, including cartilage, bone, and tendon. They are large, complex molecules that consist of a core protein called aggrecan core protein, which is surrounded by a meshwork of negatively charged glycosaminoglycan chains. In the context of cartilage, aggrecans are the primary component of the proteoglycan matrix, which provides the tissue with its unique properties, such as its ability to resist compression and absorb shock. Aggrecans also play a role in regulating the growth and differentiation of chondrocytes, the cells that produce and maintain cartilage. In the medical field, aggrecans are often studied in relation to various diseases and conditions that affect cartilage, such as osteoarthritis, rheumatoid arthritis, and osteogenesis imperfecta. Changes in the levels or composition of aggrecans have been observed in these conditions, and they may contribute to the development and progression of cartilage damage.
In the medical field, sulfates refer to compounds that contain the sulfate ion (SO4^2-). Sulfates are commonly found in many minerals and are also produced by the body as a byproduct of metabolism. Sulfates are often used in medical treatments, particularly in the treatment of respiratory conditions such as asthma and chronic obstructive pulmonary disease (COPD). They work by helping to thin mucus in the lungs, making it easier to cough up and reducing the risk of infection. Sulfates are also used in the treatment of certain skin conditions, such as psoriasis and eczema, as well as in the treatment of gout, a type of arthritis caused by high levels of uric acid in the blood. In addition to their therapeutic uses, sulfates are also used in the production of a variety of industrial and commercial products, including detergents, fertilizers, and plastics.
Dermatan sulfate is a type of glycosaminoglycan, which is a complex carbohydrate found in the extracellular matrix of connective tissues in the body. It is a major component of the proteoglycans found in the skin, cartilage, and other connective tissues. Dermatan sulfate is synthesized by cells in the connective tissue and is involved in a variety of biological processes, including cell signaling, tissue development, and wound healing. It also plays a role in the regulation of inflammation and the immune response. In the medical field, dermatan sulfate is used as a diagnostic tool to help identify certain diseases and conditions, such as inflammatory bowel disease, osteoarthritis, and certain types of cancer. It is also used in the development of new drugs and therapies for these conditions.
Neurocan is a type of proteoglycan, which is a complex molecule made up of a protein core and chains of carbohydrates. It is a glycosaminoglycan that is found in the extracellular matrix of the central nervous system, including the brain and spinal cord. Neurocan is involved in the development and maintenance of the nervous system, and it plays a role in regulating cell growth and differentiation. It is also thought to be involved in the formation of synapses, which are the connections between neurons that allow them to communicate with each other. In the medical field, neurocan is being studied as a potential target for the treatment of neurological disorders such as multiple sclerosis and Alzheimer's disease.
Lectins, C-Type are a type of carbohydrate-binding proteins that are found in a variety of plants, animals, and microorganisms. They are characterized by the presence of a conserved cysteine residue in their carbohydrate recognition domain, which is responsible for their binding specificity to specific carbohydrate structures. C-Type lectins are involved in a wide range of biological processes, including immune response, cell adhesion, and cell signaling. They are also used in medical research and have potential therapeutic applications, such as in the treatment of cancer, infectious diseases, and inflammatory disorders. In the medical field, C-Type lectins are often studied for their ability to bind to specific carbohydrate structures on the surface of cells, which can be used to target and modulate cellular processes. They are also used as diagnostic tools to detect specific carbohydrate structures in biological samples, such as in the diagnosis of certain diseases or to monitor the progression of a disease.
Extracellular matrix (ECM) proteins are a diverse group of proteins that are secreted by cells and form a complex network within the extracellular space. These proteins provide structural support to cells and tissues, regulate cell behavior, and play a crucial role in tissue development, homeostasis, and repair. ECM proteins are found in all tissues and organs of the body and include collagens, elastin, fibronectin, laminins, proteoglycans, and many others. These proteins interact with each other and with cell surface receptors to form a dynamic and highly regulated ECM that provides a physical and chemical environment for cells to thrive. In the medical field, ECM proteins are important for understanding the development and progression of diseases such as cancer, fibrosis, and cardiovascular disease. They are also used in tissue engineering and regenerative medicine to create artificial ECMs that can support the growth and function of cells and tissues. Additionally, ECM proteins are used as diagnostic and prognostic markers in various diseases, and as targets for drug development.
Receptors, N-Acetylglucosamine (NAG) are a type of protein receptors found on the surface of cells in the immune system. These receptors are responsible for recognizing and binding to N-acetylglucosamine (NAG), a sugar molecule that is commonly found on the surface of bacteria and other microorganisms. When NAG receptors bind to NAG, it triggers a signaling cascade within the cell that leads to the activation of immune cells and the production of inflammatory molecules, which help to fight off the invading microorganisms. NAG receptors are also involved in the regulation of cell growth and differentiation, and have been implicated in the development of certain diseases, including cancer and autoimmune disorders.
Keratan sulfate (KS) is a type of glycosaminoglycan (GAG) that is found in the extracellular matrix of connective tissues throughout the body. It is particularly abundant in the cornea, skin, and joint cartilage. In the medical field, KS is important because it plays a role in the structure and function of many tissues. For example, in the cornea, KS helps to maintain its transparency and elasticity, while in joint cartilage, it helps to provide shock absorption and lubrication. Abnormalities in KS production or metabolism can lead to a variety of diseases and conditions, including corneal dystrophies, osteoarthritis, and certain types of cancer. Therefore, understanding the biology of KS and its role in health and disease is an important area of research in the medical field.
In the medical field, disaccharides are two monosaccharide units (simple sugars) that are joined together by a glycosidic bond. Disaccharides are commonly found in foods and are broken down by the body into their constituent monosaccharides during digestion. Some common examples of disaccharides include sucrose (table sugar), lactose (milk sugar), and maltose (malt sugar). Disaccharides are an important source of energy for the body and are also used in the production of various foods and beverages.
Heparin is a medication that is used to prevent and treat blood clots. It is a natural anticoagulant that works by inhibiting the activity of enzymes that are involved in the formation of blood clots. Heparin is typically administered intravenously, but it can also be given by injection or applied topically to the skin. It is commonly used to prevent blood clots in people who are at risk due to surgery, pregnancy, or other medical conditions. Heparin is also used to treat blood clots that have already formed, such as deep vein thrombosis (DVT) and pulmonary embolism (PE). It is important to note that heparin can have serious side effects, including bleeding, and should only be used under the supervision of a healthcare professional.
Syndecans are a family of transmembrane proteoglycans that are found on the surface of many different types of cells in the human body. They are involved in a variety of cellular processes, including cell adhesion, migration, and signaling. Syndecans are composed of a core protein that is linked to a glycosaminoglycan chain, which is a long chain of sugar molecules. The glycosaminoglycan chain is responsible for the interactions between syndecans and other molecules in the extracellular matrix, such as growth factors and matrix proteins. In the medical field, syndecans are being studied for their potential role in a variety of diseases, including cancer, cardiovascular disease, and inflammatory disorders.
Polysaccharide lyases are a group of enzymes that break down complex carbohydrates, such as starch, glycogen, and cellulose, into simpler sugars. These enzymes are important in the human body for the digestion and absorption of carbohydrates, as well as in the production of certain types of bacteria and the breakdown of plant material. There are several different types of polysaccharide lyases, each of which targets a specific type of carbohydrate. For example, amylases break down starch into maltose and other simpler sugars, while cellulases break down cellulose into glucose. These enzymes are produced by the pancreas, salivary glands, and other organs in the digestive system, and are also found in certain types of bacteria. In the medical field, polysaccharide lyases are sometimes used to treat conditions related to carbohydrate metabolism, such as diabetes and malabsorption disorders. They may also be used in the production of certain types of biofuels and other industrial products.
Tenascin is a large extracellular matrix protein that is expressed in a variety of tissues during development, wound healing, and tissue repair. It is synthesized by fibroblasts and other cells in response to injury or tissue remodeling, and it plays a role in regulating cell migration, adhesion, and differentiation. In the medical field, tenascin is often studied in the context of cancer, where it is overexpressed in many types of tumors and is associated with poor prognosis. It is also involved in the development of fibrosis, a condition characterized by the excessive accumulation of scar tissue in organs and tissues. In addition, tenascin has been shown to play a role in the immune response, and it is involved in the regulation of angiogenesis, the formation of new blood vessels. Overall, tenascin is a complex and multifunctional protein that plays a critical role in many aspects of tissue biology and disease.
Heparin lyase is an enzyme that breaks down heparin, a type of polysaccharide that is commonly used as an anticoagulant medication. Heparin lyase is produced by certain bacteria and can cause heparin resistance, which can lead to increased bleeding and other complications in patients who are taking heparin. Heparin resistance can occur when bacteria in the body produce heparin lyase, which breaks down the heparin molecules, rendering them less effective at preventing blood clots. This condition is typically treated with alternative anticoagulant medications or by administering higher doses of heparin.
Sulfotransferases are a group of enzymes that transfer a sulfate group from a donor molecule to an acceptor molecule. These enzymes play important roles in the metabolism of many drugs, hormones, and other substances in the body. They are also involved in the detoxification of harmful substances, such as environmental pollutants and toxins. Sulfotransferases are found in many tissues throughout the body, including the liver, kidney, and brain. They are classified into different families based on their substrate specificity and mechanism of action. Some of the most well-known families of sulfotransferases include the cytosolic sulfotransferases (SULTs) and the membrane-bound sulfotransferases (SULTs). In the medical field, sulfotransferases are important for understanding the metabolism and pharmacology of drugs. They can affect the efficacy and toxicity of drugs by modifying their chemical structure and altering their interactions with receptors and enzymes. Sulfotransferases are also being studied as potential targets for the development of new drugs for the treatment of various diseases, including cancer, cardiovascular disease, and neurological disorders.
Spinal cord injuries (SCI) are a type of injury that occurs when the spinal cord is damaged or disrupted, usually as a result of trauma or disease. The spinal cord is a bundle of nerves that runs down the back of the neck and lower back, and it is responsible for transmitting signals between the brain and the rest of the body. When the spinal cord is injured, it can result in a range of symptoms, depending on the location and severity of the injury. These can include loss of sensation or movement in the affected area, difficulty with bladder or bowel control, and changes in sexual function. SCI can be caused by a variety of factors, including car accidents, falls, sports injuries, and acts of violence. Treatment for SCI typically involves a combination of medical and rehabilitative care, and the goal is to help individuals with SCI regain as much function as possible and improve their quality of life.
Hyaluronic acid is a naturally occurring glycosaminoglycan (GAG) found in the human body. It is a polysaccharide composed of repeating disaccharide units of glucuronic acid and N-acetylglucosamine. Hyaluronic acid is a major component of the extracellular matrix in connective tissues, including the skin, joint cartilage, and synovial fluid. In the medical field, hyaluronic acid is used in various therapeutic applications, including: 1. Joint injections: Hyaluronic acid is used as a viscosupplement to treat osteoarthritis in the knee, shoulder, and hip joints. It helps to lubricate the joint and reduce friction, thereby reducing pain and improving mobility. 2. Skin care: Hyaluronic acid is used in skincare products to hydrate and plump the skin, reduce the appearance of fine lines and wrinkles, and improve skin elasticity. 3. Wound healing: Hyaluronic acid is used in wound dressings to promote healing by providing a moist environment that supports the growth of new tissue. 4. Eye surgery: Hyaluronic acid is used in eye surgery to help maintain the shape of the cornea and prevent corneal swelling after surgery. Overall, hyaluronic acid has a wide range of medical applications due to its unique properties, including its ability to attract and retain water, its ability to modulate cell behavior, and its ability to promote tissue repair and regeneration.
Sulfur radioisotopes are radioactive isotopes of sulfur, which are used in various medical applications. These isotopes are typically produced by bombarding stable sulfur atoms with high-energy particles, such as protons or neutrons. One commonly used sulfur radioisotope in medicine is sulfur-35 (35S), which has a half-life of approximately 87 days. It is used in a variety of diagnostic and therapeutic applications, including: * Radiolabeling of biomolecules: 35S can be used to label proteins, peptides, and other biomolecules, allowing researchers to study their structure, function, and interactions with other molecules. * Imaging of tumors: 35S-labeled compounds can be used to image tumors in animals or humans, allowing doctors to monitor the growth and spread of tumors. * Radioimmunotherapy: 35S can be used to label antibodies, which can then be targeted to specific cells or tissues in the body, delivering a dose of radiation to kill cancer cells or other diseased cells. Other sulfur radioisotopes, such as sulfur-32 (32S) and sulfur-33 (33S), are also used in medical applications, although they are less commonly used than 35S.
In the medical field, a cicatrix is a scar that forms after the healing of a wound or injury. It is typically a raised, thickened area of skin that is usually pale or lighter in color than the surrounding skin. Cicatrices can be caused by a variety of factors, including surgery, burns, acne, and skin infections. They can range in size and appearance, and may be permanent or fade over time. In some cases, cicatrices may cause discomfort or interfere with the function of the affected area. Treatment options for cicatrices may include topical creams, laser therapy, or surgical procedures.
Decorin is a protein that is found in the extracellular matrix of connective tissues in the human body. It is a member of the small leucine-rich proteoglycan (SLRP) family of proteins, which are involved in the regulation of tissue structure and function. Decorin is primarily found in the skin, where it plays a role in maintaining the integrity of the dermis and preventing the excessive accumulation of collagen fibers. It is also found in other connective tissues, such as tendons, ligaments, and cartilage. In the medical field, decorin is of interest because it has been implicated in a number of diseases and conditions, including skin disorders, such as psoriasis and scleroderma, as well as joint disorders, such as osteoarthritis and rheumatoid arthritis. It is also being studied as a potential target for the development of new treatments for these conditions.
Syndecan-4 is a transmembrane protein that is expressed on the surface of many different types of cells, including epithelial cells, endothelial cells, and fibroblasts. It is a member of the syndecan family of proteoglycans, which are large, complex molecules that are composed of a core protein and a variety of attached carbohydrates. Syndecan-4 plays a number of important roles in the body. One of its main functions is to serve as a receptor for various growth factors and other signaling molecules, which can bind to the protein and trigger a variety of cellular responses. It is also involved in the regulation of cell adhesion and migration, and has been implicated in a number of different diseases and conditions, including cancer, cardiovascular disease, and inflammatory disorders. In the medical field, syndecan-4 is the subject of ongoing research, and there is interest in developing drugs and therapies that target the protein in order to treat various diseases and conditions.
Glucosamine is a naturally occurring amino sugar that is found in the shells of crustaceans and in the cartilage of animals. It is also synthesized in the human body from the amino acid glutamine and the sugar glucose. In the medical field, glucosamine is often used as a dietary supplement to support joint health and reduce the symptoms of osteoarthritis, a degenerative joint disease that affects millions of people worldwide. It is believed to work by stimulating the production of proteoglycans, which are essential components of cartilage that help to cushion and lubricate joints. There is some evidence to suggest that glucosamine may be effective in reducing joint pain and stiffness, improving joint function, and slowing the progression of osteoarthritis. However, more research is needed to confirm these effects and to determine the optimal dosage and duration of treatment. It is important to note that glucosamine supplements are not regulated by the FDA and may contain varying amounts of the active ingredient. Therefore, it is important to choose a high-quality supplement from a reputable manufacturer and to consult with a healthcare provider before starting any new supplement regimen.
Biglycan is a proteoglycan, which is a complex molecule made up of proteins and carbohydrates. It is a type of small leucine-rich proteoglycan (SLRP) that is found in the extracellular matrix of connective tissues in the body. In the medical field, biglycan is known to play a role in the regulation of cell growth and differentiation, as well as in the formation and maintenance of tissues such as cartilage, bone, and blood vessels. It has also been implicated in various diseases, including osteoarthritis, atherosclerosis, and certain types of cancer.
Syndecan-1 is a type of cell surface proteoglycan that plays a role in cell adhesion, migration, and signaling. It is expressed on the surface of many different types of cells, including epithelial cells, endothelial cells, and fibroblasts. Syndecan-1 is composed of a core protein and a number of covalently attached glycosaminoglycan chains, which give it a complex and dynamic structure. In the medical field, syndecan-1 is of interest because it is involved in a number of different diseases and conditions, including cancer, cardiovascular disease, and inflammatory disorders. It is also being studied as a potential therapeutic target for the treatment of these conditions.
Glycosides are a class of organic compounds that are formed by the attachment of a sugar molecule (a glycosyl group) to a non-sugar molecule (a aglycone). In the medical field, glycosides are often found in plants and are used for a variety of therapeutic purposes, including as heart medications, diuretics, and anti-inflammatory agents. One of the most well-known examples of a glycoside is digitalis, which is derived from the foxglove plant and is used to treat heart failure and atrial fibrillation. Digitalis works by slowing down the heart rate and strengthening the contractions of the heart muscle, which can help to improve blood flow and reduce symptoms of heart failure. Other examples of glycosides used in medicine include strophanthin, which is used as a heart medication, and glycyrrhizin, which is used as an anti-inflammatory agent and to treat liver disease. Glycosides can be synthesized in the laboratory or obtained from natural sources, and they are often used in combination with other medications to enhance their therapeutic effects or to reduce their side effects. However, glycosides can also have toxic effects if they are not used properly, so they must be prescribed and monitored carefully by a healthcare professional.
Hyaluronoglucosaminidase (also known as hyaluronidase) is an enzyme that breaks down hyaluronic acid, a complex carbohydrate found in the extracellular matrix of connective tissue. It is primarily produced by cells in the immune system, such as neutrophils and macrophages, and is involved in the process of inflammation. In the medical field, hyaluronoglucosaminidase is used as a diagnostic tool to detect and monitor certain diseases, such as cancer, rheumatoid arthritis, and osteoarthritis. It is also used in certain medical procedures, such as tissue repair and wound healing, to break down hyaluronic acid and facilitate the migration of cells to the site of injury. In addition, hyaluronoglucosaminidase has been studied for its potential therapeutic applications in various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. However, more research is needed to fully understand its role in these conditions and to develop effective treatments.
Chlorates are a class of inorganic salts that contain the chlorate ion (ClO3-). They are typically white or colorless solids that are soluble in water. Chlorates are used in a variety of applications, including as oxidizing agents, water treatment chemicals, and as ingredients in some medications. In the medical field, chlorates are sometimes used as a treatment for certain types of heart rhythm disorders, such as atrial fibrillation. They work by slowing down the electrical activity in the heart, which can help to regulate the heart's rhythm. Chlorates are also used as a source of chlorine in the production of certain medications, such as chloramphenicol. However, it is important to note that chlorates can also have toxic effects on the body, particularly on the thyroid gland. High levels of chlorate exposure can lead to hypothyroidism, which is a condition in which the thyroid gland does not produce enough thyroid hormones. As a result, chlorates are typically used with caution in medical settings, and their use is closely monitored by healthcare professionals.
Syndecan-2 is a type of cell surface proteoglycan that plays a role in cell adhesion, migration, and signaling. It is expressed on the surface of many different types of cells, including epithelial cells, endothelial cells, and fibroblasts. Syndecan-2 is composed of a core protein and a number of covalently attached glycosaminoglycan chains, which give it a complex and dynamic structure. In the medical field, syndecan-2 is of interest because it has been implicated in a number of different diseases and conditions, including cancer, cardiovascular disease, and inflammatory disorders. For example, changes in the expression or function of syndecan-2 have been observed in many types of cancer, and it is thought to play a role in the progression and metastasis of these diseases. Additionally, syndecan-2 has been shown to be involved in the regulation of blood vessel formation, which is important for the development of cardiovascular disease. Overall, syndecan-2 is an important molecule that plays a role in many different cellular processes, and its study is of great interest in the medical field.
Glypicans are a family of proteoglycans that are found in the extracellular matrix of animals. They are composed of a core protein with attached glycosaminoglycan chains, which give them their unique properties. Glypicans play important roles in a variety of biological processes, including cell signaling, cell adhesion, and tissue development. They are also involved in the regulation of growth and differentiation, and have been implicated in a number of diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. In the medical field, glypicans are being studied as potential targets for the development of new therapies for these and other diseases.
Nerve tissue proteins are proteins that are found in nerve cells, also known as neurons. These proteins play important roles in the structure and function of neurons, including the transmission of electrical signals along the length of the neuron and the communication between neurons. There are many different types of nerve tissue proteins, each with its own specific function. Some examples of nerve tissue proteins include neurofilaments, which provide structural support for the neuron; microtubules, which help to maintain the shape of the neuron and transport materials within the neuron; and neurofilament light chain, which is involved in the formation of neurofibrillary tangles, which are a hallmark of certain neurodegenerative diseases such as Alzheimer's disease. Nerve tissue proteins are important for the proper functioning of the nervous system and any disruption in their production or function can lead to neurological disorders.
Uronic acids are a type of carbohydrate that are found in the human body. They are composed of a uronic acid residue, which is a type of carboxylic acid, and a sugar residue. Uronic acids are important components of the extracellular matrix, which is the network of proteins and carbohydrates that surrounds cells in the body. They are also found in the cell walls of plants and bacteria. There are two main types of uronic acids: glucuronic acid and galacturonic acid. Glucuronic acid is the most common type and is found in many different types of molecules, including glycosaminoglycans, proteoglycans, and certain types of lipids. Galacturonic acid is found in pectin, a type of carbohydrate that is found in the cell walls of plants. Uronic acids play important roles in many different biological processes, including cell signaling, inflammation, and the formation and maintenance of tissues. They are also involved in the metabolism of certain drugs and toxins.
Oligosaccharides are short chains of sugar molecules that are composed of three to ten monosaccharide units. They are also known as "oligos" or "short-chain carbohydrates." In the medical field, oligosaccharides have been studied for their potential health benefits, including their ability to improve gut health, boost the immune system, and reduce the risk of chronic diseases such as diabetes and obesity. Some specific types of oligosaccharides that have been studied in the medical field include: 1. Prebiotics: These are oligosaccharides that selectively stimulate the growth of beneficial bacteria in the gut, such as Bifidobacteria and Lactobacilli. 2. Galactooligosaccharides (GOS): These are oligosaccharides that are found naturally in breast milk and have been shown to improve gut health and immune function in infants. 3. Fructooligosaccharides (FOS): These are oligosaccharides that are found in many fruits and vegetables and have been shown to improve gut health and reduce the risk of chronic diseases. Overall, oligosaccharides are an important class of carbohydrates that have potential health benefits and are being studied in the medical field for their potential therapeutic applications.
Syndecan-3 is a type of transmembrane proteoglycan that is expressed on the surface of many different types of cells, including epithelial cells, endothelial cells, and fibroblasts. It is a member of the syndecan family of cell surface proteoglycans, which are involved in a variety of cellular processes, including cell adhesion, migration, and signaling. In the medical field, syndecan-3 is of interest because it has been implicated in a number of different diseases and conditions. For example, it has been shown to play a role in the development of certain types of cancer, including breast cancer and colon cancer. It is also involved in the regulation of the immune system and has been implicated in the development of autoimmune diseases such as rheumatoid arthritis. In addition to its role in disease, syndecan-3 is also being studied for its potential therapeutic applications. For example, it has been shown to have anti-inflammatory properties and is being investigated as a potential treatment for inflammatory diseases such as rheumatoid arthritis and inflammatory bowel disease. It is also being studied as a potential target for cancer therapy, as it is overexpressed in many types of cancer cells.
In the medical field, Nitrous Acid (also known as Nitric Oxide Dioxide or Nitrous Dioxide) is a chemical compound with the formula HNO2. It is a colorless gas that is highly reactive and can be produced by the reaction of nitric oxide (NO) with oxygen (O2) in the presence of water (H2O). Nitrous Acid is not commonly used in medicine, but it has been studied for its potential therapeutic effects. It has been shown to have anti-inflammatory and analgesic properties, and it has been used in the treatment of certain types of cancer and inflammatory bowel disease. However, Nitrous Acid is also a toxic gas that can cause respiratory distress and other health problems if inhaled in high concentrations. Therefore, its use in medicine is carefully regulated and monitored to ensure its safe and effective use.
Monoclonal antibodies (mAbs) are laboratory-made proteins that can mimic the immune system's ability to fight off harmful pathogens, such as viruses and bacteria. They are produced by genetically engineering cells to produce large quantities of a single type of antibody, which is specific to a particular antigen (a molecule that triggers an immune response). In the medical field, monoclonal antibodies are used to treat a variety of conditions, including cancer, autoimmune diseases, and infectious diseases. They can be administered intravenously, intramuscularly, or subcutaneously, depending on the condition being treated. Monoclonal antibodies work by binding to specific antigens on the surface of cells or pathogens, marking them for destruction by the immune system. They can also block the activity of specific molecules involved in disease processes, such as enzymes or receptors. Overall, monoclonal antibodies have revolutionized the treatment of many diseases, offering targeted and effective therapies with fewer side effects than traditional treatments.
Glucuronidase is an enzyme that breaks down glucuronides, which are conjugated forms of various substances, including drugs, hormones, and toxins. In the medical field, glucuronidase is often used as a diagnostic tool to detect the presence of specific substances in the body. For example, in the field of forensic toxicology, glucuronidase can be used to detect the presence of drugs such as cocaine, amphetamines, and opioids in biological samples, such as urine or blood. This is because these drugs are often metabolized in the body by conjugation with glucuronic acid, forming glucuronides. By measuring the levels of glucuronides in a sample, forensic toxicologists can determine whether a person has recently used these drugs. In addition to its use in forensic toxicology, glucuronidase is also used in the treatment of certain medical conditions. For example, in the treatment of certain types of cancer, glucuronidase can be used to break down conjugated toxins that have accumulated in the body, potentially reducing their toxicity and improving patient outcomes.
Sulfatases are a group of enzymes that catalyze the hydrolysis of sulfate esters. In the medical field, sulfatases are important because they play a role in the metabolism of various compounds, including hormones, lipids, and carbohydrates. There are several types of sulfatases, each with its own specific substrate and function. For example, arylsulfatase A is involved in the metabolism of glycosaminoglycans, which are important components of connective tissue. Deficiency of arylsulfatase A can lead to a rare genetic disorder called metachromatic leukodystrophy. Another example is heparan sulfate sulfatase, which is involved in the degradation of heparan sulfate proteoglycans, which are important for cell signaling and tissue development. Deficiency of heparan sulfate sulfatase can lead to a rare genetic disorder called mucopolysaccharidosis type VII. Sulfatases are also important in the treatment of certain diseases. For example, the enzyme heparanase is involved in the degradation of heparan sulfate proteoglycans, which can promote tumor growth and metastasis. Inhibitors of heparanase are being developed as potential cancer therapies. Overall, sulfatases play a critical role in many biological processes and are important targets for research and therapy in the medical field.
Acetylgalactosamine (GalNAc) is a type of sugar molecule that is found in the human body. It is a component of many glycoproteins and glycolipids, which are complex carbohydrates that are attached to proteins and lipids, respectively. GalNAc is also a building block of the polysaccharide chondroitin sulfate, which is found in the extracellular matrix of many tissues, including cartilage and the brain. In the medical field, GalNAc is used as a substrate for the synthesis of certain drugs, such as those used to treat viral infections and cancer. It is also being studied as a potential target for the development of new therapies for a variety of diseases, including diabetes, obesity, and neurodegenerative disorders.
Sulfuric acid is a strong acid that is commonly used in the medical field for various purposes. It is a colorless, odorless, and corrosive liquid that is highly soluble in water. In the medical field, sulfuric acid is used as a chemical reagent in various laboratory procedures, such as the preparation of buffers, the extraction of proteins, and the analysis of biological samples. It is also used as a component in some medications, such as certain antacids and laxatives. However, sulfuric acid is highly caustic and can cause severe burns and tissue damage if it comes into contact with the skin or eyes. Therefore, it is important to handle sulfuric acid with extreme caution and to follow proper safety protocols when working with it.
Chondrosarcoma is a type of cancer that arises from cartilage cells in the body. It is a rare cancer that typically affects adults, although it can occur in children as well. Chondrosarcoma can develop in any part of the body where cartilage is present, but it most commonly occurs in the bones of the pelvis, shoulder, and thigh. Chondrosarcoma is classified into different grades based on how aggressive the cancer is and how quickly it grows. Grade I chondrosarcomas are slow-growing and have a good prognosis, while grade II and III chondrosarcomas are more aggressive and have a poorer prognosis. Treatment for chondrosarcoma typically involves surgery to remove the tumor, followed by radiation therapy or chemotherapy to kill any remaining cancer cells. The prognosis for chondrosarcoma depends on the grade of the cancer, the location of the tumor, and the patient's overall health.
N-Acetylgalactosaminyltransferases (NAGT) are a family of enzymes that transfer the N-acetylgalactosamine (GalNAc) residue from UDP-GalNAc to specific acceptor molecules, such as glycoproteins and glycolipids. These enzymes play a crucial role in the biosynthesis of complex carbohydrates, also known as glycans, which are essential for many cellular processes, including cell-cell recognition, signaling, and immune function. In the medical field, NAGTs are of particular interest because defects in these enzymes can lead to a group of rare genetic disorders known as mucopolysaccharidoses (MPSs). MPSs are characterized by the accumulation of undegraded glycosaminoglycans (GAGs) in the lysosomes of cells, leading to a range of symptoms, including skeletal abnormalities, intellectual disability, and organ dysfunction. NAGT deficiencies are responsible for several forms of MPS, including MPS I, MPS II, and MPS VII. In addition to their role in MPSs, NAGTs are also being studied for their potential therapeutic applications in other diseases, such as cancer and neurodegenerative disorders. For example, some researchers are exploring the use of NAGT inhibitors as targeted therapies for cancer, as these enzymes are often upregulated in cancer cells and are involved in processes such as cell proliferation and invasion.
Iduronic acid is a naturally occurring uronic acid that is found in the glycosaminoglycan chains of proteoglycans in connective tissue. It is a derivative of glucuronic acid, which is a common component of many polysaccharides in the body. Iduronic acid is involved in the formation and maintenance of connective tissue, and it plays a role in the regulation of cell signaling and the immune response. In the medical field, iduronic acid is sometimes used as a diagnostic tool to study the structure and function of connective tissue, and it may also be used as a therapeutic agent to treat certain conditions that affect the connective tissue, such as osteoarthritis and rheumatoid arthritis.
Phosphoadenosine phosphosulfate (PAPS) is a molecule that plays a crucial role in the metabolism of sulfur-containing amino acids and other sulfur-containing compounds in the body. It is synthesized from adenosine triphosphate (ATP) and sulfate, and is involved in the formation of various sulfur-containing molecules, such as glutathione, coenzyme A, and sulfated glycosaminoglycans. In the medical field, PAPS is often studied in the context of various diseases and disorders, including cystic fibrosis, where it is involved in the metabolism of the amino acid cysteine. PAPS is also involved in the metabolism of drugs and xenobiotics, and its levels can be used as a biomarker for certain diseases, such as liver disease and cancer. Additionally, PAPS is a target for the development of new drugs for the treatment of various diseases, including cancer and inflammatory disorders.
Collagen is a protein that is found in the extracellular matrix of connective tissues throughout the body. It is the most abundant protein in the human body and is responsible for providing strength and support to tissues such as skin, bones, tendons, ligaments, and cartilage. In the medical field, collagen is often used in various medical treatments and therapies. For example, it is used in dermal fillers to plump up wrinkles and improve skin texture, and it is also used in wound healing to promote tissue regeneration and reduce scarring. Collagen-based products are also used in orthopedic and dental applications, such as in the production of artificial joints and dental implants. In addition, collagen is an important biomarker for various medical conditions, including osteoporosis, rheumatoid arthritis, and liver disease. It is also used in research to study the mechanisms of tissue repair and regeneration, as well as to develop new treatments for various diseases and conditions.
Fibroblast Growth Factor 2 (FGF2) is a protein that plays a crucial role in the growth and development of various tissues in the human body. It is a member of the fibroblast growth factor family of proteins, which are involved in a wide range of biological processes, including cell proliferation, differentiation, migration, and survival. In the medical field, FGF2 is often studied in relation to various diseases and conditions, including cancer, cardiovascular disease, and neurological disorders. For example, FGF2 has been shown to promote the growth and survival of cancer cells, making it a potential target for cancer therapy. It has also been implicated in the development of cardiovascular disease, as it can stimulate the growth of blood vessels and contribute to the formation of atherosclerotic plaques. In addition, FGF2 plays a role in the development and maintenance of the nervous system, and has been implicated in various neurological disorders, including Alzheimer's disease, Parkinson's disease, and multiple sclerosis. It is also involved in the regulation of bone growth and remodeling, and has been studied in the context of osteoporosis and other bone diseases. Overall, FGF2 is a complex and multifaceted protein that plays a critical role in many different biological processes, and its function and regulation are the subject of ongoing research in the medical field.
In the medical field, "Disease Models, Animal" refers to the use of animals to study and understand human diseases. These models are created by introducing a disease or condition into an animal, either naturally or through experimental manipulation, in order to study its progression, symptoms, and potential treatments. Animal models are used in medical research because they allow scientists to study diseases in a controlled environment and to test potential treatments before they are tested in humans. They can also provide insights into the underlying mechanisms of a disease and help to identify new therapeutic targets. There are many different types of animal models used in medical research, including mice, rats, rabbits, dogs, and monkeys. Each type of animal has its own advantages and disadvantages, and the choice of model depends on the specific disease being studied and the research question being addressed.
Hexosamines are a type of sugar molecule that are found in the human body. They are composed of a hexose (a sugar with six carbon atoms) and an amine group. Hexosamines are important components of the glycosaminoglycan (GAG) molecules that are found in the extracellular matrix of connective tissue. GAGs are complex carbohydrates that play a variety of roles in the body, including providing structural support to tissues, regulating cell signaling, and participating in the immune response. Hexosamines are also found in other types of molecules, such as glycoproteins and proteoglycans. In the medical field, hexosamines are of interest because they have been implicated in a number of diseases, including cancer, diabetes, and inflammatory disorders.
Dextran sulfate is a polysaccharide compound that is derived from the bacterial fermentation of cornstarch. It is used in a variety of medical applications, including as a diagnostic tool for detecting blood clots, as an anticoagulant to prevent blood clots from forming, and as a component of certain types of chemotherapy drugs. Dextran sulfate is also used in the treatment of certain types of liver disease, such as cirrhosis, by helping to reduce the buildup of scar tissue in the liver. In addition, it has been studied for its potential use in the treatment of certain types of cancer, such as colon cancer, by helping to stimulate the immune system to attack cancer cells.
Membrane glycoproteins are proteins that are attached to the cell membrane through a glycosyl group, which is a complex carbohydrate. These proteins play important roles in cell signaling, cell adhesion, and cell recognition. They are involved in a wide range of biological processes, including immune response, cell growth and differentiation, and nerve transmission. Membrane glycoproteins can be classified into two main types: transmembrane glycoproteins, which span the entire cell membrane, and peripheral glycoproteins, which are located on one side of the membrane.
Glycoproteins are a type of protein that contains one or more carbohydrate chains covalently attached to the protein molecule. These carbohydrate chains are made up of sugars and are often referred to as glycans. Glycoproteins play important roles in many biological processes, including cell signaling, cell adhesion, and immune response. They are found in many different types of cells and tissues throughout the body, and are often used as markers for various diseases and conditions. In the medical field, glycoproteins are often studied as potential targets for the development of new drugs and therapies.
Fibronectins are a family of large, soluble glycoproteins that are found in the extracellular matrix of connective tissues. They are synthesized by a variety of cells, including fibroblasts, endothelial cells, and epithelial cells, and are involved in a wide range of cellular processes, including cell adhesion, migration, and differentiation. Fibronectins are composed of two large subunits, each containing three distinct domains: an N-terminal domain, a central domain, and a C-terminal domain. The central domain contains a high-affinity binding site for fibronectin receptors on the surface of cells, which allows cells to adhere to the extracellular matrix and migrate through it. Fibronectins play a critical role in the development and maintenance of tissues, and are involved in a variety of pathological processes, including wound healing, tissue fibrosis, and cancer. They are also important in the immune response, as they can bind to and activate immune cells, and can modulate the activity of various cytokines and growth factors.
Glucuronic acid is a naturally occurring organic acid that is produced by the liver as a byproduct of the metabolism of carbohydrates. It is a key component of the glycoprotein molecule hyaluronic acid, which is found in the extracellular matrix of connective tissue throughout the body. In the medical field, glucuronic acid is often used as a precursor in the synthesis of other important molecules, such as bile acids and some hormones. It is also used in the treatment of certain medical conditions, such as hyperuricemia (high levels of uric acid in the blood), where it is used to convert excess uric acid into a more water-soluble form that can be excreted from the body. In addition, glucuronic acid is used in the production of certain drugs and dietary supplements, and it has been shown to have potential anti-inflammatory and anti-cancer effects in laboratory studies. However, more research is needed to fully understand the therapeutic potential of glucuronic acid in the treatment of human diseases.
Recombinant proteins are proteins that are produced by genetically engineering bacteria, yeast, or other organisms to express a specific gene. These proteins are typically used in medical research and drug development because they can be produced in large quantities and are often more pure and consistent than proteins that are extracted from natural sources. Recombinant proteins can be used for a variety of purposes in medicine, including as diagnostic tools, therapeutic agents, and research tools. For example, recombinant versions of human proteins such as insulin, growth hormones, and clotting factors are used to treat a variety of medical conditions. Recombinant proteins can also be used to study the function of specific genes and proteins, which can help researchers understand the underlying causes of diseases and develop new treatments.
Polysaccharides are complex carbohydrates that are composed of long chains of monosaccharide units linked together by glycosidic bonds. They are found in many different types of biological materials, including plant cell walls, animal tissues, and microorganisms. In the medical field, polysaccharides are often used as drugs or therapeutic agents, due to their ability to modulate immune responses, promote wound healing, and provide other beneficial effects. Some examples of polysaccharides that are used in medicine include hyaluronic acid, chondroitin sulfate, heparin, and dextran.
Laminin is a type of protein that is found in the basement membrane, which is a thin layer of extracellular matrix that separates tissues and organs in the body. It is a major component of the extracellular matrix and plays a crucial role in maintaining the structural integrity of tissues and organs. Laminin is a large, complex protein that is composed of several subunits. It is synthesized by cells in the basement membrane and is secreted into the extracellular space, where it forms a network that provides support and stability to cells. In the medical field, laminin is of great interest because it is involved in a number of important biological processes, including cell adhesion, migration, and differentiation. It is also involved in the development and maintenance of many different types of tissues, including the nervous system, skeletal muscle, and the cardiovascular system. Laminin has been the subject of extensive research in the medical field, and its role in various diseases and conditions is being increasingly understood. For example, laminin has been implicated in the development of certain types of cancer, as well as in the progression of neurodegenerative diseases such as Alzheimer's and Parkinson's. As a result, laminin is a potential target for the development of new therapies for these and other diseases.
Xylose is a type of sugar that is found in the cell walls of plants. It is a monosaccharide, which means it is a simple sugar made up of one molecule of carbon, hydrogen, and oxygen. In the medical field, xylose is sometimes used as a diagnostic tool to test for certain conditions, such as celiac disease or malabsorption syndromes. In these tests, a person is given a solution containing xylose and then their blood is tested to see how well their body is able to absorb it. If the body is not able to absorb xylose properly, it may be a sign of an underlying medical condition.
Glycoside hydrolases are a group of enzymes that catalyze the hydrolysis of glycosidic bonds in carbohydrates. These enzymes are involved in a wide range of biological processes, including digestion, metabolism, and signaling. In the medical field, glycoside hydrolases are often used as diagnostic tools to study carbohydrate metabolism and to develop new treatments for diseases related to carbohydrate metabolism, such as diabetes and obesity. They are also used in the production of biofuels and other industrial products.
Lipoprotein lipase (LPL) is an enzyme that plays a crucial role in the metabolism of lipids (fats) in the human body. It is primarily found in the capillary endothelial cells of adipose tissue (fat tissue) and muscle tissue, where it is responsible for hydrolyzing triglycerides (fatty acids) from circulating lipoproteins, such as chylomicrons and very low-density lipoproteins (VLDL). The hydrolysis of triglycerides by LPL releases free fatty acids, which can then be taken up by adipose tissue and muscle cells for energy production or storage. LPL also plays a role in the metabolism of high-density lipoproteins (HDL), the "good" cholesterol, by hydrolyzing triglycerides in HDL particles. Abnormalities in LPL activity can lead to a variety of metabolic disorders, including hypertriglyceridemia (elevated levels of triglycerides in the blood), familial chylomicronemia syndrome, and lipemia retinalis. In addition, LPL has been implicated in the development of atherosclerosis, a condition characterized by the buildup of plaque in the arteries, which can lead to heart attack and stroke.
Sulfur isotopes are atoms of sulfur that have different numbers of neutrons in their nuclei, resulting in different atomic masses. In the medical field, sulfur isotopes are often used in diagnostic imaging techniques, such as positron emission tomography (PET) scans. For example, sulfur-35 (35S) and sulfur-75 (75S) are commonly used as tracers to study the metabolism of sulfur-containing compounds in the body, such as amino acids and neurotransmitters. These isotopes can be administered to a patient in the form of a radiolabeled compound, and the distribution and metabolism of the compound can be monitored using PET imaging. This information can be used to diagnose and monitor a variety of medical conditions, including neurological disorders, cancer, and cardiovascular disease.
Chondroitin sulfate proteoglycan
Rho family of GTPases
Stem cell marker
Collagen, type XV, alpha 1
WikiGenes - CSPG4 - chondroitin sulfate proteoglycan 4
VCAN gene: MedlinePlus Genetics
Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan. | Journal of Experimental Medicine |...
Immediate Hypersensitivity Reactions: Background, Pathophysiology, Epidemiology
ALSF Childhood Cancer Research Grants | Page 76 | Alex's Lemonade Stand Foundation for Childhood Cancer
Michele Lemons, Ph.D | Assumption University
The extracellular matrix regulates cortical layer dynamics and cross-columnar frequency integration in the auditory cortex |...
Protective Antibodies against Placental Malaria and Poor Outcomes during Pregnancy, Benin - Volume 21, Number 5-May 2015 -...
12 Ingredients for Natural Arthritis Treatment of Joint Pain - Healthynewage.com
Hans-Georg Kuhn | University of Gothenburg
WO2021050634A1 - Recombinant microorganisms for in vivo production of sulfated glycosaminoglycans - Google Patents
Aggrecan Products: R&D Systems
L-Lysine 500 Mg 100 Vegetarian Caps
Genetic alterations and epigenetic alterations of cancer‑associated fibroblasts (Review)
Update on Perineuronal Net Staining With Wisteria floribunda Agglutinin (WFA)
Extracellular Matrix | Pearltrees
Histone modifications affect timing of oligodendrocyte progenitor differentiation in the developing rat brain | Journal of...
Loss of Chondroitin Sulfate Is Detrimental | Cox Technic
Joint Pain in the Workplace | Blogs | CDC
Arthraid capsules for Joint Health- MerryClinic
Glucosamine Chondroitin with MSM | Pure Encapsulations | Joint Health
Synthesis and Applications of Synthetic Peptides | IntechOpen
The performance of cosmetic products on the skin's firmness and tonicity - Premium Beauty News
Perlman, Robert L. 2008 - Office of NIH History and Stetten Museum
Arsenite induces tissue factor synthesis through Nrf2 activation in cultured human aortic smooth muscle cells
SMART: TSPN domain annotation
Wolfson Centre for Age Related Diseases - Research output - King's College London
University of Nebraska Medical Center - Research output - Research Nebraska
- As chemically specialized forms of the extracellular matrix in the central nervous system, polyanionic perineuronal nets (PNs) contain diverse constituents, including chondroitin sulfate proteoglycans (CSPGs), hyaluronic acid, and tenascins. (nih.gov)
- They are divided in four groups: hyaluronic acid, keratan sulfate, chondroitin/dermatan sulfate, andheparan sulfate. (premiumbeautynews.com)
- Chondroitinase ABC or chondroitinase AC treatment of the CSPG digested the chondroitin sulfate glycosaminoglycan, yielding a core protein that migrated with an apparent molecular weight of 38,000. (silverchair.com)
- Each Aggrecan molecule contains approximately 100 and 30 keratan sulfate and glycosaminoglycan (GAG) sidechains, respectively. (rndsystems.com)
- Glucosamine promotes the synthesis of the glycosaminoglycan chondroitin sulfate. (drvitaminsolutions.com)
- Skin decorin (DCN) is an antiadhesive dermatan sulfate-rich proteoglycan that interacts with thrombospondin-1 (TSP) and inhibits fibroblast adhesion to TSP [Winnemoller et al. (embl.de)
- Iduronate sulfatase deficiency leads to the subsequent GAG accumulation of heparan sulfate and chondroitin sulfate B (dermatan sulfate) in the body. (medscape.com)
- Other than water, the mesoglea is composed of several substances including fibrous proteins like collagen and heparan sulphate proteoglycans. (pearltrees.com)
- Binding is mediated by VAR2CSA, a parasite antigen coded by the var gene, which interacts with chondroitin sulfate A (CSA). (cdc.gov)
- From NCBI Gene: This gene encodes an enzyme that transfers N-acetylglucosamine (GalNAc) to the core tetrasaccharide linker and to elongating chondroitin sulfate chains in proteoglycans. (nih.gov)
- Pure Encapsulations Glucosamine and Chondroitin with MSM offers highly purified constituents for healthy cartilage formation and joint movement ease. (drvitaminsolutions.com)
- Ph.D. dissertation title: "Inhibition of regeneration in the injured, adult spinal cord: potential role of chondroitin sulfate proteoglycans, specifically aggrecan. (assumption.edu)
- Intact aggrecan and chondroitin-sulfate depleted aggrecan inhibit axon growth in the adult rat spinal cord. (assumption.edu)
- Proteoglycan synthesis decreases, which decreases the osmotic swelling and the traffic of oxygen and nutrients to the disk. (medscape.com)
- Aggrecan belongs to the chondroitin sulfate (CS) proteoglycan family, which also includes Versican, Brevican, and Neurocan. (rndsystems.com)
- Adaptation of sensory neurons to hyalectin and decorin proteoglycans. (assumption.edu)
- The murine Ia-associated chondroitin sulfate proteoglycan (CSPG) was studied both biochemically and immunochemically to determine the nature of its core protein. (silverchair.com)
- Biochemically, aging increases the ratio of keratin sulfate to chondroitin sulfate, and it also changes the proportion of chondroitin-4-sulfate to chondroitin-6-sulfate, with a parallel decrease in water content. (medscape.com)
- 2] Aging and degeneration have in common decreased water and proteoglycan content in the disks, combined with increased collagen. (medscape.com)
- Chondroitin Sulfate reduces inflammation and assists the Glucosamine in protecting against future cartilage degeneration. (healthynewage.com)
- It combines most popular anti-inflammatory agents such as Glucosamine, Chondroitin, MSM, vitamin, mineral and some Chinese herbal medicine, such as Corydalis Yanhusuo, to help control the joints inflammation, repair the cartilage, and relieve the pain. (merryclinic.com)
- Glucosamine 1000 mg and Chondroitin Sulfate 134 mg are substances found naturally in the body. (merryclinic.com)
- Various studies have indicated the combination of glucosamine, chondroitin, and MSM in Pure Encapsulations Glucosamine with MSM provides the needed nutrients for optimal cartilage composition, connective tissue strength, and joint mobility & function. (drvitaminsolutions.com)
- Sulfur-containing methylsulfonylmethane (MSM) is included in this glucosamine and chondroitin combination to provide an enhanced spectrum of nutrients for optimal cartilage matrix composition, connective tissue strength, and joint comfort. (drvitaminsolutions.com)
- Several studies indicate that the combination of glucosamine HCl and chondroitin sulfate has positive effects on joint mobility and comfort. (drvitaminsolutions.com)
- Chondroitin sulfate is responsible for building the ground substance of cartilage, molecules known as proteoglycans. (drvitaminsolutions.com)
- 58) Low proteoglycan (CS/GAG) concentrations in all the discs of a spine precede disc degeneration. (coxtechnic.com)
- In 1976, the enzyme deficiency in Morquio syndrome type IVA (galactosamine-6-sulfatase deficiency [ie, N -acetyl-galactosamine-6-sulfate sulfatase deficiency]) was identified. (medscape.com)
- Chondroitin sulfate and disc herniation and degeneration is a large topic to study. (coxtechnic.com)
- Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan. (silverchair.com)
- Chondroitin Sulfate is part of a large protein molecule (proteoglycan) that gives cartilage elasticity. (merryclinic.com)
- It stimulates the production of glycosaminoglycans and proteoglycans, two essential building blocks of cartilage. (healthynewage.com)
- The diversity of proteoglycans and their high interaction with growth factors and their receptors provides structural basis for a multitude of biological functions. (premiumbeautynews.com)
- In particular, chondroitin sulfate proteoglycans (CSPGs) have been found to be involved in almost every aspect of this well-orchestrated yet delicate process. (nih.gov)
- In the adult mammalian CNS, chondroitin sulfate proteoglycans (CSPGs) and myelin-associated inhibitors (MAIs) stabilize neuronal structure and restrict compensatory sprouting following injury. (nih.gov)
- Chondroitin sulfate proteoglycans (CSPGs) act as potent inhibitors of axonal growth and neuroplasticity after spinal cord injury (SCI). (bvsalud.org)
- The barrier to their regrowth is largely due to chemicals called chondroitin sulphate proteoglycans (CSPGs). (nih.gov)
- however, proteins called chondroitin sulfate proteoglycans (CSPGs) that appear at sites of injury prevent these cells from re-growing and reconnecting their axons to appropriate targets. (nih.gov)
- Axon regrowth after spinal cord injury (SCI) is inhibited by several types of inhibitory extracellular molecules in the central nervous system (CNS), including chondroitin sulfate proteoglycans (CSPGs), which also are components of perineuronal nets (PNNs). (nsf.gov)
- Versican: a versatile extracellular matrix proteoglycan in cell biology. (medlineplus.gov)
- Proteoglycans are found throughout the human body, forming the intricate extracellular matrix. (nih.gov)
- The scar is comprised of astrocytes which increase their expression of extracellular matrix molecules, especially chondroitin sulfate proteoglycans. (nih.gov)
- Hyaluronic acid (HA) and proteoglycans (such as dermatan sulphate (DS) and chondroitin sulphate (CS)) are the main components of the extracellular matrix of the skin, along with collagen and elastin. (mdpi.com)
- Cells comprising human tissues are embedded in, and supported by, extracellular matrices composed of collagens, proteoglycans, and associated proteins. (nih.gov)
- GAGs are carbohydrate polymers and are usually attached to extracellular matix proteins to form proteoglycans (hyaluronic acid is a notable exception, see below). (wikidoc.org)
- Described below are the different types of proteoglycan found within the extracellular matrix. (wikidoc.org)
- It occurs as a proteoglycan (PG) in which two or three HS chains are attached in close proximity to cell suface or extracellular matrix proteins. (wikidoc.org)
- In the extracellular matrix, especially basement membranes , the multi-domain proteins perlecan , agrin and collagen XVIII are the main proteins to which heparan sulfate is attached. (wikidoc.org)
- Chondroitin sulfate proteoglycans are the foremost component of the extracellular matrix in the central nervous system . (satterwhitechiropractic.com)
- 6. Surfen-mediated blockade of extratumoral chondroitin sulfate glycosaminoglycans inhibits glioblastoma invasion. (nih.gov)
- Both chondroitin sulfate and heparan sulfate interact with two families of receptors: the LAR family, which includes Receptor Protein Tyrosine Phosphatase RPTP) σ RPTP-δ and the Leukocyte Common Antigen Receptor (LAR), and two members of the Nogo Receptor familiy, NgR1 and NgR3. (nih.gov)
- Heparan sulfate (HS) is a linear polysaccharide found in all animal tissues. (wikidoc.org)
- But curiously, PTPσ also binds to heparin sulfate proteoglycans (HSPGs), molecules that promote axonal growth. (nih.gov)
- CSPG4 represents an integral membrane chondroitin sulfate proteoglycan expressed by human malignant melanoma cells. (nih.gov)
- Chondroitin sulfate shows benefits in treating central nervous system diseases such as multiple sclerosis . (satterwhitechiropractic.com)
- Glucosamine is an essential building block for the formation of glycosaminoglycans GAGs and proteoglycans, the main components of cartilage tissue. (vitaminlife.com)
- There are several reports showing that taking chondroitin with glucosamine increases the effects of warfarin. (nih.gov)
- Taking chondroitin sulfate together with glucosamine hydrochloride might reduce blood levels of glucosamine. (nih.gov)
- It's also not clear if this interaction occurs with other forms of glucosamine, such as glucosamine sulfate. (nih.gov)
- Used with glucosamine, chondroitin sulfate alleviates pain and inflammation from osteoarthritis and reportedly has a beneficial effect on degenerated joints. (nih.gov)
- Thus dietary supplements containing glucosamine and chondroitin sulfate have a potential market of tens of millions of Americans who suffer from osteoarthritis, athletes and dancers who may have joint overuse, and aging baby boomers interested in maintaining their joints. (nih.gov)
- Glucosamine and chondroitin provide structural building blocks for macromolecules, such as proteoglycans, which support healthy joint cartilage. (acuatlanta.net)
- SynovX™ Recovery features methylsulfonylmethane (MSM) blended with naturally occurring, clinically researched glucosamine sulfate and chondroitin sulfate. (myvillagegreen.com)
- NOW Extra Strength Glucosamine & Chondroitin combines two well-known joint support ingredients in their sulfate forms. (vitaminlife.com)
- Glucosamine, an amino sugar naturally present in the body, is a form of glucosamine sulfate. (thesupplementswiki.com)
- Chondroitin and glucosamine are often combined to make glucosamine a powerful component for joint problems because of its anti-inflammatory properties. (thesupplementswiki.com)
- Chondroitin sulfate and glucosamine sulfate are particularly important nutrients to the disc. (satterwhitechiropractic.com)
- Chondroitin sulfate proteoglycans inhibit regeneration, neuroprotection, and plasticity following spinal cord injury. (cam.ac.uk)
- 3. Chondroitin sulfate proteoglycans potently inhibit invasion and serve as a central organizer of the brain tumor microenvironment. (nih.gov)
- An injectable solution containing chondroitin sulfate and sodium hyaluronate is approved by the FDA to protect the eye during cataract surgery. (nih.gov)
- The sodium salt of chondroitin sulfate, which is the commercially available form, has a different Chemical Abstracts Services number [CAS No. 9082-07-9]. (nih.gov)
- We have establihed that all of these interactions depend upon sulfation: HS and highly sulfated CS bind with high affinity to all five of these receptors. (nih.gov)
- Current research is directed at understanding the structural features of these receptors that mediate their interactions with proteoglycan GAG chains. (nih.gov)
- 4. Perturbing chondroitin sulfate proteoglycan signaling through LAR and PTPσ receptors promotes a beneficial inflammatory response following spinal cord injury. (nih.gov)
- Chondroitin sulfate is a chemical found in human and animal cartilage. (nih.gov)
- Chondroitin sulfate is one of the building blocks of cartilage. (nih.gov)
- Salmon skin, a rich source of collagen, contains cartilage proteoglycan, which modulates healthy inflammatory response function in joints responding to exercise-related stress, thus promoting comfort. (acuatlanta.net)
- Proteoglycans contribute to structural resilience by trapping water in the cartilage matrix. (acuatlanta.net)
- Chondroitin sulfates contribute to the tensile strength of cartilage, tendons , ligaments and walls of the aorta . (wikidoc.org)
- Patients with conditions like osteoarthritis - a result of wear and tear on cartilage and joints which many of us Oxford back pain sufferers experience as we age - may benefit from chondroitin sulfate. (satterwhitechiropractic.com)
- Hyaluronan and chondroitin sulfate proteoglycans in the supramolecular organization of the mammalian vitreous body. (medlineplus.gov)
- It consists of an extended protein core to which many chondroitin sulfate and keratan sulfate (linear sulfated polysaccharide) chains are attached. (nih.gov)
- Oral consumption of chondroitin, sulfate has a positive impact on the osteoarthritic joints. (thesupplementswiki.com)
- Sequestration of infected erythrocytes in the placenta is mediated by VAR2CSA, the P. falciparum erythrocyte membrane protein 1 variant that binds to chondroitin sulfate A (CSA) on the syncytiotrophoblast ( 11 , 12 ). (cdc.gov)
- Technical Products and Impurities: Chondroitin sulfate [CAS No. 9007-28-7] is a mixture of derivatives of chondroitin which have a sulfate moiety esterified to the galactosamine moiety of chondroitin. (nih.gov)
- Some of the GlcA residues are epimerized to IdoA, while either of the two sugars in a disaccharide pair can be sulfate on any of several positions. (nih.gov)
- Chondroitin sulfate is possibly safe when used together with other ingredients in an eye drop. (nih.gov)
Spinal cord i1
- Chondroitin sulfate proteoglycans prevent immune cell phenotypic conversion and inflammation resolution via TLR4 in rodent models of spinal cord injury. (bvsalud.org)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Chondroitin Sulfate Proteoglycan 5 (CSPG5) in Tissue homogenates, cell lysates and other biological fluids. (clinical-trial-logistics.com)
- 5. Chondroitin Sulfate Proteoglycans Negatively Modulate Spinal Cord Neural Precursor Cells by Signaling Through LAR and RPTPσ and Modulation of the Rho/ROCK Pathway. (nih.gov)
- 14. Chondroitin sulfate content and decorin expression in glioblastoma are associated with proliferative activity of glioma cells and disease prognosis. (nih.gov)
- Description: A sandwich ELISA kit for detection of Chondroitin Sulfate Proteoglycan 5 from Rat in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (clinical-trial-logistics.com)
- Keratan sulfates have a variable sulfate content and unlike many other GAGs, does not contain uronic acid . (wikidoc.org)
- Aggrecan is a bottlebrush shaped high molecular weight proteoglycan. (nih.gov)
- Oxford chiropractic patients can feel this care on each visit…and hear the latest information like the following about chondroitin sulfate and its benefit for your matrices! (satterwhitechiropractic.com)
- It is covalently attached to the core protein to form a proteoglycan. (labex-gral.fr)
- Chondroitin sulfate is brought to the attention of the Chemical Selection Working Group because it is widely used in dietary supplement that would be consumed over a period of many years to maximize potential beneficial effects. (nih.gov)
- We have identified diifferences in the interaction of the LAR family members with proteoglycans which may explain their differential actions on neurons. (nih.gov)
- Research has shown that chondroitin sulfate reduces arthritic pain, improves joint function and reduces joint swelling and stiffness. (satterwhitechiropractic.com)
- However, until more is known, do not take chondroitin sulfate if you have prostate cancer or are at high risk for developing it (you have a brother or father with prostate cancer). (nih.gov)
- Virtually no information on the potential toxicity of chondroitin sulfate was found in the available literature. (nih.gov)
- Description: A competitive ELISA for quantitative measurement of Canine Chondroitin Sulfate Proteoglycan 5 (CSPG5) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (clinical-trial-logistics.com)
- This effect has not been shown with chondroitin sulfate supplements. (nih.gov)
- Early research suggests that chondroitin might cause the spread or recurrence of prostate cancer. (nih.gov)