Biglycan
Decorin
Extracellular Matrix Proteins
Chondroitin Sulfate Proteoglycans
Versicans
Collagen Type VI
Dermatan Sulfate
Keratan Sulfate
Aggrecans
Glycosaminoglycans
Extracellular Matrix
Chondroitin ABC Lyase
Encyclopedias as Topic
Connective tissues: matrix composition and its relevance to physical therapy. (1/269)
In the last 2 decades, the understanding of CT structure and function has increased enormously. It is now clear that the cells of the various CTs synthesize a variety of ECM components that act not only to underpin the specific biomechanical and functional properties of tissues, but also to regulate a variety of cellular functions. Importantly for the physical therapist, and as discussed above, CTs are responsive to changes in the mechanical environment, both naturally occurring and applied. The relative proportions of collagens and PGs largely determine the mechanical properties of CTs. The relationship between the fibril-forming collagens and PG concentration is reciprocal. Connective tissues designed to resist high tensile forces are high in collagen and low in total PG content (mostly dermatan sulphate PGs), whereas CTs subjected to compressive forces have a greater PG content (mostly chondroitin sulphate PGs). Hyaluronan has multiple roles and not only provides tissue hydration and facilitation of gliding and sliding movements but also forms an integral component of large PG aggregates in pressure-resisting tissues. The smaller glycoproteins help to stabilize and link collagens and PGs to the cell surface. The result is a complex interacting network of matrix molecules, which determines both the mechanical properties and the metabolic responses of tissues. Patients with CT problems affecting movement are frequently examined and treated by physical therapists. A knowledge of the CT matrix composition and its relationship to the biomechanical properties of these tissues, particularly the predictable responses to changing mechanical forces, offers an opportunity to provide a rational basis for treatments. The complexity of the interplay among the components, however, requires that further research be undertaken to determine more precisely the effects of treatments on the structure and function of CTs. (+info)Distinct secondary structures of the leucine-rich repeat proteoglycans decorin and biglycan. Glycosylation-dependent conformational stability. (2/269)
Biglycan and decorin have been overexpressed in eukaryotic cells and two major glycoforms isolated under native conditions: a proteoglycan substituted with glycosaminoglycan chains; and a core protein form secreted devoid of glycosaminoglycans (Hocking, A. M., Strugnell, R. A., Ramamurthy, P., and McQuillan, D. J. (1996) J. Biol. Chem. 271, 19571-19577; Ramamurthy, P., Hocking, A. M., and McQuillan, D. J. (1996) J. Biol. Chem. 271, 19578-19584). Far-UV CD spectroscopy of decorin and biglycan proteoglycans indicates that, although they are predominantly beta-sheet, biglycan has a significantly higher content of alpha-helical structure. Decorin proteoglycan and core protein are very similar, whereas the biglycan core protein exhibits closer similarity to the decorin glycoforms than to the biglycan proteoglycan form. However, enzymatic removal of the chondroitin sulfate chains from biglycan proteoglycan does not induce a shift to the core protein structure, suggesting that the final form is influenced by polysaccharide addition only during biosynthesis. Fluorescence emission spectroscopy demonstrated that the single tryptophan residue, which is at a conserved position at the C-terminal domain of both biglycan and decorin, is found in similar microenvironments. This indicates that in this specific domain the different glycoforms do exhibit apparent conservation of structure. Exposure of decorin and biglycan to 10 M urea resulted in an increase in fluorescent intensity, which indicates that the emission from tryptophan in the native state is quenched. Comparison of urea-induced protein unfolding curves provide further evidence that decorin and biglycan assume different structures in solution. Decorin proteoglycan and core protein unfold in a manner similar to a classic two-state model, in which there is a steep transition to an unfolded state between 1 and 2 M urea. The biglycan core protein also shows a similar steep transition. However, biglycan proteoglycan shows a broad unfolding transition between 1 and 6 M urea, probably indicating the presence of stable unfolding intermediates. (+info)Decorin is a Zn2+ metalloprotein. (3/269)
Decorin is ubiquitously distributed in the extracellular matrix of mammals and a member of the proteoglycan family characterized by a core protein dominated by leucine-rich repeat motifs. We show here that decorin extracted from bovine tissues under denaturing conditions or produced in recombinant "native" form by cultured mammalian cells has a high affinity for Zn2+ as demonstrated by equilibrium dialyses. The Zn2+-binding sites are localized to the N-terminal domain of the core protein that contains 4 Cys residues in a spacing reminiscent of a zinc finger. A recombinant 41-amino acid long peptide representing the N-terminal domain of decorin has full Zn2+ binding activity and binds two Zn2+ ions with an average KD of 3 x 10(-7) M. Binding of Zn2+ to this peptide results in a change in secondary structure as shown by circular dichroism spectroscopy. Biglycan, a proteoglycan that is structurally closely related to decorin contains a similar high affinity Zn2+-binding segment, whereas the structurally more distantly related proteoglycans, epiphycan and osteoglycin, do not bind Zn2+ with high affinity. (+info)Resistance of small leucine-rich repeat proteoglycans to proteolytic degradation during interleukin-1-stimulated cartilage catabolism. (4/269)
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)Differential regulation of extracellular matrix molecules by mechanical strain of fetal lung cells. (5/269)
We have previously shown that an intermittent mechanical strain regimen (5% elongation, 60 cycles/min, 15 min/h) that simulates fetal breathing movements stimulated fetal rat lung cell proliferation. Because normal lung growth requires proper coordination between cell proliferation and extracellular matrix (ECM) remodeling, we subjected organotypic cultures of fetal rat lung cells (day 19 of gestation, term = 22 days) to this strain regimen and examined alterations in ECM gene and protein expression. Northern analysis revealed that mechanical strain reduced messages for procollagen-alpha1(I) and biglycan and increased the levels of mRNA for collagen-alpha1(IV) and -alpha2(IV), whereas laminin beta-chain mRNA levels remained constant. Regardless of mRNA changes, mechanical strain increased the protein content of type I and type IV collagen as well as of biglycan in the medium. Mechanical strain did not affect gene expression of several matrix metalloproteinases (MMPs), such as MMP-1 (interstitial collagenase), MMP-2 (gelatinase A), and MMP-3 (stromelysin-1). Neither collagenase nor gelatinase (A and B) activities in conditioned medium were affected by mechanical strain. Tissue inhibitor of metalloproteinase activities in conditioned medium remained unchanged during the 48-h intermittent mechanical stretching. These data suggest that an intermittent mechanical strain differentially regulates gene and protein expression of ECM molecules in fetal lung cells. The observed increase in matrix accumulation appears to be mainly a result of an increased synthesis of ECM molecules and not of decreasing activity of degradative enzymes. (+info)The macromolecular characteristics of cartilage proteoglycans do not change when synthesis is up-regulated by link protein peptide. (6/269)
Previous studies have shown that a synthetic, unglycosylated analogue of the N-terminal peptide from link protein can function as a growth factor and up-regulate proteoglycan biosynthesis in explant cultures of normal human articular cartilage from a wide age range of subjects (McKenna et al., Arthritis Rheum. 41 (1998) 157-162). The present work further shows that link peptide increased proteoglycan synthesis by cartilage cultured in both the presence and absence of serum, suggesting that the mechanism of up-regulation may be different from that of insulin-like growth factors. The proteoglycans synthesised during stimulation with link peptide were of normal hydrodynamic size and the ratio of core protein to glycosaminoglycan side chains and the proportions of the large proteoglycan aggrecan to the small proteoglycans, decorin and biglycan, remained constant. Aggrecan molecules were equally capable of forming aggregates as those from control tissues and the relative proportions of decorin and biglycan were unchanged showing that both were co-ordinately up-regulated. These results confirmed that this novel peptide is a potent stimulator of proteoglycan synthesis by articular cartilage and showed that the newly synthesised proteoglycans were of normal composition. (+info)External beam radiation after stent implantation increases neointimal hyperplasia by augmenting smooth muscle cell proliferation and extracellular matrix accumulation. (7/269)
OBJECTIVES: We sought to examine the effects of high volume external beam radiation (EBR) after stent implantation on neointimal hyperplasia, smooth muscle cell (SMC) proliferation, presence of inflammatory cells and expression of extracellular matrix (ECM). BACKGROUND: Endovascular irradiation has been shown to reduce restenosis rates after angioplasty in preliminary trials, but conflicting results have been reported for the effects of external beam irradiation. METHODS: Forty-three Palmaz-Schatz stents were implanted into iliac arteries of New Zealand White rabbits. The arteries were externally irradiated after stent implantation with a single dose of 8 Gy (at day 3) or 16 Gy in two fractions (8 Gy at days 3 and 4) by means of a linear accelerator. In the control rabbits, no radiation was applied after stent implantation. Smooth muscle cells, macrophages and ECM were studied by immunohistochemistry at one and 12 weeks after stent implantation. Collagen type I and biglycan messenger ribonucleic acid (mRNA) levels were assessed by Northern blot analysis at one week. Neointimal cell densities and arterial lumen stenosis were measured by histomorphometry at 12 weeks. RESULTS: At 1 week, SMC proliferation at the site of stent implantation was increased after EBR with 8 and 16 Gy (26 +/- 5%, 32 +/- 3% vs. 17 +/- 8%; p < 0.01, 16 Gy vs. control). External beam radiation with 8 and 16 Gy augmented SMC proliferation proximal and distal to the angioplasty site (11 +/- 3%, 14 +/- 3 vs. 6 +/- 1%; p < 0.01, 16 Gy vs. control). Collagen type I and biglycan mRNA levels were elevated in stented arteries after EBR with 16 Gy. At 12 weeks, a marked decrease in neointimal cell density (248 +/- 97 vs. 498 +/- 117 SMCs/0.1 mm2 neointima; p < 0.005 vs. control) was noted after EBR with 16 Gy. Irradiation with 8 and 16 Gy increased arterial lumen stenosis compared with nonirradiated control rabbits (45 +/- 7%, 55 +/- 9% vs. 33 +/- 7%; p < 0.05, 8 Gy and p < 0.001, 16 Gy vs. control). CONCLUSIONS: High volume external beam radiation at doses of 8 or 16 Gy causes restenosis by augmenting proliferative activity at and adjacent to the site of stent implantation, and by dose-dependent up-regulation of extracellular matrix expression. The study suggests that excessive matrix accumulation is an important determinant of failure of radiation therapy to prevent restenosis. (+info)Cyclic expression of mRNA transcripts for connective tissue components in the mouse ovary. (8/269)
In the ovary, differentiation of germinal cells into primordial follicles, functional ovulatory follicles and corpus luteum, all take place in a connective tissue matrix. We postulated that extracellular matrix (ECM) of the ovary participates actively in ovarian functions. To test this, the mRNA levels for several ECM components were determined in the mouse ovary at six distinct stages of the 4-day oestrous cycle. Northern analysis revealed statistically significant cyclic expression patterns for the mRNAs coding for type III, IV and VI collagens as well as for the small proteoglycan, biglycan, and for syndecan-1 and osteonectin. The cyclic changes observed in the mRNAs for these structural components exceeded those for matrix metalloproteinases (MMP)-2, -9 and -13, and for tissue inhibitors of matrix metalloproteinases (TIMP)-1, -2 and -3, where the changes were not statistically significant, despite their apparent role in ECM remodelling in the ovary. These observations support the hypothesis that cyclic changes in the production and degradation of ECM are part of normal ovarian function connected with follicular maturation, rupture and corpus luteum formation. (+info)Biglycan is a type of small leucine-rich proteoglycan (SLRP) that is found in the extracellular matrix of various tissues, including bone, cartilage, and tendons. It plays important roles in the organization and stabilization of the extracellular matrix, as well as in the regulation of cell behavior and signaling pathways.
Biglycan is composed of a core protein and one or more glycosaminoglycan (GAG) chains, which are long, unbranched polysaccharides made up of repeating disaccharide units. The GAG chains attach to the core protein via specific serine residues, forming a proteoglycan.
In addition to its structural roles, biglycan has been shown to interact with various growth factors and cytokines, modulating their activity and influencing cellular responses such as proliferation, differentiation, and migration. Dysregulation of biglycan expression or function has been implicated in several diseases, including osteoarthritis, cancer, and fibrosis.
Decorin is a small proteoglycan, a type of protein with a attached sugar chain, that is found in the extracellular matrix of connective tissues in the body. It is composed of a core protein and one or more glycosaminoglycan (GAG) chains, specifically dermatan sulfate. Decorin plays important roles in the organization and biomechanical properties of collagen fibrils, regulation of cell proliferation and migration, and modulation of growth factor activity. It has been studied for its potential role in various physiological and pathological processes, including wound healing, fibrosis, and cancer.
Extracellular matrix (ECM) proteins are a group of structural and functional molecules that provide support, organization, and regulation to the cells in tissues and organs. The ECM is composed of a complex network of proteins, glycoproteins, and carbohydrates that are secreted by the cells and deposited outside of them.
ECM proteins can be classified into several categories based on their structure and function, including:
1. Collagens: These are the most abundant ECM proteins and provide strength and stability to tissues. They form fibrils that can withstand high tensile forces.
2. Proteoglycans: These are complex molecules made up of a core protein and one or more glycosaminoglycan (GAG) chains. The GAG chains attract water, making proteoglycans important for maintaining tissue hydration and resilience.
3. Elastin: This is an elastic protein that allows tissues to stretch and recoil, such as in the lungs and blood vessels.
4. Fibronectins: These are large glycoproteins that bind to cells and ECM components, providing adhesion, migration, and signaling functions.
5. Laminins: These are large proteins found in basement membranes, which provide structural support for epithelial and endothelial cells.
6. Tenascins: These are large glycoproteins that modulate cell adhesion and migration, and regulate ECM assembly and remodeling.
Together, these ECM proteins create a microenvironment that influences cell behavior, differentiation, and function. Dysregulation of ECM proteins has been implicated in various diseases, including fibrosis, cancer, and degenerative disorders.
Proteoglycans are complex, highly negatively charged macromolecules that are composed of a core protein covalently linked to one or more glycosaminoglycan (GAG) chains. They are a major component of the extracellular matrix (ECM) and play crucial roles in various biological processes, including cell signaling, regulation of growth factor activity, and maintenance of tissue structure and function.
The GAG chains, which can vary in length and composition, are long, unbranched polysaccharides that are composed of repeating disaccharide units containing a hexuronic acid (either glucuronic or iduronic acid) and a hexosamine (either N-acetylglucosamine or N-acetylgalactosamine). These GAG chains can be sulfated to varying degrees, which contributes to the negative charge of proteoglycans.
Proteoglycans are classified into four major groups based on their core protein structure and GAG composition: heparan sulfate/heparin proteoglycans, chondroitin/dermatan sulfate proteoglycans, keratan sulfate proteoglycans, and hyaluronan-binding proteoglycans. Each group has distinct functions and is found in specific tissues and cell types.
In summary, proteoglycans are complex macromolecules composed of a core protein and one or more GAG chains that play important roles in the ECM and various biological processes, including cell signaling, growth factor regulation, and tissue structure maintenance.
Chondroitin sulfate proteoglycans (CSPGs) are complex molecules found in the extracellular matrix of various connective tissues, including cartilage. They are composed of a core protein covalently linked to one or more glycosaminoglycan (GAG) chains, such as chondroitin sulfate and dermatan sulfate.
CSPGs play important roles in the structure and function of tissues, including:
1. Regulating water content and providing resilience to tissues due to their high negative charge, which attracts cations and bound water molecules.
2. Interacting with other matrix components, such as collagen and elastin, to form a highly organized network that provides tensile strength and elasticity.
3. Modulating cell behavior by interacting with various growth factors, cytokines, and cell surface receptors, thereby influencing processes like cell adhesion, proliferation, differentiation, and migration.
4. Contributing to the maintenance of the extracellular matrix homeostasis through their involvement in matrix turnover and remodeling.
In articular cartilage, CSPGs are particularly abundant and contribute significantly to its load-bearing capacity and overall health. Dysregulation of CSPGs has been implicated in various pathological conditions, such as osteoarthritis, where altered proteoglycan composition and content can lead to cartilage degradation and joint dysfunction.
Versican is a type of proteoglycan, which is a complex protein molecule that contains one or more long sugar chains (glycosaminoglycans) attached to it. Proteoglycans are important components of the extracellular matrix (the material that provides structural support and regulates cell behavior in tissues and organs).
Versican is primarily found in the extracellular matrix of connective tissues, including skin, tendons, ligaments, and blood vessels. It plays a role in regulating cell adhesion, migration, and proliferation, as well as in maintaining the structural integrity of tissues. Versican has been implicated in various physiological and pathological processes, such as embryonic development, wound healing, inflammation, and cancer progression.
There are several isoforms of versican (V0, V1, V2, and V3) that differ in their structure and function, depending on the specific glycosaminoglycan chains attached to them. Abnormal expression or regulation of versican has been associated with various diseases, including cancer, fibrosis, and inflammatory disorders.
Collagen Type VI is a type of collagen that is widely expressed in various tissues, including skeletal muscle, skin, and blood vessels. It is a major component of the extracellular matrix and plays important roles in maintaining tissue structure and function. Collagen Type VI forms microfilaments that provide structural support to the basement membrane and regulate cell-matrix interactions. Mutations in the genes encoding collagen Type VI can lead to several inherited connective tissue disorders, such as Bethlem myopathy and Ullrich congenital muscular dystrophy.
Dermatan sulfate is a type of glycosaminoglycan, which is a long, unbranched sugar chain found on the proteoglycan core protein in the extracellular matrix of animal tissues. It is composed of repeating disaccharide units of iduronic acid and N-acetylgalactosamine, with alternating sulfation at the 4-position of the iduronic acid and the 6-position of the galactosamine.
Dermatan sulfate is found in various tissues, including skin, heart valves, and blood vessels, where it plays important roles in regulating cell behavior, tissue development, and homeostasis. It also binds to a variety of growth factors, cytokines, and enzymes, modulating their activities and contributing to the regulation of various biological processes.
Abnormalities in dermatan sulfate metabolism can lead to several genetic disorders, such as Hunter syndrome and Hurler-Scheie syndrome, which are characterized by skeletal abnormalities, cardiac defects, and neurological impairment.
Keratan sulfate is a type of glycosaminoglycan (GAG), which is a complex carbohydrate found in connective tissues, including the cornea and cartilage. It is composed of repeating disaccharide units of galactose and N-acetylglucosamine, with sulfate groups attached to some of the sugar molecules.
Keratan sulfate is unique among GAGs because it contains a high proportion of non-sulfated sugars and is often found covalently linked to proteins in structures called proteoglycans. In the cornea, keratan sulfate plays important roles in maintaining transparency and regulating hydration. In cartilage, it contributes to the elasticity and resilience of the tissue.
Abnormalities in keratan sulfate metabolism have been associated with several genetic disorders, including corneal dystrophies and skeletal dysplasias.
Aggrecan is a large, complex proteoglycan molecule found in the extracellular matrix of articular cartilage and other connective tissues. It is a key component of the structural framework of these tissues, helping to provide resiliency, cushioning, and protection to the cells within. Aggrecan contains numerous glycosaminoglycan (GAG) chains, which are negatively charged molecules that attract water and ions, creating a swelling pressure that contributes to the tissue's load-bearing capacity.
The medical definition of 'Aggrecans' can be described as:
1. A large proteoglycan molecule found in articular cartilage and other connective tissues.
2. Composed of a core protein with attached glycosaminoglycan (GAG) chains, primarily chondroitin sulfate and keratan sulfate.
3. Plays a crucial role in the biomechanical properties of articular cartilage by attracting water and ions, creating a swelling pressure that contributes to the tissue's load-bearing capacity.
4. Aggrecan degradation or loss is associated with various joint diseases, such as osteoarthritis, due to reduced structural integrity and shock-absorbing capabilities of articular cartilage.
Glycosaminoglycans (GAGs) are long, unbranched polysaccharides composed of repeating disaccharide units. They are a major component of the extracellular matrix and connective tissues in the body. GAGs are negatively charged due to the presence of sulfate and carboxyl groups, which allows them to attract positively charged ions and water molecules, contributing to their ability to retain moisture and maintain tissue hydration and elasticity.
GAGs can be categorized into four main groups: heparin/heparan sulfate, chondroitin sulfate/dermatan sulfate, keratan sulfate, and hyaluronic acid. These different types of GAGs have varying structures and functions in the body, including roles in cell signaling, inflammation, and protection against enzymatic degradation.
Heparin is a highly sulfated form of heparan sulfate that is found in mast cells and has anticoagulant properties. Chondroitin sulfate and dermatan sulfate are commonly found in cartilage and contribute to its resiliency and ability to withstand compressive forces. Keratan sulfate is found in corneas, cartilage, and bone, where it plays a role in maintaining the structure and function of these tissues. Hyaluronic acid is a large, nonsulfated GAG that is widely distributed throughout the body, including in synovial fluid, where it provides lubrication and shock absorption for joints.
The extracellular matrix (ECM) is a complex network of biomolecules that provides structural and biochemical support to cells in tissues and organs. It is composed of various proteins, glycoproteins, and polysaccharides, such as collagens, elastin, fibronectin, laminin, and proteoglycans. The ECM plays crucial roles in maintaining tissue architecture, regulating cell behavior, and facilitating communication between cells. It provides a scaffold for cell attachment, migration, and differentiation, and helps to maintain the structural integrity of tissues by resisting mechanical stresses. Additionally, the ECM contains various growth factors, cytokines, and chemokines that can influence cellular processes such as proliferation, survival, and differentiation. Overall, the extracellular matrix is essential for the normal functioning of tissues and organs, and its dysregulation can contribute to various pathological conditions, including fibrosis, cancer, and degenerative diseases.
Chondroitin ABC lyase, also known as chondroitinase ABC or chondroitin sulfate eliminase, is an enzyme that breaks down chondroitin sulfate proteoglycans (CSPGs), which are major components of the extracellular matrix in various tissues including cartilage. CSPGs contain chondroitin sulfate chains, which are long, negatively charged polysaccharides composed of alternating sugars (N-acetylgalactosamine and glucuronic acid) with sulfate groups attached at specific positions.
Chondroitin ABC lyase cleaves chondroitin sulfate chains by removing a disaccharide unit from the polymer, resulting in the formation of unsaturated bonds between the remaining sugars. This enzymatic activity has been used in research to study the structure and function of CSPGs and their role in various biological processes, such as cell migration, tissue repair, and neural plasticity. Additionally, chondroitin ABC lyase has potential therapeutic applications for treating conditions associated with excessive accumulation of CSPGs, such as fibrosis and some neurological disorders.
An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.
Analytical chemistry is a branch of chemistry that focuses on the identification and quantification of chemical components within a sample. This field involves developing and using various analytical techniques and methods to determine the presence, concentration, structure, and purity of different chemicals or compounds in a mixture.
Some common analytical techniques include:
1. Spectroscopy: Using light or other electromagnetic radiation to study the interaction between matter and energy, providing information about the composition, structure, and properties of a sample. Examples include UV-Vis, IR, NMR, and mass spectrometry.
2. Chromatography: A separation technique that separates components in a mixture based on their interactions with a mobile phase (gas or liquid) and a stationary phase (solid or liquid). Common methods include gas chromatography (GC), liquid chromatography (LC), and thin-layer chromatography (TLC).
3. Electrochemical analysis: Measuring the electrical properties of a sample, such as potential, current, or resistance, to determine its composition or concentration. Examples include potentiometry, voltammetry, and conductometry.
4. Thermal analysis: Examining the physical and chemical changes that occur in a sample when it is heated or cooled, providing information about its composition, structure, and properties. Techniques include differential scanning calorimetry (DSC), thermogravimetric analysis (TGA), and dynamic mechanical analysis (DMA).
5. Spectrometry: Measuring the intensity of light dispersed by a sample as a function of wavelength or frequency to determine its composition, structure, or properties. Examples include atomic absorption spectroscopy (AAS), inductively coupled plasma mass spectrometry (ICP-MS), and X-ray fluorescence spectrometry (XRF).
Analytical chemists often work in various industries, such as pharmaceuticals, food, environmental testing, and forensics, to ensure product quality, safety, and compliance with regulations. They may also contribute to research and development efforts by developing new analytical methods or improving existing ones.
Biglycan
Proteoglycan
WNT1-inducible-signaling pathway protein 1
Fibromodulin
SGCA
TWSG1
Decorin
SGCG
JPH3
TGFBR3
Transforming growth factor, beta 3
TGF beta 1
TGF beta 2
Asporin
ZBTB7B
PLA2G1B
Versican
Ancient protein
MFAP2
Osteoglycin
Lumican
Skin
Marian Young
B4GALT7
BGN
Matrilin-3
Underworld: Rise of the Lycans
Biglycan - Wikipedia
Biglycan (Cytokines & Cells Encyclopedia - COPE)
Rat BGN(Biglycan) ELISA Kit - iBiomagazine
Mouse Biglycan (BGN) ELISA Kit - Doron Scientific
Degradation of small leucine-rich repeat proteoglycans by matrix metalloprotease-13: identification of a new biglycan cleavage...
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Molecular modelling study of the 3D structure of the biglycan core protein, using homology modelling techniques | Vlachakis |...
Evaluation of a 4-protein serum biomarker panel-biglycan, annexin-A6, myeloperoxidase, and protein S100-A9 (B-AMP)-for the...
Novel Regulatory Mechanisms for the Proteoglycans Decorin and Biglycan During Muscle Formation and Muscular Dystrophy. Matrix...
SGCA - Wikipedia
Distinct epigenetic programs regulate cardiac myocyte development and disease in the human heart in vivo | Nature Communications
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Effects of cleavage by a disintegrin and metalloproteinase with thrombospondin motifs-4 on gene expression and protein content...
Tendinopathy--from basic science to treatment
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Inhibition of the renin-angiotensin system causes concentric hypertrophy of renal arterioles in mice and humans
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SMART: LRR domain annotation
Mouse Serum Amyloid A1/A2 Antibody AF2948: R&D Systems
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Decorin11
- The composition of GAG chains of biglycan and decorin originating from the same tissue has been reported to be similar. (wikipedia.org)
- It has been reported that biglycan interacts more strongly with collagen type II than collagen type I. Biglycan has been reported to compete with decorin for the same binding site on collagen. (wikipedia.org)
- Novel Regulatory Mechanisms for the Proteoglycans Decorin and Biglycan During Muscle Formation and Muscular Dystrophy. (cienciavida.org)
- In this study, we report a novel antimicrobial role played by SLRPs biglycan, decorin, fibromodulin and osteoadherin, specifically in promoting the eradication of S. pyogenes in a human sepsis model of infection. (lu.se)
- Biglycan and decorin induce TLR2 and TLR4 signaling cascades resulting in secretion of proinflammatory and chemotactic molecules and recruitment of professional phagocytes. (lu.se)
- Decorin and biglycan are two small leucine-rich proteoglycans (SLRPs) that regulate collagen fibrillogenesis and extracellular matrix assembly in tendon. (allergy-link.com)
- We hypothesized that knockdown of decorin in mature tendons would result in detrimental changes to tendon structure and mechanics while knockdown of biglycan would have a minor effect on these parameters. (allergy-link.com)
- To achieve this objective, we created tamoxifen-inducible mouse knockdown models targeting decorin or biglycan inactivation. (allergy-link.com)
- Contrary to our hypothesis, knockdown of decorin resulted in minor alterations to tendon structure and no changes to mechanics while knockdown of biglycan resulted in broad changes to tendon structure and mechanics. (allergy-link.com)
- Knockdown of decorin and biglycan produced similar changes to tendon microstructure by increasing the collagen fibril diameter relative to wild-type controls. (allergy-link.com)
- Overall, the extensive changes to tendon structure and mechanics after knockout of biglycan, but not decorin, provides evidence that biglycan plays a major role in the maintenance of tendon structure and mechanics in mature mice during homeostasis. (allergy-link.com)
Leucine-rich r2
- Biglycan is a small leucine-rich repeat proteoglycan (SLRP) which is found in a variety of extracellular matrix tissues, including bone, cartilage and tendon. (wikipedia.org)
- formerly it was known as proteoglycan-I (PG-I). Biglycan consists of a protein core containing leucine-rich repeat regions and two glycosaminoglycan (GAG) chains consisting of either chondroitin sulfate (CS) or dermatan sulfate (DS), with DS being more abundant in most connective tissues. (wikipedia.org)
Proteoglycan1
- Biglycan is a particularly important proteoglycan for binding to lipoprotein in human blood vessels, thus being a significant cause of atherosclerosis. (wikipedia.org)
Evidence that biglycan1
- There is also evidence that biglycan binds to TGF-beta 1. (wikipedia.org)
Proteoglycans2
ELISA Kit1
- Description: A sandwich ELISA kit for detection of Biglycan from Rat in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (ibiomagazine.org)
Proteins2
- over 90% homology has been reported for rat, mouse, bovine and human biglycan core proteins. (wikipedia.org)
- We noticed a reduction of particular plasma and muscle proteins with increasing PMIs, as well as an increased deamidation of biglycan, a protein with a role in modulating bone growth and mineralization. (northumbria.ac.uk)
Protein8
- Biglycan core protein binds to the growth factors BMP-4 and influences its bioactivity. (wikipedia.org)
- Biglycan interacts with collagen, both via the core protein and GAG chains. (wikipedia.org)
- Human Recombinant Biglycan, also called as TVN-102, is a small, naturally occurring extracellular matrix protein found in muscle. (kuickresearch.com)
- It was found that the final model of biglycan resembles in structure its template protein bearing a set of distinct parallel β-sheet structure patterns. (jmolbiochem.com)
- Overall comparison of the model of biglycan to the recently determined x-ray structure of the same protein returns a very low Root Mean Square Deviation (RMSD), which confirms the viability of the model and its reliability as a platform for the study biglycan interactions. (jmolbiochem.com)
- The authors present results from the development of a serum-based, 4-protein (biglycan, myeloperoxidase, annexin-A6, and protein S100-A9) biomarker panel for EAC. (usuhs.edu)
- The authors present results from the development of a serum-based, 4-protein (biglycan, myeloperoxidase, annexin-A6, and protein S100-A9) biomarker panel for EAC.METHODS: A vertically integrated, proteomics-based biomarker discovery approach was used to identify candidate serum biomarkers for the detection of EAC. (usuhs.edu)
- ADAMTS-5 activity induced the release of ADAMTS-specific versican (DPEAAE(441)) and aggrecan ((374)ALGS) fragments as well as biglycan and link protein from the aortic wall. (ox.ac.uk)
SGCA1
- Biglycan has been shown to interact with SGCA. (wikipedia.org)
Aggrecan1
- Major molecular changes include increased expression of type III collagen, fibronectin, tenascin C, aggrecan and biglycan. (nih.gov)
Collagen1
- Specifically, knockdown of biglycan resulted in reduced insertion modulus, maximum stress, dynamic modulus, stress relaxation, and increased collagen fiber realignment during loading. (allergy-link.com)
Serum2
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Biglycan (BGN) in serum, plasma, tissue homogenates and other biological fluids. (ibiomagazine.org)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Rat Biglycan (BGN) in samples from serum, plasma, tissue homogenates and other biological fluids with no significant corss-reactivity with analogues from other species. (ibiomagazine.org)
Gene3
- In humans, biglycan is encoded by the BGN gene which is located on the X chromosome. (wikipedia.org)
- Knock-out mice that have had the gene for biglycan suppressed (Bgn -/-) have an osteoporosis-like phenotype with reduced growth rate and lower bone mass than mice that can express biglycan. (wikipedia.org)
- Biglycan is highly expressed in tumor stroma, associated with angiogenesis gene expression and prognosis of human breast cancer patients. (biomedcentral.com)
Symbol1
- biglycan [Source:HGNC Symbol;Acc:HGNC. (gsea-msigdb.org)
Amino2
- The CS/DS chains are attached at amino acids 5 and 10 in human biglycan. (wikipedia.org)
- The biglycan model bears a very hydrophobic amino acid region towards its inner cavity that acquires an arc-like structure. (jmolbiochem.com)
Bone1
- Biglycan is believed to play a role in the mineralization of bone. (wikipedia.org)
Tissue1
- a Comparison of biglycan mRNA expression was analyzed in normal mammary glands ( n = 61) and breast cancer tissue ( n = 389) using Oncomine. (biomedcentral.com)
Survival1
- c Kaplan-Meier analysis was used to assess breast cancer patients with high or low biglycan mRNA expression in distant metastasis-free survival (DMFS) using a Kaplan-Meier plotter tool. (biomedcentral.com)
Human3
- Non-glycanated forms of biglycan (no GAG chains) increase with age in human articular cartilage. (wikipedia.org)
- Tivorsan pharmaceutical, a company focusing on developing drugs and treatments for all kinds of Duchenne Muscular Dystrophy (DMD) and other neuromuscular disorders, declared that food and Drug Association (FDA) has granted Orphan drug designation to its leading drug candidate, Human Recombinant Biglycan for the treatment of DMD. (kuickresearch.com)
- Importantly, ADAMTS-5 proteolytic activity reduced the LDL binding ability of biglycan and released LDL from human aortic lesions. (ox.ac.uk)
Comparison1
- b Comparison of biglycan mRNA expression was analyzed in 14 patient-matched tumor epithelium and tumor-associated stroma specimens using Oncomine. (biomedcentral.com)
