Aggrecans
Hyalin
Keratan Sulfate
A sulfated mucopolysaccharide initially isolated from bovine cornea. At least two types are known. Type I, found mostly in the cornea, contains D-galactose and D-glucosamine-6-O-sulfate as the repeating unit; type II, found in skeletal tissues, contains D-galactose and D-galactosamine-6-O-sulfate as the repeating unit.
Extracellular Matrix Proteins
Macromolecular organic compounds that contain carbon, hydrogen, oxygen, nitrogen, and usually, sulfur. These macromolecules (proteins) form an intricate meshwork in which cells are embedded to construct tissues. Variations in the relative types of macromolecules and their organization determine the type of extracellular matrix, each adapted to the functional requirements of the tissue. The two main classes of macromolecules that form the extracellular matrix are: glycosaminoglycans, usually linked to proteins (proteoglycans), and fibrous proteins (e.g., COLLAGEN; ELASTIN; FIBRONECTINS; and LAMININ).
Lectins, C-Type
Chondroitin Sulfates
Derivatives of chondroitin which have a sulfate moiety esterified to the galactosamine moiety of chondroitin. Chondroitin sulfate A, or chondroitin 4-sulfate, and chondroitin sulfate C, or chondroitin 6-sulfate, have the sulfate esterified in the 4- and 6-positions, respectively. Chondroitin sulfate B (beta heparin; DERMATAN SULFATE) is a misnomer and this compound is not a true chondroitin sulfate.
Cartilage, Articular
Hoof and Claw
Procollagen N-Endopeptidase
An extracellular endopeptidase which excises a block of peptides at the amino terminal, nonhelical region of the procollagen molecule with the formation of collagen. Absence or deficiency of the enzyme causes accumulation of procollagen which results in the inherited connective tissue disorder--dermatosparaxis. EC 3.4.24.14.
ADAM Proteins
Chondroitin Sulfate Proteoglycans
Encyclopedias as Topic
Glycosaminoglycans
Hyaluronic Acid
Joints
Chondroitin
Sequence Analysis, DNA
Mesenchymal Stromal Cells
Bone-marrow-derived, non-hematopoietic cells that support HEMATOPOETIC STEM CELLS. They have also been isolated from other organs and tissues such as UMBILICAL CORD BLOOD, umbilical vein subendothelium, and WHARTON JELLY. These cells are considered to be a source of multipotent stem cells because they include subpopulations of mesenchymal stem cells.
Chondrogenesis
Mesenchymal Stem Cell Transplantation
Bone Marrow Cells
Cell Differentiation
Orthotic Devices
Andorra
Osteoarthritis
A progressive, degenerative joint disease, the most common form of arthritis, especially in older persons. The disease is thought to result not from the aging process but from biochemical changes and biomechanical stresses affecting articular cartilage. In the foreign literature it is often called osteoarthrosis deformans.
Osteoarthritis, Knee
Noninflammatory degenerative disease of the knee joint consisting of three large categories: conditions that block normal synchronous movement, conditions that produce abnormal pathways of motion, and conditions that cause stress concentration resulting in changes to articular cartilage. (Crenshaw, Campbell's Operative Orthopaedics, 8th ed, p2019)
Association of the aggrecan keratan sulfate-rich region with collagen in bovine articular cartilage. (1/821)
Aggrecan, the predominant large proteoglycan of cartilage, is a multidomain macromolecule with each domain contributing specific functional properties. One of the domains contains the majority of the keratan sulfate (KS) chain substituents and a protein segment with a proline-rich hexapeptide repeat sequence. The function of this domain is unknown but the primary structure suggests a potential for binding to collagen fibrils. We have examined binding of aggrecan fragments encompassing the KS-rich region in a solid-phase assay. A moderate affinity (apparent Kd = 1.1 microM) for isolated collagen II, as well as collagen I, was demonstrated. Enzymatic digestion of the KS chains did not alter the capacity of the peptide to bind to collagen, whereas cleavage of the protein core abolished the interaction. The distribution of the aggrecan KS-rich region in bovine tarsometatarsal joint cartilage was investigated using immunoelectron microscopy. Immunoreactivity was relatively low in the superficial zone and higher in the intermediate and deep zones of the uncalcified cartilage. Within the pericellular and territorial matrix compartments the epitopes representing the aggrecan KS-rich region were detected preferentially near or at collagen fibrils. Along the fibrils, epitope reactivity was non-randomly distributed, showing preference for the gap region within the D-period. Our data suggest that collagen fibrils interact with the KS-rich regions of several aggrecan monomers aligned within a proteoglycan aggregate. The fibril could therefore serve as a backbone in at least some of the aggrecan complexes. (+info)Fatty acids modulate the composition of extracellular matrix in cultured human arterial smooth muscle cells by altering the expression of genes for proteoglycan core proteins. (2/821)
In diabetes-associated microangiopathies and atherosclerosis, there are alterations of the extracellular matrix (ECM) in the intima of small and large arteries. High levels of circulating nonesterified fatty acids (NEFAs) are present in insulin resistance and type 2 diabetes. High concentrations of NEFAs might alter the basement membrane composition of endothelial cells. In arteries, smooth muscle cells (SMCs) are the major producers of proteoglycans and glycoproteins in the intima, and this is the site of lipoprotein deposition and modification, key events in atherogenesis. We found that exposure of human arterial SMCs to 100-300 micromol/albumin-bound linoleic acid lowered their proliferation rate and altered cell morphology. SMCs expressed 2-10 times more mRNA for the core proteins of the proteoglycans versican, decorin, and syndecan 4 compared with control cells. There was no change in expression of fibronectin and perlecan. The decorin glycosaminoglycan chains increased in size after exposure to linoleic acid. The ECM produced by cells grown in the presence of linoleic acid bound 125I-labeled LDL more tightly than that of control cells. Darglitazone, a peroxisome proliferator-activated receptor (PPAR)-gamma ligand, neutralized the NEFA-mediated induction of the decorin gene. This suggests that some of the NEFA effects are mediated by PPAR-gamma. These actions of NEFAs, if present in vivo, could contribute to changes of the matrix of the arterial intima associated with micro- and macroangiopathies. (+info)Immune responses to cartilage link protein and the G1 domain of proteoglycan aggrecan in patients with osteoarthritis. (3/821)
OBJECTIVE: To determine whether patients with osteoarthritis (OA) express cellular immunity to cartilage link protein (LP) and the G1 globular domain of proteoglycan (PG) aggrecan, and whether immunity to the G1 domain is influenced by the removal of keratan sulfate (KS). METHODS: LP and the G1 globular domain of PG were isolated from human and/or bovine cartilage and used in proliferation assays with peripheral blood lymphocytes (PBL) from 42 patients with OA and 40 healthy control subjects. RESULTS: Patients with OA expressed a higher prevalence of cellular immunity to human cartilage LP (42.4%) compared with the control group (13.3%). The prevalence of immune reactivity to bovine LP in patients with OA was lower (35.7%) compared with the immunity to human LP, but remained similar in the control group (13.8%). PBL from patients with OA exhibited low reactivity to the native G1 domain of bovine PG. However, removal of KS chains from the G1 globular domain resulted in increased cellular immune responses to the G1 domain in OA patients (45.8%) compared with the control group (7.7%). CONCLUSION: These results indicate the presence of immunity to cartilage-derived LP and the G1 globular domain of PG aggrecan in patients with OA and the inhibitory effect of KS chains on the G1 domain on the expression of this immunity in OA patients. This immune reactivity is commonly observed in patients with inflammatory joint disease and can experimentally induce arthritis. Thus, it may be involved in the pathogenesis of OA. (+info)Changes in joint cartilage aggrecan after knee injury and in osteoarthritis. (4/821)
OBJECTIVE: To determine the concentrations of aggrecan fragments in synovial fluid from patients with knee joint injury, osteoarthritis (OA), or acute pyrophosphate arthritis (PPA; pseudogout), and to test their relative reactivity with the 846 epitope, a putative marker of cartilage aggrecan synthesis. METHODS: Samples of knee joint fluid from 385 patients and 9 healthy-knee volunteers were obtained in a cross-sectional study. Study groups were acute PPA/ pseudogout (n = 60), anterior cruciate ligament (ACL) rupture (n = 159), meniscus lesion (n = 129), and primary knee OA (n = 37). The 846 epitope on aggrecan was assayed by competitive solution-phase radioimmunoassay. Aggrecan fragments were assayed by enzyme-linked immunosorbent assay using a monoclonal antibody (1-F21). Cartilage oligomeric matrix protein (COMP), C-propeptide of type II collagen (CPII), bone sialoprotein, matrix metalloproteinases 1 and 3, and tissue inhibitor of metalloproteinases 1 were previously quantified by immunoassays. RESULTS: Reactivity of the 846 epitope was increased in all study groups compared with the reference group, and was highest in patients with primary OA. The median levels (in microg fetal aggrecan equivalents/ml) of the epitope were 0.28 (range 0.24-0.47) in the reference group, 0.48 (range 0.26-1.32) in PPA/pseudogout, 0.61 (range 0.12-2.87) in ACL rupture, 0.53 (range 0.22-3.02) in meniscus lesion, and 0.68 (range 0.31-4.31) in primary OA. The 846 epitope reactivity per microg aggrecan fragments in the joint fluid was higher in late-stage OA than in early-stage OA. Epitope 846 reactivity correlated positively with several markers of matrix turnover, particularly with COMP (r(s) = 0.421) and CPII (r(s) = 0.307). CONCLUSION: The observed differences in 846 epitope reactivity in synovial fluid, and its concentration in relation to aggrecan and other markers of matrix turnover, were consistent with marked ongoing changes in aggrecan turnover after joint injury and in the development of OA. OA is thus a disease characterized by dynamic changes in tissue macromolecule turnover, which is reflected by measurable changes in aggrecan epitopes in the synovial fluid. (+info)Longitudinal and cross-sectional variability in markers of joint metabolism in patients with knee pain and articular cartilage abnormalities. (5/821)
OBJECTIVE: To determine the within- and between-patient variability in the concentrations of synovial fluid, serum and urine markers of joint tissue metabolism in a cohort of patients with knee pain and cartilage changes consistent with early-stage knee osteoarthritis. DESIGN: Samples of synovial fluid, serum, and urine were obtained from 52 patients on eight different occasions during 1 year, as part of a clinical trial in patients with cartilage abnormalities and knee pain. In joint fluid, aggrecan fragments were quantified by dye precipitation and enzyme-linked immunosorbent assay (ELISA), and matrix metalloproteinases-1 and -3, and tissue inhibitor of metalloproteinases-1 by sandwich ELISAs. In serum, keratan sulfate was quantified by ELISA. Type I collagen N-telopeptide cross-links in urine were determined by ELISA. RESULTS: The degree of cross-sectional variability in marker concentrations did not vary between the different sampling occasions, and did not differ between the periods of weeks 0 (baseline), 1-4 (treatment) and 13-26 (follow-up). Both between-patient and within-patient coefficients of variation varied for markers in different body fluid compartments, with the lowest variability for serum keratan sulfate, followed by urine type I collagen N-telopeptide crosslinks, and the highest for synovial fluid markers. For synovial fluid, aggrecan fragments showed the least variability, and matrix metalloproteinases the highest. One patient with septic arthritis showed a fivefold peak increase in joint fluid aggrecan fragment concentrations, while the concentration of matrix metalloproteinase-3 increased 100-fold. CONCLUSIONS: Molecular markers of joint tissue metabolism have been suggested as, for example, outcome measures for clinical trials of disease-modifying drugs in osteoarthritis. This report is the first to present data on between- and within-patient variability for such molecular markers in three different body fluid compartments in stable cohort of patients. The availability of such data enables calculations to determine the number of patients needed in prospective studies using these markers as outcome measures. (+info)Resistance of small leucine-rich repeat proteoglycans to proteolytic degradation during interleukin-1-stimulated cartilage catabolism. (6/821)
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)Alcohol promotes in vitro chondrogenesis in embryonic facial mesenchyme. (7/821)
Ethanol is a well-recognized teratogen in vertebrates that can perturb the development of the facial primordia and various other embryonic structures. However,the mechanisms underlying alcohol's effects on embryogenesis are currently unclear. Recent evidence suggests that the cranial neural crest, which forms the entire facial skeleton, may be a particularly sensitive target of ethanol teratogenicity. In the present study we have examined the influence of in vitro ethanol exposure on cartilage differentiation in micromass cultures of mesenchymal cells isolated from the various facial primordia (maxillary, mandibular, frontonasal, and hyoid processes) of the stage 24 chick embryo. In all four populations of facial mesenchyme, exposure to 1-1.5% ethanol promoted marked increases in Alcian blue-positive cartilage matrix formation, a rise in 35SO4 accumulation into matrix glycosaminoglycans, and enhanced expression of cartilage-characteristic type II collagen and aggrecan gene transcripts. In frontonasal and mandibular mesenchyme cultures, which undergo extensive spontaneous cartilage formation, ethanol treatment quantitatively elevated both matrix production and cartilage-specific gene transcript expression. In cultures of maxillary process and hyoid arch mesenchyme, which form little or no cartilage spontaneously, ethanol exposure induced the formation of chondrogenic cell aggregates and the appearance of aggrecan and type II collagen mRNAs. These actions were not restricted to ethanol, since tertiary butanol treatment also enhanced cartilage differentiation in facial mesenchyme cultures. Our findings demonstrate a potent stimulatory effect of alcohol on the differentiation of prechondrogenic mesenchyme of the facial primordia. Further analysis of this phenomenon might yield insight into the developmental mechanisms underlying the facial dysmorphologies associated with embryonic ethanol exposure. (+info)The early molecular natural history of experimental osteoarthritis. I. Progressive discoordinate expression of aggrecan and type II procollagen messenger RNA in the articular cartilage of adult animals. (8/821)
OBJECTIVE: To quantify changes in the chondrocyte metabolism of aggrecan core protein and type II procollagen messenger RNA (mRNA) during the early and middle phases of experimental osteoarthritis (OA) in animals. METHODS: Experimental OA was induced by transecting the cranial cruciate ligament of the stifle joint in adult animals; articular cartilage was harvested and analyzed after 4, 10, and 32 weeks. RESULTS: Northern blot analysis revealed no change in aggrecan mRNA 4 weeks after surgery compared with aggrecan mRNA in the unoperated contralateral control joints; aggrecan mRNA levels became significantly elevated by 10 and 32 weeks after surgery. In OA cartilage, type II procollagen mRNA was dramatically and progressively elevated at all times after surgery. The relative increases in type II procollagen mRNA exceeded the relative increases in aggrecan mRNA at all times after surgery, and these differences increased progressively over time. Articular chondrocytes became activated globally (total RNA increases) and specifically (mRNA increase) early after joint injury and remained activated throughout the early and middle phases of this experimental OA. CONCLUSION: The early natural history of experimental OA is characterized by a progressive imbalance in the mRNA expression of aggrecan and type II procollagen in articular chondrocytes. These results suggest that the stimuli for the transcription of these 2 genes are fundamentally different in this animal model. (+info)
Blocking aggrecanase cleavage in the aggrecan interglobular domain abrogates cartilage erosion and promotes cartilage repair ...
JCI -
Blocking aggrecanase cleavage in the aggrecan interglobular domain abrogates cartilage erosion and promotes cartilage...
T-cell recognition of differentially tolerated epitopes of cartilage proteoglycan aggrecan in arthritis<...
Apolipoprotein A-1 is a novel inducer of aggrecan breakdown in cultured articular cartilage - ORA - Oxford University Research...
Aggrecan Neoepitope Antibody [DyLight 650] (NB100-74350C): Novus Biologicals
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An ARGS-aggrecan assay for analysis in blood and synovial fluid - Danish National Research Database-Den Danske...
Engineering of tissue inhibitor of metalloproteinases mutants as potential therapeutics | Arthritis Research & Therapy | Full...
Aggrecan Antibody, N-terminal neoepitope ARG, 100 ug - MD Bioproducts
Dipen - Drugs.com
Identifying synovial tissue-derived catabolic factors of cartilage aggrecan
Rat Aggrecan (AGC) ELISA Kit - DL-AGC-Ra-96 DLdevelop - Antibody-An...
Gentaur Molecular :Kamiya \ Aggrecan Clone 3C7 \ MC-1003
ACAN Gene - GeneCards | PGCA Protein | PGCA Antibody
Extracts of normal mature articular cartilage contain aggrecan molecules which bear
Studies of the articular cartilage proteoglycan aggrecan in health and osteoarthritis. Evidence for molecular heterogeneity and...
ADAMTS4 (aggrecanase-1) interaction with the C-terminal domain of fibronectin inhibits proteolysis of aggrecan<...
ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan<...
TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5). - The Kennedy Institute of Rheumatology
archive-com.com: cell-research.com - Cell Research
Antibody-based exosite inhibitors of ADAMTS-5 (aggrecanase-2).
Conference Contribution | Dipen Shah®
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Aggrecans | Profiles RNS
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Characterization and localization of citrullinated proteoglycan aggrecan in human articular cartilage<...
heparan sulfate proteoglycan core protein - oi
T Cell Cytokine Responses to Cartilage Aggrecan in BALB/c Mice | Biochemical Society Transactions
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Versican - Wikipedia
Zonal responsiveness of the human intervertebral disc to bone morphogenetic protein-2<...
Perineuronal net formation and structure in aggrecan knockout mice | Read by QxMD
Dysregulated miR-98-5p contributes to excessive apoptosis of nucleus pulposus cells by BMP2 in human intervertebral disc...
Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications. -...
Hyaluronic acid - Wikipedia
socket.rb\lib\socket\ext - ruby.git - The Ruby Programming Language
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Aggrecan
Proteases capable of degrading aggrecans are called aggrecanases, and they are members of the ADAM (A Disintegrin And ... Nap RJ, Szleifer I (November 2008). "Structure and interactions of aggrecans: statistical thermodynamic approach". Biophys. J. ...
Aggrecanase
... s act on large proteoglycans known as aggrecans, which are components of connective tissues such as cartilage. The ...
Aggrecans | Profiles RNS
"Aggrecans" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... This graph shows the total number of publications written about "Aggrecans" by people in this website by year, and whether " ... Below are the most recent publications written about "Aggrecans" by people in Profiles. ...
A proteomic analysis of adult rat bone reveals the presence of cartilage/chondrocyte markers
Proteoglycan aggrecan-induced arthritis: a murine autoimmune model of rheumatoid arthritis
MEDLINE - Resultado p gina 1
MEDLINE - Resultado p gina 1
Cartilage Bones Joints Flashcards by Jason Hsu | Brainscape
Julie Glowacki, Ph.D. | Harvard Catalyst Profiles | Harvard Catalyst
Aggrecan - Wikipedia
Brevican
Summary Report | CureHunter
Triflex - GNC Joint Product - ProgressiveHealth.com
Aggrecanase - Wikipedia
Emerging Treatments for OA: New Therapies Target Joint Pain, Not Just Structural Damage - The Rheumatologist
Identification of two novel mutations in the COMP gene in six families with pseudoachondroplasia
In vitro chondrogenesis of bone marrow-derived mesenchymal stem cells in a photopolymerizing hydrogel<...
TY - JOUR. T1 - In vitro chondrogenesis of bone marrow-derived mesenchymal stem cells in a photopolymerizing hydrogel. AU - Williams, Christopher G.. AU - Kim, Tae Kyun. AU - Taboas, Anya. AU - Malik, Athar. AU - Manson, Paul. AU - Elisseeff, Jennifer Hartt. PY - 2003/8. Y1 - 2003/8. N2 - Mesenchymal stem cells (MSCS) from skeletally mature goats were encapsulated in a photopolymerizing poly(ethylene glycol)-based hydrogel and cultured with or without transforming growth factor β1 (TGF) to study the potential for chondrogenesis in a hydrogel scaffold system amenable to minimally invasive implantation. Chondrogenic differentiation was evaluated by histological, biochemical, and RNA analyses for the expression of cartilage extracellular matrix components. The two control groups studied were MSCs cultured in monolayer and MSCs encapsulated in the hydrogel and cultured for 6 weeks in chondrogenic medium without TGF-β1 (6wk-TGF). The three experimental time points for encapsulated cells studied ...
US20010014475A1 - Method for fabricating cell-containing implants
- Google Patents
Culture of chondrocytes in alginate surrounded by fibrin gel: characteristics of the cells over a period of eight weeks |...
Positive cells in the surrounding fibrin gel appeared at two weeks (fig 4B). At this time aggrecans were mainly seen in the ... A major portion of the aggrecans diffused into the medium in the 0.5% alginate cultures at two weeks. The diffusion of newly ... The maintenance of the alginate gel with newly synthesised aggrecans in the CAM and in the ITM could be seen in paraffin ... However, the lower the alginate content in the beads the more newly synthesised aggrecans escaped from the gel, and this 35S ...
WikiGenes - Acan - aggrecan
Full text] New developments in the treatment of osteoarthritis - focus on b | OARRR
Recent studies support the promise of using lubricin as a therapy for OA.6 Aggrecans are formed by a core protein which is ... Other proteins include noncollagenous, aggrecans, leucine-rich repeated, structural, regulatory, and others (Table 1, Figures 1 ... MMP-13 being the most involved in cleaving type II collagen and aggrecans and MMP-7 as an early predictor of OA, as much as 10 ... 47 It has been proven that IL-10 is involved in stimulating the synthesis of type II collagen and aggrecans and decreases TNFα ...
https://www.thefreelibrary.com/The+effects+of+closed+kinetic+chain+exercise+on+articular+cartilage...-a0455988801
A hyaluronic acid binding peptide-polymer system for treating osteoarthritis<...
TY - JOUR. T1 - A hyaluronic acid binding peptide-polymer system for treating osteoarthritis. AU - Faust, Heather J.. AU - Sommerfeld, Sven D.. AU - Rathod, Sona. AU - Rittenbach, Andrew. AU - Ray, Sangeeta. AU - Tsui, Benjamin. AU - Pomper, Martin Gilbert. AU - Amzel, Mario L. AU - Singh, Anirudha. AU - Elisseeff, Jennifer Hartt. PY - 2018/11/1. Y1 - 2018/11/1. N2 - Hyaluronic acid (HA) is found naturally in synovial fluid and is utilized therapeutically to treat osteoarthritis (OA). Here, we employed a peptide-polymer cartilage coating platform to localize HA to the cartilage surface for the purpose of treating post traumatic osteoarthritis. The objective of this study was to increase efficacy of the peptide-polymer platform in reducing OA progression in a mouse model of post-traumatic OA without exogenous HA supplementation. The peptide-polymer is composed of an HA-binding peptide (HABP) conjugated to a heterobifunctional poly (ethylene glycol) (PEG) chain and a collagen binding peptide ...
Osteo Sport from Applied Nutriceuticals - ProgressiveHealth.com
US5779651A - Medical apparatus for the diagnosis of cartilage degeneration via spatial mapping of compression-induced...
Direct link
Cartilage proteins dissipate forces and cushion joints : - AskNature
Synthesis and sorting of proteoglycans | Journal of Cell Science
MicroRNAs' Involvement in Osteoarthritis and the Prospects for Treatments
Static compression of single chondrocytes catabolically modifies single-cell gene Expression<...
TY - JOUR. T1 - Static compression of single chondrocytes catabolically modifies single-cell gene Expression. AU - Leipzig, Nic D.. AU - Athanasiou, Kyriacos A.. PY - 2008/3/15. Y1 - 2008/3/15. N2 - Previous work has established that mechanical forces can lead to quantifiable alterations in cell function. However, how forces change gene expression in a single cell and the mechanisms of force transmission to the nucleus are poorly understood. Here we demonstrate that the gene expression of proteins related to the extracellular matrix in single articular chondrocytes is modified by compressive forces in a dosage-dependent manner. Increasing force exposure catabolically shifts single-cell mRNA levels of aggrecan, collagen IIa, and tissue inhibitor of metalloproteinase-1. Cytohistochemistry reveals that the majority of strain experienced by the cell is also experienced by the nucleus, resulting in considerable changes in nuclear volume and structure. Transforming growth factor-β1 and insulin-like ...
Prospective evaluation of serum biomarker levels and cartilage repair by autologous chondrocyte transplantation and subchondral...
Effects of high mobility … - Göteborgs universitet
Proteoglycans2
- Aggrecanases act on large proteoglycans known as aggrecans, which are components of connective tissues such as cartilage. (wikipedia.org)
- Correlations were made between 27 obstetric factors and 8 biological indicators including doubling time at passage (P)1 and P2, the percentage of proteoglycans and collagens, and the relative transcriptional expression of Sox-9, aggrecans, and total type 2 collagen (Coll2T). (biomedcentral.com)
Collagen3
- It cleaves both type II collagen and aggrecans. (the-rheumatologist.org)
- In cartilage, ECM forms a major fraction of the tissue, type II collagen and aggrecans being the most abundant macromolecules. (diva-portal.org)
- We have arbitrarily divided the ECM into two sections: (1) The collagen: PG complex itself, including the external membrane-bound PG, (e.g., aggrecans and decorin) and (2) The perturbations caused by the effects of the surrounding internal and external environment. (omicsonline.org)
Glycosaminoglycans1
- While glucosamine is used to make glycosaminoglycans, chondroitin sulfate refers to a group of glycosaminoglycans called aggrecans. (progressivehealth.com)
Proteins2
- and other ECM proteins are embedded in the matrix of aggrecans. (soccerati.com)
- hundreds of these aggrecans are bound noncovalently by link proteins to long polymers of hyaluronic acid. (kenhub.com)
MeSH1
- Aggrecans" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (umassmed.edu)
Collagens1
- Collagens and aggrecans, which are the major components of the ECM in the IVD, are synthesized by the IVD, and broken down by MMPs and aggrecanases [ 5 ] to achieve dynamic equilibrium. (biomedcentral.com)
Substances1
- Glucosamine is a major joint support nutrient that stimulates the manufacture of substances called aggrecans. (ibuypharmacy.co.nz)
Intervertebral Discs1
- They work with aggrecans to protect intervertebral discs by producing swelling pressure that counters compressive loads on tissue. (dailybenefit.com)
Proteoglycan1
- Many of the proteoglycan molecules are linked to hyaluronic acid, forming massive molecules, molecules such as aggrecans aggregate, of enormous electrochemical domains that attract osmotically active cations (e.g. (scribd.com)
Protein3
- Proteases capable of degrading aggrecans are called aggrecanases, and they are members of the ADAM (A Disintegrin And Metalloprotease) protein family. (wikipedia.org)
- En plus, cette dernière a montré de différents effets sur plusieurs voies de signalisation stimulées par l'IL-1β et le TNF-α telles que les voies des MAPKs (Mitogen activated protein kinase), de l'AKT, et de la p70 S6 kinase. (umontreal.ca)
- La Rapamycine a inhibé partiellement l'activation de la phosphorylation de l'ERK1/2 MAPK (extracellular signal-regulated protein kinase MAPK) en présence du TNF-α seulement. (umontreal.ca)
Cytokines1
- Introduction: During the pathogenesis of osteoarthritis, the pro-inflammatory cytokines IL-1β (Interleukin-1 beta) and TNF-α (Tumor necrosis factor alpha) stimulate the degradation of aggrecans by aggrecanase-1 or ADAMTS-4 (A disintegrin and metalloproteinase with thrombospondin motif). (umontreal.ca)
Aggregate1
- Aggrecans aggregate to form the cartilage. (progressivehealth.com)
Major2
- This graph shows the total number of publications written about "Aggrecans" by people in this website by year, and whether "Aggrecans" was a major or minor topic of these publications. (umassmed.edu)
- In particular, the tendency of the aggrecans to stick together under compressive force, then come apart moments after represents a major compression-dissipation system. (asknature.org)
Units1
- These structural units, called aggrecans, are important for the elasticity, resilience and shock-absorbing properties of cartilage. (healthchemist.co.nz)
Important1
- Aggrecans are important for the elasticity, resilience and shock-absorbing properties of cartilage. (ibuypharmacy.co.nz)