Collagen Type IX: A fibril-associated collagen usually found crosslinked to the surface of COLLAGEN TYPE II fibrils. It is a heterotrimer containing alpha1(IX), alpha2(IX) and alpha3(IX) subunits.Collagen: A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH).Cartilage: A non-vascular form of connective tissue composed of CHONDROCYTES embedded in a matrix that includes CHONDROITIN SULFATE and various types of FIBRILLAR COLLAGEN. There are three major types: HYALINE CARTILAGE; FIBROCARTILAGE; and ELASTIC CARTILAGE.Collagen Type I: The most common form of fibrillar collagen. It is a major constituent of bone (BONE AND BONES) and SKIN and consists of a heterotrimer of two alpha1(I) and one alpha2(I) chains.Collagen Type III: A fibrillar collagen consisting of three identical alpha1(III) chains that is widely distributed in many tissues containing COLLAGEN TYPE I. It is particularly abundant in BLOOD VESSELS and may play a role in tissues with elastic characteristics.Collagen Type IV: A non-fibrillar collagen found in the structure of BASEMENT MEMBRANE. Collagen type IV molecules assemble to form a sheet-like network which is involved in maintaining the structural integrity of basement membranes. The predominant form of the protein is comprised of two alpha1(IV) subunits and one alpha2(IV) subunit, however, at least six different alpha subunits can be incorporated into the heterotrimer.Collagen Type II: A fibrillar collagen found predominantly in CARTILAGE and vitreous humor. It consists of three identical alpha1(II) chains.Collagen Type XI: A fibrillar collagen found primarily in interstitial CARTILAGE. Collagen type XI is heterotrimer containing alpha1(XI), alpha2(XI) and alpha3(XI) subunits.Collagen Type V: A fibrillar collagen found widely distributed as a minor component in tissues that contain COLLAGEN TYPE I and COLLAGEN TYPE III. It is a heterotrimeric molecule composed of alpha1(V), alpha2(V) and alpha3(V) subunits. Several forms of collagen type V exist depending upon the composition of the subunits that form the trimer.Fibrillar Collagens: A family of structurally related collagens that form the characteristic collagen fibril bundles seen in CONNECTIVE TISSUE.Collagen Type VI: A non-fibrillar collagen that forms a network of MICROFIBRILS within the EXTRACELLULAR MATRIX of CONNECTIVE TISSUE. The alpha subunits of collagen type VI assemble into antiparallel, overlapping dimers which then align to form tetramers.Extracellular Matrix: A meshwork-like substance found within the extracellular space and in association with the basement membrane of the cell surface. It promotes cellular proliferation and provides a supporting structure to which cells or cell lysates in culture dishes adhere.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).Receptors, Collagen: Collagen receptors are cell surface receptors that modulate signal transduction between cells and the EXTRACELLULAR MATRIX. They are found in many cell types and are involved in the maintenance and regulation of cell shape and behavior, including PLATELET ACTIVATION and aggregation, through many different signaling pathways and differences in their affinities for collagen isoforms. Collagen receptors include discoidin domain receptors, INTEGRINS, and glycoprotein VI.Chick Embryo: The developmental entity of a fertilized chicken egg (ZYGOTE). The developmental process begins about 24 h before the egg is laid at the BLASTODISC, a small whitish spot on the surface of the EGG YOLK. After 21 days of incubation, the embryo is fully developed before hatching.Pepsin A: Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.Chondroitin Lyases: Enzymes which catalyze the elimination of delta-4,5-D-glucuronate residues from polysaccharides containing 1,4-beta-hexosaminyl and 1,3-beta-D-glucuronosyl or 1,3-alpha-L-iduronosyl linkages thereby bringing about depolymerization. EC 4.2.2.4 acts on chondroitin sulfate A and C as well as on dermatan sulfate and slowly on hyaluronate. EC 4.2.2.5 acts on chondroitin sulfate A and C.Proteoglycans: Glycoproteins which have a very high polysaccharide content.Cartilage, Articular: A protective layer of firm, flexible cartilage over the articulating ends of bones. It provides a smooth surface for joint movement, protecting the ends of long bones from wear at points of contact.Collagen Type XVIII: A non-fibrillar collagen found in BASEMENT MEMBRANE. The C-terminal end of the alpha1 chain of collagen type XVIII contains the ENDOSTATIN peptide, which can be released by proteolytic cleavage.Procollagen: A biosynthetic precursor of collagen containing additional amino acid sequences at the amino-terminal and carboxyl-terminal ends of the polypeptide chains.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Collagen Type X: A non-fibrillar collagen found primarily in terminally differentiated hypertrophic CHONDROCYTES. It is a homotrimer of three identical alpha1(X) subunits.Matrilin Proteins: PROTEOGLYCANS-associated proteins that are major components of EXTRACELLULAR MATRIX of various tissues including CARTILAGE; and INTERVERTEBRAL DISC structures. They bind COLLAGEN fibers and contain protein domains that enable oligomer formation and interaction with other extracellular matrix proteins such as CARTILAGE OLIGOMERIC MATRIX PROTEIN.Collagen Type XII: A fibril-associated collagen found in many tissues bearing high tensile stress, such as TENDONS and LIGAMENTS. It is comprised of a trimer of three identical alpha1(XII) chains.Fibronectins: Glycoproteins found on the surfaces of cells, particularly in fibrillar structures. The proteins are lost or reduced when these cells undergo viral or chemical transformation. They are highly susceptible to proteolysis and are substrates for activated blood coagulation factor VIII. The forms present in plasma are called cold-insoluble globulins.Chondrocytes: Polymorphic cells that form cartilage.Hydroxyproline: A hydroxylated form of the imino acid proline. A deficiency in ASCORBIC ACID can result in impaired hydroxyproline formation.Fibroblasts: Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.Basement Membrane: A darkly stained mat-like EXTRACELLULAR MATRIX (ECM) that separates cell layers, such as EPITHELIUM from ENDOTHELIUM or a layer of CONNECTIVE TISSUE. The ECM layer that supports an overlying EPITHELIUM or ENDOTHELIUM is called basal lamina. Basement membrane (BM) can be formed by the fusion of either two adjacent basal laminae or a basal lamina with an adjacent reticular lamina of connective tissue. BM, composed mainly of TYPE IV COLLAGEN; glycoprotein LAMININ; and PROTEOGLYCAN, provides barriers as well as channels between interacting cell layers.Breast Neoplasms: Tumors or cancer of the human BREAST.Cell Line, Tumor: A cell line derived from cultured tumor cells.Focal Adhesion Protein-Tyrosine Kinases: A family of non-receptor, PROLINE-rich protein-tyrosine kinases.Matrix Metalloproteinases: A family of zinc-dependent metalloendopeptidases that is involved in the degradation of EXTRACELLULAR MATRIX components.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Cross-Linking Reagents: Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.Riboflavin: Nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. The richest natural source is yeast. It occurs in the free form only in the retina of the eye, in whey, and in urine; its principal forms in tissues and cells are as FLAVIN MONONUCLEOTIDE and FLAVIN-ADENINE DINUCLEOTIDE.Protein-Lysine 6-Oxidase: An enzyme oxidizing peptidyl-lysyl-peptide in the presence of water & molecular oxygen to yield peptidyl-allysyl-peptide plus ammonia & hydrogen peroxide. EC 1.4.3.13.Keratoconus: A noninflammatory, usually bilateral protrusion of the cornea, the apex being displaced downward and nasally. It occurs most commonly in females at about puberty. The cause is unknown but hereditary factors may play a role. The -conus refers to the cone shape of the corneal protrusion. (From Dorland, 27th ed)Photosensitizing Agents: Drugs that are pharmacologically inactive but when exposed to ultraviolet radiation or sunlight are converted to their active metabolite to produce a beneficial reaction affecting the diseased tissue. These compounds can be administered topically or systemically and have been used therapeutically to treat psoriasis and various types of neoplasms.Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.Mice, Inbred DBAHSP47 Heat-Shock Proteins: Basic glycoprotein members of the SERPIN SUPERFAMILY that function as COLLAGEN-specific MOLECULAR CHAPERONES in the ENDOPLASMIC RETICULUM.Arthritis, Experimental: ARTHRITIS that is induced in experimental animals. Immunological methods and infectious agents can be used to develop experimental arthritis models. These methods include injections of stimulators of the immune response, such as an adjuvant (ADJUVANTS, IMMUNOLOGIC) or COLLAGEN.ArthritisMice, Inbred C57BLArthritis, Rheumatoid: A chronic systemic disease, primarily of the joints, marked by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures. Etiology is unknown, but autoimmune mechanisms have been implicated.Biotechnology: Body of knowledge related to the use of organisms, cells or cell-derived constituents for the purpose of developing products which are technically, scientifically and clinically useful. Alteration of biologic function at the molecular level (i.e., GENETIC ENGINEERING) is a central focus; laboratory methods used include TRANSFECTION and CLONING technologies, sequence and structure analysis algorithms, computer databases, and gene and protein structure function analysis and prediction.Patents as Topic: Exclusive legal rights or privileges applied to inventions, plants, etc.Poultry: Domesticated birds raised for food. It typically includes CHICKENS; TURKEYS, DUCKS; GEESE; and others.Erythrocytes: Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.Foot: The distal extremity of the leg in vertebrates, consisting of the tarsus (ANKLE); METATARSUS; phalanges; and the soft tissues surrounding these bones.

COL9A3: A third locus for multiple epiphyseal dysplasia. (1/80)

Multiple epiphyseal dysplasia (MED), an autosomal dominant osteochondrodysplasia, is a clinically and genetically heterogeneous disorder characterized by mild short stature and early-onset osteoarthritis. The phenotypic spectrum includes the mild Ribbing type, the more severe Fairbank type, and some unclassified forms. Linkage studies have identified two loci for MED. One of these, EDM1, is on chromosome 19, in a region that contains the cartilage oligomeric matrix protein (COMP) gene. Mutations have been identified in this gene in patients with the Ribbing type, the Fairbank type, and unclassified forms of MED. The second locus, EDM2, maps to chromosome 1, in a region spanning COL9A2. Recently, a splice-site mutation was found in COL9A2, causing skipping of exon 3 in one family with MED. Because of the exclusion of the EDM1 and EDM2 loci in some families, the existence of a third locus has been postulated. We report here one family with MED, evaluated clinically and radiologically and tested for linkage with candidate genes, including COMP, COL9A1, COL9A2, and COL9A3. No linkage was found with COMP, COL9A1, or COL9A2, but an inheritance pattern consistent with linkage was observed with COL9A3. Mutation analysis of COL9A3 identified an A-->T transversion in the acceptor splice site of intron 2 in affected family members. The mutation led to skipping of exon 3 and an in-frame deletion of 12 amino acid residues in the COL3 domain of the alpha3(IX) chain and thus appeared to be similar to that reported for COL9A2. This is the first disease-causing mutation identified in COL9A3. Our results also show that COL9A3, located on chromosome 20, is a third locus for MED.  (+info)

An allele of COL9A2 associated with intervertebral disc disease. (2/80)

Intervertebral disc disease is one of the most common musculoskeletal disorders. A number of environmental and anthropometric risk factors may contribute to it, and recent reports have suggested the importance of genetic factors as well. The COL9A2 gene, which codes for one of the polypeptide chains of collagen IX that is expressed in the intervertebral disc, was screened for sequence variations in individuals with intervertebral disc disease. The analysis identified a putative disease-causing sequence variation that converted a codon for glutamine to one for tryptophan in six out of the 157 individuals but in none of 174 controls. The tryptophan allele cosegregated with the disease phenotype in the four families studied, giving a lod score (logarithm of odds ratio) for linkage of 4.5, and subsequent linkage disequilibrium analysis conditional on linkage gave an additional lod score of 7.1.  (+info)

Complete sequence of the 23-kilobase human COL9A3 gene. Detection of Gly-X-Y triplet deletions that represent neutral variants. (3/80)

We report the complete sequence of the human COL9A3 gene that encodes the alpha3 chain of heterotrimeric type IX collagen, a member of the fibril-associated collagens with interrupted triple helices family of collagenous proteins. Nucleotide sequencing defined over 23,000 base pairs (bp) of the gene and about 3000 bp of the 5'-flanking sequences. The gene contains 32 exons. The domain and exon organization of the gene is almost identical to a related gene, the human COL9A2 gene. However, exon 2 of the COL9A3 gene codes for one -Gly-X-Y- triplet less than exon 2 of the COL9A2 gene. The difference is compensated by an insertion of 9 bp coding for an additional triplet in exon 4 of the COL9A3 gene. As a result, the number of -Gly-X-Y- repeats in the third collagenous domain remains the same in both genes and ensures the formation of an in-register triple helix. In the course of screening this gene for mutations, heterozygosity for separate 9-bp deletions within the COL1 domain were identified in two kindreds. In both instances, the deletions did not co-segregate with any disease phenotype, suggesting that they were neutral variants. In contrast, similar deletions in triple helical domain of type I collagen are lethal. To study whether alpha3(IX) chains with the deletion will participate in the formation of correctly folded heterotrimeric type IX collagen, we expressed mutant alpha3 chains together with normal alpha1 and alpha2 chains in insect cells. We show here that despite the deletion, mutant alpha3 chains were secreted as heterotrimeric, triple helical molecules consisting of three alpha chains in a 1:1:1 ratio. The results suggest that the next noncollagenous domain (NC2) is capable of correcting the alignment of the alpha chains, and this ensures the formation of an in-register triple helix.  (+info)

A mutation in COL9A1 causes multiple epiphyseal dysplasia: further evidence for locus heterogeneity. (4/80)

Multiple epiphyseal dysplasia (MED) is an autosomal dominantly inherited chondrodysplasia. It is clinically highly heterogeneous, partially because of its complex genetic background. Mutations in four genes, COL9A2, COL9A3, COMP, and MATR3, all coding for cartilage extracellular matrix components (i.e., the alpha2 and alpha 3 chains of collagen IX, cartilage oligomeric matrix protein, and matrilin-3), have been identified in this disease so far, but no mutations have yet been reported in the third collagen IX gene, COL9A1, which codes for the alpha1(IX) chain. MED with apparently recessive inheritance has been reported in some families. A homozygous R279W mutation was recently found in the diastrophic dysplasia sulfate transporter gene, DTDST, in a patient with MED who had a club foot and double-layered patella. The series consisted of 41 probands with MED, 16 of whom were familial and on 4 of whom linkage analyses were performed. Recombination was observed between COL9A1, COL9A2, COL9A3, and COMP and the MED phenotype in two of the families, and between COL9A2, COL9A3, and COMP and the phenotype in the other two families. Screening of COL9A1 for mutations in the two probands from the families in which this gene was not involved in the recombinations failed to identify any disease-causing mutations. The remaining 37 probands were screened for mutations in all three collagen IX genes and in the COMP gene. The probands with talipes deformities or multipartite patella were also screened for the R279W mutation in DTDST. The analysis resulted in identification of three mutations in COMP and one in COL9A1, but none in the other two collagen IX genes. Two of the probands with a multipartite patella had the homozygous DTDST mutation. The results show that mutations in COL9A1 can cause MED, but they also suggest that mutations in COL9A1, COL9A2, COL9A3, COMP, and DTDST are not the major causes of MED and that there exists at least one additional locus.  (+info)

Chondrocyte phenotype and cell survival are regulated by culture conditions and by specific cytokines through the expression of Sox-9 transcription factor. (5/80)

OBJECTIVE: To investigate the effects of culture conditions, serum and specific cytokines such as insulin-like growth factor (IGF) 1 and interleukin (IL) 1alpha on phenotype and cell survival in cultures of Syrian hamster embryonic chondrocyte-like cells (DES4(+).2). METHODS: Proteins and RNA extracted from subconfluent and confluent early- and late-passage DES4(+).2 cells cultured in the presence or absence of serum and IL-1alpha or IGF-1 or both cytokines together were analysed for the expression of chondrocyte-specific genes and for the chondrogenic transcription factor Sox-9 by Western and Northern blotting. Apoptosis was assessed by agarose gel electrophoresis of labelled low-molecular weight DNA extracted from DES4(+).2 cells and another Syrian hamster embryonic chondrocyte-like cell line, 10W(+).1, cultured under the different conditions and treatments. RESULTS: Early passage DES4(+).2 cells expressed chondrocyte-specific molecules such as collagen types alpha1(II) and alpha1(IX), aggrecan, biglycan and link protein and collagen types alpha1(I) and alpha1(X) mRNAs, suggesting a prehypertrophic chondrocyte-like phenotype. The expression of all genes investigated was cell density- and serum-dependent and was low to undetectable in cell populations from later passages. Early-passage DES4(+).2 and 10W(+).1 cells survived when cultured at low cell density, but died by apoptosis when cultured at high cell density in the absence of serum or IGF-1. IGF-1 and IL-1alpha had opposite and antagonistic effects on the chondrocyte phenotype and survival. Whereas IL-1alpha acting alone suppressed cartilage-specific gene expression without significantly affecting cell survival, IGF-1 increased the steady-state mRNA levels and relieved the IL-1alpha-induced suppression of all the chondrocyte-specific genes investigated; it also enhanced chondrocyte survival. Suppression of the chondrocyte phenotype by the inflammatory cytokine IL-1alpha correlated with marked down-regulation of the transcription factor Sox-9, which was relieved by IGF-1. The expression of the Sox9 gene was closely correlated with the expression of the chondrocyte-specific genes under all conditions and treatments. CONCLUSIONS: The results suggest that the effects of cartilage anabolic and catabolic cytokines IGF-1 and IL-1alpha on the expression of the chondrocyte phenotype are mediated by Sox-9. As Sox-9 appears to be essential for matrix production, the potent effect of IL-1alpha in suppressing Sox-9 expression may limit the ability of cartilage to repair during inflammatory joint diseases.  (+info)

Contacts with fibrils containing collagen I, but not collagens II, IX, and XI, can destabilize the cartilage phenotype of chondrocytes. (6/80)

OBJECTIVE: Cell-matrix interactions are important regulators of cellular functions, including matrix synthesis, proliferation and differentiation. This is well exemplified by the characteristically labile phenotype of chondrocytes that is lost in monolayer culture but is stabilized in suspension under appropriate conditions. We were interested in the role of collagen suprastructures in maintaining or destabilizing the cartilage phenotype of chondrocytes. DESIGN: Primary sternal chondrocytes from 17-day-old chick embryos were cultured in gels of fibrils reconstituted from soluble collagen I from various sources. The culture media either contained or lacked FBS. Cells were cultured for up to 28 days and the evolution of the phenotype of the cells was assessed by their collagen expression (collagens II and X for differentiated chondrocytes and hypertrophic chodrocytes, repectively; collagen I for phenotypically modulated cells), or by their secretion of alkaline phosphatase (hypertrophic cartilage phenotype). RESULTS: The cells often retained their differentiated phenotype only if cultured with serum. Under serum-free conditions, cartilage characteristics were lost. The cells acquired a fibroblast-like shape and, later, synthesized collagen I instead of cartilage collagens. Shape changes were influenced by beta1-integrin-activity, whereas other matrix receptors were important for alterations of collagen patterns. Heterotypic fibrils reconstituted from collagens II, IX, and XI did not provoke this phenotypic instability. CONCLUSIONS: Chondrocytes sensitively recognize the suprastructures of collagen fibrils in their environment. Cellular interactions with fibrils with appropriate molecular organizations, such as that in cartilage fibrils, result in the maintenance of the differentiated cartilage phenotype. However, other suprastructures, e.g. in reconstituted fibrils mainly containing collagen I, lead to cell-matrix interactions incompatible with the cartilage phenotype. The maintenance of the differentiated traits of chondrocytes is pivotal for the normal function of, e.g., articular cartilage. If pathologically altered matrix suprastructures lead to a dysregulation of collagen production also in vivo compromised cartilage functions inevitably will be propagated further.  (+info)

Articular cartilage repair using a tissue-engineered cartilage-like implant: an animal study. (7/80)

OBJECTIVE: Because articular cartilage has limited ability to repair itself, treatment of (osteo)chondral lesions remains a clinical challenge. We aimed to evaluate how well a tissue-engineered cartilage-like implant, derived from chondrocytes cultured in a novel patented, scaffold-free bioreactor system, would perform in minipig knees with chondral, superficial osteochondral, and full-thickness articular defects. DESIGN: For in vitro implant preparation, we used full-thickness porcine articular cartilage and digested chondrocytes. Bioreactors were seeded with 20x10(6) cells and incubated for 3 weeks. Subsequent to culture, tissue cartilage-like implants were divided for assessment of viability, formaldehyde-fixed and processed by standard histological methods. Some samples were also prepared for electron microscopy (TEM). Proteoglycans and collagens were identified and quantified by SDS-PAGE gels. For in vivo studies in adult minipigs, medial parapatellar arthrotomy was performed unilaterally. Three types of defects were created mechanically in the patellar groove of the femoral condyle. Tissue-engineered cartilage-like implants were placed using press-fit fixation, without supplementary fixation devices. Control defects were not grafted. Animals could bear full weight with an unlimited range of motion. At 4 and 24 weeks postsurgery, explanted knees were assessed using the modified ICRS classification for cartilage repair. RESULTS: After 3-4 weeks of bioreactor incubation, cultured chondrocytes developed a 700-microm- to 1-mm-thick cartilage-like tissue. Cell density was similar to that of fetal cartilage, and cells stained strongly for Alcian blue and safranin O. The percentage of viable cells remained nearly constant (approximately 90%). Collagen content was similar to that of articular cartilage, as shown by SDS-PAGE. At explantation, the gross morphological appearance of grafted defects appeared like normal cartilage, whereas controls showed irregular fibrous tissue covering the defect. Improved histologic appearance was maintained for 6 months postoperatively. Although defects were not always perfectly level upon implantation at explanation the implant level matched native cartilage levels with no tissue hypertrophy. Once in place, implants remodelled to tissues with decreased cell density and a columnar organization. CONCLUSIONS: Repair of cartilage defects with a tissue-engineered implant yielded a consistent gross cartilage repair with a matrix predominantly composed of type II collagen up to 6 months after implantation. This initial result holds promise for the use of this unique bioreactor/tissue-engineered implant in humans.  (+info)

The chick transcriptional repressor Nkx3.2 acts downstream of Shh to promote BMP-dependent axial chondrogenesis. (8/80)

Previously, we demonstrated that Shh acts early in the development of the axial skeleton, to induce a prochondrogenic response to later BMP signaling. Here, we demonstrate that somitic expression of the transcription factor Nkx3.2 is initiated by Shh and sustained by BMP signals. Misexpression of Nkx3.2 in somitic tissue confers a prochondrogenic response to BMP signals. The transcriptional repressor activity of Nkx3.2 is essential for this factor to promote chondrogenesis. Conversely, a "reverse function" mutant of Nkx3.2 that has been converted into a transcriptional activator inhibits axial chondrogenesis in vivo. We conclude that Nkx3.2 is a critical mediator of the actions of Shh during axial cartilage formation, acting to inhibit expression of factors that interfere with the prochondrogenic effects of BMPs.  (+info)

Putative uncharacterized protein COL9A1 (Collagen, type IX, alpha 1, isoform CRA_b) contains a PF01391 domain.. Putative uncharacterized protein COL9A1 (Collagen, type IX, alpha 1, isoform CRA_b) contains a PF01391 domain.. Putative uncharacterized protein COL9A1 (Collagen, type IX, alpha 1, isoform CRA_b) contains a PF01391 domain.. Putative uncharacterized protein COL9A1 (Collagen, type IX, alpha 1, isoform CRA_b) contains a PF01391 domain.. Putative uncharacterized protein COL9A1 (Collagen, type IX, alpha 1, isoform CRA_b) contains a PF01391 domain.. Putative uncharacterized protein COL9A1 (Collagen, type IX, alpha 1, isoform CRA_b) contains a PF01391 domain.. Putative uncharacterized protein COL9A1 (Collagen, type IX, alpha 1, isoform CRA_b) contains a PF01391 domain.. Putative uncharacterized protein COL9A1 (Collagen, type IX, alpha 1, isoform CRA_b) contains a PF01391 domain.. Putative uncharacterized protein COL9A1 (Collagen, type IX, alpha 1, isoform CRA_b) contains a PF01391 ...
Autosomal recessive inheritance has been described in some Stickler syndrome families. Individuals in these families were reported to have clinical findings similar to STL1, STL2, and Marshall syndrome. The cause has been documented to be mutations in collagen IX genes. Collagen IX is a heterotrimeric molecule composed of α1(IX), α2(IX) and α3(IX) chains encoded by the COL9A1, COL9A2 and COL9A3 genes. Analysis of the collagen IX genes is indicated in those instances of Stickler syndrome where autosomal recessive inheritance is suspected. Autosomal dominant mutations in the collagen IX genes cause some cases of multiple epiphyseal dysplasia.. Copy number variation (CNV) analysis of the Stickler syndrome genes is also offered as a panel. Additionally, CTGT offers a comprehensive test (both NGS and CNV panels) for these genes. Panel genes are also offered as individual sequencing and deletion/duplication tests unless otherwise indicated.. Read less ...
Human COL9A1 derived in Human Cells. The whole cell lysate is provided in 1X Sample Buffer.Browse all transfected cell lysate positive controls
Buy our Recombinant Human COL4A3BP protein. Ab95897 is a protein fragment produced in Escherichia coli and has been validated in SDS-PAGE, MS. Abcam provides…
Original concerns that cloning caused early-onset osteoarthritis in Dolly the sheep are unfounded, say experts at the University of Nottingham and the University of Glasgow.
Allen, KD, Griffin, TM, Rodriguiz, RM, Wetsel, WC, Kraus, VB, Huebner, JL, Boyd, LM, and Setton, LA. "Decreased physical function and increased pain sensitivity in mice deficient for type IX collagen." Arthritis Rheum 60, no. 9 (September 2009): 2684-2693. Full Text ...
pep:known chromosome:VEGA66:2:180597790:180622189:1 gene:OTTMUSG00000016344 transcript:OTTMUST00000039291 gene_biotype:protein_coding transcript_biotype:protein_coding gene_symbol:Col9a3 description:procollagen type IX alpha 3 ...
Mouse polyclonal antibody raised against a full-length human COL4A3 protein. COL4A3 (AAI56139.1, 1 a.a. ~ 1670 a.a) full-length human protein. (H00001285-B01P) - Products - Abnova
Human COL8A2 partial ORF ( NP_005193.1, 626 a.a. - 696 a.a.) recombinant protein with GST-tag at N-terminal. (H00001296-Q01) - Products - Abnova
Studies have shown that both Type I and Type II Collagen undergo fibrillogenesis under similar conditions, namely at near normal body temperature and pH. It is understood that accessory proteins or chaperone proteins can either speed up or slow down fibrillogenesis in Type I Collagen. However, there is a lack of research on how these same proteins can regulate the kinetics of fibril formation in Type II Collagen. If certain proteins are found to speed up Type II fibril formation, they could greatly decrease the time required for healing in cartilage injuries or diseases, especially those due to the inherent lack of vascularity in cartilage. On the other hand, some proteins may slow down Type II fibril formation and have applications in diseases that are caused by excessive fibril formation such as fibrosis or scar formation. To test the effects of specific accessory proteins, recombinant forms of these proteins were added with Collagen Type II in a buffered solution at 7.4 pH, and a temperature of 25⁰
This gene encodes the alpha chain of type XIX collagen, a member of the FACIT collagen family (fibril-associated collagens with interrupted helices). Although the function of this collagen is not known, other members of this collagen family are found in association with fibril-forming collagens such as type I and II, and serve to maintain the integrity of the extracellular matrix. The transcript produced from this gene has an unusually large 3 UTR which has not been completely sequenced. [provided by RefSeq, Jul 2008 ...
Université de Liège - ULg , Département de langues et littératures romanes , Langues et littératures espagnoles et hispano-américaines ,] ...
ferrassin condimentada televisor autofinances ventilassis Eliana esmaluc maçonaré benzol desinterlineàreu coltellejàreu basculé[email protected] ...
Recent studies of OA cartilage have identified both messenger RNA (mRNA) and the protein for specific MMPs as well as a collagenase mediated type II collagen degradation product, suggesting that MMPs contribute to the intrinsic chondrocyte mediated degenerative changes of the cartilage matrix in OA.8,12,13 As yet the factors responsible for their expression remain uncertain, although the proinflammatory cytokines interleukin 1 (IL1) and tumour necrosis factor α (TNFα) have been implicated.1,8 The increased levels of histamine found in OA synovial fluids3 have suggested a role for this mediator in the pathophysiology of this disease. Evidence presented here shows that histamine up regulates both MMP-13 and MMP-3 production by chondrocytes. Both these MMPs are important in the degradation of articular cartilage; MMP-13 can degrade collagen type II, and MMP-3 can degrade proteoglycan and collagen types IX and XI, and activate procollagenase-1.14 Earlier studies have shown that chondrocytes ...
Lumbar Disc Disease Treatment procedures are available at Apollo Hospital Indraprastha from Price on request. Find out what other patients experienced and read their reviews.
Show moreCollagen XIV is a fibril-associated collagen with an interrupted triple helix (FACIT). Previous studies have shown that this collagen type regulates early stages of fibrillogenesis in connective tissues of high mechanical demand. Mice null for Collagen XIV are viable, however formation of the interstitial collagen network is defective in tendons and skin leading to reduced biomechanical function. The assembly of a tightly regulated collagen network is also required in the heart, not only for structural support but also for controlling cellular processes. Collagen XIV is highly expressed in the embryonic heart, notably within the cardiac interstitium of the developing myocardium, however its role has not been elucidated. To test this, we examined cardiac phenotypes in embryonic and adult mice devoid of Collagen XIV. From as early as E11.5, Col14a1(-/-) mice exhibit significant perturbations in mRNA levels of many other collagen types and remodeling enzymes (MMPs, TIMPs) within the ...
Collagen, type XV, alpha 1, also known as COL15A1, is a human gene.[1] This gene encodes the alpha chain of type XV collagen, a member of the FACIT collagen family (fibril-associated collagens with interrupted helices). Type XV collagen has a wide tissue distribution but the strongest expression is localized to basement membrane zones so it may function to adhere basement membranes to underlying connective tissue stroma. Mouse studies have shown that collagen XV deficiency is associated with muscle and microvessel deterioration.[1] ...
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Study Design. Prospective cohort study. Objective. To study biomechanical factors in relation to symptomatic lumbar disc disease. Summary of Background Data. The importance of biomechanical factors in lumbar disc disease have been questioned the past decade and knowledge from large prospective studies is lacking.. Methods. The study basis is a cohort of 263 529 Swedish construction workers who participated in a national occupational health surveillance programme from 1971 until 1992. The workers job title, smoking habits, body weight, height and age were registered at the examinations. The occurrence of hospitalization due to lumbar disc disease from January 1 1987 until December 31 2003 was collected from a linkage with the Swedish Hospital Discharge Register.. Results. There was an increased risk for hospitalization due to lumbar disc disease for several occupational groups compared to white-collar workers and foremen. Occupational groups with high biomechanical loads had the highest risks, ...
Lumbar disc disease (LDD) is among the most common ailments in Western societies.1 In the military, LDD often results in significant impairments and contributes greatly to health care costs and disability.2 Military training often results in exacerbation or presentation of LDD related symptoms. LDD appears to be a multifactorial disorder in which genetics play an important role, as it is evident from several recent studies.3. Collagen is the most abundant structural component of the extracellular matrix. Changes in collagen cross linking have been identified in degenerative disc disease, and LDD was recently associated with a polymorphism of the collagen type IX (COL9A3) gene.3 Type I collagen is the major protein in skin, ligaments, and bone; both COL1A1 and COL1A2 are present in the main components of the intervertebral disc, the annulus fibrosus (primarily) and the nucleus pulposus (secondarily).4. A G→T polymorphism within the COL1A1 regulatory region that affects the recognition site for ...
Researchers from the University of Utah School of Medicine report that there is a heritable predisposition to lumbar disc disease, according to a Medscape Medical News article based on a study published this month in the Journal of Bone and Joint Surgery. For the study, authors analyzed data from the Utah Population Database, which allows medical information to be tracked on the states founding pioneers and their descendents, and the University of Utah Health Sciences Center data warehouse, which has diagnosis and procedure data on all patients treated at the university hospital. Together the databases contain information on more than 2.4 million patients. Researchers included only patients and control participants with at least 3 generations of genealogical data. Of the people who qualified for the study, 1,254 had at least 1 diagnosis of lumbar disc disease or lumbar disc herniation, along with the requisite genealogical data. The authors tested for heritability by estimating the relative ...
Researchers from the University of Utah School of Medicine report that there is a heritable predisposition to lumbar disc disease, according to a Medscape Medical News article based on a study published this month in the Journal of Bone and Joint Surgery. For the study, authors analyzed data from the Utah Population Database, which allows medical information to be tracked on the states founding pioneers and their descendents, and the University of Utah Health Sciences Center data warehouse, which has diagnosis and procedure data on all patients treated at the university hospital. Together the databases contain information on more than 2.4 million patients. Researchers included only patients and control participants with at least 3 generations of genealogical data. Of the people who qualified for the study, 1,254 had at least 1 diagnosis of lumbar disc disease or lumbar disc herniation, along with the requisite genealogical data. The authors tested for heritability by estimating the relative ...
Symptoms of lumbar disc disease include back and leg pain, which may radiate down into the hand. This pain may be associated with numbness and tingling over the leg and foot, which may feel like it is "asleep". Additionally, weakness of the leg and foot muscles may develop.. It is important to recognize that the presence of a disc bulge or protrusion does not necessarily require surgical intervention. Many people who have degenerated or bulging discs that never develop symptoms, and most have only minor symptoms which can be treated with over-the-counter medications. Even those who develop more severe symptoms requiring a visit to their physician can be treated successfully with medication and physical therapy. We work with all of these health care practicioners to choose the treatment option that best meets our patients needs and desires.. ...
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A collection of disease information resources and questions answered by our Genetic and Rare Diseases Information Specialists for Multiple epiphyseal dysplasia 6
Multiple epiphyseal dysplasia 1 (EDM1) [MIM:132400]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal. {ECO:0000269,PubMed:11084047, ECO:0000269,PubMed:11565064, ECO:0000269,PubMed:21922596, ECO:0000269,PubMed:7670472, ECO:0000269,PubMed:9021009, ECO:0000269,PubMed:9184241, ...
Complete information for COMP gene (Protein Coding), Cartilage Oligomeric Matrix Protein, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Oftpred Colírio is a medicine available in a number of countries worldwide. A list of US medications equivalent to Oftpred Colírio is available on the Drugs.com website.
Paseo Colón 70 is a 19-story high-rise building in San Javier, Región de Murcia, Spain. View a detailed profile of the structure 252187 including further data and descriptions in the Emporis database.
OBJECTIVE:,br /,To test the hypothesis that physiological cyclic loading during a 30-min walking exercise causes an increase in serum cartilage oligomeric matrix protein (COMP) concentration in a healthy population.,br /,METHODS:,br /,Blood samples (5 ml) were drawn from 10 physically active adults immediately before and after, and 0.5h, 1.5h, 3.5h and 5.5h after a 30-min walking exercise on a level outdoor walking track at self-selected normal speed. On a separate day, blood samples were drawn from the same 10 subjects during 6h while they were resting in a chair. Serum COMP concentrations were determined using a commercial enzyme-linked immunosorbent assay (COMP ELISA). An activity monitor was used to record basic time-distance measurements of gait. Serum COMP concentrations within the exercise protocol and within the resting protocol were compared using separate repeated measures analyses of variance (alpha=0.05).,br /,RESULTS:,br /,In the exercise protocol, a first increase (9.7%; P=0.003) ...
What is Stickler Syndrome Stickler syndrome is a genetic condition that is characterized by serious problems in vision, hearing, problems of the joints and
Mechanical support in animals is performed by connective tissues. The soft tissues consist of collagen fibres embedded in a highly hydrated proteoglycan gel. By considering them as fibrous composite materials, a unifying theme can be found to explain their mechanical behaviour in terms of their structure and composition. Interactions between fibres and matrix are essential to their functioning in this way. Calculations are made of the maximum stress transfer per D-period required to enable collagen fibres of a given axial ratio to provide effective reinforcing. Weak non-specific interactions are shown to be sufficient. A mechanical function is proposed for type X collagen in the epiphyseal growth plate on the basis that it modifies and supplements the properties of the type II fibrils. This provides extra reinforcing and, hence, a greater stiffness to the cartilage to compensate for the reduced amount of extracellular matrix. ...
Garc a MM et al (2014) report a case of autosomal recessive multiple epiphyseal dysplasia (EDM4/rMED) due to paternal UPD. This disorder is characterised by childhood onset joint pain at the hips and knees, brachydactyly, shortened (or normal) stature and in some cases congenital clubfoot. ...
Individuals affected with pseudoachondroplasia are similar in height as those with achondroplasia, but their head size is the same as that of average-sized people. They also lack the facial features of patients with achondroplasia. It usually goes undiagnosed until the child is 2 to 3 years old.
public: HRG_RESULT Initialize (IX_DEV_ID device_id, const IX_INFO *p_info); HRG_RESULT StartTimer( ); HRG_RESULT StopTimer( ); HRG_RESULT GetElapsedSeconds(double *p_seconds); HRG_RESULT GetTreadmillInfo(IX_DEV_INFO *p_info); HRG_RESULT GeTreadmillStatus(IX_DEV_STATUS *p_status); HRG_RESULT GetSpeed(doulbe *p_speed); HRG_RESULT GetSpeedRange(IX_SCALAR_RANGE *p_range); HRG_RESULT GetSpeedUnits(IX_ITEM_UNITS *p_units); HRG_RESULT SetSpeed(double speed); HRG_RESULT GetIncline(double *p_incline); HRG_RESULT GetInclineRange((IX_SCALAR_RANGE *p_range); HRG_RESULT GetInclineUnits(IX_ITEM_UNITS *p_units); HRG_RESULT SetIncline(double incline); HRG_RESULT GetHeartRate(double *p_heart_rate); HRG_RESULT GetHeartRateRange(IX_SCALAR_RANGE *p_range); HRG_RESULT GetHeartRateUnits(IX_ITEM_UNITS *p_units); HRG_RESULT GetPower(double *p_power); HRG_RESULT GetPowerRange(IX_SCALAR_RANGE *p_range); HRG_RESULT GetPowerUnits(IX_ITEM_UNITS *p_units); HRG_RESULT GetPace(double *p_pace); HRG_RESULT ...
... El libro del pensador nativo americano Jack Forbes, Colón y otros caníbales, era uno de los textos fundamentales del movimiento anticivilización cuando fue publicado por primera vez en 1978. Su historia del terrorismo, el genocidio
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Matrilin-3 gene is mapped on chromosome 2p24-p23 that can form homo-tetramers as well as hetero-oligomers together with subunit of matrilin-1. It present in the cartilage extracellular matrix functions in the development and homeostasis of cartilage and bone. Particularly it is located in the extracellular matrix surrounding the cells that makes-up tendons and ligaments near the chondrocytes that is essential in bone formation in which spine, hips and limbs start with the formation of cartilage then converted into bone. Matrilin-3 is a mandatory component of mature articular cartilage that restricted in chondrocytes from the tangential zone and upper middle cartilage zone therefore, it is an integral component of articular cartilage matrix and its augmented expression in osteoarthritis might be a cellular response to the modified microenvironment in the disease. Matrilin-3 gene mutations implicated in multiple epiphyseal dysplasias a generalized skeletal dysplasia associated with morbidity in ...
Older individuals today are participating in athletic activities in greater and greater numbers, whether it is weekend sports enthusiasts or highly competitive senior athletes. Degeneration of the lumbar disc, associated degenerative facet arthritis, and spinal stenosis are the most common causes of low back and leg pain in the aging populati...
COMP Full-Length MS Protein Standard (NP_000086), Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. The protein encoded by this gene is a noncollagenous extracellular matrix (ECM) protein. It consists of five identical glycoprotein subunits, each with EGF-like and calcium-binding (thrombospondin-like) domains. Oligomerization results from formation of a five-stranded coiled coil and disulfides. Binding to other ECM proteins such as collagen appears to depend on divalent cations. Mutations can cause the osteochondrodysplasias pseudochondroplasia (PSACH) and multiple epiphyseal dysplasia (MED).
Up to 50 million Americans have tinnitus on a regular basis with between 2-3 million suffering from tinnitus where it affects daily living. The Inhibitor™ Tinnitus Masking Device is a new tinnitus treatment device recently available in the United States for use of temporary relief of tinnitus. The device emits an ultra high frequency sound for 60 seconds via bone conduction when applied to the mastoid. Patients reporting tinnitus will be provided the opportunity to demonstrate the device to observe any changes in their tinnitus. The device may be demonstrated up to 5 times. The investigators will be recording the the degree and duration of change in tinnitus perception following treatment with the Inhibitor™ Tinnitus Masking Device. Patients may provide a genetic sample (typically via saliva sample) to look for expression of a particular genetic marker that may be associated with tinnitus. The investigators will be collect samples from both people with tinnitus and those without tinnitus to ...
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Al-Gazali and Bakalinova (1998) described a multiply consanguineous Omani family in the UAE, in which four out of the 13 children presented with symptoms of macrocephaly, frontal lobe atrophy, and distinctive facial appearance. The first case was a boy. CT scan of his brain in his few months showed slightly dilated lateral ventricles. He had a squint in the left eye, which was operated upon. His developmental milestones were delayed, and by the age of 10-years, he showed increased swelling of the upper and lower limbs, particularly around the elbows, macrocephaly with frontal bossing, hypertelorism, flat malar regions, low set ears, short neck, and slight pectus excavatum. All joints were prominent, and there was non-pitting edema of lower limbs. Both testes were undescended. Skeletal survey showed a big skull with dysplasia of the epiphyses of the long bones. The patients sister showed the same dysmorphic features. Non-pitting edema in her case involved the entire lower limbs, including the ...
Normal healthy tendons are mostly composed of parallel arrays of collagen fibres closely packed together. The dry mass of normal tendons, which makes up about 30% of the total mass with water, is composed of about 86% collagen, 2% elastin, 1-5% proteoglycans, and 0.2% inorganic components such as copper, manganese, and calcium.[2][3] The collagen portion is made up of 97-98% type I collagen, with small amounts of other types of collagen. These include type II collagen in the cartilaginous zones, type III collagen in the reticulin fibres of the vascular walls, type IX collagen, type IV collagen in the basement membranes of the capillaries, type V collagen in the vascular walls, and type X collagen in the mineralized fibrocartilage near the interface with the bone.[2][4] Collagen fibres coalesce into macroaggregates. After secretion from the cell, the terminal peptides are cleaved by procollagen N- and C-proteinases, and the tropocollagen molecules spontaneously assemble into insoluble fibrils. A ...
Lumbar disc disease IS NOT A DISEASE. It is a terribly misnamed finding on MRI. All this means is that the some of the discs are more dried out than others--this happens to every over time. Sometimes these discs cause pain but most time THEY DONT!!!!! Please, please, please, consider going to a physical therapist or chiropractor with advanced skills in treating the spine. I am a PT and am biased towards PTs but if you have been given a diagnosis of DDD (degnerative disc disease) and have not tried SEVERAL different PTs (dont assume we are all the same) or several chiropractors, I hope you consider this. In most cases, people can return to work--they just have to rehabilitate correctly. Good luck. I wish I could be of more help.. ...
Anti-COL3A1 polyclonal antibody (STJ92388) was developed using a synthesized peptide derived from the N-terminal region of human COL3A1 at AA range: 50-130. This antibody is applicable for use in immunohistochemistry, immunofluorescence, ELISA and immunoc
购买我们的重组人COMP蛋白。Ab124873为全长蛋白,在HEK 293细胞中生产并经过SDS-PAGE, Western blot实验验证。Abcam提供免费的实验方案,操作技巧及专业的支持。
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Retrieved from "https://en.wikipedia.org/w/index.php?title=Collagen,_type_XX,_alpha_1&oldid=705418915" ...
Research into synthetic collagen is ongoing; as of 2011, partial success has been achieved in replicating collagen's structure ... Probably best known as a gelling agent in cooking, different types and grades of gelatin are used in a wide range of food and ... It has been suggested that Hydrolyzed collagen be merged into this article. (Discuss) Proposed since July 2018. ... "Type A & B Process Definition". Vyse Gelatin Company. 26 October 2009. Archived from the original on 1 March 2015. Retrieved 16 ...
It has been reported that biglycan interacts more strongly with collagen type II than collagen type I. Biglycan has been ... Pogány G, Hernandez DJ, Vogel KG (August 1994). "The in vitro interaction of proteoglycans with type I collagen is modulated by ... "Binding of the proteoglycan decorin to collagen type VI". J. Biol. Chem. 267 (8): 5250-6. PMID 1544908. Bowe MA, Mendis DB, ... "Interaction of biglycan with type I collagen". J. Biol. Chem. 270 (6): 2776-83. doi:10.1074/jbc.270.6.2776. PMID 7852349. ...
This condition is caused by a mutation of COL7A1, the gene that codes for a type of collagen 7. Epidermis (skin) Dermis Lamina ... Anchoring fibrils (composed largely of type VII collagen) extend from the basal lamina of epithelial cells and attach to the ... Keene, Douglas R.; Sakai, Lynn Y.; Lunstrum, Gregory P.; Morris, Nicholas P.; Burgeson, Robert E. (1987). "Type VII collagen ... Burgeson, Robert E. (1993). "Type VII Collagen, Anchoring Fibrils, and Epidermolysis Bullosa". Journal of Investigative ...
Horton, WA, Campbell, D, Machado, MA & Chou, J; Campbell; Machado; Chou (1989). "Type II collagen screening in the human ... Gajko-Galicka, A (2002). "Mutations in type I collagen genes resulting in osteogenesis imperfecta in humans". Acta biochimica ... "Ehlers-Danlos syndrome and type III collagen abnormalities: a variable clinical spectrum". Clinical Genetics 53 (6): 440-446. ... Type 2: brusk (hovedkomponent). Sykdommer[rediger , rediger kilde]. Ett tusen mutasjoner er blitt identifisert i tolv av mer ...
Each type of connective tissue in animals has a type of ECM: collagen fibers and bone mineral comprise the ECM of bone tissue; ... Fibrillar (Type I, II, III, V, XI). *Facit (Type IX, XII, XIV) ... Collagen[edit]. Collagens are the most abundant protein in the ... Other (Type VI, VII, XIII). Elastin[edit]. Elastins, in contrast to collagens, give elasticity to tissues, allowing them to ... Karsenty G, Park RW (1995). "Regulation of type I collagen genes expression". International Reviews of Immunology. 12 (2-4): ...
suggest that type IX collagen, a collagen active specifically in the construction of cartilage, plays a key role in ... also discovered type IX collagen accumulated within the Pseudoachondroplasia chondrocytes. This discovery indicated the ... such as type IX collagen, and that it is not solely the result of the effects of mutant molecules on the production and ... particularly with type IX collagen (Hetch et al. 1995). Achondroplasia Dwarfism Reference, Genetics Home. "pseudoachondroplasia ...
Collagen is exposed at the site of injury, the collagen promotes platelets to adhere to the injury site. Platelets release ... TypesEdit. Hemostasis can be achieved in various other ways if the body cannot do it naturally (or needs help) during surgery ... Some main types of hemostasis used in emergency medicine include: *Chemical/topical- This is a topical agent often used in ... Which hemostasis type used is determined based on the situation.[8]. Developmental Haemostasis refers to the differences in the ...
These mice have greater susceptibility to an asthma-like phenotype than wild-type animals. They are resistant to collagen- ... Two years is a common life expectancy in wild-type house mice. FVB mice show above average activity and anxiety. Because of ... Rods are lost within 9 weeks of birth, while cones may persist until 18 months of age. ...
Collagen type IV alpha-3-binding protein, also known as ceramide transfer protein (CERT) or StAR-related lipid transfer protein ... "Entrez Gene: COL4A3BP collagen, type IV, alpha 3 (Goodpasture antigen) binding protein". Merrill AH (Jul 2002). "De novo ... that specifically phosphorylates the N-terminal region of the non-collagenous domain of the alpha 3 chain of type IV collagen, ... PH domain of wild-type CERT has been found to recognize specifically PI4P and therefore CERT targets the Golgi apparatus or the ...
... with type IV collagen". The Journal of Biological Chemistry. 265 (28): 17281-4. PMID 2211625. Rosen V, Wozney JM, Wang EA, ... 16 (4): 1013-9. PMID 11642720. Kloen P, Di Paola M, Borens O, Richmond J, Perino G, Helfet DL, Goumans MJ (September 2003). " ... 9 (2): 283-9. doi:10.1016/0888-7543(91)90254-C. PMID 2004778. Paralkar VM, Nandedkar AK, Pointer RH, Kleinman HK, Reddi AH ( ... 20 (1-4): 313-9. doi:10.3109/03008208909023902. PMID 2612162. Wozney JM, Rosen V, Celeste AJ, Mitsock LM, Whitters MJ, Kriz RW ...
Kwok, H. H.; Yue, P. Y. K.; Mak, N. K.; Wong, R. N. S. (2012). "Ginsenoside Rb1 induces type I collagen expression through ... "Differences in osteoblast miRNA induced by cell binding domain of collagen and silicate-based synthetic bone". Journal of ... 84 (4): 532-9. doi:10.1016/j.bcp.2012.05.023. PMID 22692056. Nishida, N.; Nagahara, M.; Sato, T.; Mimori, K.; Sudo, T.; Tanaka ... 9 (7): 824-833. doi:10.1158/1541-7786.MCR-10-0529. PMID 21628394. Gunaratne, P. H.; Lin, Y. C.; Benham, A. L.; Drnevich, J.; ...
Its autophosphorylation is achieved by all collagens so far tested (type I to type VI). A closely related family member is the ... gene is a RTK that is widely expressed in normal and transformed epithelial cells and is activated by various types of collagen ... Vogel W, Gish GD, Alves F, Pawson T (Dec 1997). "The discoidin domain receptor tyrosine kinases are activated by collagen". ... Mohan RR, Mohan RR, Wilson SE (Jan 2001). "Discoidin domain receptor (DDR) 1 and 2: collagen-activated tyrosine kinase ...
"Early-onset degeneration of the intervertebral disc and vertebral end plate in mice deficient in type IX collagen". Arthritis ... "Decreased physical function and increased pain sensitivity in mice deficient for type IX collagen". Arthritis Rheum. 60 (9): ... understanding a role for collagen genetic mutations in onset of arthritis and intervertebral disc pathology, development of ... quantitative collagen organization, and proteoglycan concentration of articular cartilage following canine meniscectomy". ...
... has been shown to interact with: ASK1, Collagen, type I, alpha 1, Glucocorticoid receptor, SENP1, TXNIP. NF-κB - by ... "C-propeptide region of human pro alpha 1 type 1 collagen interacts with thioredoxin". Biochemical and Biophysical Research ... Plants have an unusually complex complement of Trxs composed of six well-defined types (Trxs f, m, x, y, h, and o) that reside ... 8 (9-10): 1635-50. doi:10.1089/ars.2006.8.1635. PMID 16987018. Yamamoto M, Yang G, Hong C, Liu J, Holle E, Yu X, Wagner T, ...
Assouti M, Vynios DH, Anagnostides ST, Papadopoulos G, Georgakopoulos CD, Gartaganis SP (Jan 2006). "Collagen type IX and HNK-1 ... doi:10.1016/S0014-5793(99)01287-9. PMID 10526176. Mitsumoto Y, Oka S, Sakuma H, Inazawa J, Kawasaki T (Apr 2000). "Cloning and ...
Burg MA, Tillet E, Timpl R, Stallcup WB (1996). "Binding of the NG2 proteoglycan to type VI collagen and other extracellular ... In human TN-C there exists, in addition to the eight constant repeats, nine extra repeats subject to alternative splicing. This ... In contrast, when these same cells use either α9β1 or αvβ6 integrins to adhere to the same third FN type III repeat, cell ... Tenascin C is a very diverse protein that can produce different functions within the same cell type. This myriad of functions ...
This is a receptor for collagen type I and IV. It consists of two subunits (α2 and β1). The α2 subunit includes a domain ... The leading role in the elimination of high-stress injury is taken by the GPIb-IX-V complex. The binding of von Willebrand ... Glycoprotein VI is one of the immunoglobulin superfamily type I transmembrane glycoproteins. It is an important collagen ... integrin upon release from keratinocytes migrating on type I collagen". J. Biol. Chem. (United States) 276 (31): 29368-74. DOI: ...
... has been shown to interact with: Beta-catenin, CDH1, CDH2, Collagen, type XVII, alpha 1, Cortactin, FYN, MUC1, Nephrin, ... tissue-specific expression of isoforms and molecular interactions with BP180/type XVII collagen". J. Cell. Biochem. 73 (3): 390 ... tissue-specific expression of isoforms and molecular interactions with BP180/type XVII collagen". J. Cell. Biochem. 73 (3): 390 ... 15 (9): 4819-24. doi:10.1128/mcb.15.9.4819. PMC 230726 . PMID 7651399. Ireton RC, Davis MA, van Hengel J, Mariner DJ, Barnes K ...
"COL9A1 collagen type IX alpha 1 [ Homo sapiens (human) ]". "COL9A2 collagen type IX alpha 2 [ Homo sapiens (human) ]". "COL9A3 ... COL9A1, COL9A2, COL9A3 are genes coding for collagen type IX, that is a component of hyaline cartilage. MATN3 protein may play ... collagen type IX alpha 3". "COMP cartilage oligomeric matrix protein [ Homo sapiens (human) ]". "MATN3 matrilin 3 [ Homo ... Types include: In the dominant form, mutations in five genes are causative: COMP (chromosome 19), COL9A1 (chromosome 6), COL9A2 ...
Minary-Jolandan, Majid; Yu, Min-Feng (2009). "Nanomechanical heterogeneity in the gap and overlap regions of type I collagen ... For example, bone has up to seven levels of biological organization, and the smallest level, i.e., single collagen fibril and ... For example, measurements have shown that nanomechanical heterogeneity exists even within single collagen fibrils as small as ... bone and its hierarchical constituents such as single collagen fibrils single living cells actin filaments and microtubules ...
The MMP-3 enzyme degrades collagen types II, III, IV, IX, and X, proteoglycans, fibronectin, laminin, and elastin. In addition ... In a study conducted using MMP-3 wild type (WT) and knockout (KO) mice, MMP-3 was shown to increase BBB permeability after ... Neutrophils carry MMP-9., which has also been shown to degrade occludin. This leads to further disruption of the BBB and BSCB ... 99 (21): 2717-9. doi:10.1161/01.cir.99.21.2717. PMID 10351963. Yoon S, Tromp G, Vongpunsawad S, Ronkainen A, Juvonen T, ...
Type-IV collagen is present in the basement membrane within normal lungs, and this is reduced in asthmatic patients. There are ... Tumstatin is a 28 kDa fragment cleaved from collagen type IV There are two subsegments of the peptide that are active; T3 ... Since tumstatin is cleaved by MMP from the collagen in the basement membrane, it has been found that there are much lower ... These studies suggest that tumstatin may be a viable treatment for many types of cancer, including but not limited to melanoma ...
By preventing polymerization of fibronectin, the deposition of collagen type I, another extracellular matrix protein, is also ... pUR4 is a recombinant peptide that is known to inhibit the polymerization of fibronectin in a number of cell types including ... 1074-9 (2009). Tomasini-Johansson, B. R., Kaufman, N. R., Ensenberger, M. G., Ozeri, V., Hanski, E., and Mosher, D. F. "A 49- ...
Research into synthetic collagen is ongoing; as of 2011, partial success has been achieved in replicating collagen's structure ... Instant types can be added to the food as they are; others need to be soaked in water beforehand. Gelatin is a mixture of ... Probably best known as a gelling agent in cooking, different types and grades of gelatin are used in a wide range of food and ... "Type A & B Process Definition". Vyse Gelatin Company. 26 October 2009. Archived from the original on 1 March 2015. Retrieved 16 ...
... type III collagen in the reticulin fibres of the vascular walls, type IX collagen, type IV collagen in the basement membranes ... The collagen portion is made up of 97-98% type I collagen, with small amounts of other types of collagen. These include type II ... type V collagen in the vascular walls, and type X collagen in the mineralized fibrocartilage near the interface with the bone.[ ... Fukuta, S.; Oyama, M.; Kavalkovich, K.; Fu, F. H.; Niyibizi, C. (1998). "Identification of types II, IX and X collagens at the ...
Several types of catenins work with N-cadherins to play an important role in learning and memory (For full article, see ... Spivey KA, Chung I, Banyard J, Adini I, Feldman HA, Zetter BR (October 2011). "A role for collagen XXIII in cancer cell ... For instance, higher levels of collagen XXIII have been associated with higher levels of catenins in cells. These heightened ... levels of collagen helped facilitate adhesions and anchorage-independent cell growth and provided evidence of collagen XXIII's ...
... show homology with the alpha chains of fibronectin and vitronectin receptors and collagen type IV". J. Leukoc. Biol. 51 (6): ... CD93 is a C-type lectin transmembrane receptor which plays a role not only in cell-cell adhesion processes but also in host ... All of them contain a C-type lectin domain, a series of epidermal growth factor like domains, a highly glycosylated mucin-like ... CD93 belongs to the Group XIV C-Type lectin family, a group containing two other members, endosialin (CD248) and thrombomodulin ...
... a minor fibrillar collagen. It is located on chromosome 6 very close to but… ... This gene encodes one of the two alpha chains of type XI collagen, ... Background of Collagen type XI alpha 2 chain antibody. This gene encodes one of the two alpha chains of type XI collagen, a ... Type XI collagen is a heterotrimer but the third alpha chain is a post-translationally modified alpha 1 type II chain. ...
Collagen XVIII/endostatin-deficient mice developed more severe glomerular and tubulointerstitial injury than wild-type mice. ... Collagen XVIII is a component of the highly specialized extracellular matrix. May 21, 2017. Norma Chavez ... Supplementing collagen XVIII-deficient mice with exogenous endostatin did not affect the progression of anti-GBM disease. Taken ... Collagen XVIII is a component of the highly specialized extracellular matrix associated with basement membranes of epithelia ...
alpha-1(IX) collagen chain. cartilage-specific short collagen. collagen IX, alpha-1 polypeptide. collagen, type IX, alpha 1. ... COL9A1 collagen type IX alpha 1 chain [Homo sapiens] COL9A1 collagen type IX alpha 1 chain [Homo sapiens]. Gene ID:1297 ... Type IX collagen is usually found in tissues containing type II collagen, a fibrillar collagen. Studies in knockout mice have ... Type IX collagen interacts with fibronectin providing an important molecular bridge in articular cartilage Title: Type IX ...
... in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type IX ... Type IX collagen, a heterotrimeric molecule, is usually found in tissues containing type II collagen, a fibrillar collagen. ... This gene encodes one of the three alpha chains of type IX collagen, the major collagen component of hyaline cartilage. ... "Entrez Gene: COL9A3 collagen, type IX, alpha 3". GeneReviews/NCBI/NIH/UW entry on Multiple Epiphyseal Dysplasia, Dominant ...
... in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type IX ... Type IX collagen is usually found in tissues containing type II collagen, a fibrillar collagen. Studies in knockout mice have ... 1989). "Molecular cloning of rat and human type IX collagen cDNA and localization of the alpha 1(IX) gene on the human ... This gene encodes one of the three alpha chains of type IX collagen, a collagen component of hyaline cartilage. ...
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collagen alpha-3(IX) chain; collagen, type IX, alpha 3. Orthologs:. Homo sapiens (human) : COL9A3 (collagen type IX alpha 3 ... collagen type IX alpha 3 chain) Sus scrofa (pig) : COL9A3 (collagen type IX alpha 3 chain) more info ... ... collagen type IX alpha 3 chain) Pan paniscus (bonobo/pygmy chimpanzee) : COL9A3 (collagen type IX alpha 3 chain) Ictidomys ... type IX, alpha 3) MGI Alliance Rattus norvegicus (Norway rat) : Col9a3 (collagen type IX alpha 3 chain) Alliance Chinchilla ...
Susceptibility of the cartilage collagens types II, IX and XI to degradation by the cysteine proteinases, cathepsins B and L.. ... types II, IX and XI, to degradation by the cysteine proteinases, cathepsins B and L. Both enzymes degrade these collagens at ... Publication type, MeSH terms, Substances. Publication type. *Research Support, Non-U.S. Govt ... Since these cathepsins can degrade cartilage collagens at pH values near neutrality, they may contribute to the destruction of ...
R R Dhawan, D C Beebe; Differential localization of collagen type IX isoform messenger RNAs during early ocular development.. ... Differential localization of collagen type IX isoform messenger RNAs during early ocular development. ... Differential localization of collagen type IX isoform messenger RNAs during early ocular development. ... PURPOSE: To determine the temporal and spatial localization of the messenger RNAs (mRNAs) for the two collagen alpha 1(IX) ...
The spatial distribution of type II and type IX collagen transcripts was analyzed by in situ hybridization. Type II collagen ... Type II collagen mRNA, cartilage proteoglycan core protein mRNA, alpha 2(IX) collagen mRNA, and transcripts of the short form ... Differential co-expression of long and short form type IX collagen transcripts during avian limb chondrogenesis in ovo ... Differential co-expression of long and short form type IX collagen transcripts during avian limb chondrogenesis in ovo ...
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... labelling with type II collagen antibodies. Results: With increasing age there is a progressive loss of type IX collagen and ... there is increasing exposure of type II collagen on the fibril surfaces with age. Conclusion: Type IX collagen and/or non- ... Vitreous Collagen Fibrils Lose Type IX Collagen and Other Surface Macromolecules During Ageing, thus Predisposing to Fibrillar ... Vitreous Collagen Fibrils Lose Type IX Collagen and Other Surface Macromolecules During Ageing, thus Predisposing to Fibrillar ...
Collagen types VI, IX bind integrin alpha10beta1 (Homo sapiens) * Collagen tupe VI network, Collagen type IX:Integrin ... Collagen type IX:Integrin alpha10beta1 [plasma membrane] (Bos taurus) Collagen tupe VI network, Collagen type IX:Integrin ... Collagen type IX:Integrin alpha10beta1 [plasma membrane] (Danio rerio) Collagen tupe VI network, Collagen type IX:Integrin ... Collagen type IX:Integrin alpha10beta1 [plasma membrane] (Rattus norvegicus) Collagen tupe VI network, Collagen type IX: ...
In contrast, MMP-9 expression was not up-regulated by treatment with Col-IV. These results demonstrate that Col-IV regulates ... In particular, MMP-2 and MMP-9 have been associated with the ability of tumor cells to metastasize due to their capacity to ... degrade type IV collagen (Col-IV), the main component of BM, and to their elevated expression in malignant tumors. However, ... Our results demonstrate that stimulation of MCF-7 cells with Col-IV promoted the secretion of MMP-9, as revealed by gelatin ...
Collagen types III, IV, V, VI, VIII, IX, XVI bind integrins alpha1beta1 and alpha2beta1 (Homo sapiens) * Collagen types III, IV ... Collagen types III, IV, V, VI, VIII, IX, XVI:Integrins alpha1beta 1, alpha2beta1 [plasma membrane] Stable Identifier ... Collagen types III, IV, V, VI, VIII, IX, XVI:Integrins alpha1beta 1, alpha2beta1 [plasma membrane] (Bos taurus) ... Collagen types III, IV, V, VI, VIII, IX, XVI:Integrins alpha1beta 1, alpha2beta1 [plasma membrane] (Canis familiaris) ...
... in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type IX ... Type IX collagen is usually found in tissues containing type II collagen, a fibrillar collagen. Studies in knockout mice have ... 1989). "Molecular cloning of rat and human type IX collagen cDNA and localization of the alpha 1(IX) gene on the human ... This gene encodes one of the three alpha chains of type IX collagen, a collagen component of hyaline cartilage. ...
Collagen IV (ColIV or Col4) is a type of collagen found primarily in the basal lamina. The collagen IV C4 domain at the C- ... Collagen IV is the more common usage, as opposed to the older terminology of "type-IV collagen".[citation needed] Collagen IV ... type IV collagen excretion reflects renal morphological alterations and type IV collagen expression in patients with type 2 ... Type III Procollagen, Type IV Collagen, Laminin, Tissue Inhibitor of Metalloproteinase, or Prolyl Hydroxylase?". Alcoholism: ...
Retrieved from "https://en.wikipedia.org/w/index.php?title=Collagen,_type_XX,_alpha_1&oldid=705418915" ...
... type IX, alpha 1, isoform CRA_b) contains a PF01391 domain.. Putative uncharacterized protein COL9A1 (Collagen, type IX, alpha ... type IX, alpha 1, isoform CRA_b) contains a PF01391 domain.. Putative uncharacterized protein COL9A1 (Collagen, type IX, alpha ... type IX, alpha 1, isoform CRA_b) contains a PF01391 domain.. Putative uncharacterized protein COL9A1 (Collagen, type IX, alpha ... type IX, alpha 1, isoform CRA_b) contains a PF01391 domain.. Putative uncharacterized protein COL9A1 (Collagen, type IX, alpha ...
Type IX collagen is a heterotrimeric collagen that associates with type II collagen fibrils and contains domains suited to ... Type IX collagen is crucial for normal hearing. Neuroscience 2005;132:493-500. 41. Suzuki N, Asamura K, Kikuchi Y, Takumi Y, ... Decreased physical function and increased pain sensitivity in mice deficient for type IX collagen.. код для вставки. код для ... The ␣2 type IX collagen tryptophan polymorphism is associated with the severity of disc degeneration in younger patients with ...
About 47% of these are collagen, 18% are anti-aging, and 12% are animal extract. A wide variety of collagen type ii options are ... chicken collagen type ii amino collagen c collagen granule firm up collagen cartilage collagen us collagen softgel oem collagen ... Tags: Undenatured Collagen Type Ii , Undenatured Collagen Type 2 , Collagen Type 2 Undenatured ... Tags: Food Addtive Ucii/collagen Type Ii , Hot Sell Ucii/collagen Type Ii , Ucii/collagen Type Ii ...
Genetic and Rare Diseases Information Center resources: Keratoconus Chiari Malformation Type 2 ... Study of the Safety and Effectiveness of Collagen Cross-Linking at an Irradiance of 9 mW/cm2 and 18 mW/cm2. The safety and ... Study of the Safety and Effectiveness of Photochemically Induced Collagen Cross-Linking at an Irradiance of 9 mW/cm2 and 18 mW/ ... The primary objective of this study is to determine the effectiveness and safety of corneal collagen cross-linking at ...
Collagen types I, II, III, V and XI self-assemble into D-periodic cross-striated fibrils. Here the D is approximately 67 nm and ... These form the most abundant collagens in vertebrates. ... There are 29 genetically distinct collagens present in animal ... IX. FACIT collagen, cartilage, assoc. with type II and XI fibrils. COL9A1, COL9A2, COL9A3. - EDM2 and EDM3. ... Type V collagen and type XI collagen are minor components of tissue and occur as fibrils with type I and type II collagen ...
Type IX collagen deficiency enhances the binding of cartilage-specific antibodies and arthritis severity. Arthritis Res Ther ... Characterization of the antibody response in mice with type II collagen-induced arthritis, using monoclonal anti-type II ... Type II collagen autoimmunity in animals and provocations leading to arthritis. Immunol Rev 1990; 118: 193-232.. Direct Link: ... Analysis of type I and IV collagens by FT-IR spectroscopy and imaging for a molecular investigation of skeletal muscle ...
The purified mass is dried to provide the desired Type I collagen product which may be ground into a powder or formed into a ... The enzyme-treated comminuted material which is rich in collagen is dispersed in an organic acid to cause the fibrillar mass to ... source such as poultry feet that incorporates a fibrillar mass of connective tissue as well as bony tissue to yield a collagen ... collagen matrix or sponge, depending on the end use therefor. ... A process for extracting type I collagen from an avian ...
  • Corrigendum to 'An injectable collagen-genipin-carbon dot hydrogel combined with photodynamic therapy to enhance chondrogenesis' Biomaterials 218 (2019) 119190. (bioportfolio.com)
  • Col9a1ⴚ/ⴚ and wild-type mice were investigated for reflexes, functional impairment (beam walking, pole climbing, wire hang, grip strength), sensorimotor skills (rotarod), mechanical sensitivity (von Frey hair), and thermal sensitivity (hot plate/tail flick). (docme.su)
  • Mice with inactivation of the Col9a1 gene, henceforth referred to as Col9a1⫺/⫺ mice, do not form functional type IX collagen molecules (12) and experience spontaneous development of premature cartilage degeneration (as early as 3 months) in the intervertebral disc, knee, and temporomandibular joint that worsens with age (up to 12 months) (12-14). (docme.su)
  • Nine of 23 human genes encoding MMPs are located in a cluster on chromosome 11, which implicate their haplotype-driven effects. (intechopen.com)
  • The primary objective of this study is to determine the effectiveness and safety of corneal collagen cross-linking at irradiance levels of 9 and 18 mW/cm2. (clinicaltrials.gov)
  • A study of corneal structure and biomechanical properties after collagen crosslinking with genipin in rabbit corneas. (bioportfolio.com)
  • Aim to assess the short-term effect of genipin collagen crosslinking (G-CXL) on corneal structure and biomechanical properties compared with ultraviolet A/riboflavin collagen crosslinking (UVA-CXL) in. (bioportfolio.com)
  • Female ApoE −/− mice on C57BL/6 background were immunized with α1α2 type IV collagen chain peptides linked to the immune-enhancer PADRE, PADRE alone or PBS at 12 weeks of age with three subsequent booster injections before the mice were killed at 23 weeks of age. (lu.se)
  • Immunization with peptides of α1α2 type IV collagen chains induced a strong IgG1antibody response against collagen type IV peptides without affecting the distribution of T cell populations, plasma cytokine or lipid levels. (lu.se)
  • Derived from chicken sternum cartilage, UC-II is a patented form of Undernatured (native) Type II Collagen that works with the immune system to support healthy joints. (iherb.com)
  • With age, the body's inability to produce and regenerate these collagen matrices leads to wear and tear on the joints, causing pain, stiffness, decreased function, and sometimes even deformities due to joint misalignments. (prweb.com)
  • Children with generalized hypermobility of the joints and musculoskeletal complaints frequently visit pediatric clinics, but many show no currently known collagen or other possibly related diseases. (aappublications.org)
  • NeoCell Super Collagen C provides hydrolyzed Collagen that is scientifically formulated for maximum absorption with other powerful beauty enhancing ingredients. (ebay.ca)
  • Super Collagen contains clinically studied BioActive NeoCell Collagen which supports healthy collagen formation throughout the body. (ebay.ca)
  • Serum Collagen Type IV for the Assessment of Fibrosis and Resistance to Interferon Therapy in Chronic Hepatitis C". Scandinavian Journal of Gastroenterology . (wikipedia.org)
  • Methods and Results -Confluent CMECs were exposed to IL-1 in serum-free medium for 24 hours, and cell-conditioned medium was assayed for plasminogen activator inhibitor type 1 (PAI-1), the primary physiological inhibitor of plasminogen activators, and for type 1 collagen with Western blotting. (ahajournals.org)
  • Interaction of collagen with serum complement: inhibition of complement-mediated hemolysis. (springer.com)
  • Anti-Collagen antibodies have been used for indirect trapping ELISA for quantitation of antigen in serum using a standard curve, for Immunoprecipitation and for native (non-denaturing, non-dissociating) PAGE and Western blotting for highly sensitive qualitative analysis. (acris-antibodies.com)
  • Recommended sample types are human EDTA plasma and serum. (olink.com)
  • Various concentrations of chitosan were used in the blend in order to study its effect on the morphology, chemical bond, tensile strength, burst pressure, hemocompatibility, and cell viability (cytotoxicity) of the tube.In vitro assessments indicated that addition of chitosan-collagen could improve cell viability and hemocompatibility. (mdpi.com)
  • Under small shear strains, {\em in vitro} collagen gels exhibit strain-stiffening while maintaining overall network integrity. (aps.org)
  • Our data indicate that both human gastric carcinoma cell lines synthesize type 1 collagen in vivo as well as in vitro and suggest that carcinoma cells may play an active role in the formation of stromal collagen in most human carcinomas. (aacrjournals.org)
  • Accordingly, the activity of the wild type RUNX2 promoter was decreased upon methylation treatment in vitro . (nature.com)
  • This gene encodes one of the three alpha chains of type IX collagen, which is a minor (5-20%) collagen component of hyaline cartilage. (nih.gov)
  • PURPOSE: To determine the temporal and spatial localization of the messenger RNAs (mRNAs) for the two collagen alpha 1(IX) isoforms during early development of the embryonic chicken eye. (arvojournals.org)
  • METHODS: The reverse transcription-polymerase chain reaction method was used to amplify mRNAs for the two collagen alpha 1(IX) isoforms. (arvojournals.org)
  • In later stages of development, mRNAs for both alpha 1(IX) chains were present predominantly in the presumptive ciliary epithelium. (arvojournals.org)
  • Type II collagen and the long form alpha 1(IX) collagen transcripts co-localized in the chondrogenic elements of the developing forelimb. (biologists.org)
  • In contrast, short form alpha 1(IX) collagen transcripts which lack the 5′ region encoding the NC4 globular amino-terminal domain were distributed throughout the non-chondrogenic, non-myogenic mesenchymal regions of the limb and were not detectable above background levels in the limb chondrogenic elements. (biologists.org)
  • The alpha-3 subunit (COL4A3) of collagen IV is thought to be the antigen implicated in Goodpasture syndrome , wherein the immune system attacks the basement membranes of the glomeruli and the alveoli upon the antigenic site on the alpha-3 subunit becomes unsequestered due to environmental exposures. (wikipedia.org)
  • Reacts with collagen, type IX, alpha 1. (novusbio.com)
  • transmembrane collagen, interacts with integrin a1b1, fibronectin and components of basement membranes like nidogen and perlecan. (news-medical.net)
  • Previous studies have shown that undenatured type II collagen (UC-II) is effective in the treatment of rheumatoid arthritis, and preliminary human and animal trials have shown it to be effective in treating osteoarthritis (OA). (medsci.org)
  • The two most common types of arthritis are osteoarthritis (OA) and rheumatoid arthritis (RA). (medsci.org)
  • One day Dr. Moore read about some studies on chicken collagen which showed that a small amount taken orally could have a preventive effect on rheumatoid arthritis. (prohealth.com)
  • The purified mass is dried to provide the desired Type I collagen product which may be ground into a powder or formed into a collagen matrix or sponge, depending on the end use therefor. (google.co.uk)
  • When Collagen Type I & III Powder is taken internally, the body receives the raw materials it needs to supplement the collagen found in all of these areas. (puritan.com)
  • Collagen Type I & III Powder is neutral in taste and specially formulated in an easy to take powdered form. (puritan.com)
  • To examine whether collagen type I α1 (COLIA1) Sp1 polymorphism is associated with osteoporosis and/or intervertebral disc degeneration in older people. (bmj.com)
  • Because both osteoporosis 7, 8 and intervertebral disc degeneration 9, 10 are largely genetically determined, it has been suggested that the inverse relationship may be attributed to a shared set of genetic factors underlying both disorders. (bmj.com)
  • Moreover, we demonstrate that network yielding is universally controlled by the ratio of the collagen thickness to the mesh size. (aps.org)
  • This result is invaluable for bioengineering fields, as this liquid crystal organization paves the way for the generation of collagen based bio-mimetic cornea matrices. (rsc.org)
  • Calcified points within collagen matrices show contrast in a moving display of blood and muscle, enabling methods of cardiac imaging technology to arrive at ratios essentially stating blood in ( cardiac input ) and blood out ( cardiac output ). (wikipedia.org)
  • Epidermal growth factor precursor (7-9 copies). (yale.edu)
  • It is a heterotrimer containing alpha1(IX), alpha2(IX) and alpha3(IX) subunits. (bioportfolio.com)
  • Collagen type XI is heterotrimer containing alpha1(XI), alpha2(XI) and alpha3(XI) subunits. (bioportfolio.com)
  • Greetings, I am looking for a plasmid probe with a cDNA sequence for Rat Type I collagen gene [alpha1(I) and/or alpha2(I)]. Does anyone know where I could get ahold of this probe - either a company or a laboratory? (bio.net)
  • We have investigated the susceptibility of both the helical and non-helical regions of isolated rat chondrosarcoma collagens, types II, IX and XI, to degradation by the cysteine proteinases, cathepsins B and L. Both enzymes degrade these collagens at temperatures from 20 to 37 degrees C and pH values from 3.5 to 7.0. (nih.gov)
  • Since these cathepsins can degrade cartilage collagens at pH values near neutrality, they may contribute to the destruction of cartilage observed in arthritis. (nih.gov)