Major component of chondrocyte EXTRACELLULAR MATRIX of various tissues including bone, tendon, ligament, SYNOVIUM and blood vessels. It binds MATRILIN PROTEINS and is associated with development of cartilage and bone.
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.
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).
An autosomal dominant disorder that is the most frequent form of short-limb dwarfism. Affected individuals exhibit short stature caused by rhizomelic shortening of the limbs, characteristic facies with frontal bossing and mid-face hypoplasia, exaggerated lumbar lordosis, limitation of elbow extension, GENU VARUM, and trident hand. (Online Mendelian Inheritance in Man, http://www.ncbi.nlm.nih.gov/Omim, MIM#100800, April 20, 2001)
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
Abnormal development of cartilage and bone.
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.
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.
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.
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.
Polymorphic cells that form cartilage.
A fibrillar collagen found predominantly in CARTILAGE and vitreous humor. It consists of three identical alpha1(II) chains.
The clear, viscous fluid secreted by the SYNOVIAL MEMBRANE. It contains mucin, albumin, fat, and mineral salts and serves to lubricate joints.
A highly glycosylated and sulfated phosphoprotein that is found almost exclusively in mineralized connective tissues. It is an extracellular matrix protein that binds to hydroxyapatite through polyglutamic acid sequences and mediates cell attachment through an RGD sequence.
Large HYALURONAN-containing proteoglycans found in articular cartilage (CARTILAGE, ARTICULAR). They form into aggregates that provide tissues with the capacity to resist high compressive and tensile forces.
Measurable and quantifiable biological parameters (e.g., specific enzyme concentration, specific hormone concentration, specific gene phenotype distribution in a population, presence of biological substances) which serve as indices for health- and physiology-related assessments, such as disease risk, psychiatric disorders, environmental exposure and its effects, disease diagnosis, metabolic processes, substance abuse, pregnancy, cell line development, epidemiologic studies, etc.
A family of related, adhesive glycoproteins which are synthesized, secreted, and incorporated into the extracellular matrix of a variety of cells, including alpha granules of platelets following thrombin activation and endothelial cells. They interact with a number of BLOOD COAGULATION FACTORS and anticoagulant factors. Five distinct forms have been identified, thrombospondin 1, -2, -3, -4, and cartilage oligomeric matrix protein (COMP). They are involved in cell adhesion, platelet aggregation, cell proliferation, angiogenesis, tumor metastasis, VASCULAR SMOOTH MUSCLE growth, and tissue repair.
A synovial hinge connection formed between the bones of the FEMUR; TIBIA; and PATELLA.
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)
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.
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.
A slowly growing malignant neoplasm derived from cartilage cells, occurring most frequently in pelvic bones or near the ends of long bones, in middle-aged and old people. Most chondrosarcomas arise de novo, but some may develop in a preexisting benign cartilaginous lesion or in patients with ENCHONDROMATOSIS. (Stedman, 25th ed)
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).
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.
A natural high-viscosity mucopolysaccharide with alternating beta (1-3) glucuronide and beta (1-4) glucosaminidic bonds. It is found in the UMBILICAL CORD, in VITREOUS BODY and in SYNOVIAL FLUID. A high urinary level is found in PROGERIA.
The formation of cartilage. This process is directed by CHONDROCYTES which continually divide and lay down matrix during development. It is sometimes a precursor to OSTEOGENESIS.
Glycoproteins which contain sialic acid as one of their carbohydrates. They are often found on or in the cell or tissue membranes and participate in a variety of biological activities.
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.
An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.
Fibrous bands or cords of CONNECTIVE TISSUE at the ends of SKELETAL MUSCLE FIBERS that serve to attach the MUSCLES to bones and other structures.
Injuries to the knee or the knee joint.
The physical state of supporting an applied load. This often refers to the weight-bearing bones or joints that support the body's weight, especially those in the spine, hip, knee, and foot.
Glycoproteins which have a very high polysaccharide content.
The inner membrane of a joint capsule surrounding a freely movable joint. It is loosely attached to the external fibrous capsule and secretes SYNOVIAL FLUID.
A specialized CONNECTIVE TISSUE that is the main constituent of the SKELETON. The principle cellular component of bone is comprised of OSTEOBLASTS; OSTEOCYTES; and OSTEOCLASTS, while FIBRILLAR COLLAGENS and hydroxyapatite crystals form the BONE MATRIX.
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.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
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.
The worsening of a disease over time. This concept is most often used for chronic and incurable diseases where the stage of the disease is an important determinant of therapy and prognosis.
Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.
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.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Pathological processes involving the chondral tissue (CARTILAGE).
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

Enhancement of cell adhesion and spreading by a cartilage-specific noncollagenous protein, cartilage matrix protein (CMP/Matrilin-1), via integrin alpha1beta1. (1/201)

Cartilage matrix protein (CMP; also known as matrilin-1), one of the major noncollagenous proteins in most cartilages, binds to aggrecan and type II collagen. We examined the effect of CMP on the adhesion of chondrocytes and fibroblasts using CMP-coated dishes. The CMP coating at 10-20 micrograms/ml enhanced the adhesion and spreading of rabbit growth plate, resting and articular chondrocytes, and fibroblasts and human epiphyseal chondrocytes and MRC5 fibroblasts. The effect of CMP on the spreading of chondrocytes was synergistically increased by native, but not heated, type II collagen (gelatin). The monoclonal antibody to integrin alpha1 or beta1 abolished CMP-induced cell adhesion and spreading, whereas the antibody to integrin alpha2, alpha3, alpha5, beta2, alpha5beta1, or alphaVbeta5 had little effect on cell adhesion or spreading. The antibody to integrin alpha1, but not to other subunits, coprecipitated 125I-CMP that was added to MRC5 cell lysates, indicating the association of CMP with the integrin alpha1 subunit. Unlabeled CMP competed for the binding to integrin alpha1 with 125I-CMP. These findings suggest that CMP is a potent adhesion factor for chondrocytes, particularly in the presence of type II collagen, and that integrin alpha1beta1 is involved in CMP-mediated cell adhesion and spreading. Since CMP is expressed almost exclusively in cartilage, this adhesion factor, unlike fibronectin or laminin, may play a special role in the development and remodeling of cartilage.  (+info)

Production of cartilage oligomeric matrix protein (COMP) by cultured human dermal and synovial fibroblasts. (2/201)

OBJECTIVE: Cartilage oligomeric matrix protein (COMP) is a large disulfide-linked pentameric protein. Each of its five subunits is approximately 100,000 Da in molecular weight. COMP was originally identified and characterized in cartilage and it has been considered a marker of cartilage metabolism because it is currently thought not to be present in other joint tissues, except for tendon. To confirm the tissue specificity of COMP expression we examined cultured human dermal fibroblasts, human foreskin fibroblasts, and normal human synovial cells for the synthesis of COMP in culture. METHOD: Normal synovial cells and normal human dermal foreskin fibroblasts were isolated from the corresponding tissues by sequential enzymatic digestions and cultured in media containing 10% fetal bovine serum until confluent. During the final 24 h of culture, the cells were labeled with 35S-methionine and 35S-cysteine in serum- and cysteine/methionine-free medium. The newly synthesized COMP molecules were immunoprecipitated from the culture media with a COMP-specific polyclonal antiserum, or with monoclonal antibodies or affinity-purified COMP antibodies. The immunoprecipitated COMP was analyzed by electrophoresis in 5.5% polyacrylamide gels. For other experiments, synovial cells cultured from the synovium of patients with rheumatoid arthritis (RA) and osteoarthritis (OA) were similarly examined. RESULTS: A comparison of the amounts of COMP produced by each cell type (corrected for the DNA content) revealed that synovial cells produced > or = 9 times more COMP than chondrocytes or dermal fibroblasts. COMP could be easily detected by immunoprecipitation in all cell types. Electrophoretic analysis revealed a distinct band with an apparent MW of 115-120 kDa in samples from each of the three cell types, regardless of the antibody used. COMP expression in cultures of synoviocytes derived from OA and RA patients showed that OA and RA synovial cells produced similar amounts of monomeric COMP of identical size to those COMP monomers produced by normal synovial cells. The addition of TGF-beta to these cultures resulted in an increase in COMP production in normal, OA and RA synovial cells (45, 116 and 115% respectively). CONCLUSION: These studies demonstrate that substantial amounts of COMP are produced by several mesenchymal cells including synoviocytes and dermal fibroblasts. These findings raise important concerns regarding the utility of measurements of COMP levels in serum or in synovial fluid as markers of articular cartilage degradation because of the likelihood that a substantial proportion of COMP or COMP fragments present in serum or synovial fluid may be produced by cells other than articular chondrocytes.  (+info)

Serum cartilage oligomeric matrix protein reflects osteoarthritis presence and severity: the Johnston County Osteoarthritis Project. (3/201)

OBJECTIVE: To characterize serum cartilage oligomeric matrix protein (COMP) levels by age and gender for a radiographically defined population free of hip and knee osteoarthritis (OA), and to examine the potential utility of COMP as a diagnostic biomarker for knee OA. METHODS: Serum samples and knee and hip radiographs were obtained at a baseline evaluation as part of the Johnston County Osteoarthritis Project, a population-based study of OA in rural North Carolina. A total of 291 Caucasian participants were randomly selected for COMP analysis, 143 patients with radiographic knee OA (Kellgren/Lawrence [K/L] grade > or = 2) and 148 controls with neither hip nor knee OA (K/L grade 0), evenly distributed by age and gender. COMP was quantified by competitive enzyme-linked immunosorbent assay with monoclonal antibody 17-C10. The natural log-transformed COMP data were analyzed using general linear models. RESULTS: Serum COMP levels were significantly elevated (P = 0.0001) in the age > or = 65 group (mean +/- SD 1,302.1 +/- 496.7 ng/ml) versus the age 45-54 and age 55-64 groups (1,058.1 +/- 432.4 and 1,038.6 +/- 313.3, respectively). Serum COMP levels of the OA group were significantly higher than those of the control group (1,208.57 +/- 487.47 ng/ml versus 1,061.83 +/- 370.58 ng/ml; P = 0.0093). Serum COMP levels also increased significantly with knee OA K/L grade (P = 0.0047), knee OA laterality (P = 0.0043), and number of knee and hip joints involved (P = 0.0001). There was no significant difference in serum COMP levels by gender or obesity. CONCLUSION: We demonstrate that in a population-based sample, serum COMP levels can distinguish an OA-affected subgroup from an unaffected subgroup and can reflect disease severity and multiple joint involvement in OA.  (+info)

A cartilage oligomeric matrix protein mutation associated with pseudoachondroplasia changes the structural and functional properties of the type 3 domain. (4/201)

Cartilage oligomeric matrix protein (COMP) is a member of the thrombospondin family of extracellular matrix glycoproteins. All members of the family contain a highly conserved region of thrombospondin type 3 sequence repeats that bind calcium. A mutation in COMP previously identified in a patient with pseudoachondroplasia resulted in abnormal sequestration of COMP in distinctive rER vesicles. The mutation, Asp-446 --> Asn, is located in the type 3 repeats of the molecule. This region was expressed in a mammalian culture with and without the mutation to study the structural or functional properties associated with the mutation. The biophysical parameters of the mutant peptide were compared with those of the wild type and revealed the following difference: secondary structural analysis by circular dichroism showed more alpha-helix content in the wild-type peptides. The calcium binding properties of the two peptides were significantly different; there were 17 calcium ions bound/wild-type COMP3 peptide compared with 8/mutant peptide. In addition, wild-type COMP3 had a higher affinity for calcium and bound calcium more cooperatively. Calcium bound by the wild-type peptide was reflected in a structural change as indicted by velocity sedimentation. Thus, the effect of the COMP mutation appears to profoundly alter the calcium binding properties and may account for the difference observed in the structure of the type 3 domain. Furthermore, the highly cooperative binding of calcium to COMP3 suggests that these type 3 sequence repeats form a single protein domain, the thrombospondin type 3 domain.  (+info)

Autoreactivity against matrilin-1 in a patient with relapsing polychondritis. (5/201)

Relapsing polychondritis (RP) is a rare inflammatory disease of cartilage. Chondritis of the auricular, nasal, and tracheal cartilages predominates in this disease, suggesting a response to a tissue-specific antigen. One potential antigen is matrilin-1, a cartilage matrix protein found uniquely in the tracheal, auricular, and nasal cartilage of adults. We describe herein a patient with RP who had both a humoral and a cellular immune response directed toward the cartilage matrix protein matrilin-1.  (+info)

Molecular cloning and expression patterns of mouse cartilage oligomeric matrix protein gene. (6/201)

OBJECTIVE: To develop transgenic mice harboring mutations in the COMP gene as animal models for pseudoachondroplasia (PSACH) and multiple epiphyseal dysplasia (MED), autosomal dominant disorders characterized by early onset osteoarthritis and epiphyseal abnormalities. As a first step in generating a mouse model for COMP mutations, we have cloned the cDNA of mouse COMP and examined its tissue expression pattern. DESIGN: Total mRNA was isolated from the skeletal tissues of newborn C57BL/6j mice and used as a template for oligo(dT) first-strand cDNA synthesis. The cDNA was used for PCR amplification of COMP using three oligonucleotide primer pairs designed from the published rat COMP cDNA sequence. Nested PCR was used to complete the sequence between the amplified fragments. The entire cDNA was sequenced and the expression pattern of the corresponding transcripts examined by Northern hybridizations. RESULTS: A full-length COMP cDNA was isolated. Analysis showed that the entire translated region of the mouse COMP gene is 2268 bp and the derived amino acid sequence shows 90% homology to human COMP. Of eight adult mouse non-cartilage tissues tested, COMP expression was detected only in testis.  (+info)

Pseudoachondroplastic dysplasia: an Iowa review from human to mouse. (7/201)

Lamellar inclusions of the rough endoplasmic reticulum in growth plate chondrocytes, first identified (1972) in the Department of Orthopaedic Surgery, University of Iowa, has become the cytochemical hallmark for the pseudoachondroplastic dysplasia (PSACH) phenotype, linking an endoplasmic reticulum storage disorder with the osteochondrodysplasia. Since this original observation, great advances have been made, leading to the molecular understanding of this altered longitudinal bone growth anomaly. A PSACH canine model suggested that abatement of cumulative vertical growth of growth plate chondrocytes seen in PSACH results from (1) altered extracellular matrix constraints for horizontal growth and (2) uncoupling of endochondral and perichondral growth that causes metaphyseal flaring. PSACH, an autosomal dominant disease, is linked to mutation of the cartilage oligomeric matrix protein (COMP) gene. Amino acid substitutions, deletions, or additions is proposed to alter COMP structure that cause its retention in the rough endoplasmic reticulum of growth plate chondrocytes, leading to (1) compositional and structural change of the extracellular matrix, and (2) altered cellular proliferation and volume expansion. Normal growth and development occurs in COMP gene knockout mice that do not synthesis COMP, demonstrating that a mutant COMP, not absence of COMP, is required for the PSACH phenotype. The mechanism by which mutant COMP induces a PSACH phenotype remains to be elucidated. At the University of Iowa a cell culture system has been developed whereby mutant COMP transgenes are introduced into chondrocytes and the expressed product COMP is retained in the endoplasmic reticulum. This readily manipulated system makes it possible to decipher systematically the system's cellular secretory processing pathway, in order to clarify the mechanism(s) by which the mutant COMP is retained within the endoplasmic reticulum. Concurrent with this is the development of transgenic mice expressing the mutant COMP used in the cell culture system. This will make it possible to establish that expression of a human PSACH-linked mutant COMP will produce a PSACH phenotype. A PSACH animal model will provide a means to characterize the mechanism of altered longitudinal bone growth and to test gene therapy approaches for correcting the anomaly.  (+info)

Cartilage oligomeric matrix protein is a calcium-binding protein, and a mutation in its type 3 repeats causes conformational changes. (8/201)

Mutations in residues in the type 3 calcium-binding repeats and COOH-terminal globular region of cartilage oligomeric matrix protein (COMP) lead to two skeletal dysplasias, pseudoachondroplasia and multiple epiphyseal dysplasia. It has been hypothesized that these mutations cause COMP to misfold and to be retained in the endoplasmic reticulum. However, this hypothesis is not supported by previous reports that COMP, when purified in the presence of EDTA, shows no obvious difference in electron microscopic appearance in the presence or absence of calcium ions. Since this discrepancy may be due to the removal of calcium during purification, we have expressed wild-type COMP and the most common mutant form found in pseudoachondroplasia, MUT3, using a mammalian expression system and have purified both proteins in the presence of calcium. Both proteins are expressed as pentamers. Direct calcium binding experiments demonstrate that wild-type COMP, when purified in the presence of calcium, is a calcium-binding protein. Rotary shadowing electron microscopy and limited trypsin digestion at various calcium concentrations show that there are conformational changes associated with calcium binding to COMP. Whereas COMP exists in a more compact conformation in the presence of calcium, it shows a more extended conformation when calcium is removed. MUT3, with a single aspartic acid deletion in the type 3 repeats, binds less calcium and presents an intermediate conformation between the calcium-replete and calcium-depleted forms of COMP. In conclusion, we show that a single mutation in the type 3 repeats of COMP causes the mutant protein to misfold. Our data demonstrate the importance of calcium binding to the structure of COMP and provide a plausible explanation for the observation that mutations in the type 3 repeats and COOH-terminal globular region lead to pseudoachondroplasia.  (+info)

Cartilage oligomeric matrix protein (COMP) is a extracellular matrix protein that is found in high concentrations in cartilaginous tissues, such as articular cartilage and intervertebral discs. It is a member of the thrombospondin family and plays a role in the organization and stability of the extracellular matrix.
It is also known to be involved in the process of osteoarthritis, a degenerative joint disease. High levels of COMP are found in the synovial fluid of patients with osteoarthritis, and it is thought to contribute to the breakdown of cartilage. Additionally, genetic variations in the COMP gene have been associated with an increased risk of developing osteoarthritis.
It also plays a role in bone development and repair, as well as in the regulation of cell growth and differentiation.

Matrilin proteins are a group of extracellular matrix (ECM) proteins that are predominantly found in cartilaginous tissues, such as articular cartilage, costal cartilage, and intervertebral discs. They belong to the von Willebrand factor A (vWF-A) domain-containing protein family and play important roles in maintaining the structural integrity and organization of the ECM.

Matrilin proteins are composed of multiple domains, including vWF-A domains, coiled-coil domains, and calcium-binding epidermal growth factor (cbEGF)-like domains. They can form multimeric complexes through their coiled-coil domains, which helps to stabilize the ECM network.

There are four known matrilin proteins in humans, designated as Matrilin-1, Matrilin-2, Matrilin-3, and Matrilin-4. Each of these proteins has distinct tissue distribution patterns and functions. For example, Matrilin-1 is primarily found in hyaline cartilage and is involved in regulating chondrocyte differentiation and matrix assembly. Matrilin-2 is widely expressed in various tissues, including cartilage, tendon, and ligament, and plays a role in maintaining the organization of collagen fibrils. Matrilin-3 is specifically expressed in articular cartilage and is involved in regulating the formation and maintenance of the cartilaginous matrix. Matrilin-4 is found in both hyaline and fibrocartilage, as well as in tendons and ligaments, and has been implicated in regulating collagen fibrillogenesis and tissue development.

Mutations in matrilin genes have been associated with various musculoskeletal disorders, such as multiple epiphyseal dysplasia (MED) and spondyloepimetaphyseal dysplasia (SEMD). These genetic defects can lead to abnormalities in the structure and organization of the ECM, resulting in joint pain, stiffness, and reduced mobility.

Extracellular matrix (ECM) proteins are a group of structural and functional molecules that provide support, organization, and regulation to the cells in tissues and organs. The ECM is composed of a complex network of proteins, glycoproteins, and carbohydrates that are secreted by the cells and deposited outside of them.

ECM proteins can be classified into several categories based on their structure and function, including:

1. Collagens: These are the most abundant ECM proteins and provide strength and stability to tissues. They form fibrils that can withstand high tensile forces.
2. Proteoglycans: These are complex molecules made up of a core protein and one or more glycosaminoglycan (GAG) chains. The GAG chains attract water, making proteoglycans important for maintaining tissue hydration and resilience.
3. Elastin: This is an elastic protein that allows tissues to stretch and recoil, such as in the lungs and blood vessels.
4. Fibronectins: These are large glycoproteins that bind to cells and ECM components, providing adhesion, migration, and signaling functions.
5. Laminins: These are large proteins found in basement membranes, which provide structural support for epithelial and endothelial cells.
6. Tenascins: These are large glycoproteins that modulate cell adhesion and migration, and regulate ECM assembly and remodeling.

Together, these ECM proteins create a microenvironment that influences cell behavior, differentiation, and function. Dysregulation of ECM proteins has been implicated in various diseases, including fibrosis, cancer, and degenerative disorders.

Achondroplasia is a genetic disorder that affects bone growth, leading to dwarfism. It is the most common form of short-limbed dwarfism and is caused by a mutation in the FGFR3 gene. This mutation results in impaired endochondral ossification, which is the process by which cartilage is converted into bone.

People with achondroplasia have a characteristic appearance, including:

* Short stature (typically less than 4 feet, 4 inches tall)
* Disproportionately short arms and legs
* Large head with a prominent forehead and flat nasal bridge
* Short fingers with a gap between the middle and ring fingers (known as a trident hand)
* Bowing of the lower legs
* A swayed back (lordosis)

Achondroplasia is usually inherited in an autosomal dominant manner, which means that a child has a 50% chance of inheriting the disorder if one parent has it. However, about 80% of cases result from new mutations in the FGFR3 gene and occur in people with no family history of the condition.

While achondroplasia can cause various medical issues, such as breathing difficulties, ear infections, and spinal cord compression, most individuals with this condition have normal intelligence and a typical lifespan. Treatment typically focuses on managing specific symptoms and addressing any related complications.

Glycoproteins are complex proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. These glycans are linked to the protein through asparagine residues (N-linked) or serine/threonine residues (O-linked). Glycoproteins play crucial roles in various biological processes, including cell recognition, cell-cell interactions, cell adhesion, and signal transduction. They are widely distributed in nature and can be found on the outer surface of cell membranes, in extracellular fluids, and as components of the extracellular matrix. The structure and composition of glycoproteins can vary significantly depending on their function and location within an organism.

Osteochondrodysplasias are a group of genetic disorders that affect the development of bones and cartilage. These conditions can result in dwarfism or short stature, as well as other skeletal abnormalities. Osteochondrodysplasias can be caused by mutations in genes that regulate bone and cartilage growth, and they are often characterized by abnormalities in the shape, size, and/or structure of the bones and cartilage.

There are many different types of osteochondrodysplasias, each with its own specific symptoms and patterns of inheritance. Some common examples include achondroplasia, thanatophoric dysplasia, and spondyloepiphyseal dysplasia. These conditions can vary in severity, and some may be associated with other health problems, such as respiratory difficulties or neurological issues.

Treatment for osteochondrodysplasias typically focuses on managing the symptoms and addressing any related health concerns. This may involve physical therapy, bracing or surgery to correct skeletal abnormalities, and treatment for any associated medical conditions. In some cases, genetic counseling may also be recommended for individuals with osteochondrodysplasias and their families.

Cartilage is a type of connective tissue that is found throughout the body in various forms. It is made up of specialized cells called chondrocytes, which are embedded in a firm, flexible matrix composed of collagen fibers and proteoglycans. This unique structure gives cartilage its characteristic properties of being both strong and flexible.

There are three main types of cartilage in the human body: hyaline cartilage, elastic cartilage, and fibrocartilage.

1. Hyaline cartilage is the most common type and is found in areas such as the articular surfaces of bones (where they meet to form joints), the nose, trachea, and larynx. It has a smooth, glassy appearance and provides a smooth, lubricated surface for joint movement.
2. Elastic cartilage contains more elastin fibers than hyaline cartilage, which gives it greater flexibility and resilience. It is found in structures such as the external ear and parts of the larynx and epiglottis.
3. Fibrocartilage has a higher proportion of collagen fibers and fewer chondrocytes than hyaline or elastic cartilage. It is found in areas that require high tensile strength, such as the intervertebral discs, menisci (found in joints like the knee), and the pubic symphysis.

Cartilage plays a crucial role in supporting and protecting various structures within the body, allowing for smooth movement and providing a cushion between bones to absorb shock and prevent wear and tear. However, cartilage has limited capacity for self-repair and regeneration, making damage or degeneration of cartilage tissue a significant concern in conditions such as osteoarthritis.

Collagen type IX is a type of collagen that is found in the extracellular matrix, particularly in the cartilage and vitreous humor of the eye. It is a heterotrimeric protein made up of three alpha chains (alpha1, alpha2, and alpha3), which are encoded by different genes (COL9A1, COL9A2, and COL9A3). Collagen type IX is thought to play a role in the organization and stability of collagen fibrils, as well as in the interaction between collagen and other extracellular matrix components. It has been implicated in various connective tissue disorders, such as Stickler syndrome and Marshall syndrome.

Articular cartilage is the smooth, white tissue that covers the ends of bones where they come together to form joints. It provides a cushion between bones and allows for smooth movement by reducing friction. Articular cartilage also absorbs shock and distributes loads evenly across the joint, protecting the bones from damage. It is avascular, meaning it does not have its own blood supply, and relies on the surrounding synovial fluid for nutrients. Over time, articular cartilage can wear down or become damaged due to injury or disease, leading to conditions such as osteoarthritis.

Osteoarthritis (OA) is a type of joint disease that is characterized by the breakdown and eventual loss of cartilage - the tissue that cushions the ends of bones where they meet in the joints. This breakdown can cause the bones to rub against each other, causing pain, stiffness, and loss of mobility. OA can occur in any joint, but it most commonly affects the hands, knees, hips, and spine. It is often associated with aging and can be caused or worsened by obesity, injury, or overuse.

The medical definition of osteoarthritis is: "a degenerative, non-inflammatory joint disease characterized by the loss of articular cartilage, bone remodeling, and the formation of osteophytes (bone spurs). It is often associated with pain, stiffness, and decreased range of motion in the affected joint."

Chondrocytes are the specialized cells that produce and maintain the extracellular matrix of cartilage tissue. They are responsible for synthesizing and secreting the collagen fibers, proteoglycans, and other components that give cartilage its unique properties, such as elasticity, resiliency, and resistance to compression. Chondrocytes are located within lacunae, or small cavities, in the cartilage matrix, and they receive nutrients and oxygen through diffusion from the surrounding tissue fluid. They are capable of adapting to changes in mechanical stress by modulating the production and organization of the extracellular matrix, which allows cartilage to withstand various loads and maintain its structural integrity. Chondrocytes play a crucial role in the development, maintenance, and repair of cartilaginous tissues throughout the body, including articular cartilage, costal cartilage, and growth plate cartilage.

Collagen Type II is a specific type of collagen that is a major component of the extracellular matrix in articular cartilage, which is the connective tissue that covers and protects the ends of bones in joints. It is also found in other tissues such as the vitreous humor of the eye and the inner ear.

Collagen Type II is a triple helix molecule composed of three polypeptide chains that contain a high proportion of the amino acids proline and hydroxyproline. This type of collagen provides structural support and elasticity to tissues, and it also plays a role in the regulation of cell behavior and signaling.

Collagen Type II is a target for autoimmune responses in conditions such as rheumatoid arthritis, where the immune system mistakenly attacks the body's own collagen, leading to joint inflammation and damage. It is also a common component of various dietary supplements and therapies used to support joint health and treat osteoarthritis.

Synovial fluid is a viscous, clear, and straw-colored fluid found in the cavities of synovial joints, bursae, and tendon sheaths. It is produced by the synovial membrane, which lines the inner surface of the capsule surrounding these structures.

The primary function of synovial fluid is to reduce friction between articulating surfaces, providing lubrication for smooth and painless movement. It also acts as a shock absorber, protecting the joints from external forces during physical activities. Synovial fluid contains nutrients that nourish the articular cartilage, hyaluronic acid, which provides its viscoelastic properties, and lubricin, a protein responsible for boundary lubrication.

Abnormalities in synovial fluid composition or volume can indicate joint-related disorders, such as osteoarthritis, rheumatoid arthritis, gout, infection, or trauma. Analysis of synovial fluid is often used diagnostically to determine the underlying cause of joint pain, inflammation, or dysfunction.

Integrin-binding sialoprotein (IBSP) is a non-collagenous protein found in bones and teeth. It is also known as bone sialoprotein II or acidic glycoprotein 34. IBSP plays a role in the regulation of biomineralization, which is the process by which minerals are deposited in biological tissues.

IBSP contains several functional domains that allow it to interact with other proteins and molecules. One such domain is an arginine-glycine-aspartic acid (RGD) motif, which can bind to integrin receptors on the surface of cells. This interaction helps regulate the attachment and behavior of cells in bone tissue.

IBSP also contains a large number of sialic acid residues, which give it its name and contribute to its negative charge. These residues may play a role in protecting the protein from degradation and helping it interact with other molecules in the extracellular matrix.

Overall, IBSP is an important component of bone tissue and plays a key role in regulating the formation and maintenance of bones and teeth.

Aggrecan is a large, complex proteoglycan molecule found in the extracellular matrix of articular cartilage and other connective tissues. It is a key component of the structural framework of these tissues, helping to provide resiliency, cushioning, and protection to the cells within. Aggrecan contains numerous glycosaminoglycan (GAG) chains, which are negatively charged molecules that attract water and ions, creating a swelling pressure that contributes to the tissue's load-bearing capacity.

The medical definition of 'Aggrecans' can be described as:

1. A large proteoglycan molecule found in articular cartilage and other connective tissues.
2. Composed of a core protein with attached glycosaminoglycan (GAG) chains, primarily chondroitin sulfate and keratan sulfate.
3. Plays a crucial role in the biomechanical properties of articular cartilage by attracting water and ions, creating a swelling pressure that contributes to the tissue's load-bearing capacity.
4. Aggrecan degradation or loss is associated with various joint diseases, such as osteoarthritis, due to reduced structural integrity and shock-absorbing capabilities of articular cartilage.

A biological marker, often referred to as a biomarker, is a measurable indicator that reflects the presence or severity of a disease state, or a response to a therapeutic intervention. Biomarkers can be found in various materials such as blood, tissues, or bodily fluids, and they can take many forms, including molecular, histologic, radiographic, or physiological measurements.

In the context of medical research and clinical practice, biomarkers are used for a variety of purposes, such as:

1. Diagnosis: Biomarkers can help diagnose a disease by indicating the presence or absence of a particular condition. For example, prostate-specific antigen (PSA) is a biomarker used to detect prostate cancer.
2. Monitoring: Biomarkers can be used to monitor the progression or regression of a disease over time. For instance, hemoglobin A1c (HbA1c) levels are monitored in diabetes patients to assess long-term blood glucose control.
3. Predicting: Biomarkers can help predict the likelihood of developing a particular disease or the risk of a negative outcome. For example, the presence of certain genetic mutations can indicate an increased risk for breast cancer.
4. Response to treatment: Biomarkers can be used to evaluate the effectiveness of a specific treatment by measuring changes in the biomarker levels before and after the intervention. This is particularly useful in personalized medicine, where treatments are tailored to individual patients based on their unique biomarker profiles.

It's important to note that for a biomarker to be considered clinically valid and useful, it must undergo rigorous validation through well-designed studies, including demonstrating sensitivity, specificity, reproducibility, and clinical relevance.

Thrombospondins (TSPs) are a family of multifunctional glycoproteins that are involved in various biological processes, including cell adhesion, migration, proliferation, differentiation, and angiogenesis. They were initially identified as calcium-binding proteins that are secreted by platelets during blood clotting (thrombosis), hence the name thrombospondin.

There are five members in the TSP family, designated as TSP-1 to TSP-5, and they share a common structure consisting of several domains, including an N-terminal domain, a series of type 1 repeats, a type 2 (von Willebrand factor C) repeat, a type 3 repeat, and a C-terminal domain.

TSP-1 and TSP-2 are secreted proteins that have been extensively studied for their roles in the regulation of angiogenesis, the process of new blood vessel formation. They bind to various extracellular matrix components, growth factors, and cell surface receptors, and can either promote or inhibit angiogenesis depending on the context.

TSP-3 to TSP-5 are expressed in a variety of tissues and play roles in cell adhesion, migration, and differentiation. They have been implicated in various pathological conditions, including cancer, fibrosis, and neurodegenerative diseases.

Overall, thrombospondins are important regulators of extracellular matrix dynamics and cell-matrix interactions, and their dysregulation has been associated with a variety of diseases.

The knee joint, also known as the tibiofemoral joint, is the largest and one of the most complex joints in the human body. It is a synovial joint that connects the thighbone (femur) to the shinbone (tibia). The patella (kneecap), which is a sesamoid bone, is located in front of the knee joint and helps in the extension of the leg.

The knee joint is made up of three articulations: the femorotibial joint between the femur and tibia, the femoropatellar joint between the femur and patella, and the tibiofibular joint between the tibia and fibula. These articulations are surrounded by a fibrous capsule that encloses the synovial membrane, which secretes synovial fluid to lubricate the joint.

The knee joint is stabilized by several ligaments, including the medial and lateral collateral ligaments, which provide stability to the sides of the joint, and the anterior and posterior cruciate ligaments, which prevent excessive forward and backward movement of the tibia relative to the femur. The menisci, which are C-shaped fibrocartilaginous structures located between the femoral condyles and tibial plateaus, also help to stabilize the joint by absorbing shock and distributing weight evenly across the articular surfaces.

The knee joint allows for flexion, extension, and a small amount of rotation, making it essential for activities such as walking, running, jumping, and sitting.

Osteoarthritis (OA) of the knee is a degenerative joint disease that affects the articular cartilage and subchondral bone in the knee joint. It is characterized by the breakdown and eventual loss of the smooth, cushioning cartilage that covers the ends of bones and allows for easy movement within joints. As the cartilage wears away, the bones rub against each other, causing pain, stiffness, and limited mobility. Osteoarthritis of the knee can also lead to the formation of bone spurs (osteophytes) and cysts in the joint. This condition is most commonly found in older adults, but it can also occur in younger people as a result of injury or overuse. Risk factors include obesity, family history, previous joint injuries, and repetitive stress on the knee joint. Treatment options typically include pain management, physical therapy, and in some cases, surgery.

Collagen type XII is a type of collagen that is found in the extracellular matrix of various tissues, including tendons, ligaments, and skin. It is a fibril-associated collagen that is closely associated with collagens type I and III. Collagen type XII has been shown to play a role in regulating the organization and diameter of collagen fibrils. Mutations in the gene for collagen type XII have been associated with certain types of muscular dystrophy and Bethlem myopathy, which are genetic disorders that affect muscle strength and tone. Additionally, it has been suggested to play a role in the development of osteoarthritis.

The extracellular matrix (ECM) is a complex network of biomolecules that provides structural and biochemical support to cells in tissues and organs. It is composed of various proteins, glycoproteins, and polysaccharides, such as collagens, elastin, fibronectin, laminin, and proteoglycans. The ECM plays crucial roles in maintaining tissue architecture, regulating cell behavior, and facilitating communication between cells. It provides a scaffold for cell attachment, migration, and differentiation, and helps to maintain the structural integrity of tissues by resisting mechanical stresses. Additionally, the ECM contains various growth factors, cytokines, and chemokines that can influence cellular processes such as proliferation, survival, and differentiation. Overall, the extracellular matrix is essential for the normal functioning of tissues and organs, and its dysregulation can contribute to various pathological conditions, including fibrosis, cancer, and degenerative diseases.

Chondrosarcoma is a type of cancer that develops in the cartilaginous tissue, which is the flexible and smooth connective tissue found in various parts of the body such as the bones, ribs, and nose. It is characterized by the production of malignant cartilage cells that can invade surrounding tissues and spread to other parts of the body (metastasis).

Chondrosarcomas are typically slow-growing tumors but can be aggressive in some cases. They usually occur in adults over the age of 40, and men are more commonly affected than women. The most common sites for chondrosarcoma development include the bones of the pelvis, legs, and arms.

Treatment for chondrosarcoma typically involves surgical removal of the tumor, along with radiation therapy or chemotherapy in some cases. The prognosis for chondrosarcoma depends on several factors, including the size and location of the tumor, the grade of malignancy, and whether it has spread to other parts of the body.

Collagen is the most abundant protein in the human body, and it is a major component of connective tissues such as tendons, ligaments, skin, and bones. Collagen provides structure and strength to these tissues and helps them to withstand stretching and tension. It is made up of long chains of amino acids, primarily glycine, proline, and hydroxyproline, which are arranged in a triple helix structure. There are at least 16 different types of collagen found in the body, each with slightly different structures and functions. Collagen is important for maintaining the integrity and health of tissues throughout the body, and it has been studied for its potential therapeutic uses in various medical conditions.

Rheumatoid arthritis (RA) is a systemic autoimmune disease that primarily affects the joints. It is characterized by persistent inflammation, synovial hyperplasia, and subsequent damage to the articular cartilage and bone. The immune system mistakenly attacks the body's own tissues, specifically targeting the synovial membrane lining the joint capsule. This results in swelling, pain, warmth, and stiffness in affected joints, often most severely in the hands and feet.

RA can also have extra-articular manifestations, affecting other organs such as the lungs, heart, skin, eyes, and blood vessels. The exact cause of RA remains unknown, but it is believed to involve a complex interplay between genetic susceptibility and environmental triggers. Early diagnosis and treatment are crucial in managing rheumatoid arthritis to prevent joint damage, disability, and systemic complications.

Hyaluronic acid is a glycosaminoglycan, a type of complex carbohydrate, that is naturally found in the human body. It is most abundant in the extracellular matrix of soft connective tissues, including the skin, eyes, and joints. Hyaluronic acid is known for its remarkable capacity to retain water, which helps maintain tissue hydration, lubrication, and elasticity. Its functions include providing structural support, promoting wound healing, and regulating cell growth and differentiation. In the medical field, hyaluronic acid is often used in various forms as a therapeutic agent for conditions like osteoarthritis, dry eye syndrome, and skin rejuvenation.

Chondrogenesis is the process of cartilage formation during embryonic development and in the healing of certain types of injuries. It involves the differentiation of mesenchymal stem cells into chondrocytes, which are the specialized cells that produce and maintain the extracellular matrix of cartilage.

During chondrogenesis, the mesenchymal stem cells condense and form a template for the future cartilaginous tissue. These cells then differentiate into chondrocytes, which begin to produce and deposit collagen type II, proteoglycans, and other extracellular matrix components that give cartilage its unique biochemical and mechanical properties.

Chondrogenesis is a critical process for the development of various structures in the body, including the skeletal system, where it plays a role in the formation of articular cartilage, growth plates, and other types of cartilage. Understanding the molecular mechanisms that regulate chondrogenesis is important for developing therapies to treat cartilage injuries and degenerative diseases such as osteoarthritis.

Sialglycoproteins are a type of glycoprotein that have sialic acid as the terminal sugar in their oligosaccharide chains. These complex molecules are abundant on the surface of many cell types and play important roles in various biological processes, including cell recognition, cell-cell interactions, and protection against proteolytic degradation.

The presence of sialic acid on the outermost part of these glycoproteins makes them negatively charged, which can affect their interaction with other molecules such as lectins, antibodies, and enzymes. Sialglycoproteins are also involved in the regulation of various physiological functions, including blood coagulation, inflammation, and immune response.

Abnormalities in sialglycoprotein expression or structure have been implicated in several diseases, such as cancer, autoimmune disorders, and neurodegenerative conditions. Therefore, understanding the biology of sialoglycoproteins is important for developing new diagnostic and therapeutic strategies for these diseases.

Collagen Type I is the most abundant form of collagen in the human body, found in various connective tissues such as tendons, ligaments, skin, and bones. It is a structural protein that provides strength and integrity to these tissues. Collagen Type I is composed of three alpha chains, two alpha-1(I) chains, and one alpha-2(I) chain, arranged in a triple helix structure. This type of collagen is often used in medical research and clinical applications, such as tissue engineering and regenerative medicine, due to its excellent mechanical properties and biocompatibility.

An Enzyme-Linked Immunosorbent Assay (ELISA) is a type of analytical biochemistry assay used to detect and quantify the presence of a substance, typically a protein or peptide, in a liquid sample. It takes its name from the enzyme-linked antibodies used in the assay.

In an ELISA, the sample is added to a well containing a surface that has been treated to capture the target substance. If the target substance is present in the sample, it will bind to the surface. Next, an enzyme-linked antibody specific to the target substance is added. This antibody will bind to the captured target substance if it is present. After washing away any unbound material, a substrate for the enzyme is added. If the enzyme is present due to its linkage to the antibody, it will catalyze a reaction that produces a detectable signal, such as a color change or fluorescence. The intensity of this signal is proportional to the amount of target substance present in the sample, allowing for quantification.

ELISAs are widely used in research and clinical settings to detect and measure various substances, including hormones, viruses, and bacteria. They offer high sensitivity, specificity, and reproducibility, making them a reliable choice for many applications.

A tendon is the strong, flexible band of tissue that connects muscle to bone. It helps transfer the force produced by the muscle to allow various movements of our body parts. Tendons are made up of collagen fibers arranged in parallel bundles and have a poor blood supply, making them prone to injuries and slow to heal. Examples include the Achilles tendon, which connects the calf muscle to the heel bone, and the patellar tendon, which connects the kneecap to the shinbone.

Knee injuries refer to damages or harm caused to the structures surrounding or within the knee joint, which may include the bones (femur, tibia, and patella), cartilage (meniscus and articular cartilage), ligaments (ACL, PCL, MCL, and LCL), tendons (patellar and quadriceps), muscles, bursae, and other soft tissues. These injuries can result from various causes, such as trauma, overuse, degeneration, or sports-related activities. Symptoms may include pain, swelling, stiffness, instability, reduced range of motion, and difficulty walking or bearing weight on the affected knee. Common knee injuries include fractures, dislocations, meniscal tears, ligament sprains or ruptures, and tendonitis. Proper diagnosis and treatment are crucial to ensure optimal recovery and prevent long-term complications.

"Weight-bearing" is a term used in the medical field to describe the ability of a body part or limb to support the weight or pressure exerted upon it, typically while standing, walking, or performing other physical activities. In a clinical setting, healthcare professionals often use the term "weight-bearing exercise" to refer to physical activities that involve supporting one's own body weight, such as walking, jogging, or climbing stairs. These exercises can help improve bone density, muscle strength, and overall physical function, particularly in individuals with conditions affecting the bones, joints, or muscles.

In addition, "weight-bearing" is also used to describe the positioning of a body part during medical imaging studies, such as X-rays or MRIs. For example, a weight-bearing X-ray of the foot or ankle involves taking an image while the patient stands on the affected limb, allowing healthcare providers to assess any alignment or stability issues that may not be apparent in a non-weight-bearing position.

Proteoglycans are complex, highly negatively charged macromolecules that are composed of a core protein covalently linked to one or more glycosaminoglycan (GAG) chains. They are a major component of the extracellular matrix (ECM) and play crucial roles in various biological processes, including cell signaling, regulation of growth factor activity, and maintenance of tissue structure and function.

The GAG chains, which can vary in length and composition, are long, unbranched polysaccharides that are composed of repeating disaccharide units containing a hexuronic acid (either glucuronic or iduronic acid) and a hexosamine (either N-acetylglucosamine or N-acetylgalactosamine). These GAG chains can be sulfated to varying degrees, which contributes to the negative charge of proteoglycans.

Proteoglycans are classified into four major groups based on their core protein structure and GAG composition: heparan sulfate/heparin proteoglycans, chondroitin/dermatan sulfate proteoglycans, keratan sulfate proteoglycans, and hyaluronan-binding proteoglycans. Each group has distinct functions and is found in specific tissues and cell types.

In summary, proteoglycans are complex macromolecules composed of a core protein and one or more GAG chains that play important roles in the ECM and various biological processes, including cell signaling, growth factor regulation, and tissue structure maintenance.

The synovial membrane, also known as the synovium, is the soft tissue that lines the inner surface of the capsule of a synovial joint, which is a type of joint that allows for smooth movement between bones. This membrane secretes synovial fluid, a viscous substance that lubricates and nourishes the cartilage and helps to reduce friction within the joint during movement.

The synovial membrane has a highly specialized structure, consisting of two layers: the intima and the subintima. The intima is a thin layer of cells that are in direct contact with the synovial fluid, while the subintima is a more fibrous layer that contains blood vessels and nerves.

The main function of the synovial membrane is to produce and regulate the production of synovial fluid, as well as to provide nutrients to the articular cartilage. It also plays a role in the immune response within the joint, helping to protect against infection and inflammation. However, abnormalities in the synovial membrane can lead to conditions such as rheumatoid arthritis, where the membrane becomes inflamed and produces excess synovial fluid, leading to pain, swelling, and joint damage.

"Bone" is the hard, dense connective tissue that makes up the skeleton of vertebrate animals. It provides support and protection for the body's internal organs, and serves as a attachment site for muscles, tendons, and ligaments. Bone is composed of cells called osteoblasts and osteoclasts, which are responsible for bone formation and resorption, respectively, and an extracellular matrix made up of collagen fibers and mineral crystals.

Bones can be classified into two main types: compact bone and spongy bone. Compact bone is dense and hard, and makes up the outer layer of all bones and the shafts of long bones. Spongy bone is less dense and contains large spaces, and makes up the ends of long bones and the interior of flat and irregular bones.

The human body has 206 bones in total. They can be further classified into five categories based on their shape: long bones, short bones, flat bones, irregular bones, and sesamoid bones.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Immunohistochemistry (IHC) is a technique used in pathology and laboratory medicine to identify specific proteins or antigens in tissue sections. It combines the principles of immunology and histology to detect the presence and location of these target molecules within cells and tissues. This technique utilizes antibodies that are specific to the protein or antigen of interest, which are then tagged with a detection system such as a chromogen or fluorophore. The stained tissue sections can be examined under a microscope, allowing for the visualization and analysis of the distribution and expression patterns of the target molecule in the context of the tissue architecture. Immunohistochemistry is widely used in diagnostic pathology to help identify various diseases, including cancer, infectious diseases, and immune-mediated disorders.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Disease progression is the worsening or advancement of a medical condition over time. It refers to the natural course of a disease, including its development, the severity of symptoms and complications, and the impact on the patient's overall health and quality of life. Understanding disease progression is important for developing appropriate treatment plans, monitoring response to therapy, and predicting outcomes.

The rate of disease progression can vary widely depending on the type of medical condition, individual patient factors, and the effectiveness of treatment. Some diseases may progress rapidly over a short period of time, while others may progress more slowly over many years. In some cases, disease progression may be slowed or even halted with appropriate medical interventions, while in other cases, the progression may be inevitable and irreversible.

In clinical practice, healthcare providers closely monitor disease progression through regular assessments, imaging studies, and laboratory tests. This information is used to guide treatment decisions and adjust care plans as needed to optimize patient outcomes and improve quality of life.

Electron microscopy (EM) is a type of microscopy that uses a beam of electrons to create an image of the sample being examined, resulting in much higher magnification and resolution than light microscopy. There are several types of electron microscopy, including transmission electron microscopy (TEM), scanning electron microscopy (SEM), and reflection electron microscopy (REM).

In TEM, a beam of electrons is transmitted through a thin slice of the sample, and the electrons that pass through the sample are focused to form an image. This technique can provide detailed information about the internal structure of cells, viruses, and other biological specimens, as well as the composition and structure of materials at the atomic level.

In SEM, a beam of electrons is scanned across the surface of the sample, and the electrons that are scattered back from the surface are detected to create an image. This technique can provide information about the topography and composition of surfaces, as well as the structure of materials at the microscopic level.

REM is a variation of SEM in which the beam of electrons is reflected off the surface of the sample, rather than scattered back from it. This technique can provide information about the surface chemistry and composition of materials.

Electron microscopy has a wide range of applications in biology, medicine, and materials science, including the study of cellular structure and function, disease diagnosis, and the development of new materials and technologies.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

Cartilage diseases refer to conditions that affect the cartilaginous tissues in the body. Cartilage is a firm, flexible connective tissue found in many areas of the body, including the joints, ribcage, ears, and nose. It provides structure and support, allows for smooth movement between bones, and protects the ends of bones from friction.

There are several types of cartilage diseases, including:

1. Osteoarthritis (OA): This is a degenerative joint disease that occurs when the protective cartilage that cushions the ends of your bones wears down over time. It can cause pain, stiffness, and loss of mobility in the affected joints.
2. Rheumatoid arthritis (RA): This is an autoimmune disorder that causes inflammation in the lining of the joints, leading to cartilage damage and bone erosion.
3. Traumatic arthritis: This occurs when a joint is injured, causing damage to the cartilage and resulting in pain, stiffness, and loss of mobility.
4. Infectious arthritis: This occurs when a joint becomes infected, leading to inflammation and potential damage to the cartilage.
5. Chondromalacia patellae: This is a condition that affects the cartilage on the back of the kneecap, causing pain and stiffness in the knee.
6. Costochondritis: This is an inflammation of the cartilage in the ribcage, causing chest pain and discomfort.
7. Nasal septal deviation: This is a condition where the cartilage that separates the nostrils is crooked or off-center, causing difficulty breathing through the nose.
8. Osteochondritis dissecans (OCD): This is a joint condition that occurs when a piece of cartilage and bone in a joint becomes detached, causing pain and stiffness.
9. Synovial chondromatosis: This is a rare condition where nodules made up of cartilage form in the lining of a joint, causing pain, swelling, and limited mobility.

Treatment for cartilage diseases varies depending on the specific condition and severity, but may include medication, physical therapy, surgery, or a combination of these.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

... (COMP), also known as thrombospondin-5, is an extracellular matrix (ECM) protein primarily ... "Cartilage oligomeric matrix protein level in rheumatic diseases: potential use as a marker for measuring articular cartilage ... "Entrez Gene: COMP cartilage oligomeric matrix protein". Paulsson M, Heinegård D (Aug 1981). "Purification and structural ... Rosenberg K, Olsson H, Mörgelin M, Heinegård D (Aug 1998). "Cartilage oligomeric matrix protein shows high affinity zinc- ...
2002). "Cartilage oligomeric matrix protein-deficient mice have normal skeletal development". Mol Cell Biol. 22 (12): 4366-71. ... 1995). "Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene ... "COMP cartilage oligomeric matrix protein [ Homo sapiens (human) ]". "MATN3 matrilin 3 [ Homo sapiens (human) ]". d Briggs, ... Paulsson M, Heinegård D (1981). "Purification and structural characterization of a cartilage matrix protein". Biochem J. 197 (2 ...
The cartilage oligomeric matrix protein is 757 aa (OMIM 2008). COMP protein is found in the extracellular matrix, a complex web ... Pseudoachondroplasia is caused by a heterozygous mutation in the gene encoding cartilage oligomeric matrix protein (COMP). ... "Serum or plasma cartilage oligomeric matrix protein concentration as a diagnostic marker in pseudoachondroplasia: differential ... We do not yet fully understand the normal function of COMP protein, though it is believed to play a part in cellular growth, ...
2006). "ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein". J. Biol. Chem. 281 (23): 15800-8. doi: ... 2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and ... This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. ... Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a ...
This enzyme catalyzes the degradation of cartilage oligomeric matrix protein (COMP) degradation. ADAMTS7 has been associated ... a metalloproteinase that directly binds to and degrades cartilage oligomeric matrix protein". FASEB Journal. 20 (7): 988-990. ... This 1686-amino acid protein belongs to the ADAMTS family and is one of 19 members known in humans. As an ADAMTS protein, ... participate in the protein's tight interaction with the extracellular matrix. ADAMTS7 was identified in a yeast two-hybrid ...
2000). "Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)". FEBS Lett. 478 (1- ... Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal ... Matrix metalloproteinase-19 (MMP-19) also known as matrix metalloproteinase RASI is an enzyme that in humans is encoded by the ... "Entrez Gene: MMP19 matrix metallopeptidase 19". Murphy G, Knäuper V, Cowell S, et al. (1999). "Evaluation of some newer matrix ...
2000). "Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)". FEBS Lett. 478 (1- ... Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal ... and contains more protein and water. In general, MMP-20 functions in enamel are to cleave enamel matrix proteins at specific ... "Entrez Gene: MMP20 matrix metallopeptidase 20 (enamelysin)". Moradian-Oldak J (2012). "Protein-mediated enamel mineralization ...
"Lubricin binds cartilage proteins, cartilage oligomeric matrix protein, fibronectin and collagen II at the cartilage surface". ... September 2017). "Cartilage oligomeric matrix protein forms protein complexes with synovial lubricin via non-covalent and ... September 2017). "Cartilage oligomeric matrix protein forms protein complexes with synovial lubricin via non-covalent and ... The role of cartilage oligomeric matrix protein (COMP) in surface-structuring of lubricin". Journal of Colloid and Interface ...
... interaction with glycosaminoglycans and cartilage oligomeric matrix protein". J. Biol. Chem. 279 (23): 24265-73. doi:10.1074/ ... Collagen alpha-1(IX) chain is a protein that in humans is encoded by the COL9A1 gene. This gene encodes one of the three alpha ... Wu JJ, Woods PE, Eyre DR (Dec 1992). "Identification of cross-linking sites in bovine cartilage type IX collagen reveals an ... Two genes of 90 and 15 kb code for similar polypeptides of the same collagen molecule". Matrix Biol. 17 (3): 237-41. doi: ...
... is inherited in an autosomal dominant manner and is caused solely by mutations in the cartilage oligomeric matrix protein COMP ... Osteochondrodysplasia is a general term for a disorder of the development (dysplasia) of bone ("osteo") and cartilage ("chondro ... and Arthropathy in two unrelated children with matrix metalloproteinase 2 variants: Genetic-skeletal correlations". Bone ...
... interacts with histone deacetylase-1 and inhibits cartilage oligomeric matrix protein gene expression and chondrogenesis". J. ... Zinc finger and BTB domain-containing protein 7A is a protein that in humans is encoded by the ZBTB7A gene. ZBTB7A has been ... ZBTB7A+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH) FactorBook ZBTB7A This article ... Pessler F, Hernandez N (2003). "Flexible DNA binding of the BTB/POZ-domain protein FBI-1". J. Biol. Chem. 278 (31): 29327-35. ...
... non-collagenous extracellular matrix components, including: 3% cartilage oligomeric matrix protein, 1-2% elastin, 1-5% ... Bone morphogenetic proteins (BMPs) are a subgroup of TGF-β superfamily that can induce bone and cartilage formation as well as ... Collagenous Extracellular Matrix Proteins and Minor Collagens in Tendon". Journal of Orthopaedic Research. 38 (1): 23-35. doi: ... "Elasticity in extracellular matrix 'shape modules' of tendon, cartilage, etc. A sliding proteoglycan-filament model". Journal ...
Kim HJ, Lee YH, Kim CK (2009). "Changes in serum cartilage oligomeric matrix protein (COMP), plasma CPK and plasma hs-CRP in ... The protein encoded by this gene is a cytoplasmic enzyme involved in cellular energy homeostasis. The encoded protein ... 2008). "Muscle RING-finger protein-1 (MuRF1) as a connector of muscle energy metabolism and protein synthesis". J. Mol. Biol. ... Li S, Bai JH, Park YD, Zhou HM (2006). "Capture of monomeric refolding intermediate of human muscle creatine kinase". Protein ...
... a type of school in the United Kingdom Cartilage oligomeric matrix protein, or COMP Comparettia, an orchid genus Comp cards, ...
... cartilage oligomeric matrix protein, bone morphogenetic protein, and other anabolic gene candidates are among the candidate ... Delivered as a protein, sprifermin (FGF18 analog), was able to increase cartilage thickness in a dose dependent manner in ... OA is mostly the result of natural aging of the joint due to biochemical changes in the cartilage extracellular matrix. While ... Genes, which contribute to protect and restore the matrix of articular cartilage, are attracting the most attention. These ...
... and serum cartilage oligomeric matrix protein (COMP) levels as a prognostic marker for incidence of both knee and hip ... a) cartilage erosion (b)cartilage ulceration (c)cartilage repair (d)osteophyte (bone spur) formation. Histopathology of ... The capsule and fluid protect the cartilage, muscles, and connective tissues. With osteoarthritis, the cartilage becomes worn ... the collagen matrix becomes more disorganized and there is a decrease in proteoglycan content within cartilage. The breakdown ...
... a new member of a family of extracellular matrix proteins related to cartilage matrix protein (matrilin-1) and von Willebrand ... a family of filamentous-forming adapter oligomeric extracellular proteins that are linked to the formation of cartilage and ... The Matrilin-3 protein is protein linked to the development of cartilage and bone, and consists of one Von Willebrand Factor A ... It is considered an extracellular matrix protein that functions as an adapter protein where the Matrilin-3 subunit can form ...
Cartilage oligomeric matrix protein. Gene map locus 19p13.1 NOTCH3: Notch homolog 3 (Drosophila): Gene map locus 19p13.1-p13.2 ... encoding protein Zinc finger protein 112 ZNF134: encoding protein Zinc finger protein 134 ZNF160: encoding protein Zinc finger ... encoding protein Zinc finger protein 180 ZNF208: encoding protein Zinc finger protein 208 ZNF224: encoding protein Zinc finger ... encoding protein Zinc finger protein 225 ZNF226: encoding protein Zinc finger protein 226 ZNF229: encoding protein Zinc finger ...
... also designated cartilage oligomeric protein or COMP). TSP-1 and TSP-2 are homotrimers, consisting of three identical subunits ... Due to their dynamic role within the extracellular matrix they are considered matricellular proteins. The first member of the ... "Matricellular proteins and biomaterials". Matrix Biology. 37: 183-191. doi:10.1016/j.matbio.2014.03.002. PMC 4167162. PMID ... As such, TSP-1 is designated a multifunctional protein. TSP-1 has multiple receptors, among which CD36, CD47 and integrins are ...
Other extracellular matrix components such as matrix metalloproteins and integrins are also frequently co-expressed with TN-C. ... These protein modules are lined up like beads on a string and give rise to long and extended molecules. At the N-terminus each ... Tenascin C is an oligomeric glycoprotein composed of individual polypeptides with molecular weights ranging from 180 to ~300kDa ... bone and cartilage. The human tenascin C gene, TN-C, is located on chromosome 9 with location of the cytogenic band at the 9q33 ...
Tropoelastin is a protein, of size 72kDa, that comes together via cross-links to form elastin in the extracellular matrix of ... Concatamers are oligomeric products of ligating a single gene with itself. This will result in repeat segments of a gene, all ... ELP networks to promote cell growth may prove indispensable in the production of tissue scaffolds that promote cartilage ... In this linear state, the ELP-protein complex cannot easily be distinguished from the extraneous proteins in the solution. ...
DIX domains are unique: the only other proteins known to have a DIX domain are Dishevelled and DIXDC1. (The single Dsh protein ... Axin is then titrated away from its oligomeric assemblies - the β-catenin destruction complex - by Dsh. Once bound to the ... They also produce extracellular matrix components, such as type I collagen and fibronectin. Aberrant activation of the Wnt ... "Researchers Offer First Direct Proof of How Arthritis Destroys Cartilage" at rochester.edu Human CTNNB1 genome location and ...
Cartilage oligomeric matrix protein (COMP), also known as thrombospondin-5, is an extracellular matrix (ECM) protein primarily ... "Cartilage oligomeric matrix protein level in rheumatic diseases: potential use as a marker for measuring articular cartilage ... "Entrez Gene: COMP cartilage oligomeric matrix protein". Paulsson M, Heinegård D (Aug 1981). "Purification and structural ... Rosenberg K, Olsson H, Mörgelin M, Heinegård D (Aug 1998). "Cartilage oligomeric matrix protein shows high affinity zinc- ...
Cartilage Oligomeric Matrix Protein (pseudoachondroplasia epiphyseal dysplasia 1 multiple), MED, THBS5, TSP5, EDM1, PSACH, EPD1 ... found in the extracellular matrix of articular, nasal and tracheal cartilage. COMP is not only cartilage-derived but is common ... For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).. Avoid multiple freeze-thaw cycles. ... COMP is a non-collagenous glycoprotein and is belongs to the thrombospondin family of extracellular proteins. COMP is a calcium ...
... ... Cartilage oligomeric matrix protein: A novel non-invasive marker for assessing cirrhosis and risk of hepatocellular carcinoma ... Core tip: We report our first results regarding the utility of serum cartilage oligomeric matrix protein (COMP), an antigen ... AIM: To assess serum cartilage oligomeric matrix protein (COMP) as a marker of cirrhosis and risk of progression to ...
The COMP concentrations were determined by use of an inhibition ELISA that had canine cartilage COMP and monoclonal antibody ... Relevance-These results supported the hypothesis that COMP concentration in serum and SF of dogs may be altered after cartilage ... Abstract Objective-To assay concentrations of cartilage oligomeric matrix protein (COMP) in canine sera and synovial fluid (SF ... Concentrations of cartilage oligomeric matrix protein in dogs with naturally developing and experimentally induced arthropathy ...
One such potential biological marker of arthritis is cartilage oligomeric matrix protein (COMP). In various studies, COMP has ... It damages the cartilage, synovium, and bone of the joints causing pain, impairment, and disability in patients. Current ... A valuable approach to monitor arthritis would be by measuring biological markers of cartilage degradation and repair to ... One such potential biological marker of arthritis is cartilage oligomeric matrix protein (COMP). In various studies, COMP has ...
... is a homopentameric protein in cartilage. The development of arthritis, like collagen-induced arthritis (CIA), involves ... These findings accentuate the importance of COMP in cartilage stability. ... indicating no difference in how collagen II antibodies interact with COMP-deficient cartilage during the initial stages of ... cartilage as a target tissue. We have investigated the development of CIA in COMP-deficient mice. COMP-deficient mice in the ...
Cartilage oligomeric matrix protein (COMP) is a soluble pentameric protein expressed in cartilage and involved in collagen ... Cartilage oligomeric matrix protein contributes to the development and metastasis of breast cancer Author ... Cartilage oligomeric matrix protein contributes to the development and metastasis of breast cancer ... This observation was confirmed in vitro as COMP-expressing cells showed better survival as well as a higher rate of protein ...
COMP: cartilage oligomeric matrix protein. *COMT: catechol-O-methyltransferase. *COQ2: coenzyme Q2, polyprenyltransferase ...
Role of Alphacalcidol to Reduce Pain and Serum Cartilage Oligomeric Matrix Protein in Elderly with Knee Osteoarthritis. In: ... Dive into the research topics of Role of Alphacalcidol to Reduce Pain and Serum Cartilage Oligomeric Matrix Protein in Elderly ... Role of Alphacalcidol to Reduce Pain and Serum Cartilage Oligomeric Matrix Protein in Elderly with Knee Osteoarthritis. / Zaki ... Role of Alphacalcidol to Reduce Pain and Serum Cartilage Oligomeric Matrix Protein in Elderly with Knee Osteoarthritis. ...
... to the procedure of marrow stimulation is thought to enhance cartilage repair as it may provide both an additional cell ... A bone marrow clot forms within the cartilage defect either as a result of marrow stimulation or during the course of the ... the basic science knowledge on MSCs and BMA and the clinical and technical aspects of marrow stimulation-based cartilage repair ... population capable of chondrogenesis and a source of growth factors stimulating cartilage repair. Moreover, the BMA clot ...
Rat COMP (Cartilage Oligomeric Matrix Protein) CLIA Kit , G-EC-01796 MSRP: ... Rat TP53 (Tumor Protein 53) CLIA Kit , G-EC-02142 Rat TP53 (Tumor Protein 53) CLIA Kit , G-EC-02142 , Gentaur Clia KitsTarget ... Rat IGFBP-3 (Insulin-Like Growth Factor Binding Protein 3) CLIA Kit , G-EC-01961 ... Rat LRP-1 (Low-Density Lipoprotein-Receptor-Related Protein) CLIA Kit , G-EC-01990 ...
Here, changes in cartilage oligomeric matrix protein (COMP), interleukin-6 (IL-6), and creatine phosphokinase (CPK) were ... Cartilage Oligomeric Matrix Protein; Creatine Phosphokinase; Static Trunk Loading ...
Cartilage Oligomeric Matrix Protein initiates cancer stem cells through activation of Jagged1-Notch3 signaling. Papadakos, K. S ... Expression of Cartilage Oligomeric Matrix Protein in colorectal cancer is an adverse prognostic factor and correlates ... Expression of cartilage oligomeric matrix protein in periampullary adenocarcinoma is associated with pancreatobiliary-type ... Extracellular matrix structure.. Theocharis, A. D., Skandalis, S. S., Gialeli, C. & Karamanos, N. K., 2015, In: Advanced Drug ...
Cartilage oligomeric matrix protein (COMP) and matrilin-3 (MATN3) are thought to bridge extracellular matrix proteins. Collagen ... Altered enchondral ossification may be associated with changes in the articular cartilage. The resultant articular cartilage is ... Histological and biochemical analyses of epiphyseal plate cartilage in one. J Bone Joint Surg Am. 1967 Dec. 49 (8):1611-27. [ ... morphologic and biochemical study of cartilage. Am J Med Genet. 1993 Feb 15. 45 (4):501-7. [QxMD MEDLINE Link]. ...
Serum cartilage oligomeric matrix protein (COMP) concentration is elevated in patients with early osteoarthritis and early ... Clinical significance of decreased serum concentration of cartilage oligomeric matrix protein in systemic juvenile idiopathic ... Expression of tegument protein pp65 of human cytomegalovirus (CMV) and its application to the analysis of viral-specific ... We newly synthesized protein pp65 with a baculovirus expression system and purified it via metal affinity chromatography... ...
1997) HLA DRB1* typing and cartilage oligomeric matrix protein (COMP) as predictors of joint destruction in recent-onset ...
Cartilage oligomeric matrix protein-angiopoietin-1 (COMP-Ang1) is an angiogenic factor for vascular angiogenesis. The aim was ...
... is caused by mutations in cartilage oligomeric matrix protein (COMP). The mechanisms underlying the mutant-COMP pathology have ... is caused by mutations in cartilage oligomeric matrix protein (COMP). The mechanisms underlying the mutant-COMP pathology have ... ALKB homologous protein 5 (ALKBH5) and fat mass and obesity-associated protein (FTO) is decreased significantly at the mRNA and ... Mutant-COMP protein does not fold properly, and it is retained in the rough endoplasmic reticulum (rER) of chondrocytes rather ...
The samples were tested for 15 biomarkers, including those related to cartilage metabolism (cartilage oligomeric matrix protein ... Further analysis showed that levels of cartilage oligomeric matrix protein, resistin, monocyte chemoattractant protein-1, and ... Similarly, higher cartilage oligomeric matrix protein levels are associated with a higher risk of knee osteoarthritis. ... The authors noted that previous research has observed high expression of monocyte chemoattractant protein-1 and resistin in ...
MedChemExpress offers high purity COMP Protein, Human (HEK293, His) with excellent lot-to-lot consistency, superior biological ... Cartilage oligomeric matrix protein; COMP; Thrombospondin-5; TSP5. AA Sequence. MVPDTACVLLLTLAALGASGQGQSPLGSDLGPQMLRELQETNAALQD ... Viral Proteins. Biotinylated Proteins. Fluorescent-labeled Proteins. GMP-grade Proteins. Animal-free Recombinant Proteins. ... Immune Checkpoint Proteins. CAR-T related Proteins. CD Antigens. Fc Receptors. Receptor Proteins. Enzymes & Regulators. ...
Cartilage oligomeric matrix protein. $5.00. USD Add to cart. * Cathepsin B. $5.00. USD Add to cart ... EF-hand domain-containing protein D2. $5.00. USD Add to cart. * EGF-containing fibulin-like extracellular matrix protein 1. $ ... Proline-rich acidic protein 1. $5.00. USD Add to cart. * Prolow-density lipoprotein receptor-related protein 1. $5.00. USD Add ... GTP-binding nuclear protein Ran. $5.00. USD Add to cart. * H-2 class I histocompatibility antigen, Q10 alpha chain. $5.00. USD ...
blood cartilage oligomeric matrix protein level + blood ceruloplasmin level + blood clusterin level + ... Protein-Protein Interactions) PhenoMiner (Quatitative Phenotypes) Gene Annotator OLGA (Gene List Generator) AllianceMine ... The amount of any cystatin (that is, of any member of the cystatin superfamily of proteins, many of which act as cysteine ...
Lesser lower extremity mechanical loading associates with a greater increase in serum cartilage oligomeric matrix protein ...
... cartilage oligomeric matrix protein, hepatocyte growth factor, kallistatin, insulin-like growth factor binding protein, acid ... Results: In the matched cohort, 17 proteins could be identified in synovial fluid and 16 proteins were detected in serum. For ... As part of a proteomic analysis of knee synovial fluid from normal and OA patients, differentially expressed proteins were ... This study aimed to use mass spectrometry assays to identify representative peptides from several proteins in synovial fluid ...
... and the cartilage markers Alanine-Arginine-Glycine-Serine (ARGS)-aggrecan, cartilage oligomeric matrix protein (COMP), and type ... and the cartilage markers Alanine-Arginine-Glycine-Serine (ARGS)-aggrecan, cartilage oligomeric matrix protein (COMP), and type ... Serum concentrations of the inflammatory marker C-reactive protein (CRP) ... Serum concentrations of the inflammatory marker C-reactive protein (CRP) ...
The subgroup B thrombospondins, designated TSP-3, -4, and COMP (cartilage oligomeric matrix protein, also designated TSP-5) are ... Click on the protein counts, or double click on taxonomic names to display all proteins containing TSP1 domain in the selected ... We have shown previously that thrombospondin 1 (TSP1), a platelet alpha-granule and extracellular matrix protein, activates ... Crystal structure of circumsporozoite protein aTSR domain, R32 native form. 3vdk. Crystal structure of circumsporozoite protein ...
The subgroup B thrombospondins, designated TSP-3, -4, and COMP (cartilage oligomeric matrix protein, also designated TSP-5) are ... Click on the protein counts, or double click on taxonomic names to display all proteins containing TSP1 domain in the selected ... We have shown previously that thrombospondin 1 (TSP1), a platelet alpha-granule and extracellular matrix protein, activates ... Crystal structure of circumsporozoite protein aTSR domain, R32 native form. 3vdk. Crystal structure of circumsporozoite protein ...
Cartilage oligomeric matrix protein contributes to the development and metastasis of breast cancer E Englund, M Bartoschek, B ... Cartilage Oligomeric Matrix Protein initiates cancer stem cells through activation of Jagged1-Notch3 signaling Konstantinos S. ... Sushi domain-containing protein 4 binds to epithelial growth factor receptor and initiates autophagy in an EGFR phosphorylation ... Bone morphogenetic protein-9 inhibits lymphatic vessel formation via activin receptor-like kinase 1 during development and ...
Regulators of cartilage oligomeric matrix protein - expression in articular cartilage, epiphyseal growth plate and zone of ... COMP (Cartilage Oligomeric Matrix Protein) Neoepitope A Novel Biomarker to Identify Symptomatic Carotid Stenosis. Sandstedt, ... Cartilage oligomeric matrix protein (COMP) neo-epitope, a novel biomarker that in combination with known risk markers ... Effect of circadian rhythm, age, training and acute lameness on serum concentrations of cartilage oligomeric matrix protein ( ...
Cartilage Oligomeric Matrix Protein Caspase-8/FLICE Caspase-9 Cathepsin L CD134 CD137/4-1BB CD152/CTLA-4 CD23 CD28 CD30 CD40 ... Amyloid Precursor Protein Androstenedione Angiopoietin-Like Protein 3 Angiopoietin-Like Protein 6 Angiopoietin-Like Protein 7 ... Growth Hormone Binding Protein Heart Fatty Acid Binding Protein Hepatocyte Growth Factor Histamine HLA-G Chemerin Chitinase 3- ... Monocyte Chemotactic Protein-1 Monomeric CRP MxA Protein Obestatin Omentin-1 Osteoblast Specific Factor 2 Osteocalcin ...
  • Cartilage oligomeric matrix protein (COMP), also known as thrombospondin-5, is an extracellular matrix (ECM) protein primarily present in cartilage. (wikipedia.org)
  • COMP is a marker of cartilage turnover. (wikipedia.org)
  • COMP is a non-collagenous glycoprotein and is belongs to the thrombospondin family of extracellular proteins. (prospecbio.com)
  • COMP is not only cartilage-derived but is common in other tissues, such as synovium and tendon. (prospecbio.com)
  • Objective -To assay concentrations of cartilage oligomeric matrix protein (COMP) in canine sera and synovial fluid (SF), to compare COMP concentrations in clinically normal dogs and dogs with joint disease, and to analyze changes in COMP concentrations in dogs with experimentally induced acute synovitis. (avma.org)
  • The COMP concentrations were determined by use of an inhibition ELISA that had canine cartilage COMP and monoclonal antibody against human COMP. (avma.org)
  • Conclusions and Clinical Relevance -These results supported the hypothesis that COMP concentration in serum and SF of dogs may be altered after cartilage degradation or synovitis. (avma.org)
  • One such potential biological marker of arthritis is cartilage oligomeric matrix protein (COMP). (escholarship.org)
  • Cartilage oligomeric matrix protein (COMP) is a homopentameric protein in cartilage. (biomedcentral.com)
  • Finally, COMP-deficient and wild-type mice responded similarly to collagen antibody-induced arthritis, indicating no difference in how collagen II antibodies interact with COMP-deficient cartilage during the initial stages of arthritis. (biomedcentral.com)
  • These findings accentuate the importance of COMP in cartilage stability. (biomedcentral.com)
  • In fact, the immunization with other cartilage proteins in some cases will cause a disease similar in type to CIA, which has been shown to be immunized with COMP [ 7 ]. (biomedcentral.com)
  • COMP is a 524-kDa homopentameric extracellular matrix glycoprotein and a member of the thrombospondin (TSP) family [ 8 ]. (biomedcentral.com)
  • Pseudoachondroplasia (PSACH) is associated with mutations in the cartilage oligomeric matrix protein (COMP) gene and the clinical characteristics include short stature, deformities of the extremities involving the epiphyses and metaphyses, early onset arthritis, and ligament laxity. (nih.gov)
  • Cartilage oligomeric matrix protein (COMP) is a soluble pentameric protein expressed in cartilage and involved in collagen organization. (lu.se)
  • In vitro experiments confirmed that COMP-expressing cells had a more invasive phenotype, which could in part be attributed to an upregulation of matrix metalloprotease-9. (lu.se)
  • This observation was confirmed in vitro as COMP-expressing cells showed better survival as well as a higher rate of protein synthesis when treated with brefeldin A, compared with control cells. (lu.se)
  • Objective: To determine the effect of Alphacalcidol supplementation on pain based on WOMAC pain index and joint cartilage condition based on cartilage oligomeric matrix protein (COMP) serum markers in knee osteoarthritis (OA) elderly patients. (ui.ac.id)
  • Here, changes in cartilage oligomeric matrix protein (COMP), interleukin-6 (IL-6), and creatine phosphokinase (CPK) were monitored before and after 1hr of exposure to static axial trunk loading and again after 1hr of prone rest. (cdc.gov)
  • Cartilage oligomeric matrix protein (COMP) and matrilin-3 (MATN3) are thought to bridge extracellular matrix proteins. (medscape.com)
  • Serum cartilage oligomeric matrix protein (COMP) concentration is elevated in patients with early osteoarthritis and early rheumatoid arthritis, and may be a biomarker of cartilage turnover. (researchgate.net)
  • Cartilage oligomeric matrix protein-angiopoietin-1 (COMP-Ang1) is an angiogenic factor for vascular angiogenesis. (koreamed.org)
  • Serum concentrations of the inflammatory marker C-reactive protein (CRP) and the cartilage markers Alanine-Arginine-Glycine-Serine (ARGS)-aggrecan, cartilage oligomeric matrix protein (COMP), and type II collagen C2C were analyzed by immunoassays. (lu.se)
  • we found that the expression of cartilage protein COMP is associated with metastases and a poor prognosis for patients with various types of solid cancers. (lu.se)
  • 500kDa) found in the extracellular matrix of articular, nasal and tracheal cartilage. (prospecbio.com)
  • Mesenchymal stem cells (MSCs) play a key role in articular cartilage repair. (hindawi.com)
  • Native and concentrated BMA have been intensively studied in the context of articular cartilage repair. (hindawi.com)
  • Such enhanced techniques of marrow stimulation have been shown to improve articular cartilage repair in both animal models and patients. (hindawi.com)
  • Altered enchondral ossification may be associated with changes in the articular cartilage. (medscape.com)
  • The resultant articular cartilage is deficient in underlying osseous support and fails to withstand normal cyclical loading. (medscape.com)
  • Binding to other ECM proteins such as collagen appears to depend on divalent cations. (wikipedia.org)
  • The development of arthritis, like collagen-induced arthritis (CIA), involves cartilage as a target tissue. (biomedcentral.com)
  • In the CIA model, an immunization against one specific cartilage protein, collagen II (CII), starts an autoimmune reaction leading to arthritis. (biomedcentral.com)
  • Collagen IX is important for the adhesive properties of cartilage. (medscape.com)
  • Tendon cells synthesize the tendon's extracellular matrix , which abounds with densely-packed collagen fibers. (handwiki.org)
  • The collagen in tendons are held together with proteoglycan (a compound consisting of a protein bonded to glycosaminoglycan groups, present especially in connective tissue) components including decorin and, in compressed regions of tendon, aggrecan , which are capable of binding to the collagen fibrils at specific locations. (handwiki.org)
  • Further analysis showed that levels of cartilage oligomeric matrix protein, resistin, monocyte chemoattractant protein-1, and nerve growth factor were significantly different between patients with psoriatic arthritis and those with osteoarthritis. (mdedge.com)
  • Osteoarthritis and Cartilage. (wikipedia.org)
  • A panel of four biomarkers of cartilage metabolism, metabolic syndrome, and inflammation could help physicians to distinguish between osteoarthritis and psoriatic arthritis, new research suggests. (mdedge.com)
  • The authors noted that previous research has observed high expression of monocyte chemoattractant protein-1 and resistin in patients with psoriatic arthritis when compared with those with osteoarthritis. (mdedge.com)
  • Similarly, higher cartilage oligomeric matrix protein levels are associated with a higher risk of knee osteoarthritis. (mdedge.com)
  • The aim of this study was to explore the associations between PA or self-reported joint function and molecular biomarkers of cartilage and inflammation in individuals with hip and/or knee osteoarthritis (OA). (lu.se)
  • Data are also lacking on their distinguishing abilities from other cartilage-damaging diseases, such as osteoarthritis (OA) and their usefulness as a monitoring tool in patients with RA. (biomedcentral.com)
  • TNF-α, and improve the histopathological features in rabbit knee cartilage with osteoarthritis. (unpad.ac.id)
  • Cartilage and bone metabolism in rheumatoid arthritis. (wikipedia.org)
  • A bone marrow clot forms within the cartilage defect either as a result of marrow stimulation or during the course of the spontaneous repair of osteochondral defects. (hindawi.com)
  • The additional application of a bone marrow aspirate (BMA) to the procedure of marrow stimulation is thought to enhance cartilage repair as it may provide both an additional cell population capable of chondrogenesis and a source of growth factors stimulating cartilage repair. (hindawi.com)
  • If bone marrow fills a cartilage defect either as a result of marrow stimulation for chondral defects or the course of the spontaneous repair of osteochondral defects, a bone marrow clot forms within the cartilage defect. (hindawi.com)
  • In the orthopaedic field, additional application of a bone marrow aspirate (BMA) to the procedure of marrow stimulation has been recently studied, since the bone marrow itself is both a source of MSCs, providing a cell population capable of chondrogenesis and of various growth factors stimulating cartilage repair [ 7 - 10 ]. (hindawi.com)
  • Skeletal dysplasias, also known as osteochondrodysplasias, are a heterogeneous group of heritable disorders characterized by abnormalities of cartilage and bone growth, resulting in abnormal shape and size of the skeleton and disproportion of the long bones, spine, and head. (medscape.com)
  • Persistent synovitis causes bone and cartilage damage, leading to joint destruction and deformity. (biomedcentral.com)
  • Generally, alkaline phosphatase (ALP), COL1A1, BSP, RUNX2, transforming growth factor-beta 1 (TGFB1), osteonectin (ON), and bone morphogenetic protein-2 (BMP2) are known to be early markers of osteoblastic differentiation, whereas OC and osteopontin (OPN) are expressed later in the differentiation process [ 20 ]. (biomedcentral.com)
  • As part of a proteomic analysis of knee synovial fluid from normal and OA patients, differentially expressed proteins were identified that could represent potential biomarkers for OA. (harvard.edu)
  • This study aimed to use mass spectrometry assays to identify representative peptides from several proteins in synovial fluid and peripheral blood, and assess their levels as biomarkers of OA progression. (harvard.edu)
  • The protein encoded by this gene is a noncollagenous extracellular matrix (ECM) protein. (wikipedia.org)
  • Methods: Multiplexed high throughput selected reaction monitoring (SRM) assays were developed to measure tryptic peptides representative of 23 proteins in matched serum and synovial fluid samples from late OA subjects at the time of joint replacement. (harvard.edu)
  • Subsequently plasma samples from the baseline visit of 173 subjects in an observational OA cohort were tested by SRM for peptides from nine of these proteins: afamin, clusterin, cartilage oligomeric matrix protein, hepatocyte growth factor, kallistatin, insulin-like growth factor binding protein, acid labile subunit, lubricin, lumican, and pigment epithelium-derived factor. (harvard.edu)
  • A high correlation between different peptides from individual proteins was observed, indicating our assays correctly measured their target proteins. (harvard.edu)
  • Scalar light instructions are able to assemble and maintain molecules of amino acids and proteins crucial to human and animal quantum health. (scalarlight.com)
  • In practice, the Scalar Light Amino Acid & Protein Program administers scalar light instructions in order to assemble and maintain amino acids and proteins inside the quantum body or scalar light force field. (scalarlight.com)
  • Below are the lists of amino acids and proteins that are assembled by way of the Scalar Light Amino Acid and Protein Program. (scalarlight.com)
  • Additionally, enzymes and micro-nutrients are likewise assembled as these nutrients serve to abet and catalyze the assembling of amino acids and proteins. (scalarlight.com)
  • The Scalar Light Amino Acid and Protein Program operates twenty-four (24) hours per day seven (7) days per week thereby assuring a constant creation and delivery of amino acids and proteins to the quantum, human body. (scalarlight.com)
  • The study showed that the reduction in transport of large amino acids by the encoded SLC7A5 protein leads to neurons switching from metabolizing lipids instead of amino acids and higher levels of neuronal cell death. (genewhisperer.com)
  • This study aimed to provide an overview of ultrasonographic cartilage evaluation in patients with rheumatoid arthritis (RA) and identify research gaps in the utilization of cartilage evaluation. (biomedcentral.com)
  • A systematic literature search of the PubMed, Embase, and Cochrane Library databases was conducted for articles published up to July 2022 using the search term variations of "cartilage," "ultrasonography," and "rheumatoid arthritis. (biomedcentral.com)
  • The search terms included were variations of "cartilage," "ultrasonography," and "rheumatoid arthritis. (biomedcentral.com)
  • Valmu L , Autero M, Siljander P, Patarroyo M and Gahmberg C G (1991) Phosphorylation of the ß-subunit of CD11/CD18 in-tegrins by protein kinase C correlates with leukocyte adhesion. (leenavalmu.fi)
  • Kovanen P E, Junttila K, Takaluoma K, Saharinen P, Valmu L , Li W and Silvennoinen O (2000) Regulation of Jak2 tyrosine kinase by protein kinase C during macrophage differentation of IL-3-dependent myeloid progenitor cell. (leenavalmu.fi)
  • Ivanov K I, Puustinen P, Gabrenaite R, Vihinen H, Rönnstrand L, Valmu L , Kalkkinen N and Mäkinen K (2003) Phosphorylation of the Potyvirus Capsid Protein by Protein Kinase CK2 and Its relevance for Virus Infection. (leenavalmu.fi)
  • A valuable approach to monitor arthritis would be by measuring biological markers of cartilage degradation and repair to reflect variations in joint remodeling. (escholarship.org)
  • TNF-α activates fibroblasts and synovial macrophages to secrete degradation enzymes and supress cartilage proteoglycan synthesis, leading to histopathological changes in cartilages. (unpad.ac.id)
  • Integrins are transmembrane receptors that mediate cell adhesion by forming links between the extracellular matrix and cytoskeleton. (biologists.com)
  • In addition, you will have the opportunity to learn microbiologic and immunologic techniques and to express and purify recombinant proteins. (lu.se)
  • Interaction with glycosaminoglycans and cartilage oligomeric matrix protein. (leenavalmu.fi)
  • We have updated the nomenclature of a number of genes based on the identification of their encoded proteins as being associated with microtubules. (genewhisperer.com)
  • The following genes that previously had placeholder symbols have recently been shown to encode proteins that are found in the lumen of microtubules. (genewhisperer.com)
  • Mapping of the genes encoding human protein matches to pathways point to targets that could explain the observed presentation of symptoms in COVID-19 disease. (danielsolis.cz)
  • It was found in the thrombospondin protein where it is repeated 3 times. (embl.de)
  • Depending on the cultivation technique we found significant differences in both gen and protein expression. (biomedcentral.com)
  • We found very high levels of expression of the central complement protein, C3, and complement inhibitor CD59 in human pancreatic islets. (lu.se)
  • Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. (medchemexpress.com)
  • Homology between human and viral proteins is an established factor in viral- or vaccine-induced autoimmunity. (danielsolis.cz)
  • SAR-CoV-2 spike proteins, and all other SARS-CoV-2 proteins, immunogenic epitopes in each SARS-CoV-2 protein were compared to human proteins in search of high local homologous matching. (danielsolis.cz)
  • Only one immunogenic epitope in a SARS-CoV-2 had no homology to human proteins. (danielsolis.cz)
  • If all of the parts of the epitopes that are homologous to human proteins are excluded from consideration due to risk of pathogenic priming, the remaining immunogenic parts of the epitopes may be still immunogenic and remain as potentially viable candidates for vaccine development. (danielsolis.cz)
  • Blom A. M . , Berggård K., Webb J. H., Villoutreix B., Lindahl G. and Dahlbäck B. (2000) Human C4b-binding protein has overlapping but not identical binding sites for C4b and streptococcal M-proteins. (lu.se)
  • Mark L., Lee W. H., Villoutreix B. O., Proctor D., Blackbourn, D., Spiller B. O. and Blom A. M. (2004) KSHV complement control protein mimics human molecular mechanisms for inhibition of the complement system. (lu.se)
  • Kask L., Hillarp A., Ramesh B., Dahlbäck B., and Blom A. M. (2002) Structural requirements for the intra-cellular subunit polymerization of the complement inhibitor C4b-binding protein. (lu.se)
  • Sjöberg A., Önnerfjord, P., Mörgelin, M., Heinegård, D. and Blom A. M. (2005) Extracellular matrix and inflammation: fibromodulin activates the classical pathway of complement by directly binding C1q. (lu.se)
  • In the chronic stage of the disease, when the erosion of the cartilage is taking place, it is possible that immune reactions to other cartilage proteins are initiated and contribute to the disease course. (biomedcentral.com)
  • Reduction of TNF-α level and histopathological improvement are found in rabbit knee cartilage with arthritis when fractionated Papuan ant nest is given. (unpad.ac.id)
  • Results: In the matched cohort, 17 proteins could be identified in synovial fluid and 16 proteins were detected in serum. (harvard.edu)
  • therefore, it is considered useful for cartilage evaluation, including small joints. (biomedcentral.com)
  • Thrombospondins are multimeric multidomain glycoproteins that function at cell surfaces and in the extracellular matrix milieu. (embl.de)
  • Keratin ( / ˈ k ɛr ə t ɪ n / [1] [2] ) is one of a family of structural fibrous proteins also known as scleroproteins . (wikipedia.org)
  • Spider silk is classified as keratin, [9] although production of the protein may have evolved independently of the process in vertebrates. (wikipedia.org)