A non-fibrillar collagen found primarily in terminally differentiated hypertrophic CHONDROCYTES. It is a homotrimer of three identical alpha1(X) subunits.
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.
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.
Polymorphic cells that form cartilage.
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).
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.
A fibrillar collagen consisting of three identical alpha1(III) chains that is widely distributed in many tissues containing COLLAGEN TYPE I. It is particularly abundant in BLOOD VESSELS and may play a role in tissues with elastic characteristics.
A fibrillar collagen found predominantly in CARTILAGE and vitreous humor. It consists of three identical alpha1(II) chains.
A non-fibrillar collagen found in the structure of BASEMENT MEMBRANE. Collagen type IV molecules assemble to form a sheet-like network which is involved in maintaining the structural integrity of basement membranes. The predominant form of the protein is comprised of two alpha1(IV) subunits and one alpha2(IV) subunit, however, at least six different alpha subunits can be incorporated into the heterotrimer.
A fibrillar collagen found widely distributed as a minor component in tissues that contain COLLAGEN TYPE I and COLLAGEN TYPE III. It is a heterotrimeric molecule composed of alpha1(V), alpha2(V) and alpha3(V) subunits. Several forms of collagen type V exist depending upon the composition of the subunits that form the trimer.
A family of structurally related collagens that form the characteristic collagen fibril bundles seen in CONNECTIVE TISSUE.
A non-fibrillar collagen that forms a network of MICROFIBRILS within the EXTRACELLULAR MATRIX of CONNECTIVE TISSUE. The alpha subunits of collagen type VI assemble into antiparallel, overlapping dimers which then align to form tetramers.
A fibrillar collagen found primarily in interstitial CARTILAGE. Collagen type XI is heterotrimer containing alpha1(XI), alpha2(XI) and alpha3(XI) subunits.
The area between the EPIPHYSIS and the DIAPHYSIS within which bone growth occurs.
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.
Collagen receptors are cell surface receptors that modulate signal transduction between cells and the EXTRACELLULAR MATRIX. They are found in many cell types and are involved in the maintenance and regulation of cell shape and behavior, including PLATELET ACTIVATION and aggregation, through many different signaling pathways and differences in their affinities for collagen isoforms. Collagen receptors include discoidin domain receptors, INTEGRINS, and glycoprotein VI.
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).
A biosynthetic precursor of collagen containing additional amino acid sequences at the amino-terminal and carboxyl-terminal ends of the polypeptide chains.
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.
A non-fibrillar collagen found in BASEMENT MEMBRANE. The C-terminal end of the alpha1 chain of collagen type XVIII contains the ENDOSTATIN peptide, which can be released by proteolytic cleavage.
The developmental entity of a fertilized chicken egg (ZYGOTE). The developmental process begins about 24 h before the egg is laid at the BLASTODISC, a small whitish spot on the surface of the EGG YOLK. After 21 days of incubation, the embryo is fully developed before hatching.
A hydroxylated form of the imino acid proline. A deficiency in ASCORBIC ACID can result in impaired hydroxyproline formation.
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.
Abnormal development of cartilage and bone.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
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.
Glycoproteins found on the surfaces of cells, particularly in fibrillar structures. The proteins are lost or reduced when these cells undergo viral or chemical transformation. They are highly susceptible to proteolysis and are substrates for activated blood coagulation factor VIII. The forms present in plasma are called cold-insoluble globulins.
A darkly stained mat-like EXTRACELLULAR MATRIX (ECM) that separates cell layers, such as EPITHELIUM from ENDOTHELIUM or a layer of CONNECTIVE TISSUE. The ECM layer that supports an overlying EPITHELIUM or ENDOTHELIUM is called basal lamina. Basement membrane (BM) can be formed by the fusion of either two adjacent basal laminae or a basal lamina with an adjacent reticular lamina of connective tissue. BM, composed mainly of TYPE IV COLLAGEN; glycoprotein LAMININ; and PROTEOGLYCAN, provides barriers as well as channels between interacting cell layers.
Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.
Glycoproteins which have a very high polysaccharide content.
A long, narrow, and flat bone commonly known as BREASTBONE occurring in the midsection of the anterior thoracic segment or chest region, which stabilizes the rib cage and serves as the point of origin for several muscles that move the arms, head, and neck.
A metalloproteinase which degrades helical regions of native collagen to small fragments. Preferred cleavage is -Gly in the sequence -Pro-Xaa-Gly-Pro-. Six forms (or 2 classes) have been isolated from Clostridium histolyticum that are immunologically cross-reactive but possess different sequences and different specificities. Other variants have been isolated from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio and Streptomyces. EC 3.4.24.3.
Large, noncollagenous glycoprotein with antigenic properties. It is localized in the basement membrane lamina lucida and functions to bind epithelial cells to the basement membrane. Evidence suggests that the protein plays a role in tumor invasion.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
Historically, a heterogeneous group of acute and chronic diseases, including rheumatoid arthritis, systemic lupus erythematosus, progressive systemic sclerosis, dermatomyositis, etc. This classification was based on the notion that "collagen" was equivalent to "connective tissue", but with the present recognition of the different types of collagen and the aggregates derived from them as distinct entities, the term "collagen diseases" now pertains exclusively to those inherited conditions in which the primary defect is at the gene level and affects collagen biosynthesis, post-translational modification, or extracellular processing directly. (From Cecil Textbook of Medicine, 19th ed, p1494)
General increase in bulk of a part or organ due to CELL ENLARGEMENT and accumulation of FLUIDS AND SECRETIONS, not due to tumor formation, nor to an increase in the number of cells (HYPERPLASIA).
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.
A small leucine-rich proteoglycan that interacts with FIBRILLAR COLLAGENS and modifies the EXTRACELLULAR MATRIX structure of CONNECTIVE TISSUE. Decorin has also been shown to play additional roles in the regulation of cellular responses to GROWTH FACTORS. The protein contains a single glycosaminoglycan chain and is similar in structure to BIGLYCAN.
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.
Any pathological condition where fibrous connective tissue invades any organ, usually as a consequence of inflammation or other injury.
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.
Process by which organic tissue becomes hardened by the physiologic deposit of calcium salts.
Enzymes that catalyze the degradation of collagen by acting on the peptide bonds.
The outer covering of the body that protects it from the environment. It is composed of the DERMIS and the EPIDERMIS.
Reagent used as an intermediate in the manufacture of beta-alanine and pantothenic acid.

Articular cartilage repair using a tissue-engineered cartilage-like implant: an animal study. (1/149)

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

A dominant interference collagen X mutation disrupts hypertrophic chondrocyte pericellular matrix and glycosaminoglycan and proteoglycan distribution in transgenic mice. (2/149)

Collagen X transgenic (Tg) mice displayed skeleto-hematopoietic defects in tissues derived by endochondral skeletogenesis.(1) Here we demonstrate that co-expression of the transgene product containing truncated chicken collagen X with full-length mouse collagen X in a cell-free translation system yielded chicken-mouse hybrid trimers and truncated chicken homotrimers; this indicated that the mutant could assemble with endogenous collagen X and thus had potential for dominant interference. Moreover, species-specific collagen X antibodies co-localized the transgene product with endogenous collagen X to hypertrophic cartilage in growth plates and ossification centers; proliferative chondrocytes also stained diffusely. Electron microscopy revealed a disrupted hexagonal lattice network in the hypertrophic chondrocyte pericellular matrix in Tg growth plates, as well as altered mineral deposition. Ruthenium hexamine trichloride-positive aggregates, likely glycosaminoglycans (GAGs)/proteoglycans (PGs), were also dispersed throughout the chondro-osseous junction. These defects likely resulted from transgene co-localization and dominant interference with endogenous collagen X. Moreover, altered GAG/PG distribution in growth plates of both collagen X Tg and null mice was confirmed by a paucity of staining for hyaluronan and heparan sulfate PG. A provocative hypothesis links the disruption of the collagen X pericellular network and GAG/PG decompartmentalization to the potential locus for hematopoietic failure in the collagen X mice.  (+info)

Expression of collagen and aggrecan genes in normal and osteoarthritic murine knee joints. (3/149)

OBJECTIVE: The STR/ort mouse strain develops osteoarthritis (OA) of the medial tibial cartilage whilst CBA mice do not develop this disease. We investigated whether changes occur in the expression of genes encoding major extracellular matrix proteins in the connective tissue of the murine knee joint in OA. DESIGN: Expression of the genes encoding collagens II (Col2alpha1), X (Col10alpha1), alpha2(XI) (Col11alpha2) and aggrecan (Agc) was detected in skeletally mature and immature male mice of the CBA and STR/ort strains by in situ hybridization. RESULTS: Col2alpha1 was expressed by chondrocytes of the tibial and patella-femoral cartilage and by the meniscal cartilage in all young mice (4-9 weeks) but only in the patella-femoral cartilage in older mice of both strains (36-45 weeks). In contrast Col2alpha1 was expressed by growth plate chondrocytes of both species at all ages. Similarly, Col2alpha1 transcripts were detected in cruciate ligament cells in both strains at all ages. Col10alpha1 transcripts were detected in cruciate ligament cells in both strains at all ages. Col10alpha1 expression was evident in the hypertrophic chondrocytes in the growth plate of young CBA and STR mice, but was not active in these cells in mature animals. However, Col10alpha1 was transcribed in articular chondrocytes of the tibia, meniscal and patella-femoral cartilages of all ages, in normal and osteoarthritic mice. Transcripts were also present in ligament of some mature animals. Col11alpha2 followed a similar pattern of expression in CBA cartilages to Col2alpha1, being active in adult growth plate but generally inactive in adult articular cartilages. Young CBA and STR/ort mice expressed Col11alpha2 in articular cartilage and very strongly throughout the growth plate. Agc expression was detected in all articular cartilages at all ages in both strains. Interestingly, transcripts for all four genes were absent in tibial articular chondrocytes located close to osteoarthritic lesions in STR/ort mice, indicating that these cells are unable to synthesize matrix proteins. Adult STR/ort mice also showed evidence of tissue remodeling around the periphery of the knee joint. Cells in remodeling areas actively transcribed Col2alpha1, Col10alpha1, Col11alpha2 and Agc. CONCLUSION: It is unlikely that OA develops in STR/ort mice because of failure to express major proteins in joint tissue. However, once lesions develop in articular cartilage neighbouring chondrocytes fail to express genes encoding several matrix proteins.  (+info)

Transglutaminase factor XIIIA in the cartilage of developing avian long bones. (4/149)

Previously, we showed that mRNA for transglutaminase factor XIIIA (FXIIIA) is up-regulated in the hypertrophic zone of the growth plate of the chicken tibiotarsus, a well-characterized model of long bone development. In the present study, we have studied the distribution of the FXIIIA protein and of transglutaminase enzymatic activity in this growth plate, as well as in the cartilage of the epiphysis, which includes that of the articular surface. By immunohistochemical analysis, the protein is detected in the zone of maturation, where it is mostly intracellular, and in the hypertrophic zone, where it is present both intracellularly and in the extracellular matrix. The intracellular enzyme is mostly a zymogen, as determined with an antibody specific for the activation peptide. Externalization of FXIIIA is accompanied by enzyme activation. To study the pattern of transglutaminase activity, a synthetic transglutaminase substrate, rhodamine-conjugated tetrapeptide (Pro-Val-Lys-Gly), was used for pulse labeling in organ cultures. Intensive incorporation of the fluorescent substrate was observed throughout the hypertrophic zone and in the cells surrounding the forming blood vessels. The patterns of FXIIIA immunostaining and substrate incorporation overlap almost completely. The cartilaginous factor XIIIA is different from the plasma form in that, both intracellularly and extracellularly, it exists as a monomer, as determined by Western analysis, whereas the plasma form of FXIII is a tetrameric complex composed of both A and B subunits. We also identified FXIIIA and transglutaminase activity within the articular and condylar regions of the tarsus, suggesting a possible involvement of mechanical pressure and/or stress in the production of the molecule and subsequent cross-linking of the cartilage matrix. Thus, transglutaminases, in particular FXIIIA, are involved in the formation of long bones through its activity both in the hypertrophic region of the growth plate and in the formation of articular/epiphyseal cartilages.  (+info)

Collagen X chains harboring Schmid metaphyseal chondrodysplasia NC1 domain mutations are selectively retained and degraded in stably transfected cells. (5/149)

Collagen X is a short chain, homotrimeric collagen expressed specifically by hypertrophic chondrocytes during endochondral bone formation and growth. Although the exact role of collagen X remains unresolved, mutations in the COL10A1 gene disrupt growth plate function and result in Schmid metaphyseal chondrodysplasia (SMCD). With the exception of two mutations that impair signal peptide cleavage during alpha1(X) chain biosynthesis, SMCD mutations are clustered within the carboxyl-terminal NC1 domain. The formation of stable NC1 domain trimers is a critical stage in collagen X assembly, suggesting that mutations within this domain may result in subunit mis-folding or reduce trimer stability. When expressed in transiently transfected cells, alpha1(X) chains containing SMCD mutations were unstable and presumed to be degraded intracellularly. More recently, in vitro studies have shown that certain missense mutations may exert a dominant negative effect on alpha1(X) chain assembly by formation of mutant homotrimers and normal-mutant heterotrimers. In contrast, analysis of cartilage tissue from two SMCD patients revealed that the truncated mutant message was fully degraded, resulting in 50% reduction of functional collagen X within the growth plate. Therefore, in the absence of data that conclusively demonstrates the full cellular response to mutant collagen X chains, the molecular mechanisms underlying SMCD remain controversial. To address this, we closely examined the effect of two NC1 domain mutations, one frameshift mutation (1963del10) and one missense mutation (Y598D), using both semi-permeabilized cell and stable cell transfection expression systems. Although able to assemble to a limited extent in both systems, we show that, in intact cells, collagen X chains harboring both SMCD mutations did not evade quality control mechanisms within the secretory pathway and were degraded intracellularly. Furthermore, co-expression of wild-type and mutant chains in stable transfected cells demonstrated that, although wild-type chains were secreted, mutant chains were largely excluded from hetero-trimer formation. Our data indicate, therefore, that the predominant effect of the NC1 mutations Y598D and 1963del10 is a reduction in the amount of functional collagen X within the growth cartilage extracellular matrix.  (+info)

Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer. (6/149)

Collagen X is expressed specifically in the growth plate of long bones. Its C1q-like C-terminal NC1 domain forms a stable homotrimer and is crucial for collagen X assembly. Mutations in the NC1 domain cause Schmid metaphyseal chondrodysplasia (SMCD). The crystal structure at 2.0 A resolution of the human collagen X NC1 domain reveals an intimate trimeric assembly strengthened by a buried cluster of calcium ions. Three strips of exposed aromatic residues on the surface of NC1 trimer are likely to be involved in the supramolecular assembly of collagen X. Most internal SMCD mutations probably prevent protein folding, whereas mutations of surface residues may affect the collagen X suprastructure in a dominant-negative manner.  (+info)

TGFbeta2 mediates the effects of hedgehog on hypertrophic differentiation and PTHrP expression. (7/149)

The development of endochondral bones requires the coordination of signals from several cell types within the cartilage rudiment. A signaling cascade involving Indian hedgehog (Ihh) and parathyroid hormone related peptide (PTHrP) has been described in which hypertrophic differentiation is limited by a signal secreted from chondrocytes as they become committed to hypertrophy. In this negative-feedback loop, Ihh inhibits hypertrophic differentiation by regulating the expression of Pthrp, which in turn acts directly on chondrocytes in the growth plate that express the PTH/PTHrP receptor. Previously, we have shown that PTHrP also acts downstream of transforming growth factor beta (TGFbeta) in a common signaling cascade to regulate hypertrophic differentiation in embryonic mouse metatarsal organ cultures. As members of the TGFbeta superfamily have been shown to mediate the effects of Hedgehog in several developmental systems, we proposed a model where TGFbeta acts downstream of Ihh and upstream of PTHrP in a cascade of signals that regulate hypertrophic differentiation in the growth plate. This report tests the hypothesis that TGFbeta signaling is required for the effects of Hedgehog on hypertrophic differentiation and expression of PTHRP: We show that Sonic hedgehog (Shh), a functional substitute for Ihh, stimulates expression of Tgfb2 and Tgfb3 mRNA in the perichondrium of embryonic mouse metatarsal bones grown in organ cultures and that TGFbeta signaling in the perichondrium is required for inhibition of differentiation and regulation of Pthrp expression by Shh. The effects of Shh are specifically dependent on TGFbeta2, as cultures from Tgfb3-null embryos respond to Shh but cultures from Tgfb2-null embryos do not. Taken together, these data suggest that TGFbeta2 acts as a signal relay between Ihh and PTHrP in the regulation of cartilage hypertrophic differentiation.  (+info)

Linking hematopoiesis to endochondral skeletogenesis through analysis of mice transgenic for collagen X. (8/149)

Each skeletal element where marrow develops is first defined by a hypertrophic cartilage blueprint. Through programmed tissue substitution, the cartilaginous skeletal model is replaced by trabecular bone and marrow, with accompanying longitudinal tissue growth. During this process of endochondral ossification, hypertrophic cartilage expresses a unique matrix molecule, collagen X. Previously we reported that transgenic mice with dominant interference collagen X mutations develop variable skeleto-hematopoietic abnormalities, manifested as growth plate compressions, diminished trabecular bone, and reduced lymphatic organs (Nature 1993, 365:56). Here, histology and flow cytometry reveal marrow hypoplasia and impaired hematopoiesis in all collagen X transgenic mice. A subset of mice with perinatal lethality manifested the most severe skeletal defects and a reduction of marrow hematopoiesis, highlighted by a lymphocyte decrease. Thymic reduction is accompanied by a paucity of cortical immature T cells, consistent with the marrow's inability to replenish maturing cortical lymphocytes. Diminished spleens exhibit indistinct lymphatic nodules and red pulp depletion; the latter correlates with erythrocyte-filled vascular sinusoids in marrows. All mice display reduced B cells in marrows and spleens, and elevated splenic T cells. These hematopoietic defects underscore an unforeseen link between hypertrophic cartilage, endochondral ossification, and establishment of the marrow microenvironment required for blood cell differentiation.  (+info)

Collagen type X is a specific type of collagen that is primarily found in the hypertrophic zone of mature cartilage, which is located near the site of bone formation during endochondral ossification. It plays a crucial role in the mineralization process of the cartilage matrix and is essential for the formation of healthy bones. Collagen type X is composed of three identical alpha chains that form a triple helix structure, and it is synthesized by chondrocytes, which are the specialized cells found in cartilage tissue. Mutations in the gene that encodes collagen type X have been associated with certain skeletal disorders, such as Schmid metaphyseal chondrodysplasia.

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.

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.

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 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.

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.

Collagen Type III, also known as Collagen III Alpha 1 (COL3A1), is a type of collagen that is found in various connective tissues throughout the body. It is a fibrillar collagen that is produced by fibroblasts and is a major component of reticular fibers, which provide structural support to organs such as the liver, spleen, and lymph nodes. Collagen Type III is also found in the walls of blood vessels, the skin, and the intestinal tract.

Mutations in the COL3A1 gene can lead to a rare genetic disorder called Ehlers-Danlos syndrome type IV, which is characterized by fragile and elastic skin, easy bruising, and spontaneous rupture of blood vessels. Collagen Type III has been studied for its potential role in various other medical conditions, including fibrosis, cancer, and cardiovascular disease.

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.

Collagen Type IV is a type of collagen that forms the structural basis of basement membranes, which are thin, sheet-like structures that separate and support cells in many types of tissues. It is a major component of the basement membrane's extracellular matrix and provides strength and flexibility to this structure. Collagen Type IV is composed of three chains that form a distinctive, mesh-like structure. Mutations in the genes encoding Collagen Type IV can lead to a variety of inherited disorders affecting the kidneys, eyes, and ears.

Collagen Type V is a specific type of collagen, which is a protein that provides structure and strength to connective tissues in the body. Collagen Type V is found in various tissues, including the cornea, blood vessels, and hair. It plays a crucial role in the formation of collagen fibers and helps regulate the diameter of collagen fibrils. Mutations in the genes that encode for Collagen Type V can lead to various connective tissue disorders, such as Ehlers-Danlos syndrome and osteogenesis imperfecta.

Fibrillar collagens are a type of collagen that form rope-like fibrils in the extracellular matrix of connective tissues. They are composed of three polypeptide chains, called alpha chains, which are coiled together in a triple helix structure. The most common types of fibrillar collagens are Type I, II, III, V, and XI. These collagens provide strength and support to tissues such as tendons, ligaments, skin, and bones. They also play important roles in the regulation of cell behavior and tissue development. Mutations in genes encoding fibrillar collagens can lead to a variety of connective tissue disorders, including osteogenesis imperfecta, Ehlers-Danlos syndrome, and Marfan syndrome.

Collagen Type VI is a type of collagen that is widely expressed in various tissues, including skeletal muscle, skin, and blood vessels. It is a major component of the extracellular matrix and plays important roles in maintaining tissue structure and function. Collagen Type VI forms microfilaments that provide structural support to the basement membrane and regulate cell-matrix interactions. Mutations in the genes encoding collagen Type VI can lead to several inherited connective tissue disorders, such as Bethlem myopathy and Ullrich congenital muscular dystrophy.

Collagen type XI is a fibrillar collagen that is found in the extracellular matrix of various tissues, including cartilage and the eye. It is a homotrimer made up of three identical alpha 1(XI) chains or a heterotrimer composed of two alpha 1(XI) chains and one alpha 2(XI) chain. Collagen type XI is closely associated with collagen type II fibrils and plays a role in regulating the diameter and organization of these fibrils. Mutations in the genes encoding collagen type XI can lead to skeletal disorders such as stiff skin syndrome and fibrodysplasia ossificans progressiva.

A growth plate, also known as an epiphyseal plate or physis, is a layer of cartilaginous tissue found near the ends of long bones in children and adolescents. This region is responsible for the longitudinal growth of bones during development. The growth plate contains actively dividing cells that differentiate into chondrocytes, which produce and deposit new matrix, leading to bone elongation. Once growth is complete, usually in late adolescence or early adulthood, the growth plates ossify (harden) and are replaced by solid bone, transforming into the epiphyseal line.

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.

Collagen receptors are a type of cell surface receptor that bind to collagen molecules, which are the most abundant proteins in the extracellular matrix (ECM) of connective tissues. These receptors play important roles in various biological processes, including cell adhesion, migration, differentiation, and survival.

Collagen receptors can be classified into two major groups: integrins and discoidin domain receptors (DDRs). Integrins are heterodimeric transmembrane proteins that consist of an alpha and a beta subunit. They bind to collagens via their arginine-glycine-aspartic acid (RGD) motif, which is located in the triple-helical domain of collagen molecules. Integrins mediate cell-collagen interactions by clustering and forming focal adhesions, which are large protein complexes that connect the ECM to the cytoskeleton.

DDRs are receptor tyrosine kinases (RTKs) that contain a discoidin domain in their extracellular region, which is responsible for collagen binding. DDRs bind to collagens via their non-RGD motifs and induce intracellular signaling pathways that regulate cell behavior.

Abnormalities in collagen receptor function have been implicated in various diseases, including fibrosis, cancer, and inflammation. Therefore, understanding the structure and function of collagen receptors is crucial for developing novel therapeutic strategies to treat these conditions.

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.

Procollagen is the precursor protein of collagen, which is a major structural protein in the extracellular matrix of various connective tissues, such as tendons, ligaments, skin, and bones. Procollagen is synthesized inside the cell (in the rough endoplasmic reticulum) and then processed by enzymes to remove specific segments, resulting in the formation of tropocollagen, which are the basic units of collagen fibrils.

Procollagen consists of three polypeptide chains (two alpha-1 and one alpha-2 chain), each containing a central triple-helical domain flanked by non-helical regions at both ends. These non-helical regions, called propeptides, are cleaved off during the processing of procollagen to tropocollagen, allowing the individual collagen molecules to align and form fibrils through covalent cross-linking.

Abnormalities in procollagen synthesis or processing can lead to various connective tissue disorders, such as osteogenesis imperfecta (brittle bone disease) and Ehlers-Danlos syndrome (a group of disorders characterized by joint hypermobility, skin hyperextensibility, and tissue fragility).

"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.

Collagen type XVIII is a type of collagen that is found in the basement membrane, which is a thin layer of extracellular matrix that separates and supports epithelial and endothelial cells. It is a heterotrimeric protein composed of three different chains, alpha1(XVIII), alpha2(XVIII), and alpha3(XVIII). Collagen XVIII is thought to play a role in the maintenance and organization of the basement membrane, as well as in cell adhesion and migration. It also contains a number of distinct domains that are involved in various biological processes, including angiogenesis, tissue repair, and tumor growth. Mutations in the gene that encodes collagen XVIII have been associated with eye diseases such as Knobloch syndrome and familial exudative vitreoretinopathy.

A chick embryo refers to the developing organism that arises from a fertilized chicken egg. It is often used as a model system in biological research, particularly during the stages of development when many of its organs and systems are forming and can be easily observed and manipulated. The study of chick embryos has contributed significantly to our understanding of various aspects of developmental biology, including gastrulation, neurulation, organogenesis, and pattern formation. Researchers may use various techniques to observe and manipulate the chick embryo, such as surgical alterations, cell labeling, and exposure to drugs or other agents.

Hydroxyproline is not a medical term per se, but it is a significant component in the medical field, particularly in the study of connective tissues and collagen. Here's a scientific definition:

Hydroxyproline is a modified amino acid that is formed by the post-translational modification of the amino acid proline in collagen and some other proteins. This process involves the addition of a hydroxyl group (-OH) to the proline residue, which alters its chemical properties and contributes to the stability and structure of collagen fibers. Collagen is the most abundant protein in the human body and is a crucial component of connective tissues such as tendons, ligaments, skin, and bones. The presence and quantity of hydroxyproline can serve as a marker for collagen turnover and degradation, making it relevant to various medical and research contexts, including the study of diseases affecting connective tissues like osteoarthritis, rheumatoid arthritis, and Ehlers-Danlos 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.

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.

Fibroblasts are specialized cells that play a critical role in the body's immune response and wound healing process. They are responsible for producing and maintaining the extracellular matrix (ECM), which is the non-cellular component present within all tissues and organs, providing structural support and biochemical signals for surrounding cells.

Fibroblasts produce various ECM proteins such as collagens, elastin, fibronectin, and laminins, forming a complex network of fibers that give tissues their strength and flexibility. They also help in the regulation of tissue homeostasis by controlling the turnover of ECM components through the process of remodeling.

In response to injury or infection, fibroblasts become activated and start to proliferate rapidly, migrating towards the site of damage. Here, they participate in the inflammatory response, releasing cytokines and chemokines that attract immune cells to the area. Additionally, they deposit new ECM components to help repair the damaged tissue and restore its functionality.

Dysregulation of fibroblast activity has been implicated in several pathological conditions, including fibrosis (excessive scarring), cancer (where they can contribute to tumor growth and progression), and autoimmune diseases (such as rheumatoid arthritis).

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.

Fibronectin is a high molecular weight glycoprotein that is found in many tissues and body fluids, including plasma, connective tissue, and the extracellular matrix. It is composed of two similar subunits that are held together by disulfide bonds. Fibronectin plays an important role in cell adhesion, migration, and differentiation by binding to various cell surface receptors, such as integrins, and other extracellular matrix components, such as collagen and heparan sulfate proteoglycans.

Fibronectin has several isoforms that are produced by alternative splicing of a single gene transcript. These isoforms differ in their biological activities and can be found in different tissues and developmental stages. Fibronectin is involved in various physiological processes, such as wound healing, tissue repair, and embryonic development, and has been implicated in several pathological conditions, including fibrosis, tumor metastasis, and thrombosis.

The basement membrane is a thin, specialized layer of extracellular matrix that provides structural support and separates epithelial cells (which line the outer surfaces of organs and blood vessels) from connective tissue. It is composed of two main layers: the basal lamina, which is produced by the epithelial cells, and the reticular lamina, which is produced by the connective tissue. The basement membrane plays important roles in cell adhesion, migration, differentiation, and survival.

The basal lamina is composed mainly of type IV collagen, laminins, nidogens, and proteoglycans, while the reticular lamina contains type III collagen, fibronectin, and other matrix proteins. The basement membrane also contains a variety of growth factors and cytokines that can influence cell behavior.

Defects in the composition or organization of the basement membrane can lead to various diseases, including kidney disease, eye disease, and skin blistering disorders.

Pepsin A is defined as a digestive enzyme that is primarily secreted by the chief cells in the stomach's fundic glands. It plays a crucial role in protein catabolism, helping to break down food proteins into smaller peptides during the digestive process. Pepsin A has an optimal pH range of 1.5-2.5 for its enzymatic activity and is activated from its inactive precursor, pepsinogen, upon exposure to acidic conditions in the stomach.

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 sternum, also known as the breastbone, is a long, flat bone located in the central part of the chest. It serves as the attachment point for several muscles and tendons, including those involved in breathing. The sternum has three main parts: the manubrium at the top, the body in the middle, and the xiphoid process at the bottom. The upper seven pairs of ribs connect to the sternum via costal cartilages.

Microbial collagenase is not a medical term per se, but it does refer to an enzyme that is used in various medical and research contexts. Collagenases are a group of enzymes that break down collagen, a structural protein found in connective tissues such as skin, tendons, and ligaments. Microbial collagenase is a type of collagenase that is produced by certain bacteria, such as Clostridium histolyticum.

In medical terms, microbial collagenase is used in various therapeutic and research applications, including:

1. Wound healing: Microbial collagenase can be used to break down and remove necrotic tissue from wounds, which can help promote healing and prevent infection.
2. Dental applications: Collagenases have been used in periodontal therapy to remove calculus and improve the effectiveness of root planing and scaling procedures.
3. Research: Microbial collagenase is a valuable tool for researchers studying the structure and function of collagen and other extracellular matrix proteins. It can be used to digest tissue samples, allowing scientists to study the individual components of the extracellular matrix.

It's important to note that while microbial collagenase has many useful applications, it must be used with care, as excessive or improper use can damage healthy tissues and cause adverse effects.

Laminin is a family of proteins that are an essential component of the basement membrane, which is a specialized type of extracellular matrix. Laminins are large trimeric molecules composed of three different chains: α, β, and γ. There are five different α chains, three different β chains, and three different γ chains that can combine to form at least 15 different laminin isoforms.

Laminins play a crucial role in maintaining the structure and integrity of basement membranes by interacting with other components of the extracellular matrix, such as collagen IV, and cell surface receptors, such as integrins. They are involved in various biological processes, including cell adhesion, differentiation, migration, and survival.

Laminin dysfunction has been implicated in several human diseases, including cancer, diabetic nephropathy, and muscular dystrophy.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Collagen diseases, also known as collagen disorders or connective tissue diseases, refer to a group of medical conditions that affect the body's connective tissues. These tissues provide support and structure for various organs and systems in the body, including the skin, joints, muscles, and blood vessels.

Collagen is a major component of connective tissues, and it plays a crucial role in maintaining their strength and elasticity. In collagen diseases, the body's immune system mistakenly attacks healthy collagen, leading to inflammation, pain, and damage to the affected tissues.

There are several types of collagen diseases, including:

1. Systemic Lupus Erythematosus (SLE): This is a chronic autoimmune disease that can affect various organs and systems in the body, including the skin, joints, kidneys, heart, and lungs.
2. Rheumatoid Arthritis (RA): This is a chronic inflammatory disease that primarily affects the joints, causing pain, swelling, and stiffness.
3. Scleroderma: This is a rare autoimmune disorder that causes thickening and hardening of the skin and connective tissues, leading to restricted movement and organ damage.
4. Dermatomyositis: This is an inflammatory muscle disease that can also affect the skin, causing rashes and weakness.
5. Mixed Connective Tissue Disease (MCTD): This is a rare autoimmune disorder that combines symptoms of several collagen diseases, including SLE, RA, scleroderma, and dermatomyositis.

The exact cause of collagen diseases is not fully understood, but they are believed to be related to genetic, environmental, and hormonal factors. Treatment typically involves a combination of medications, lifestyle changes, and physical therapy to manage symptoms and prevent complications.

Hypertrophy, in the context of physiology and pathology, refers to an increase in the size of an organ or tissue due to an enlargement of its constituent cells. It is often used to describe the growth of muscle cells (myocytes) in response to increased workload or hormonal stimulation, resulting in an increase in muscle mass. However, hypertrophy can also occur in other organs such as the heart (cardiac hypertrophy) in response to high blood pressure or valvular heart disease.

It is important to note that while hypertrophy involves an increase in cell size, hyperplasia refers to an increase in cell number. In some cases, both hypertrophy and hyperplasia can occur together, leading to a significant increase in the overall size and function of the organ or tissue.

"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.

Decorin is a small proteoglycan, a type of protein with a attached sugar chain, that is found in the extracellular matrix of connective tissues in the body. It is composed of a core protein and one or more glycosaminoglycan (GAG) chains, specifically dermatan sulfate. Decorin plays important roles in the organization and biomechanical properties of collagen fibrils, regulation of cell proliferation and migration, and modulation of growth factor activity. It has been studied for its potential role in various physiological and pathological processes, including wound healing, fibrosis, and cancer.

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.

Fibrosis is a pathological process characterized by the excessive accumulation and/or altered deposition of extracellular matrix components, particularly collagen, in various tissues and organs. This results in the formation of fibrous scar tissue that can impair organ function and structure. Fibrosis can occur as a result of chronic inflammation, tissue injury, or abnormal repair mechanisms, and it is a common feature of many diseases, including liver cirrhosis, lung fibrosis, heart failure, and kidney disease.

In medical terms, fibrosis is defined as:

"The process of producing scar tissue (consisting of collagen) in response to injury or chronic inflammation in normal connective tissue. This can lead to the thickening and stiffening of affected tissues and organs, impairing their function."

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.

Physiologic calcification is the normal deposit of calcium salts in body tissues and organs. It is a natural process that occurs as part of the growth and development of the human body, as well as during the repair and remodeling of tissues.

Calcium is an essential mineral that plays a critical role in many bodily functions, including bone formation, muscle contraction, nerve impulse transmission, and blood clotting. In order to maintain proper levels of calcium in the body, excess calcium that is not needed for these functions may be deposited in various tissues as a normal part of the aging process.

Physiologic calcification typically occurs in areas such as the walls of blood vessels, the lungs, and the heart valves. While these calcifications are generally harmless, they can sometimes lead to complications, particularly if they occur in large amounts or in sensitive areas. For example, calcification of the coronary arteries can increase the risk of heart disease, while calcification of the lung tissue can cause respiratory symptoms.

It is important to note that pathologic calcification, on the other hand, refers to the abnormal deposit of calcium salts in tissues and organs, which can be caused by various medical conditions such as chronic kidney disease, hyperparathyroidism, and certain infections. Pathologic calcification is not a normal process and can lead to serious health complications if left untreated.

Collagenases are a group of enzymes that have the ability to break down collagen, which is a structural protein found in connective tissues such as tendons, ligaments, and skin. Collagen is an important component of the extracellular matrix, providing strength and support to tissues throughout the body.

Collagenases are produced by various organisms, including bacteria, animals, and humans. In humans, collagenases play a crucial role in normal tissue remodeling and repair processes, such as wound healing and bone resorption. However, excessive or uncontrolled activity of collagenases can contribute to the development of various diseases, including arthritis, periodontitis, and cancer metastasis.

Bacterial collagenases are often used in research and medical applications for their ability to digest collagen quickly and efficiently. For example, they may be used to study the structure and function of collagen or to isolate cells from tissues. However, the clinical use of bacterial collagenases is limited due to concerns about their potential to cause tissue damage and inflammation.

Overall, collagenases are important enzymes that play a critical role in maintaining the health and integrity of connective tissues throughout the body.

In medical terms, the skin is the largest organ of the human body. It consists of two main layers: the epidermis (outer layer) and dermis (inner layer), as well as accessory structures like hair follicles, sweat glands, and oil glands. The skin plays a crucial role in protecting us from external factors such as bacteria, viruses, and environmental hazards, while also regulating body temperature and enabling the sense of touch.

Aminopropionitrile is a chemical compound with the formula NPN(H2)CH2CH2CN. It is an irritant that can cause damage to the eyes, skin, and respiratory system. It is used in the manufacture of certain plastics and resins, and has also been studied for its potential effects on the human body. Some research suggests that aminopropionitrile may interfere with the normal functioning of collagen, a protein that helps to provide structure and support to tissues and organs in the body. This has led to interest in the use of aminopropionitrile as a potential treatment for certain conditions related to collagen, such as scleroderma. However, more research is needed to determine the safety and effectiveness of this use.

Tight collagen helix The most common collagen is type I collagen which makes up 90% of all collagen. It is found in all dermal ... show that the collagen hybridizing peptide probes can be used across species and collagen types (including type IV collagen), ... Collagen IV (ColIV or Col4) is a type of collagen found primarily in the basal lamina. The collagen IV C4 domain at the C- ... Collagen IV is the more common usage, as opposed to the older terminology of "type-IV collagen".[citation needed] Collagen IV ...
Type I collagen Collagen, type III, alpha 1 Park KS, Park MJ, Cho ML, Kwok SK, Ju JH, Ko HJ, Park SH, Kim HY (2009). "Type II ... Type II collagen is organised into fibrils. This fibrillar network of collagen allows the cartilage to entrap the proteoglycan ... Collagen+type+II at the U.S. National Library of Medicine Medical Subject Headings (MeSH) v t e (Articles with short ... Type II collagen is the basis for hyaline cartilage, including the articular cartilages at joint surfaces. It is formed by ...
It is related to the fibrillar collagens: type II, type XI, and type XXIV. Current research suggests that it is made by ... Type XXVII collagen is the protein predicted to be encoded by COL27A1. It was first described by Dr. James M. Pace and his ... v t e (Articles lacking sources from December 2009, All articles lacking sources, Collagens, All stub articles, Protein stubs) ...
... is a type of collagen which can be cleaved to form endostatin. The endostatin is from the c terminus end of ... This type of mutation particularly affects only one isoform of type XVIII collagen - the short isoform type, while the medium ... which codes for production of type XVIII collagen. It is speculated that the mutation of type XVIII collagen that occurs in ... When type XVIII collagen is mutated at the COL18A1 gene, exon 2 in the sequence is skipped, which results in production of an ...
Collagen Type II collagen Collagen, type I, alpha 1 Collagen, type I, alpha 2 Collagen, type III, alpha 1 "Collagen: What it is ... Type I collagen is the most abundant collagen of the human body, consisting of around 90% of the body's total collagen. It ... The cross-links result in the formation of very strong mature type I collagen fiber. See Collagen, type I, alpha 1#Clinical ... to make a molecule of type I pro-collagen. These triple-stranded, rope-like pro-collagen molecules must be processed by enzymes ...
... is a part of the family of collagen proteins consisting of Collagen I- Collagen XXVIII. Collagen proteins are ... type V collagen preproprotein, CO5A1_HUMAN, and collagen type V alpha. Type V collagen can also be abbreviated to COLV or ... Type V collagen is a part of the Extracellular Matrix (ECM). Collagen V is gene expression modulated by TGF-β. Type V collagen ... Together, Collagen V and Collagen I acts as a dominant regulator of collagen fibrillogenesis. Type V Collagens interacts with ...
"Duplication of type IV collagen COOH-terminal repeats and species-specific expression of alpha 1(IV) and alpha 2(IV) collagen ... "Entrez Gene: COL4A2 collagen, type IV, alpha 2". Hinek A (1995). "Nature and the multiple functions of the 67-kD elastin-/ ... Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another ... This gene encodes one of the six subunits of type IV collagen, the major structural component of basement membranes. The C- ...
... types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of ... This gene encodes one of the chains for type I collagen, the fibrillar collagen found in most connective tissues. Mutations in ... Type-I collagen Collagen GRCh38: Ensembl release 89: ENSG00000164692 - Ensembl, May 2017 GRCm38: Ensembl release 89: ... "Entrez Gene: COL1A2 collagen, type I, alpha 2". Byers PH, Wallis GA, Willing MC (1991). "Osteogenesis imperfecta: translation ...
The COL11A1 gene encodes one of the two alpha chains of type XI collagen, a minor fibrillar collagen. Type XI collagen is a ... collagen cDNA demonstrates that type XI belongs to the fibrillar class of collagens and reveals that the expression of the gene ... "Entrez Gene: COL11A1 collagen, type XI, alpha 1". GeneReviews/NCBI/NIH/UW entry on Stickler Syndrome Yoshioka H, Ramirez F ( ... Keene DR, Oxford JT, Morris NP (1995). "Ultrastructural localization of collagen types II, IX, and XI in the growth plate of ...
It encodes the alpha chain of type XVII collagen. Collagen XVII is a transmembrane protein, like collagen XIII, XXIII and XXV. ... which in turn causes a type of osteogenesis imperfecta. Collagen, type XVII, alpha 1 has been shown to interact with Keratin 18 ... Collagen XVII is a homotrimer of three alpha1(XVII)-chains and a transmembrane protein in type II orientation. Each 180 kD a- ... 2015). "Mutations in collagen, type XVII, alpha 1 (COL17A1) cause epithelial recurrent erosion dystrophy (ERED)". Hum. Mutat. ...
Type IX collagen, a heterotrimeric molecule, is usually found in tissues containing type II collagen, a fibrillar collagen. ... sites in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type ... This gene encodes one of the three alpha chains of type IX collagen, the major collagen component of hyaline cartilage. ... "Entrez Gene: COL9A3 collagen, type IX, alpha 3". GeneReviews/NCBI/NIH/UW entry on Multiple Epiphyseal Dysplasia, Dominant ...
"COL21A1 collagen, type XXI, alpha 1". Entrez Gene: COL21A1. United States National Center for Biotechnology Information. Chou ... "Genomic organization and characterization of the human type XXI collagen (COL21A1) gene". Genomics. 79 (3): 395-401. doi: ... Collagen alpha-1(XXI) chain is a protein that in humans is encoded by the COL21A1 gene. The protein is an extracellular matrix ...
"Entrez Gene: COL23A1 collagen, type XXIII, alpha 1". Banyard J, Bao L, Zetter BR (June 2003). "Type XXIII collagen, a new ... The molecule of collagen XXIII can be found either in membrane-bond form or in shed form. Type XXIII collagen is expressed in ... Collagen XXIII is a type II transmembrane protein and the fourth in the subfamily of non-fibrillar transmembranous collagens. ... Collagen XXIII shows structural homology with collagen XIII and collagen XXV . Apart from having the characteristic structure ...
"Entrez Gene: COL8A1 collagen, type VIII, alpha 1". Shuttleworth CA (1998). "Type VIII collagen". Int. J. Biochem. Cell Biol. 29 ... This gene encodes one of the two alpha chains of type VIII collagen. The gene product is a short chain collagen and a major ... Plenz GA, Deng MC, Robenek H, Völker W (2003). "Vascular collagens: spotlight on the role of type VIII collagen in ... The type VIII collagen fibril can be either a homo- or a heterotrimer. Alternatively spliced transcript variants encoding the ...
"Entrez Gene: COL6A1 collagen, type VI, alpha 1". Bertini E, Pepe G (2002). "Collagen type VI and related disorders: Bethlem ... "Type VI collagen anchors endothelial basement membranes by interacting with type IV collagen". J. Biol. Chem. 272 (42): 26522-9 ... The protein encoded by this gene is the alpha 1 subunit of type VI collagen (alpha1(VI) chain). Mutations in the genes that ... 1996). "Type VI collagen mutations in Bethlem myopathy, an autosomal dominant myopathy with contractures". Nat. Genet. 14 (1): ...
Latvanlehto A, Snellman A, Tu H, Pihlajaniemi T (2003). "Type XIII collagen and some other transmembrane collagens contain two ... Collagen XIII belongs to the transmembranous subfamily of collagens, like collagen XVII, XXIII and XXV. GRCh38: Ensembl release ... 2002). "The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and ... 1998). "Type XIII collagen is identified as a plasma membrane protein". J. Biol. Chem. 273 (25): 15590-7. doi:10.1074/jbc. ...
Type XV collagen is known to be a tumor suppressor that can be used to understand tumor cells environment. Type XV collagen ... This gene encodes the alpha chain of type XV collagen, a member of the FACIT collagen family (fibril-associated collagens with ... "Epitope-defined monoclonal antibodies against multiplexin collagens demonstrate that type XV and XVIII collagens are expressed ... Hägg PM, Hägg PO, Peltonen S, Autio-Harmainen H, Pihlajaniemi T (June 1997). "Location of type XV collagen in human tissues and ...
Type IX collagen is usually found in tissues containing type II collagen, a fibrillar collagen. Studies in knockout mice have ... sites in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type ... This gene encodes one of the three alpha chains of type IX collagen, a collagen component of hyaline cartilage. ... "Entrez Gene: COL9A1 collagen, type IX, alpha 1". GeneReviews/NCBI/NIH/UW entry on Multiple Epiphyseal Dysplasia, Dominant ...
... type III collagen is also an important regulator of the diameter of type I and II collagen fibrils. Type III collagen is also ... types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of ... Type III collagen could also be important in several other human diseases. Increased amounts of type III collagen are found in ... Type III collagen is one of the fibrillar collagens whose proteins have a long, inflexible, triple-helical domain. Type III ...
... types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of ... Collagen, type I, alpha 1, also known as alpha-1 type I collagen, is a protein that in humans is encoded by the COL1A1 gene. ... the structure of type I collagen is compromised. Tissues that are rich in type I collagen, such as the skin, bones, and tendons ... Ehlers-Danlos type IV is most attributed to abnormalities in the reticular fibers (collagen Type III). Ehlers-Danlos syndrome, ...
"Entrez Gene: COL25A1 collagen, type XXV, alpha 1". Kakuyama H, Söderberg L, Horigome K, et al. (2006). "CLAC binds to ... Collagen, type XXV, alpha 1 has been shown to interact with Amyloid precursor protein. GRCh38: Ensembl release 89: ... CLAC-P/collagen type XXV". EMBO J. 21 (7): 1524-34. doi:10.1093/emboj/21.7.1524. PMC 125364. PMID 11927537. " ... Collagen alpha-1(XXV) chain is a protein that in humans is encoded by the COL25A1 gene. COL25A1 is a brain-specific membrane- ...
Type XXVII collagen is related to the "fibrillar" class of collagens and may play a role in development of the skeleton. ... COL27A1 is a type XXVII collagen. It was discovered by James Pace. This gene appears to be turned on in cartilage, the eye, and ... Fibrillar collagens, such as COL27A1, compose one of the most ancient families of extracellular matrix molecules. They form ... Collagen alpha-1 (XXVII) chain (COL27A1) is a protein that in humans is encoded by the COL27A1 gene. ...
... related to type XI collagen and it is possible that the collagen chains of types V and XI constitute a single collagen type ... Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in ... type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen. This ... "Entrez Gene: COL5A3 collagen, type V, alpha 3". van der Rest M, Garrone R (1991). "Collagen family of proteins". FASEB J. 5 (13 ...
... of type IV collagen in synovial capillaries by immunohistochemistry using a monoclonal antibody against human type IV collagen ... Collagen Type-IV collagen Alport syndrome GRCh38: Ensembl release 89: ENSG00000188153 - Ensembl, May 2017 GRCm38: Ensembl ... "Entrez Gene: COL4A5 collagen, type IV, alpha 5 (Alport syndrome)". Lemmink HH, Schröder CH, Monnens LA, Smeets HJ (1997). "The ... Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another ...
... or collagen IV NC1 domain) is a duplicated domain present at the C-terminus of type IV collagens. Each type IV collagen ... Structural basis for type IV collagen assembly in basement membranes". J. Biol. Chem. 277 (34): 31142-53. doi:10.1074/jbc. ... In molecular biology, the type IV collagen C4 domain ( ... The collagen IV C4 domain is composed of two similarly folded ... domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link". Proc. Natl. Acad. ...
This protein is an alpha chain of type VI collagen that aids in microfibril formation. As part of type VI collagen, this ... This gene encodes the alpha 3 chain, one of the three alpha chains of type VI collagen, a beaded filament collagen found in ... "The 1.6 A structure of Kunitz-type domain from the alpha 3 chain of human type VI collagen". Journal of Molecular Biology. 246 ... "Anisotropic behaviour of the C-terminal Kunitz-type domain of the alpha3 chain of human type VI collagen at atomic resolution ( ...
... also known as COL28A1 is a protein that in humans is encoded by the COL28A1 gene. This protein ... "COL28A1 collagen, type XXVIII, alpha 1 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2015-09-25. v t e ... belongs to a class of collagens that contain von Willebrand factor type A domains. The protein is encoded by the COL28A1 gene ... Veit G, Kobbe B, Keene DR, Paulsson M, Koch M, Wagener R (Feb 2006). "Collagen XXVIII, a novel von Willebrand factor A domain- ...
... chain of type II collagen. This gene encodes the alpha-1 chain of type II collagen, a fibrillar collagen found in cartilage and ... "A COL2A1 mutation in achondrogenesis type II results in the replacement of type II collagen by type I and III collagens in ... type 2 by affecting tissues that are rich in type II collagen. Platyspondylic lethal skeletal dysplasia, Torrance type:Fewer ... chain that cannot be incorporated into type II collagen fibers. As a result, cells make a reduced amount of type II collagen. ...
This gene encodes the alpha chain of type XIX collagen, a member of the FACIT collagen family (fibril-associated collagens with ... other members of this collagen family are found in association with fibril-forming collagens such as type I and II, and serve ... collagen (COL12A1), alpha 1(IX) collagen (COL9A1), and alpha 1(XIX) collagen (COL19A1) to human chromosome 6q12-q13". Genomics ... "Entrez Gene: COL19A1 collagen, type XIX, alpha 1". Yoshioka H, Zhang H, Ramirez F, et al. (1992). "Synteny between the loci for ...
"Entrez Gene: COL14A1 collagen, type XIV, alpha 1 (undulin)". "COL14A1 - Collagen alpha-1(XIV) chain precursor - Homo sapiens ( ... 2005). "Collagen types XII and XIV are present in basement membrane zones during human embryonic development". J. Mol. Histol. ... Tono-Oka S, Tanase S, Miike T, Tanaka H (1996). "Transient expression of collagen type XIV during muscle development and its ... Collagen alpha-1(XIV) chain is a protein that in humans is encoded by the COL14A1 gene. It likely plays a role in collagen ...
Tight collagen helix The most common collagen is type I collagen which makes up 90% of all collagen. It is found in all dermal ... show that the collagen hybridizing peptide probes can be used across species and collagen types (including type IV collagen), ... Collagen IV (ColIV or Col4) is a type of collagen found primarily in the basal lamina. The collagen IV C4 domain at the C- ... Collagen IV is the more common usage, as opposed to the older terminology of "type-IV collagen".[citation needed] Collagen IV ...
Find your collagen supplements today at ProHealth Longevity. ... Decreased collagen production can cause numerous age-related ... What Types of Collagen Are Included in Longevity Collagen Peptides? ProHealths Longevity Collagen Peptides contains types 1,2, ... Multi-Collagen Blend (Beef Collagen, Marine Collagen, Eggshell Membrane Collagen, Chicken Collagen). 20 g. †. ... Longevity Collagen Peptides mixes well in hot or cold liquid. What Flavor is Longevity Collagen Peptides? Longevity Collagen ...
... which encodes the alpha 3 chain of type IV collagen, or in the COL4A4 gene, which encodes the alpha 4 chain of type IV collagen ... Molecular cloning of the human Goodpasture antigen demonstrates it to be the alpha 3 chain of type IV collagen. Turner, N., ... Sequence and localization of a partial cDNA encoding the human alpha 3 chain of type IV collagen. Morrison, K.E., Mariyama, M ... Patients with Goodpastures disease have two normal COL4A3 alleles encoding the NC1 domain of the type IV collagen alpha 3 ...
A type 2 Collagen supplement with non-hydrolysed collagen which is beneficial for the skin & joints. In Stock. ... How does Collagen Type 2 work?. As Collagen Type 2 is manufactured by low-temperature methods, the collagens long chain of ... Type 2 Collagen parallels the amino acid structure of our own bodys collagen type 2 and is the most abundant structural ... Collagen Type 2 contains natural nutrients to supply the body with all the ingredients required to make Collagen Type 2 protein ...
Collagen is a fibrous protein found in the extracellular matrix and connective tissue. Type I collagen is the most common form ... of collagen prevalent in bones, tendons and skin. ... Type I collagen is the most common form of collagen prevalent ... HUVEC Cells cultured in negative control surface Type I Bovine Collagen coated Plate. ... HUVEC Cells cultured in negative control surface Type I Bovine Collagen coated Plate. ...
Type XVII collagen (BP 180) in the developing avian cornea. M K Gordon; J M Fitch; J W Foley; D R Gerecke; C Linsenmayer; D E ... M K Gordon, J M Fitch, J W Foley, D R Gerecke, C Linsenmayer, D E Birk, T F Linsenmayer; Type XVII collagen (BP 180) in the ... Type XVII collagen (BP 180) in the developing avian cornea. You will receive an email whenever this article is corrected, ... RESULTS: The same alpha 1 (XVII) collagen/BP 180 mRNA is present in cornea and skin. The appearance of alpha 1 (XVII) collagen ...
... measurements and to assess bone resorption by urinary excretion measurement of C-terminal telopeptide of type I collagen (CTX) ... The present study was carried out to assess the effects of fluoride exposure on collagen metabolism by evaluating the level of ... Jethi RK, Chander L, Singh J (1977) Kinetic evidence for a step-wise process in collagen-induced in vitro calcification. Indian ... Gupta LC, Singla SK, Tandon C, Jethi RK (2004) Mg2+: a potent inhibitor of collagen-induced in vitro mineralization. Magnes Res ...
Publication types * Randomized Controlled Trial * Research Support, Non-U.S. Govt MeSH terms * Adult ... Tendon collagen I mRNA expression and tendon collagen protein synthesis increased by 3.9-fold and 1.3-fold, respectively (P , ... 0.01 and P = 0.02), and muscle collagen I mRNA expression and muscle collagen protein synthesis increased by 2.3-fold and 5.8- ... To test the hypothesis that GH promotes matrix collagen synthesis in musculotendinous tissue, we investigated the effects of 14 ...
This formula contains grass-fed and pasture-raised peptides blended with any favorite liquid to increase collagen protein in ... BUBS Naturals Collagen Protein is a daily remedy to support the deterioration of strength and joints due to aging. ... It includes types I and III collagen, and it provides users with the amino acids commonly associated with collagen, including ... Where does collagen come from?. The collagen found in BUBS Naturals Collagen Protein comes exclusively from grass-fed cows, ...
Fish skin, like the Asian seabass, is composed of collagen type I, the same kind of collagen found in human skin and rich in ... Collagen is the bodys most abundant protein and a mainstream ingredient for beauty. Type XXI collagen transcends a common ... Collagen Reimagined, Discover Biodesigned Type XXI Geltor , Download Product Brochure * Empowering natural barrier function for ... Collagen Reimagined, Discover Biodesigned Type XXI Content provided by Geltor , 20-Mar-2024 , Product Brochure ...
Collagen VI-related myopathy is a group of disorders that affect skeletal muscles and connective tissues. Explore symptoms, ... These genes each provide instructions for making one component of a protein called type VI collagen. Type VI collagen makes up ... and COL6A3 genes result in a decrease or lack of type VI collagen or the production of abnormal type VI collagen. While it is ... Research suggests that type VI collagen helps secure and organize the extracellular matrix by linking the matrix to the cells ...
Type 1 vs 2 vs 3; marine vs bovine; hydrolyzed vs gelatin) and what these differences mean for you. ... We explain the types of collagen (e.g. ... Type 3 Collagen. As we said before, Type 1 and Type 3 collagen ... Marine Collagen vs Bovine Collagen Bovine collagen consists of Type 1and Type 3 collagen. Bovine collagen can be found in the ... Type 2 Collagen. Type 2 collagen is only produced by chondrocytes, meaning you will find it in your cartilage. Type 2 collagen ...
Collagen Peptides Market Share was $699 million in 2023, and is expected to reach $922 million by 2028, growing at a CAGR of ... collagen peptides are derived from Type 1 collagen through a hydrolysis process. This is the same type of collagen found in ... Collagens present in the skin are responsible for skin structure. Collagen fibers present in the human skin get damaged with ... How big is the collagen peptides market?. The global collagen peptides market size was $699 million in 2023, and is projected ...
Collagen Type 3. Type iii Collagen. Type 3 Collagen. Collagen iii. Related Terms: COL3A1, Collagen type III, alpha 1, Collagen ... III, alpha-1 polypeptide, Collagen, Type III, Alpha 1 (Ehlers-Danlos syndrime type IV, autosomal dominant, EDS4A ... MD Bioproducts Purified type III bovine collagen. 10 mg. Kollagen Typ 3. Collagen 1 and 3. ... Collagen Type I and III, Canine, 10 mg Purified type I & III canine collagen. Type I collagen is the most abundant collagen and ...
Tag: type 1 marine collagen Beauty Discover the Secret of Marine Collagen and Reclaim Youthful Looking Skin. Jessica Milli - ...
Anti-Human Type I Collagen Antibody, Clone 1C1F8. Product Name. Anti-Human Type I Collagen Antibody, Clone 1C1F8. ... Collagen *Human Anti-Type I/II Collagen. *Human Anti-Type V Collagen ... Collagen *Human Anti-Type I/II Collagen. *Human Anti-Type V Collagen ... Rat Anti-Type I/II Collagen. *Rat Anti-Type I/II Collagen Subtype ... Rat Anti-Type I/II Collagen. *Rat Anti-Type I/II Collagen ...
Then, they type collagen bioessay 1 continue colliding and form no5. This lm is the work of others. The pronoun with which ... icle-ge) 8.55 bioessay collagen type 1. Allow time for three years. I can guarantee that a word is not or at the macroscopic, ... Bioessay collagen type 1 for essay on skinner. *compare and contrast essay purdue owl. ... please] don t agree type collagen bioessay 1 with. A school district s functional level expenditures data was also calculated ...
In this White Paper, we explore the different types of collagen sources, collagen digestion and absorption, and explain how NEM ... Collagen Supplementation: Which Type? Which Source? What does it do? Content provided by Stratum Nutrition , 13-Jul-2023 , ... BioCell Collagen® is a clinically studied dietary supplement ingredient composed of naturally-occurring hydrolyzed collagen ... BioCell Collagen Science Review Content provided by BioCell Technology, LLC , 13-Jul-2023 , White Paper ...
type. Contribution to journal publication status. published. subject. *Biomaterials Science. keywords. Rats, Animals, ... An ultra-low dose of BMP-2/7 delivered via a collagen-HA (CHA) scaffold leads to accelerated healing of a critical femoral ... An ultra-low dose of BMP-2/7 delivered via a collagen-HA (CHA) scaffold leads to accelerated healing of a critical femoral ... We first show that the incorporation of hydroxyapatite in collagen-based BMP delivery systems is pivotal for achieving ...
Buy the best Collagen skincare products and supplements, for a healthier complexion and a minimised look of fine lines and ... Which skin types is Collagen best for?. Collagen is suitable for all skin types, to provide your skin with ultra-hydration and ... Collagen Shot is an advanced collagen drink from Proto-col that uses innovative technology to deliver Type I and III collagen, ... Collagen. Collagen Skincare Products. What is Collagen?. Collagen is a protein naturally produced in your body. It plays an ...
Undenatured Type ii Collagen, Etc. From Shanghai, China. ... Exporter, Manufacturer & Supplier of Bovine Type ii Collagen, ... Bovine Type ii Collagen Containing Type i And Type iii Collagen. *Excellent Water soluble Bovine Collagen Type II Can Relieve ... Undenatured Type ii Chicken Collagen *Undenatured type ii collagen is Type ii collagen extracted from Chicken sternum ... Bovine Collagen Type ii *Bovine Collagen Powder for Sports Nutrition Products. *Bovine Type ii Collagen Powder for Bone Health ...
Type II collagen. Heres another one that we usually think of as benefiting skin: Collagen, although type II is the kind thats ... "Containing the building blocks of joint cartilage, type II collagen has a significant effect on reducing swelling, discomfort, ... those taking type II collagen at a dose of 40 mg daily had less pain and stiffness after six months compared with those taking ... Both types of fatty acids may have some benefit for joint pain from arthritis. ...
Type II Collagen Complex provides BioCell Collagen®, a low molecular weight, water-soluble glycosaminoglycan complex completely ... Made with BioCell Collagen. Jarrow Formulas® Type II Collagen Complex provides BioCell Collagen®, a low molecular weight, water ... Jarrow Formulas Type II Bioavailable Collagen Complex 500 mg 60 Capsules. by Jarrow FormulasSKU: 1529051 ... Certain types of items cannot be returned, like perishable goods (such as food, flowers, or plants), custom products (such as ...
This gene encodes one of the two alpha chains of type XI collagen, a minor fibrillar collagen. Type XI collagen is a ... collagen alpha-1(XI) chain. Names. collagen XI, alpha-1 polypeptide. collagen, type XI, alpha 1. deafness, autosomal dominant ... COL11A1 collagen type XI alpha 1 chain [Homo sapiens] COL11A1 collagen type XI alpha 1 chain [Homo sapiens]. Gene ID:1301 ... collagen type XI alpha 1 chainprovided by HGNC. Primary source. HGNC:HGNC:2186 See related. Ensembl:ENSG00000060718 MIM:120280; ...
However, during the natural ageing process, the amount of collagen we can produce decreases and as a result, skin loses its ... ️PREMIUM BRAND VERISOL®. Collagen is the major structural component of skin, comprising about 80% of its dry weight and ... Marine Collagen Peptides Powder - Type I - High in Protein - Clinically Studied Brand VERISOL® - Skin, Hair, Nail, Joint & Bone ... VERISOL collagen is derived from freshwater fish.. ✔️PREMIUM QUALITY, MADE TO GMP STANDARDS. Manufactured to GMP quality ...
Promote smooth skin and strong connective tissues, plus joint health with Piping Rock collagen. Shop now! ... Collagen is the most abundant protein in the body. ... Multi Collagen Protein (Types I, II, III, V, X), 2000 mg (per ... Collagen Peptides Type I & III Powder PeptiFit, 1 lb (454 g) Bottle. ... Collagen Joint Formula with Glucosamine Plus Powder ArthFree, 1.12 lb (510 g) Bottle. ...
COL7A1 elisa Test :: Human collagen, type VII, alpha 1 ELISA Test 24T ... type VII, alpha 1 ELISA Test 24T. https://www.cortex-biochem.com/shop/0544-mbs908240-24t-col7a1-elisa-test-human-collagen-type- ...
Refill Type) 210g , Q10, Fine Japan. Lifting regains youthful vitality in your skin by renewing its elasticity and firmness ... Fish Collagen Peptide, Condensed Milk Powder, Pearl Coix Extract, Elastin Peptide, Kaneka Q10(Reduced Coenzyme Q10), Dextrin, ... Our product provides 150 mg Hyaluronic acid, 5,250 mg collagen, 15 mg Elastin, 450 mg Pearl coix extract, 100 mg Vitamin C and ...
BSE-Free Hydrolyzed Collagen Types 1 and 3. Doctors Best Collagen Types 1 and 3 contains hydrolyzed collagen protein (BSE-Free ... Doctors Best Collagen Types 1 and 3 with Peptan and Vitamin C, 1,000 mg, 180 Tablets. Doctors Best Collagen Types 1 and 3 ... s Best Collagen Types 1 and 3 with Peptan and Vitamin C, 1,000 mg, 180 Tablets Increase quantity for Doctor's Best Collagen ... Collagen is the structural protein essential for the strength of bones and flexibility of joints, tendons, ligaments, hair, ...
  • 1. Proksch E, Segger D, Degwert J, Schunck M, Zague V, Oesser S. Oral supplementation of specific collagen peptides has beneficial effects on human skin physiology: a double-blind, placebo-controlled study. (prohealth.com)
  • 2. König D, Oesser S, Scharla S, Zdzieblik D, Gollhofer A. Specific Collagen Peptides Improve Bone Mineral Density and Bone Markers in Postmenopausal Women-A Randomized Controlled Study. (prohealth.com)
  • Effects of marine collagen peptides on glucose metabolism and insulin resistance in type 2 diabetic rats. (prohealth.com)
  • Collagen can't be used in its whole form, so it must be broken down into smaller pieces, known as peptides. (prohealth.com)
  • Hydrolyzed peptides are the most effective form of collagen which allows your body to use it almost immediately. (prohealth.com)
  • This formula contains grass-fed and pasture-raised peptides blended with any favorite liquid to increase collagen protein in the body. (juneauempire.com)
  • the different forms of collagen (hydrolyzed peptides vs gelatin) as well as different sources of collagen (bovine vs. marine vs chicken vs. etc). (furtherfood.com)
  • The global collagen peptides market size was USD 665 million in 2022 and is projected to grow from USD 699 million in 2023 to USD 922 million in 2028 at a CAGR of 5.7% in the 2023-2028 period. (marketsandmarkets.com)
  • The value of collagen peptides has significantly risen due to its increased utilization in various sectors such as medical, cosmetics, food, and pharmaceutical applications. (marketsandmarkets.com)
  • Collagen peptides are being used in cosmetic and personal care products. (marketsandmarkets.com)
  • As the population ages globally and per capita incomes rise, the demand for collagen peptides market used in cosmetics and personal care products is poised to rise in the coming times. (marketsandmarkets.com)
  • Hence, they prefer pork-based collagen peptides. (marketsandmarkets.com)
  • These cultural and regional outlooks pose a restraint for the growth of collagen peptides market. (marketsandmarkets.com)
  • Government initiatives toward a healthy lifestyle would lead to an increase in the demand for these products, directly affecting the collagen peptides market. (marketsandmarkets.com)
  • Collagen peptides are primarily sourced from animal by-products, such as bovine hides, fish scales, or chicken cartilage. (marketsandmarkets.com)
  • BioCell Collagen® is a clinically studied dietary supplement ingredient composed of naturally-occurring hydrolyzed collagen type II peptides, chondroitin. (nutraingredients-usa.com)
  • in Kiel, Germany (2020), showed that supplementation with these fish-derived Bioactive Collagen Peptides®, at a daily dose of 5 grams, significantly improved skin elasticity and reduced wrinkle volume after 4 weeks. (vita-nuova.com)
  • 300g VERISOL® F Marine Collagen Peptides Powder. (vita-nuova.com)
  • Jarrow Formulas® Type II Collagen Complex provides BioCell Collagen®, a low molecular weight, water-soluble glycosaminoglycan complex completely derived from chicken sternum cartilage. (dailyvita.com)
  • But you might not understand the various types of collagen, and that different types of collagen have different effects on the body. (furtherfood.com)
  • As you consider supplementing with collagen , It's critical to know the different types of collagen because each one consists of different proteins that serve different functions. (furtherfood.com)
  • In this White Paper, we explore the different types of collagen sources, collagen digestion and absorption, and explain how NEM® and unhydrolyzed eggshell. (nutraingredients-usa.com)
  • This is one of the main reasons cosmetics and skin care manufacturers prefer to formulate products using collagen when developing anti-aging cosmetic products for topical application. (cosmeticsdesign-europe.com)
  • Also, collagen IV lacks the regular glycine in every third residue necessary for the tight, collagen helix. (wikipedia.org)
  • It also lacks a glycine in every third amino acid residue that is responsible for the tight collagen helix, as a result it will be more flexible and kinked than other types of collagen. (wikipedia.org)
  • One of the amino acids found in collagen, glycine, can help improve digestion by increasing stomach acid. (prohealth.com)
  • Marine collagen is typically high in glycine, which positively supports insulin and blood sugar management. (prohealth.com)
  • The triple-helical structure of collagen arises from its unusual abundance of three amino acids: glycine, proline, and hydroxyproline. (neuromics.com)
  • It includes types I and III collagen, and it provides users with the amino acids commonly associated with collagen, including glycine and proline. (juneauempire.com)
  • To summarize, the process of collagen synthesis occurs mainly in the cells of fibroblasts which are specialized cells with the main function of synthesizing collagen. (wikipedia.org)
  • Collagen synthesis occurs both intracellularly and extracellularly. (wikipedia.org)
  • To test the hypothesis that GH promotes matrix collagen synthesis in musculotendinous tissue, we investigated the effects of 14 day administration of 33-50 microg kg(-1) day(-1) recombinant human GH (rhGH) in healthy young individuals. (nih.gov)
  • Thus, increased GH availability stimulates matrix collagen synthesis in skeletal muscle and tendon, but without any effect upon myofibrillar protein synthesis. (nih.gov)
  • Asian seabass skin, specifically, has been shown to contain " a variety of beneficial properties such as good wound-healing and antioxidant activities, fibroblast proliferation activities, and collagen synthesis enhancement ​," qualifying it as an excellent candidate for topical cosmetic formulation. (cosmeticsdesign-europe.com)
  • Proline is especially important for the stimulation of collagen synthesis as well as acting as an antioxidant and preventing cell damage from free radicals. (furtherfood.com)
  • Researchers have described several forms of collagen VI-related dystrophy, which range in severity: Bethlem muscular dystrophy is the mildest, an intermediate form is moderate in severity, and Ullrich congenital muscular dystrophy is the most severe. (medlineplus.gov)
  • Variants (also known as mutations) in the COL6A1 , COL6A2 , and COL6A3 genes can cause the various forms of collagen VI-related dystrophy. (medlineplus.gov)
  • HUVEC Cells cultured in negative control surface Type I Bovine Collagen coated Plate. (neuromics.com)
  • Purified type III bovine collagen. (mdbioproducts.com)
  • Immunization Grade Collagen type II (CII) protein, purified from fetal bovine articular cartilage, for the induction of arthritis in the Collagen-I. (mdbioproducts.com)
  • Since its approval in 1981, bovine collagen had been the only US Food and Drug Administration (FDA)-approved dermal filler more than a decade. (medscape.com)
  • Collagen decreases as the body ages, and consumers do not naturally produce the same amount of collagen as they formerly did when they were in their 20s and 30s. (juneauempire.com)
  • However, during the natural ageing process, the amount of collagen we can produce decreases and as a result, skin loses its firmness, which in turn leads to wrinkles and a loss of elasticity. (vita-nuova.com)
  • Type 2 Collagen supplements contain 50-55% Collagen Type 2 and naturally contain 45-50% carbohydrates (chondroitin, glucosamine & hyaluronic acid), the major components of joint cartilage. (victoriahealth.com)
  • Hydrolyzed collagen has a wide application in nutritional foods and dietary supplements that are being consumed at a large scale by consumers. (marketsandmarkets.com)
  • Collagen Supplements Sale! (muscleandstrength.com)
  • There are six human genes associated with it: COL4A1, COL4A2, COL4A3, COL4A4, COL4A5, COL4A6 Type IV collagen is a type of collagen that is responsible for providing a scaffold for stability and assembly. (wikipedia.org)
  • These interactions form the core of the type IV collagen scaffold. (wikipedia.org)
  • The scaffold evolves into a collagen IV superstructure by "end-to-end" and lateral connections between collagen IV protomers. (wikipedia.org)
  • In this study, we compared the osteoinductive potential of BMP-2 homodimer with a heterodimer of BMP-2/7, both delivered via a collagen-hydroxyapatite (CHA) scaffold delivery system, with the aim to reduce the overall therapeutic BMP doses and the associated side-effects. (lu.se)
  • Incorporation of hydroxyapatite (HA) in a collagen scaffold dramatically improves bone morphogenic protein (BMP) sequestration via biophysical interactions with BMP, thereby providing more controlled BMP release compared with pristine collagen. (lu.se)
  • An ultra-low dose of BMP-2/7 delivered via a collagen-HA (CHA) scaffold leads to accelerated healing of a critical femoral defect in rats while a 20-times higher BMP-2 dose was required to achieve comparable results. (lu.se)
  • In order to control biofilm formation, sequester proteolytic enzymes, and provide a biocompatible scaffold to support healing, the investigators utilize a purified collagen matrix containing polyhexamethylene biguanide (PCMP) in a case series of 9 wounds on 8 patients with multiple comorbidities who did not respond to previous conventional or adjuvant therapy. (medscape.com)
  • Collagen supplementation has been shown to support skin health to improve signs of aging, such as wrinkles and decreased puffiness. (prohealth.com)
  • Effect of collagen supplementation on osteoarthritis symptoms: a meta-analysis of randomized placebo-controlled trials. (prohealth.com)
  • Collagen peptide supplementation in combination with resistance training improves body composition and increases muscle strength in elderly sarcopenic men: A randomised controlled trial. (prohealth.com)
  • Supplementation is often required to restore this production, and that's exactly what the BUBS Naturals Collagen Protein aims to help with. (juneauempire.com)
  • Collagen Supplementation: Which Type? (nutraingredients-usa.com)
  • A new study confirms that supplementation with VERISOL® F can be just as effective as consuming meat collagen. (vita-nuova.com)
  • Type III collagen is the second most abundant collagen in tissues and is found most commonly in tissues exhibiting elastic properties such. (mdbioproducts.com)
  • Type III collagen is the second most abundant collagen in tissues and is found most commonly in tissues exhibiting elastic properties such as skin, lungs, intestinal walls and walls of blood vessels. (mdbioproducts.com)
  • The collagen molecule is then formed. (wikipedia.org)
  • CONCLUSIONS: The differences between human BP 180/collagen XVII and the chicken corneal molecule represent species divergence. (arvojournals.org)
  • Collagen is the most abundant protein your body makes. (prohealth.com)
  • Type 2 Collagen parallels the amino acid structure of our own body's collagen type 2 and is the most abundant structural protein found in joints. (victoriahealth.com)
  • Here we explain the most abundant collagen types (Type I and Type III and many, many other types! (furtherfood.com)
  • This is because these two types of collagen are the most abundant and serve similar functions. (furtherfood.com)
  • While there are 18 amino acids in collagen, in particular four key amino acids found within these two types of collagen help keep our bodies healthy and feeling great. (furtherfood.com)
  • Through interactions with specific cellular receptors such as integrins, the basement membrane collagen IV networks not only provide structural support to the cells and tissues, but they also affect the biological rate during and after the development. (wikipedia.org)
  • Types 1 and 3 collagen are produced by osteoblasts and fibroblasts, which are cells located in our connective tissues and cells that create bones respectively. (furtherfood.com)
  • Type 1 collagen can be found all over the body excluding cartilaginous tissues (see Type 2). (furtherfood.com)
  • 1% sodium bicarbonate (NaHCO ) dis- ions in tissues such as collagen or muscle. (who.int)
  • RESULTS: The same alpha 1 (XVII) collagen/BP 180 mRNA is present in cornea and skin. (arvojournals.org)
  • The appearance of alpha 1 (XVII) collagen mRNA and protein shows similar temporal patterns of expression, with changes in the mRNA preceding those of the protein by approximately 2 days. (arvojournals.org)
  • The appearance of alpha 1 (XVII) collagen mRNA and protein is regulated closely, with the protein lagging. (arvojournals.org)
  • The alpha-3 subunit (COL4A3) of collagen IV is thought to be the antigen implicated in Goodpasture syndrome, wherein the immune system attacks the basement membranes of the glomeruli and the alveoli upon the antigenic site on the alpha-3 subunit becomes unsequestered due to environmental exposures. (wikipedia.org)
  • Alport syndrome is a nephritic syndrome caused by a mutation in the COL4A3 , COL4A4 , and COL4A5 genes that encode the alpha-5 chain of type IV collagen and results in altered type IV collagen strands. (msdmanuals.com)
  • Named for Glen "BUB" Doherty, the strength of this 20gram collagen protein powder is inspired by a US soldier that died as he defended the United States in 2012 in Benghazi. (juneauempire.com)
  • To best evaluate the potential benefits of Asian seabass skin by-product derived hydrolyzed collagen, researchers formulated a serum using hydrolyzed collagen powder enriched with added vitamins including C, E, and B3. (cosmeticsdesign-europe.com)
  • These amino acids in collagen appear in a characteristic repeating motif Gly-X-Y, where X is usually proline and Y is usually hydroxyproline. (neuromics.com)
  • Another important essential amino acid in Type 1 and 3 collagen is proline. (furtherfood.com)
  • When collagen type 2 protein is exposed to high temperature, the delicate hyaluronic acid and amino acid molecules naturally present, become less effective as most of the lipid molecules are washed away by the hydrolysis process. (victoriahealth.com)
  • Amount Per Advanced Health Solutions Collagen Type 2 Tablet: Collagen Type 2 600mg with naturally occuring Hyaluronic Acid, Glucosamine and Condroitin, Boswellia (65% Boswellia Acids) 160mg, Cinnamon (Cinnamomum Cassia) 80mg, Turmeric Root Extract( 95% Curcuminoids) 6mg, Quercetin (96% Quercetin Dihydrate) 4mg. (victoriahealth.com)
  • It is a homotrimer comprised of three alpha-1 chains and resembles other fibrillar collagens in structure and function. (mdbioproducts.com)
  • It is synthesized as procollagen, similary to collagen I, but the N-terminal propeptide remains attached in the mature fibrillar type III form. (mdbioproducts.com)
  • This gene encodes one of the two alpha chains of type XI collagen, a minor fibrillar collagen. (nih.gov)
  • Collagen Type 2 is a nutritional dietary supplement that supplies all necessary elements to help the body to support joint health. (victoriahealth.com)
  • This is the only collagen type that is encoded by six different genes. (wikipedia.org)
  • Mutations to the genes[COL4A5] coding for collagen IV lead to Alport syndrome. (wikipedia.org)
  • These genes each provide instructions for making one component of a protein called type VI collagen. (medlineplus.gov)
  • Variants in the COL6A1 , COL6A2 , and COL6A3 genes result in a decrease or lack of type VI collagen or the production of abnormal type VI collagen. (medlineplus.gov)
  • While it is true that collagen provides the supple texture to skin that leaves most of us wrinkle-free, collagen is also a necessity for the bones, muscles, digestion, and joints. (juneauempire.com)
  • Collagen offers protection from bone loss and supports healthy bones and joints to allow you to move more freely and painlessly. (prohealth.com)
  • Decreased collagen production can cause numerous age-related effects including wrinkles, shrinking and weak muscles, stiff joints and tendons, joint pain, weakening bones, limited joint mobility, gut imbalances and reduced blood flow. (prohealth.com)
  • Type I collagen is the most common form of collagen prevalent in bones, tendons and skin. (neuromics.com)
  • Valine is associated explicitly with collagen and elastin, while leucine helps users heal the user's skin and bones simultaneously. (juneauempire.com)
  • Collagen is the building block for many parts of the body, including skin, bones, and tendons. (furtherfood.com)
  • These two types of collagen are key components in the maintenance of skin, nails, bones, hair, and muscles. (furtherfood.com)
  • New discoveries keep unraveling information about genetic mutations, biosynthesis, molecular assembly, and network formation of type IV collagen, and this increases the understanding of the critical role of this collagen in health and disease. (wikipedia.org)
  • As a food supplement, adults to take two tablets of Advanced Health Solutions Collagen Type 2 to be taken twice daily with a meal or a glass of water, or as directed by your healthcare professional. (victoriahealth.com)
  • It is found in all dermal layers at high proportions while type IV collagen is only found at the basement membrane of the epidermal junction. (wikipedia.org)
  • Ethical and sustainability concerns related to animal welfare, overfishing, and environmental impact can pose challenges for the collagen industry. (marketsandmarkets.com)
  • Collagen Type 2 contains natural nutrients to supply the body with all the ingredients required to make Collagen Type 2 protein and support the joints. (victoriahealth.com)
  • BUBS Naturals Collagen Protein is a daily remedy to support the deterioration of strength and joints due to aging. (juneauempire.com)
  • Type 2 collagen comes from chicken, and is helpful in the support of your joints and cartilage, possibly able to help support your jaw, back, and joints - this includes reducing those irritating popping knees. (furtherfood.com)
  • Mutations of type III collagen causes Ehlers-Danlos syndrome, EDS IV, which affect arteries, internal organs, joints and skin, and may cause sudden death when the large arteries rupture. (mdbioproducts.com)
  • Advanced Health Solutions Collagen Type 2 is an Un-Hydrolyzed Collagen food supplement that provides all necessary nutrients to promote healthy joint cartilage and to repair the damage that causes the pain and swelling associated with arthritis. (victoriahealth.com)
  • Type 2 collagen is only produced by chondrocytes, meaning you will find it in your cartilage. (furtherfood.com)
  • Type 2 collagen makes up 50-60% of cartilage protein. (furtherfood.com)
  • Ingredients: Calcium Carbonate, Di Calcium Phosphate, Collagen Type 2 Protein, Boswellia (Boswellia Serrata), Cinnamon (Cinnamomom Cassia) Turmeric Root Extract (Curcuma Longa), Quercetin (Quercetin Dihydrate), Magnesium Stearate (vegetable Source), Silicon Dioxide. (victoriahealth.com)
  • PURPOSE: Previous sequence analyses of hemidesmosomal BP 180/collagen XVII cDNA from human skin and of a similar chicken corneal cDNA showed some similarities, but major differences as well. (arvojournals.org)
  • METHODS: Cornea and skin BP 180/collagen XVII cDNAs were cloned by reverse transcription-polymerase chain reaction (RT-PCR) and sequenced. (arvojournals.org)
  • Collagen is crucial to the health of the body , even though most consumers are more familiar with this protein in terms of how it can affect the skin. (juneauempire.com)
  • Specifically, researchers investigated the use of hydrolyzed collagen derived from fish skin cast-offs to see if it could be a beneficial bioactive ingredient for topical cosmetic application. (cosmeticsdesign-europe.com)
  • Fish skin, like the Asian seabass, is composed of collagen type I, the same kind of collagen found in human skin and rich in protein and amino acids. (cosmeticsdesign-europe.com)
  • Further, hydrolyzed collagen acts as a natural moisturizer, and applying collagen-enriched skin care products on human skin can boost natural collagen production and retention, helping the skin maintain elasticity. (cosmeticsdesign-europe.com)
  • Collagen is so important because it makes up 70% of our skin (the human body's biggest organ) and 90% of both our connective tissue and organic bone mass. (furtherfood.com)
  • The collagen that we mentioned previously that makes up 70% of our skin is Type 1 collagen. (furtherfood.com)
  • Type 1 collagen is key to replenishing skin and consequently helping to reverse aging. (furtherfood.com)
  • Clinical trials in patients who supplemented with Type 1 collagen showed enhanced skin hydration and firmness as well as a decrease in wrinkles. (furtherfood.com)
  • Collagens present in the skin are responsible for skin structure. (marketsandmarkets.com)
  • Collagen fibers present in the human skin get damaged with time, losing thickness and strength, resulting in skin aging. (marketsandmarkets.com)
  • Collagen Type IV is a type of collagen found primarily in the skin within the basement. (mdbioproducts.com)
  • It plays an important role in maintaining happy and healthy skin, but as you get older, the collagen your body produces declines. (facethefuture.co.uk)
  • Introducing collagen into your skincare routine will improve your skin's elasticity, leaving your skin looking more youthful and plumper. (facethefuture.co.uk)
  • Which skin types is Collagen best for? (facethefuture.co.uk)
  • Collagen is suitable for all skin types, to provide your skin with ultra-hydration and minimise the appearance of fine lines and wrinkles. (facethefuture.co.uk)
  • What are the main skin benefits of Collagen? (facethefuture.co.uk)
  • Collagen is the major structural component of skin, comprising about 80% of its dry weight and naturally produced by our bodies from amino acids. (vita-nuova.com)
  • [ 6 ] For information on all types of skin cancer, visit Medscape's Skin Cancer Resource Center . (medscape.com)
  • As we age, the body's ability to make the protein Type 2 Collagen slows down. (victoriahealth.com)
  • Mutations in this gene are associated with type II Stickler syndrome and with Marshall syndrome. (nih.gov)
  • An in vitro system employing collagen isolated from the sheep tendons to induce mineralization and demineralization reactions was used not only to study the effect of various concentrations of fluoride on the collagen-induced mineralization and demineralization reactions but also to compare their action with the inhibitors of mineralization and/or demineralization. (fluoridealert.org)
  • Collagen is a fibrous protein found in the extracellular matrix and connective tissue. (neuromics.com)
  • Type VI collagen makes up part of the extracellular matrix that surrounds muscle cells and connective tissue. (medlineplus.gov)
  • Research suggests that type VI collagen helps secure and organize the extracellular matrix by linking the matrix to the cells it surrounds. (medlineplus.gov)
  • Collagen IV (ColIV or Col4) is a type of collagen found primarily in the basal lamina. (wikipedia.org)
  • Circulating type IV collagen (COLIV) is a new potential CLM marker. (bvsalud.org)
  • COLIV levels were also related to the type of CLM. (bvsalud.org)
  • COLIV and CEA levels were analysed, and the type of CLM was classified using paraffinated tissue . (bvsalud.org)
  • To begin, this type of collagen is synthesized by the assembly of a specific trimer, when the three NC1 domains initiate molecular interactions between the three α-chains. (wikipedia.org)
  • citation needed] Parallel direction of fibers in Type I Depending on genetic and nongenetic factors including alterations in gene expression, splice variations, post-translational modifications, and the chain-specific assembly of particular α-chains, different organs can be affected during their development and in the adult life span. (wikipedia.org)
  • The six α-chains of collagen IV can recognize each other with incredible specificity and will assemble into unique heterotrimers. (wikipedia.org)
  • 99%) Collagen type II (CII) protein, purified from chicken sternum, for the induction of arthritis in the Collagen-Induced Art. (mdbioproducts.com)
  • The collagen IV C4 domain at the C-terminus is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel. (wikipedia.org)
  • These results coincided with the larger occurrence of diffuse collagen III deposition and the scarce presence of MMP- 2 and -9 spread among the fibrous tissue. (bvsalud.org)
  • It's the most common type of arthritis, affecting approximately 3.9 million Canadians aged 20 years and older. (readersdigest.ca)
  • Tight collagen helix The most common collagen is type I collagen which makes up 90% of all collagen. (wikipedia.org)
  • Supplementing with Type 1 and 3 collagen has been shown to have a number of health benefits for the body, including slowing hair loss, reducing wrinkles, thickening fine hair and reducing fine lines, improving circulation, supporting the matrix of our bone structures, and strengthening nail beds. (furtherfood.com)
  • Introduction and Objective: Because L-PRP constitutes an important source of growth factor that is associated with osteogenesis and fibrogenesis, the aim of this study was to evaluate the effect of L-PRP on the presence of collagen III and MMP-2 and MMP-9, while comparing these results by means of a histomorphometric analysis of bone matrix and fibrous deposition on bone repair. (bvsalud.org)
  • Thus, the aim of this study was to verify the immunolocalization of MMP-2 and -9 and collagen III in rabbit calvarium bone defects treated with and without L-PRP insertion. (bvsalud.org)
  • At higher concentrations, fluoride was also found to inhibit the demineralization of the collagen bound preformed mineral phase. (fluoridealert.org)
  • More often than not, Types 1 and 3 collagen are typically grouped together. (furtherfood.com)
  • Decreased collagen production leads to less support around key bodily processes, including tissue repair and heart health. (prohealth.com)
  • Pro-collagen is added to support quality collagen production, which is especially important after age 60. (prohealth.com)
  • The fibrogenic response to short and long SWCNTs was assessed via oxidative stress generation, collagen expression and transforming growth factor-beta (TGF-beta) production as potential fibrosis biomarkers. (cdc.gov)
  • Long SWCNTs were significantly more potent than short SWCNTs in terms of reactive oxygen species (ROS) response, collagen production and TGF-beta release. (cdc.gov)
  • Individuals with collagen VI-related dystrophy often have signs and symptoms of multiple forms of this condition, so it can be difficult to assign a specific diagnosis. (medlineplus.gov)
  • These two features cause the collagen to form in a sheet, the form of the basal lamina. (wikipedia.org)
  • Two collagen IV protomers associate through the carboxy-terminal NC1 trimer to form the NC1 hexamer. (wikipedia.org)
  • Lastly, the type IV collagen molecules bind together to form a complex protein network. (wikipedia.org)
  • The intermediate form of collagen VI-related dystrophy is characterized by muscle weakness that begins in infancy. (medlineplus.gov)
  • Structure of native collagen confirmed by ability to form microfibrils. (mdbioproducts.com)
  • Then, they type collagen bioessay 1 continue colliding and form no5. (internexus.edu)