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Von Willebrand Factor Type C Domain
Von Willebrand factor, type C (VWFC or VWC)is a protein domain is found in various blood plasma proteins: complement factors B, C2, CR3 and CR4; the integrins (I-domains); collagen types VI, VII, XII and XIV; and other extracellular proteins. Function Although the majority of VWA-containing proteins are extracellular, the most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription, DNA repair, ribosomal and membrane transport and the proteasome. A common feature appears to be involvement in multiprotein complexes. Proteins that incorporate vWF domains participate in numerous biological events (e.g. cell adhesion, migration, homing, pattern formation, and signal transduction), involving interaction with a large array of ligands. Mutation effects A number of human diseases arise from mutations in VWA domains. The domain is named after the von Willebrand factor (VWF) type C repeat which is found in multidomain protein/mult ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Domain
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer aft ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Von Willebrand Factor C And EGF Domain-containing Protein
The term ''von'' () is used in German language surnames either as a nobiliary particle indicating a noble patrilineality, or as a simple preposition used by commoners that means ''of'' or ''from''. Nobility directories like the ''Almanach de Gotha'' often abbreviate the noble term ''von'' to ''v.'' In medieval or early modern names, the ''von'' particle was at times added to commoners' names; thus, ''Hans von Duisburg'' meant "Hans from he city ofDuisburg". This meaning is preserved in Swiss toponymic surnames and in the Dutch or Afrikaans ''van'', which is a cognate of ''von'' but does not indicate nobility. Usage Germany and Austria The abolition of the monarchies in Germany and Austria in 1919 meant that neither state has a privileged nobility, and both have exclusively republican governments. In Germany, this means that legally ''von'' simply became an ordinary part of the surnames of the people who used it. There are no longer any legal privileges or constraints assoc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Mucin 5B
Mucin-5B (MUC-5B) is a protein that in humans is encoded by the ''MUC5B'' gene and by ''Muc5b'' gene in mouse. It is one of the five gel-forming mucins. MUC-5B can be found in whole saliva, normal lung mucus, and cervical mucus. In some diseases such as COPD, chronic rhinosinusitis (CRS), and H. pylori-associated gastric disease. Synthesis All mucins are synthesized in secretory cells known, dependent on the tissue they are located in, as goblet cell Goblet cells are simple columnar epithelial cells that secrete gel-forming mucins, like mucin 5AC. The goblet cells mainly use the merocrine method of secretion, secreting vesicles into a duct, but may use apocrine methods, budding off their secre ...s or mucous cells. Their creation, while still not completely understood, begins in the endoplasmic reticulum. From there, the Golgi apparatus build the O-linked glycans found in mucins. Finally, they are packaged into secretory granules. References 05B {{protein-stu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Mucin 2
Mucin 2, oligomeric mucus gel-forming, also known as MUC2, is a protein that in humans is encoded by the ''MUC2'' gene. Function This gene encodes a member of the mucin protein family. The protein encoded by this gene, also called mucin 2, is secreted onto mucosal surfaces. Mucin 2 is particularly prominent in the gut where it is secreted from goblet cells in the epithelial lining into the lumen of the large intestine. There, mucin 2, along with small amounts of related-mucin proteins, polymerizes into a gel of which 80% by weight is oligosaccharide side-chains that are added as post-translational modifications to the mucin proteins. This gel provides an insoluble mucous barrier that serves to protect the intestinal epithelium. Genetics The mucin 2 protein features a central domain containing tandem repeats rich in threonine and proline Proline (symbol Pro or P) is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Mucin
Mucins () are a family of high molecular weight, heavily glycosylated proteins (glycoconjugates) produced by epithelial tissues in most animals. Mucins' key characteristic is their ability to form gels; therefore they are a key component in most gel-like secretions, serving functions from lubrication to cell signalling to forming chemical barriers. They often take an inhibitory role. Some mucins are associated with controlling mineralization, including nacre formation in mollusks, calcification in echinoderms and bone formation in vertebrates. They bind to pathogens as part of the immune system. Overexpression of the mucin proteins, especially MUC1, is associated with many types of cancer. Although some mucins are membrane-bound due to the presence of a hydrophobic membrane-spanning domain that favors retention in the plasma membrane, most mucins are secreted as principal components of mucus by mucous membranes or are secreted to become a component of saliva. Genes Human muci ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Collagen, Type V, Alpha 2
Collagen alpha-2(V) chain is a protein that in humans is encoded by the ''COL5A2'' gene. This gene encodes an alpha chain for one of the low abundance fibrillar collagens. Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in tissues containing type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen. This gene product is closely related to type XI collagen and it is possible that the collagen chains of types V and XI constitute a single collagen type with tissue-specific chain combinations. Mutations in this gene are associated with Ehlers-Danlos syndrome, classical type, formerly known as types I and II. See also * Type-V collagen *TSR1 RTS 1 (french: RTS Un) is a Swiss public television channel owned by RTS Radio Télévision Suisse, the public broadcaster for the Romand people. History Launched on 1 May 1954 to succeed Télé Genà ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Collagen, Type III, Alpha 1
Type III Collagen is a homotrimer, or a protein composed of three identical peptide chains (monomers), each called an alpha 1 chain of type III collagen. Formally, the monomers are called collagen type III, alpha-1 chain and in humans are encoded by the gene. Type III collagen is one of the fibrillar collagens whose proteins have a long, inflexible, triple-helical domain. Protein structure and function Type III collagen is synthesized by cells as a pre-procollagen. The signal peptide is cleaved off producing a procollagen molecule. Three identical type III procollagen chains come together at the carboxy-terminal ends, and the structure is stabilized by the formation of disulphide bonds. Each individual chain folds into left-handed helix and the three chains are then wrapped together into a right-handed superhelix, the triple helix. Prior to assembling the super-helix, each monomer is subjected to a number of post-translational modifications that occur while the monomer is b ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Collagen, Type II, Alpha 1
Collagen, type II, alpha 1 (primary osteoarthritis, spondyloepiphyseal dysplasia, congenital), also known as COL2A1, is a human gene that provides instructions for the production of the pro-alpha1(II) chain of type II collagen. Function This gene encodes the alpha-1 chain of type II collagen, a fibrillar collagen found in cartilage and the vitreous humor of the eye. Mutations in this gene are associated with achondrogenesis, chondrodysplasia, early onset familial osteoarthritis, SED congenita, Langer-Saldino achondrogenesis, Kniest dysplasia, Stickler syndrome type I, and spondyloepimetaphyseal dysplasia Strudwick type. In addition, defects in processing chondrocalcin, a calcium binding protein that is the C-propeptide of this collagen molecule, are also associated with chondrodysplasia. There are two transcripts identified for this gene. Type II collagen, which adds structure and strength to connective tissues, is found primarily in cartilage, the jelly-like substance that ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Collagen, Type I, Alpha 1
Collagen, type I, alpha 1, also known as alpha-1 type I collagen, is a protein that in humans is encoded by the gene. ''COL1A1'' encodes the major component of type I collagen, the fibrillar collagen found in most connective tissues, including cartilage. Function Collagen is a protein that strengthens and supports many tissues in the body, including cartilage, bone, tendon, skin and the white part of the eye (sclera). The gene produces a component of type I collagen, called the pro-alpha1(I) chain. This chain combines with another pro-alpha1(I) chain and also with a pro-alpha2(I) chain (produced by the gene) to make a molecule of type I procollagen. These triple-stranded, rope-like procollagen molecules must be processed by enzymes outside the cell. Once these molecules are processed, they arrange themselves into long, thin fibrils that cross-link to one another in the spaces around cells. The cross-links result in the formation of very strong mature type I collagen fibers ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Collagen
Collagen () is the main structural protein in the extracellular matrix found in the body's various connective tissues. As the main component of connective tissue, it is the most abundant protein in mammals, making up from 25% to 35% of the whole-body protein content. Collagen consists of amino acids bound together to form a triple helix of elongated fibril known as a collagen helix. It is mostly found in connective tissue such as cartilage, bones, tendons, ligaments, and skin. Depending upon the degree of mineralization, collagen tissues may be rigid (bone) or compliant (tendon) or have a gradient from rigid to compliant (cartilage). Collagen is also abundant in corneas, blood vessels, the gut, intervertebral discs, and the dentin in teeth. In muscle tissue, it serves as a major component of the endomysium. Collagen constitutes one to two percent of muscle tissue and accounts for 6% of the weight of the skeletal muscle tissue. The fibroblast is the most common cell that crea ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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