Information about Collagen Xvii
Collagen XVII, previously called BP180, is a transmembrane protein which plays a critical role in maintaining the linkage between the intracellular and the extracellular structural elements involved in epidermal adhesion [1].
Structure
Collagen XVII is a homotrimer of three alpha1(XVII)-chains [2] and a transmembrane protein in type II orientation. Each 180 kD a-chain contains a globular intracellular domain of approximately 70 kDa, which interacts with beta4-integrin, plectin, and BP230 [3][4] and is necessary for the stable attachment of hemidesmosomes to keratin intermediate filaments. The large C-terminal ectodomain with a molecular mass of approximately 120 kDa consists of 15 collagenous subdomains, characterized by typical collagenous G-X-Y repeat sequences, flanked by 16 short non-collagenous stretches. The overall structure of the ectodomain is that of a flexible, rod like triple-helix [5] [6] with a significant thermal stability [7][8]. The membrane proximal part of the ectodomain, within amino acids 506-519, is responsible for binding to alpha 6 integrin, this binding seems to be important for the collagen XVII integration into hemidesmosomes. The largest collagenous domain, Col15, which contains 232 amino acids (amino acids 567-808), contributes significantly to stability of collagen XVII homotrimer. The C-terminus of collagen XVII binds to laminin 5, and correct integration of laminin 5 into the matrix requires collagen XVII.Pathology
Mutations in the human collagen XVII gene, COL17A1, lead to the absence or structural alterations of collagen XVII [9]. The functional consequences include diminished epidermal adhesion and skin blistering in response to minimal shearing forces . The disorder is called junctional epidermolysis bullosa, an autosomal recessive skin disease with variable clinical phenotypes. Morphological characteristics of junctional epidermolysis bullosa are rudimentary hemidesmosomes and subepidermal tissue separation. Clinical hallmarks, in addition to blisters and erosions of the skin and mucous membranes, include nail dystrophy, loss of hair, and dental anomalies. Collagen XVII also plays a role as an autoantigen in acquired subepithelial blistering disorders [10]. Most immunodominant epitopes lie within the NC16A domain, and the binding of the autoantibodies perturbs adhesive functions of the collagen XVII, and this (together with inflammation-related processes) leads to epidermal-dermal separation and skin blistering.Shedding
Collagen XVII is constitutively shed from the keratinocyte surface within NC16A domain by TACE (TNF-Alpha Converting Enzyme), metalloproteinase of the ADAM family [11]. The shedding is lipid raft dependent [12]. Collagen XVII is extracellularly phosphorylated by ecto-casein kinase 2 within the NC16A domain, phosphorylation negatively regulates ectodomain shedding.Images
Caption1 | Caption2 |
References
1. ^ Franzke, C. W., Bruckner, P., and Bruckner-Tuderman, L. (2005) Collagenous transmembrane proteins: recent insights into biology and pathology. J.Biol. Chem. 280: 4005-4008
2. ^ Hirako, Y., Usukura, J., Nishizawa, Y., and Owaribe, K. (1996) Demonstration of the molecular shape of BP180, a 180-kDa bullous pemphigoid antigen and its potential for trimer formation. J.Biol. Chem. 271: 13739-13745
3. ^ Hopkinson, S. B., Findlay, K., deHart, G. W., and Jones, J. C. (1998) Interaction of BP180 (type XVII collagen) and alpha 6 integrin is necessary for stabilization of hemidesmosome structure. J.Invest Dermatol. 111: 1015-1022
4. ^ Hopkinson, S. B. and Jones, J. C. (2000) The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmosome. Mol. Biol.Cell 11: 277-286
5. ^ Hirako, Y., Usukura, J., Nishizawa, Y., and Owaribe, K. (1996) Demonstration of the molecular shape of BP180, a 180-kDa bullous pemphigoid antigen and its potential for trimer formation. J.Biol. Chem. 271: 13739-13745
6. ^ Hirako, Y., Usukura, J., Uematsu, J., Hashimoto, T., Kitajima, Y., and Owaribe, K. (1998) Cleavage of BP180, a 180-kDa bullous pemphigoid antigen, yields a 120-kDa collagenous extracellular polypeptide. J.Biol. Chem. 273: 9711-9717
7. ^ Schacke, H., Schumann, H., Hammami-Hauasli, N., Raghunath, M., and Bruckner-Tuderman, L. (1998) Two forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomain. J.Biol. Chem. 273: 25937-25943
8. ^ Areida, S. K., Reinhardt, D. P., Muller, P. K., Fietzek, P. P., Kowitz, J., Marinkovich, M. P., and Notbohm, H. (2001) Properties of the collagen type XVII ectodomain. Evidence for n- to c-terminal triple helix folding. J.Biol. Chem. 276: 1594-1601
9. ^ Zillikens, D. and Giudice, G. J. (1999) BP180/type XVII collagen: its role in acquired and inherited disorders or the dermal-epidermal junction. Arch Dermatol. Res 291: 187-194
10. ^ Zillikens, D. (1999) Acquired skin disease of hemidesmosomes. J.Dermatol. Sci. 20: 134-154
11. ^ Franzke, C. W., Tasanen, K., Borradori, L., Huotari, V., and Bruckner-Tuderman, L. (2004) Shedding of collagen XVII/BP180: structural motifs influence cleavage from cell surface. J.Biol. Chem. 279: 24521-24529
12. ^ Zimina EP, Bruckner-Tuderman L, Franzke CW. (2005). Shedding of collagen XVII ectodomain depends on plasma membrane microenvironment. J Biol Chem. 280(40):34019-24.
2. ^ Hirako, Y., Usukura, J., Nishizawa, Y., and Owaribe, K. (1996) Demonstration of the molecular shape of BP180, a 180-kDa bullous pemphigoid antigen and its potential for trimer formation. J.Biol. Chem. 271: 13739-13745
3. ^ Hopkinson, S. B., Findlay, K., deHart, G. W., and Jones, J. C. (1998) Interaction of BP180 (type XVII collagen) and alpha 6 integrin is necessary for stabilization of hemidesmosome structure. J.Invest Dermatol. 111: 1015-1022
4. ^ Hopkinson, S. B. and Jones, J. C. (2000) The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmosome. Mol. Biol.Cell 11: 277-286
5. ^ Hirako, Y., Usukura, J., Nishizawa, Y., and Owaribe, K. (1996) Demonstration of the molecular shape of BP180, a 180-kDa bullous pemphigoid antigen and its potential for trimer formation. J.Biol. Chem. 271: 13739-13745
6. ^ Hirako, Y., Usukura, J., Uematsu, J., Hashimoto, T., Kitajima, Y., and Owaribe, K. (1998) Cleavage of BP180, a 180-kDa bullous pemphigoid antigen, yields a 120-kDa collagenous extracellular polypeptide. J.Biol. Chem. 273: 9711-9717
7. ^ Schacke, H., Schumann, H., Hammami-Hauasli, N., Raghunath, M., and Bruckner-Tuderman, L. (1998) Two forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomain. J.Biol. Chem. 273: 25937-25943
8. ^ Areida, S. K., Reinhardt, D. P., Muller, P. K., Fietzek, P. P., Kowitz, J., Marinkovich, M. P., and Notbohm, H. (2001) Properties of the collagen type XVII ectodomain. Evidence for n- to c-terminal triple helix folding. J.Biol. Chem. 276: 1594-1601
9. ^ Zillikens, D. and Giudice, G. J. (1999) BP180/type XVII collagen: its role in acquired and inherited disorders or the dermal-epidermal junction. Arch Dermatol. Res 291: 187-194
10. ^ Zillikens, D. (1999) Acquired skin disease of hemidesmosomes. J.Dermatol. Sci. 20: 134-154
11. ^ Franzke, C. W., Tasanen, K., Borradori, L., Huotari, V., and Bruckner-Tuderman, L. (2004) Shedding of collagen XVII/BP180: structural motifs influence cleavage from cell surface. J.Biol. Chem. 279: 24521-24529
12. ^ Zimina EP, Bruckner-Tuderman L, Franzke CW. (2005). Shedding of collagen XVII ectodomain depends on plasma membrane microenvironment. J Biol Chem. 280(40):34019-24.
Protein: fibrous proteins | |
|---|---|
| Collagen | Type-I (COL1A1) - Type-II (COL2A1) - Type-III - Type-IV - Type-V - Type XI (COL11A2) - Type-XVII - Type-XVIII |
| Keratin/Cytokeratin | type I (10, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21), type II (1, 2A, 3, 4, 5, 6A, 7, 8, 9), Hair (Type I, Type II), Beta |
| other | Elastin - |
Collagen is the main protein of connective tissue in animals and the most abundant protein in mammals, [1] making up about 25% of the total protein content.
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Uses
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Integrins are cell surface receptors that interact with the extracellular matrix and mediate various intracellular signals. They define cellular shape, mobility, and regulate the cell cycle.
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Plectin is a giant protein (c500 kDa) found in nearly all mammalian cells which acts as a link between the three main components of the cytoskeleton: actin microfilaments, microtubules and intermediate filaments.
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Hemidesmosomes (HD) are very small stud- or rivet-like structures on the inner basal surface of keratinocytes in the epidermis of skin. They are similar in form to desmosomes.
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Keratins are a family of fibrous structural proteins; tough and insoluble, they form the hard but nonmineralized structures found in reptiles, birds, amphibians and mammals. They are rivaled as biological materials in toughness only by chitin.
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MeSH D004820 Epidermolysis Bullosa (EB) is a rare genetic disease characterized by the presence of extremely fragile skin and recurrent blister formation, resulting from minor mechanical friction or trauma.
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Bullous pemphigoid
Classification & external resources
ICD-10 L 12.0
ICD-9 694.5
Bullous pemphigoid, also referred to as BP, is a chronic autoimmune skin disease, involving the formation of blisters below the surface of the skin and
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Classification & external resources
ICD-10 L 12.0
ICD-9 694.5
Bullous pemphigoid, also referred to as BP, is a chronic autoimmune skin disease, involving the formation of blisters below the surface of the skin and
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Proteins are large organic compounds made of amino acids arranged in a linear chain and joined together by peptide bonds between the carboxyl and amino groups of adjacent amino acid residues.
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Fibrous proteins, also called scleroproteins, are long filamentous protein molecules that form one of the two main classes of tertiary structure protein (the other being globular proteins). Fibrous proteins are only found in animals.
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Collagen is the main protein of connective tissue in animals and the most abundant protein in mammals, [1] making up about 25% of the total protein content.
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Uses
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Identifiers
Symbol COL1A2
Alt. Symbols OI4
Entrez 1278
HUGO 2198
OMIM 120160
RefSeq NM_000089
UniProt P08123
Other data
Locus Chr. 7 q21.3-22.1 Type-I collagen is the most abundant collagen of the human body.
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Symbol COL1A2
Alt. Symbols OI4
Entrez 1278
HUGO 2198
OMIM 120160
RefSeq NM_000089
UniProt P08123
Other data
Locus Chr. 7 q21.3-22.1 Type-I collagen is the most abundant collagen of the human body.
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COL1A1 (collagen, type I, alpha 1) is a human gene that is one of several genes that provide instructions for making components of collagen. Collagen is a protein that strengthens and supports many tissues in the body, including cartilage, bone, tendon, skin and the white
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Type-II collagen is the basis for articular cartilage and hyaline cartilage.
It makes up 50% of all protein in cartilage and 85-90% of collagen of articular cartilage.
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It makes up 50% of all protein in cartilage and 85-90% of collagen of articular cartilage.
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COL2A1 (collagen, type II, alpha 1 (primary osteoarthritis, spondyloepiphyseal dysplasia, congenital)) is a human gene that provides instructions for the production of the pro-alpha1(II) chain of type II collagen.
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Type-III collagen is a fibrous scleroprotein in bone and cartilage and tendon and other connective tissue; yields gelatin on boiling.
Scleroprotein is a simple protein found in horny and cartilaginous tissues and in the lens of the eye.
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Scleroprotein is a simple protein found in horny and cartilaginous tissues and in the lens of the eye.
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Type-IV collagen is a type of collagen found primarily in the basal lamina. The C-terminus domain is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel.
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Type-V collagen is a form of fibrillar[1] collagen associated with classical Ehlers-Danlos syndrome.
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Genes
- COL5A1 , COL5A2 , COL5A3
References
1.
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COL11A2 (collagen, type XI, alpha 2) is a human gene that is one of several genes that provide instructions for the production of type XI collagen. The COL11A2 gene produces one component of this type of collagen, called the pro-alpha2(XI) chain.
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Type XVIII collagen is a type of collagen which can be cleaved to form endostatin.
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External links
- MeSH Collagen+Type+XVIII
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Keratins are a family of fibrous structural proteins; tough and insoluble, they form the hard but nonmineralized structures found in reptiles, birds, amphibians and mammals. They are rivaled as biological materials in toughness only by chitin.
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Cytokeratins are intermediate filament keratins found in the intracytoplasmic cytoskeleton of epithelial tissue. There are two types of cytokeratins: the low weight, acidic type I cytokeratins and the high weight, basic or neutral type II cytokeratins.
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Type I keratins (or Type I cytokeratins) constitutes the Type I intermediate filaments (IFs) of the intracytoplasmatic cytoskeleton, which is present in all mammalian epithelial cells.
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Keratin 10 is a type I cytokeratin. Mutations in the gene encoding this protein are associated with the variants of epidermolytic hyperkeratosis in which the palms and soles of the feet are unaffected.
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Keratin 12 is a keratin found expressed in corneal epithelia. Mutations in the gene encoding this protein lead to Meesmann corneal dystrophy.
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Keratin 13 is a type I cytokeratin, it is paired with keratin 4 and found in the suprabasal layers of non-cornified stratified epithelia. Mutations in the gene encoding this protein and keratin 4 have been associated with the autosomal dominant disorder White Sponge Nevus.
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Keratin 14 is a type I cytokeratin. It is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells.
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Keratin 15 is a type I cytokeratin. It is found in some progenitor basal cells within complex epithelia.
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Keratin 16 is a type I cytokeratin. It is paired with keratin 6 in a number of epithelial tissues, including nail bed, esophagus, tongue, and hair follicles. Mutations in the gene encoding this protein are associated with the genetic skin disorders pachyonychia congenita,
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Keratin 17 is a type I cytokeratin. It is found in nail beds, hair follicles, sebaceous glands, and other epidermal appendages. Mutations in the gene encoding this protein lead to Jackson-Lawler type pachyonychia congenita and steatocystoma multiplex.
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Keratin 18 is a type I cytokeratin. It is, together with its filament partner keratin 8, perhaps the most commonly found products of the intermediate filament gene family. They are expressed in single layer epithelial tissues of the body.
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