Collagen, type XVII, alpha 1

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COL17A1
Identifiers
AliasesCOL17A1, BA16H23.2, BP180, BPA-2, BPAG2, LAD-1, ERED, collagen type XVII alpha 1, collagen type XVII alpha 1 chain
External IDsOMIM: 113811 HomoloGene: 133558 GeneCards: COL17A1
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)[1]
Chromosome 10 (human)
Genomic location for COL17A1
Genomic location for COL17A1
Band10q25.1Start104,031,286 bp[1]
End104,086,002 bp[1]
RNA expression pattern
PBB GE COL17A1 204636 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_130778
NM_000494

n/a

RefSeq (protein)

NP_000485

n/a

Location (UCSC)Chr 10: 104.03 – 104.09 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

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.[3]

This gene encodes the alpha chain of type XVII collagen. Collagen XVII is a transmembrane protein, like collagen XIII, XXIII and XXV. Collagen XVII is a structural component of hemidesmosomes, multiprotein complexes at the dermal-epidermal basement membrane zone that mediate adhesion of keratinocytes to the underlying membrane. It also appears to be a key protein in maintaining the integrity of the corneal epithelium.[4] Mutations in this gene are associated with both generalized atrophic benign and junctional epidermolysis bullosa as well as recurrent corneal erosions. Two homotrimeric forms of type XVII collagen exist. The full length form is the transmembrane protein. A soluble form, referred to as either ectodomain or LAD-1, is generated by proteolytic processing of the full length form.[5]

Structure[edit]

Collagen XVII is a homotrimer of three alpha1(XVII)-chains [6] 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 [7][8] 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 [9][10] with a significant thermal stability.[11][12] 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 (citation needed). 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[edit]

Mutations in the human collagen XVII gene, COL17A1, lead to the absence or structural alterations and mutations of collagen XVII.[13] The functional consequences include diminished epidermal adhesion and skin blistering in response to minimal shearing forces. The disorder caused by biallelic COL17A1 mutations and 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.[14] 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.

Other mutations make the epithelium of the cornea in the eye brittle, which results in dominantly inherited recurrent corneal erosion dystrophy (ERED). Whole-exome sequencing first identified a heterozygous mutation (c.2816C>T, p.T939I) that segregated with ERED in a large Swedish pedigree dating back 200 years.[15] Another synonymous mutation (c.3156C>T) was proposed to introduce a cryptic donor site, resulting in aberrant splicing, a theory which subsequently was confirmed in several families with ERED from different countries.[4][16]

Shedding[edit]

Collagen XVII is constitutively shed from the keratinocyte surface within NC16A domain by TACE (TNF-Alpha Converting Enzyme), metalloproteinase of the ADAM family.[17] The shedding is lipid raft dependent.[18] Collagen XVII is extracellularly phosphorylated by ecto-casein kinase 2 within the NC16A domain, phosphorylation negatively regulates ectodomain shedding.[19]

SPARC and osteogenesis imperfecta[edit]

The SPARC gene is completely associated with homozygous mutations in collagen XVII, which in turn causes a type of osteogenesis imperfecta.[20][21]

Interactions[edit]

Collagen, type XVII, alpha 1 has been shown to interact with Keratin 18,[22] Actinin alpha 4,[23] Dystonin,[8][24] Actinin, alpha 1,[23] CTNND1[25] and ITGB4.[26][27]

See also[edit]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000065618 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:". 
  3. ^ Franzke, C. W.; Bruckner, P.; Bruckner-Tuderman, L. (2005). "Collagenous transmembrane proteins: recent insights into biology and pathology". J. Biol. Chem. 280: 4005–4008. doi:10.1074/jbc.R400034200. PMID 15561712. 
  4. ^ a b Oliver, V.F.; van Bysterveldt, K.A.; Cadzow, M.; et al. (2016). "A COL17A1 Splice-Altering Mutation Is Prevalent in Inherited Recurrent Corneal Erosions". Ophthalmology. 123 (4): 709–722. doi:10.1016/j.ophtha.2015.12.008. PMID 26786512. 
  5. ^ "Entrez Gene: COL17A1 collagen, type XVII, alpha 1". 
  6. ^ Hirako, Y.; Usukura, J.; Nishizawa, Y.; 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 (23): 13739–13745. doi:10.1074/jbc.271.23.13739. PMID 8662839. 
  7. ^ Hopkinson, S. B.; Findlay, K.; Jones, J. C.; Jones, JC (1998). "Interaction of BP180 (type XVII collagen) and alpha 6 integrin is necessary for stabilization of hemidesmosome structure". J. Invest. Dermatol. 111 (6): 1015–1022. doi:10.1046/j.1523-1747.1998.00452.x. PMID 9856810. 
  8. ^ a b Hopkinson, S B; Jones J C (January 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. UNITED STATES. 11 (1): 277–86. doi:10.1091/mbc.11.1.277. ISSN 1059-1524. PMC 14774Freely accessible. PMID 10637308. 
  9. ^ Hirako, Y.; Usukura, J.; Nishizawa, Y.; 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 (23): 13739–13745. doi:10.1074/jbc.271.23.13739. PMID 8662839. 
  10. ^ Hirako, Y.; Usukura, J.; Uematsu, J.; Hashimoto, T.; Kitajima, Y.; 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. doi:10.1074/jbc.273.16.9711. 
  11. ^ Schacke, H.; Schumann, H.; Hammami-Hauasli, N.; Raghunath, M.; Bruckner-Tuderman, L. (1998). "Two forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomain". J. Biol. Chem. 273 (40): 25937–25943. doi:10.1074/jbc.273.40.25937. PMID 9748270. 
  12. ^ Areida, S. K.; Reinhardt, D. P.; Muller, P. K.; Fietzek, P. P.; Kowitz, J.; Marinkovich, M. P.; 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. doi:10.1074/jbc.M008709200. PMID 11042218. 
  13. ^ Zillikens, D.; Giudice, G. J. (1999). "BP180/type XVII collagen: its role in acquired and inherited disorders or the dermal-epidermal junction". Arch. Dermatol. Res. 291 (4): 187–194. doi:10.1007/s004030050392. PMID 10335914. 
  14. ^ Zillikens, D. (1999). "Acquired skin disease of hemidesmosomes". J.Dermatol. Sci. 20 (2): 134–154. doi:10.1016/S0923-1811(99)00019-5. PMID 10379705. 
  15. ^ Jonsson, F.; Byström, B.; Davidson, A.E.; et al. (2015). "Mutations in collagen, type XVII, alpha 1 (COL17A1) cause epithelial recurrent erosion dystrophy (ERED)". Hum. Mutat. 36 (4): 463–473. doi:10.1002/humu.22764. PMID 25676728. 
  16. ^ Lin, B:R.; Le, D.J.; Chem, Y.; et al. (2016). "Whole exome sequencing and segregation analysis confirms that a mutation in COL17A1 is the cause of epithelial recurrent erosion dystrophy in a large dominant pedigree previously mapped to chromosome 10q23-q24". PLOS ONE. 11 (6): e0157418. Bibcode:2016PLoSO..1157418L. doi:10.1371/journal.pone.0157418. PMC 4911149Freely accessible. PMID 27309958. 
  17. ^ Franzke, C. W.; Tasanen, K.; Borradori, L.; Huotari, V.; Bruckner-Tuderman, L. (2004). "Shedding of collagen XVII/BP180: structural motifs influence cleavage from cell surface". J. Biol. Chem. 279: 24521–24529. doi:10.1074/jbc.M308835200. PMID 15047704. 
  18. ^ Zimina EP, Bruckner-Tuderman L, Franzke C (2005). "Shedding of collagen XVII ectodomain depends on plasma membrane microenvironment". J Biol Chem. 280 (40): 34019–24. doi:10.1074/jbc.M503751200. PMID 16020548. 
  19. ^ Zimina EP, Fritsch A, Schermer B, Bakulina AY, Bashkurov M, Benzing T, Bruckner-Tuderman L (2007). "Extracellular phosphorylation of collagen XVII by ecto-casein kinase 2 inhibits ectodomain shedding". J Biol Chem. 282 (31): 22737–46. doi:10.1074/jbc.M701937200. PMID 17545155. 
  20. ^ Reference, Genetics Home. "SPARC gene". Genetics Home Reference. 
  21. ^ "OMIM Entry - # 616507 - OSTEOGENESIS IMPERFECTA, TYPE XVII; OI17". omim.org. 
  22. ^ Aho, S; Uitto J (March 1999). "180-kD bullous pemphigoid antigen/type XVII collagen: tissue-specific expression and molecular interactions with keratin 18". J. Cell. Biochem. UNITED STATES. 72 (3): 356–67. doi:10.1002/(SICI)1097-4644(19990301)72:3<356::AID-JCB5>3.0.CO;2-M. ISSN 0730-2312. PMID 10022517. 
  23. ^ a b Gonzalez, A M; Otey C; Edlund M; Jones J C (December 2001). "Interactions of a hemidesmosome component and actinin family members". J. Cell Sci. England. 114 (Pt 23): 4197–206. ISSN 0021-9533. PMID 11739652. 
  24. ^ Koster, January; Geerts Dirk; Favre Bertrand; Borradori Luca; Sonnenberg Arnoud (January 2003). "Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly". J. Cell Sci. England. 116 (Pt 2): 387–99. doi:10.1242/jcs.00241. ISSN 0021-9533. PMID 12482924. 
  25. ^ Aho, S; Rothenberger K; Uitto J (June 1999). "Human p120ctn catenin: tissue-specific expression of isoforms and molecular interactions with BP180/type XVII collagen". J. Cell. Biochem. UNITED STATES. 73 (3): 390–9. doi:10.1002/(SICI)1097-4644(19990601)73:3<390::AID-JCB10>3.0.CO;2-1. ISSN 0730-2312. PMID 10321838. 
  26. ^ Aho, S; Uitto J (February 1998). "Direct interaction between the intracellular domains of bullous pemphigoid antigen 2 (BP180) and beta 4 integrin, hemidesmosomal components of basal keratinocytes". Biochem. Biophys. Res. Commun. UNITED STATES. 243 (3): 694–9. doi:10.1006/bbrc.1998.8162. ISSN 0006-291X. PMID 9500991. 
  27. ^ Schaapveld, R Q; Borradori L; Geerts D; van Leusden M R; Kuikman I; Nievers M G; Niessen C M; Steenbergen R D; Snijders P J; Sonnenberg A (July 1998). "Hemidesmosome formation is initiated by the beta4 integrin subunit, requires complex formation of beta4 and HD1/plectin, and involves a direct interaction between beta4 and the bullous pemphigoid antigen 180". J. Cell Biol. UNITED STATES. 142 (1): 271–84. doi:10.1083/jcb.142.1.271. ISSN 0021-9525. PMC 2133016Freely accessible. PMID 9660880. 

Further reading[edit]