{{Short description|Mammalian protein found in humans}} {{cs1 config|name-list-style=vanc|display-authors=6}} {{Infobox_gene}} '''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, identified by Diaz and colleagues in 1990.<ref>{{cite journal | vauthors = Franzke CW, Bruckner P, Bruckner-Tuderman L | title = Collagenous transmembrane proteins: recent insights into biology and pathology | journal = The Journal of Biological Chemistry | volume = 280 | issue = 6 | pages = 4005–4008 | date = February 2005 | pmid = 15561712 | doi = 10.1074/jbc.R400034200 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Diaz LA, Ratrie H, Saunders WS, Futamura S, Squiquera HL, Anhalt GJ, Giudice GJ | title = Isolation of a human epidermal cDNA corresponding to the 180-kD autoantigen recognized by bullous pemphigoid and herpes gestationis sera. Immunolocalization of this protein to the hemidesmosome | journal = The Journal of Clinical Investigation | volume = 86 | issue = 4 | pages = 1088–1094 | date = October 1990 | pmid = 1698819 | pmc = 296836 | doi = 10.1172/JCI114812 }}</ref>
COL17A1 is the official name of the gene. It 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.<ref name="Oliver_2016">{{cite journal | vauthors = Oliver VF, van Bysterveldt KA, Cadzow M, Steger B, Romano V, Markie D, Hewitt AW, Mackey DA, Willoughby CE, Sherwin T, Crosier PS, McGhee CN, Vincent AL | title = A COL17A1 Splice-Altering Mutation Is Prevalent in Inherited Recurrent Corneal Erosions | journal = Ophthalmology | volume = 123 | issue = 4 | pages = 709–722 | date = April 2016 | pmid = 26786512 | doi = 10.1016/j.ophtha.2015.12.008 | doi-access = free }}</ref> Mutations in this gene are associated with both generalized atrophic benign and junctional epidermolysis bullosa,<ref>{{cite journal | vauthors = Bardhan A, Bruckner-Tuderman L, Chapple IL, Fine JD, Harper N, Has C, Magin TM, Marinkovich MP, Marshall JF, McGrath JA, Mellerio JE, Polson R, Heagerty AH | title = Epidermolysis bullosa | journal = Nature Reviews. Disease Primers | volume = 6 | issue = 1 | article-number = 78 | date = September 2020 | pmid = 32973163 | doi = 10.1038/s41572-020-0210-0 | s2cid = 221861310 }}</ref> as well as recurrent corneal erosions, and expression of this gene is abnormal in various cancers.<ref name="Thangavelu_2016">{{cite journal | vauthors = Thangavelu PU, Krenács T, Dray E, Duijf PH | title = In epithelial cancers, aberrant ''COL17A1'' promoter methylation predicts its misexpression and increased invasion | journal = Clinical Epigenetics | volume = 8 | page = 120 | year = 2016 | pmid = 27891193 | pmc = 5116176 | doi = 10.1186/s13148-016-0290-6 | doi-access = free | article-number = 120 }}</ref> 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.<ref name="entrez">{{cite web | title = Entrez Gene: COL17A1 collagen, type XVII, alpha 1 | url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=1308 }}</ref>
== Structure == Collagen XVII is a homotrimer of three alpha1(XVII)-chains <ref>{{cite journal | vauthors = Hirako Y, Usukura J, Nishizawa Y, Owaribe K | title = Demonstration of the molecular shape of BP180, a 180-kDa bullous pemphigoid antigen and its potential for trimer formation | journal = The Journal of Biological Chemistry | volume = 271 | issue = 23 | pages = 13739–13745 | date = June 1996 | pmid = 8662839 | doi = 10.1074/jbc.271.23.13739 | title-link = bullous pemphigoid | doi-access = free }}</ref> 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 <ref>{{cite journal | vauthors = Hopkinson SB, Findlay K, deHart GW, Jones JC | title = Interaction of BP180 (type XVII collagen) and alpha6 integrin is necessary for stabilization of hemidesmosome structure | journal = The Journal of Investigative Dermatology | volume = 111 | issue = 6 | pages = 1015–1022 | date = December 1998 | pmid = 9856810 | doi = 10.1046/j.1523-1747.1998.00452.x | doi-access = free }}</ref><ref name="Hopkinson_2000" /> 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<ref>{{cite journal | vauthors = Hirako Y, Usukura J, Nishizawa Y, Owaribe K | title = Demonstration of the molecular shape of BP180, a 180-kDa bullous pemphigoid antigen and its potential for trimer formation | journal = The Journal of Biological Chemistry | volume = 271 | issue = 23 | pages = 13739–13745 | date = June 1996 | pmid = 8662839 | doi = 10.1074/jbc.271.23.13739 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Hirako Y, Usukura J, Uematsu J, Hashimoto T, Kitajima Y, Owaribe K | title = Cleavage of BP180, a 180-kDa bullous pemphigoid antigen, yields a 120-kDa collagenous extracellular polypeptide | journal = The Journal of Biological Chemistry | volume = 273 | issue = 16 | pages = 9711–9717 | date = April 1998 | pmid = 9545306 | doi = 10.1074/jbc.273.16.9711 | doi-access = free }}</ref> with a significant thermal stability.<ref>{{cite journal | vauthors = Schäcke H, Schumann H, Hammami-Hauasli N, Raghunath M, Bruckner-Tuderman L | title = Two forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomain | journal = The Journal of Biological Chemistry | volume = 273 | issue = 40 | pages = 25937–25943 | date = October 1998 | pmid = 9748270 | doi = 10.1074/jbc.273.40.25937 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Areida SK, Reinhardt DP, Muller PK, Fietzek PP, Kowitz J, Marinkovich MP, Notbohm H | title = Properties of the collagen type XVII ectodomain. Evidence for n- to c-terminal triple helix folding | journal = The Journal of Biological Chemistry | volume = 276 | issue = 2 | pages = 1594–1601 | date = January 2001 | pmid = 11042218 | doi = 10.1074/jbc.M008709200 | doi-access = free }}</ref> 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|date=November 2021}}. 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, {{Gene|COL17A1}}, lead to the absence or structural alterations and mutations of collagen XVII.<ref>{{cite journal | vauthors = Zillikens D, Giudice GJ | title = BP180/type XVII collagen: its role in acquired and inherited disorders or the dermal-epidermal junction | journal = Archives of Dermatological Research | volume = 291 | issue = 4 | pages = 187–194 | date = April 1999 | pmid = 10335914 | doi = 10.1007/s004030050392 | s2cid = 27592712 }}</ref> 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 Bullous pemphigoid (BP) and herpes gestationis (HG), both acquired subepithelial blistering disorders.<ref>{{cite journal | vauthors = Zillikens D | title = Acquired skin disease of hemidesmosomes | journal = Journal of Dermatological Science | volume = 20 | issue = 2 | pages = 134–154 | date = June 1999 | pmid = 10379705 | doi = 10.1016/S0923-1811(99)00019-5 }}</ref><ref>{{cite journal | vauthors = Diaz LA, Ratrie H, Saunders WS, Futamura S, Squiquera HL, Anhalt GJ, Giudice GJ | title = Isolation of a human epidermal cDNA corresponding to the 180-kD autoantigen recognized by bullous pemphigoid and herpes gestationis sera. Immunolocalization of this protein to the hemidesmosome | journal = The Journal of Clinical Investigation | volume = 86 | issue = 4 | pages = 1088–1094 | date = October 1990 | pmid = 1698819 | pmc = 296836 | doi = 10.1172/JCI114812 }}</ref> Most immunodominant epitopes lie within the NC16A domain,<ref>{{cite journal | vauthors = Giudice GJ, Emery DJ, Zelickson BD, Anhalt GJ, Liu Z, Diaz LA | title = Bullous pemphigoid and herpes gestationis autoantibodies recognize a common non-collagenous site on the BP180 ectodomain | journal = Journal of Immunology | volume = 151 | issue = 10 | pages = 5742–5750 | date = November 1993 | pmid = 8228259 | doi = 10.4049/jimmunol.151.10.5742 }}</ref> 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.<ref>{{cite journal | vauthors = Liu Z, Diaz LA, Troy JL, Taylor AF, Emery DJ, Fairley JA, Giudice GJ | title = A passive transfer model of the organ-specific autoimmune disease, bullous pemphigoid, using antibodies generated against the hemidesmosomal antigen, BP180 | journal = The Journal of Clinical Investigation | volume = 92 | issue = 5 | pages = 2480–2488 | date = November 1993 | pmid = 7693763 | pmc = 288433 | doi = 10.1172/JCI116856 }}</ref>
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.<ref>{{cite journal | vauthors = Jonsson F, Byström B, Davidson AE, Backman LJ, Kellgren TG, Tuft SJ, Koskela T, Rydén P, Sandgren O, Danielson P, Hardcastle AJ, Golovleva I | title = Mutations in collagen, type XVII, alpha 1 (COL17A1) cause epithelial recurrent erosion dystrophy (ERED) | journal = Human Mutation | volume = 36 | issue = 4 | pages = 463–473 | date = April 2015 | pmid = 25676728 | doi = 10.1002/humu.22764 | s2cid = 13562400 | doi-access = free }}</ref> 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.<ref name="Oliver_2016" /><ref>{{cite journal | vauthors = Lin BR, Le DJ, Chen Y, Wang Q, Chung DD, Frausto RF, Croasdale C, Yee RW, Hejtmancik FJ, Aldave AJ | title = 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 | journal = PLOS ONE | volume = 11 | issue = 6 | article-number = e0157418 | year = 2016 | pmid = 27309958 | pmc = 4911149 | doi = 10.1371/journal.pone.0157418 | doi-access = free | bibcode = 2016PLoSO..1157418L }}</ref>
==Cancer== Expression of the COL17A1 gene is abnormal in various cancers.<ref name="Thangavelu_2016" /> For example, it was found abnormal in five epithelial cancer types, including breast cancer, cervical cancer, head and neck cancer and two types of lung cancer. Decreased expression was observed for breast cancer, while increased expression was observed for the other cancers.<ref name="Thangavelu_2016" />
==Shedding== Collagen XVII is constitutively shed from the keratinocyte surface within NC16A domain by TACE (TNF-Alpha Converting Enzyme), metalloproteinase of the ADAM family.<ref>{{cite journal | vauthors = Franzke CW, Tasanen K, Borradori L, Huotari V, Bruckner-Tuderman L | title = Shedding of collagen XVII/BP180: structural motifs influence cleavage from cell surface | journal = The Journal of Biological Chemistry | volume = 279 | issue = 23 | pages = 24521–24529 | date = June 2004 | pmid = 15047704 | doi = 10.1074/jbc.M308835200 | doi-access = free }}</ref> The shedding is lipid raft dependent.<ref>{{cite journal | vauthors = Zimina EP, Bruckner-Tuderman L, Franzke CW | title = Shedding of collagen XVII ectodomain depends on plasma membrane microenvironment | journal = The Journal of Biological Chemistry | volume = 280 | issue = 40 | pages = 34019–34024 | date = October 2005 | pmid = 16020548 | doi = 10.1074/jbc.M503751200 | doi-access = free }}</ref> Collagen XVII is extracellularly phosphorylated by ecto-casein kinase 2 within the NC16A domain, phosphorylation negatively regulates ectodomain shedding.<ref>{{cite journal | vauthors = Zimina EP, Fritsch A, Schermer B, Bakulina AY, Bashkurov M, Benzing T, Bruckner-Tuderman L | title = Extracellular phosphorylation of collagen XVII by ecto-casein kinase 2 inhibits ectodomain shedding | journal = The Journal of Biological Chemistry | volume = 282 | issue = 31 | pages = 22737–22746 | date = August 2007 | pmid = 17545155 | doi = 10.1074/jbc.M701937200 | doi-access = free }}</ref>
==SPARC and osteogenesis imperfecta== The SPARC gene is completely associated with homozygous mutations in collagen XVII, which in turn causes a type of osteogenesis imperfecta.<ref>{{cite web | vauthors = Reference GH | title = SPARC gene | url = http://ghr.nlm.nih.gov/gene/SPARC | archive-url = https://web.archive.org/web/20170730082150/https://ghr.nlm.nih.gov/gene/SPARC | archive-date = July 30, 2017 | website = Genetics Home Reference }}</ref><ref>{{cite web | title = OMIM Entry - # 616507 - OSTEOGENESIS IMPERFECTA, TYPE XVII; OI17 | url = http://omim.org/entry/616507 | website = omim.org }}</ref>
== Interactions ==
Collagen, type XVII, alpha 1 has been shown to interact with Keratin 18,<ref name="Aho_1999">{{cite journal | vauthors = Aho S, Uitto J | title = 180-kD bullous pemphigoid antigen/type XVII collagen: tissue-specific expression and molecular interactions with keratin 18 | journal = Journal of Cellular Biochemistry | volume = 72 | issue = 3 | pages = 356–367 | date = March 1999 | pmid = 10022517 | doi = 10.1002/(SICI)1097-4644(19990301)72:3<356::AID-JCB5>3.0.CO;2-M | s2cid = 30404639 }}</ref> Actinin alpha 4,<ref name="Gonzalez_2001">{{cite journal | vauthors = Gonzalez AM, Otey C, Edlund M, Jones JC | title = Interactions of a hemidesmosome component and actinin family members | journal = Journal of Cell Science | volume = 114 | issue = Pt 23 | pages = 4197–4206 | date = December 2001 | pmid = 11739652 | doi = 10.1242/jcs.114.23.4197 }}</ref> Dystonin,<ref name="Hopkinson_2000">{{cite journal | vauthors = Hopkinson SB, Jones JC | title = 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 | journal = Molecular Biology of the Cell | volume = 11 | issue = 1 | pages = 277–286 | date = January 2000 | pmid = 10637308 | pmc = 14774 | doi = 10.1091/mbc.11.1.277 }}</ref><ref name="Koster_2003">{{cite journal | vauthors = Koster J, Geerts D, Favre B, Borradori L, Sonnenberg A | title = Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly | journal = Journal of Cell Science | volume = 116 | issue = Pt 2 | pages = 387–399 | date = January 2003 | pmid = 12482924 | doi = 10.1242/jcs.00241 | s2cid = 16745491 }}</ref> Actinin, alpha 1,<ref name="Gonzalez_2001" /> CTNND1<ref name=pmid10321838>{{cite journal | vauthors = Aho S, Rothenberger K, Uitto J | title = Human p120ctn catenin: tissue-specific expression of isoforms and molecular interactions with BP180/type XVII collagen | journal = Journal of Cellular Biochemistry | volume = 73 | issue = 3 | pages = 390–399 | date = June 1999 | pmid = 10321838 | doi = 10.1002/(SICI)1097-4644(19990601)73:3<390::AID-JCB10>3.0.CO;2-1 | s2cid = 43899550 }}</ref> and ITGB4.<ref name="Aho_1998">{{cite journal | vauthors = Aho S, Uitto J | title = Direct interaction between the intracellular domains of bullous pemphigoid antigen 2 (BP180) and beta 4 integrin, hemidesmosomal components of basal keratinocytes | journal = Biochemical and Biophysical Research Communications | volume = 243 | issue = 3 | pages = 694–699 | date = February 1998 | pmid = 9500991 | doi = 10.1006/bbrc.1998.8162 | bibcode = 1998BBRC..243..694A }}</ref><ref name="Schaapveld_1998">{{cite journal | vauthors = Schaapveld RQ, Borradori L, Geerts D, van Leusden MR, Kuikman I, Nievers MG, Niessen CM, Steenbergen RD, Snijders PJ, Sonnenberg A | title = 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 | journal = The Journal of Cell Biology | volume = 142 | issue = 1 | pages = 271–284 | date = July 1998 | pmid = 9660880 | pmc = 2133016 | doi = 10.1083/jcb.142.1.271 }}</ref>
== See also == * List of target antigens in pemphigoid
== References == {{Reflist}}
== Further reading == {{refbegin | 2}} * {{cite journal | vauthors = Giudice GJ, Emery DJ, Diaz LA | title = Cloning and primary structural analysis of the bullous pemphigoid autoantigen BP180 | journal = The Journal of Investigative Dermatology | volume = 99 | issue = 3 | pages = 243–250 | date = September 1992 | pmid = 1324962 | doi = 10.1111/1523-1747.ep12616580 | doi-access = free }} * {{cite journal | vauthors = Li KH, Sawamura D, Giudice GJ, Diaz LA, Mattei MG, Chu ML, Uitto J | title = Genomic organization of collagenous domains and chromosomal assignment of human 180-kDa bullous pemphigoid antigen-2, a novel collagen of stratified squamous epithelium | journal = The Journal of Biological Chemistry | volume = 266 | issue = 35 | pages = 24064–24069 | date = December 1991 | pmid = 1748679 | doi = 10.1016/S0021-9258(18)54393-3 | doi-access = free }} * {{cite journal | vauthors = Sawamura D, Li KH, Nomura K, Sugita Y, Christiano AM, Uitto J | title = Bullous pemphigoid antigen: cDNA cloning, cellular expression, and evidence for polymorphism of the human gene | journal = The Journal of Investigative Dermatology | volume = 96 | issue = 6 | pages = 908–915 | date = June 1991 | pmid = 2045679 | doi = 10.1111/1523-1747.ep12475433 | doi-access = free }} * {{cite journal | vauthors = McGrath JA, Gatalica B, Christiano AM, Li K, Owaribe K, McMillan JR, Eady RA, Uitto J | title = Mutations in the 180-kD bullous pemphigoid antigen (BPAG2), a hemidesmosomal transmembrane collagen (COL17A1), in generalized atrophic benign epidermolysis bullosa | journal = Nature Genetics | volume = 11 | issue = 1 | pages = 83–86 | date = September 1995 | pmid = 7550320 | doi = 10.1038/ng0995-83 | s2cid = 23732185 }} * {{cite journal | vauthors = Myers JC, Sun MJ, D'Ippolito JA, Jabs EW, Neilson EG, Dion AS | title = Human cDNA clones transcribed from an unusually high-molecular-weight RNA encode a new collagen chain | journal = Gene | volume = 123 | issue = 2 | pages = 211–217 | date = January 1993 | pmid = 7916703 | doi = 10.1016/0378-1119(93)90126-N }} * {{cite journal | vauthors = Hirako Y, Usukura J, Nishizawa Y, Owaribe K | title = Demonstration of the molecular shape of BP180, a 180-kDa bullous pemphigoid antigen and its potential for trimer formation | journal = The Journal of Biological Chemistry | volume = 271 | issue = 23 | pages = 13739–13745 | date = June 1996 | pmid = 8662839 | doi = 10.1074/jbc.271.23.13739 | doi-access = free }} * {{cite journal | vauthors = McGrath JA, Gatalica B, Li K, Dunnill MG, McMillan JR, Christiano AM, Eady RA, Uitto J | title = Compound heterozygosity for a dominant glycine substitution and a recessive internal duplication mutation in the type XVII collagen gene results in junctional epidermolysis bullosa and abnormal dentition | journal = The American Journal of Pathology | volume = 148 | issue = 6 | pages = 1787–1796 | date = June 1996 | pmid = 8669466 | pmc = 1861650 }} * {{cite journal | vauthors = Gatalica B, Pulkkinen L, Li K, Kuokkanen K, Ryynänen M, McGrath JA, Uitto J | title = Cloning of the human type XVII collagen gene (COL17A1), and detection of novel mutations in generalized atrophic benign epidermolysis bullosa | journal = American Journal of Human Genetics | volume = 60 | issue = 2 | pages = 352–365 | date = February 1997 | pmid = 9012408 | pmc = 1712405 }} * {{cite journal | vauthors = Jonkman MF, Scheffer H, Stulp R, Pas HH, Nijenhuis M, Heeres K, Owaribe K, Pulkkinen L, Uitto J | title = Revertant mosaicism in epidermolysis bullosa caused by mitotic gene conversion | journal = Cell | volume = 88 | issue = 4 | pages = 543–551 | date = February 1997 | pmid = 9038345 | doi = 10.1016/S0092-8674(00)81894-2 | s2cid = 18970859 | doi-access = free }} * {{cite journal | vauthors = Borradori L, Koch PJ, Niessen CM, Erkeland S, van Leusden MR, Sonnenberg A | title = The localization of bullous pemphigoid antigen 180 (BP180) in hemidesmosomes is mediated by its cytoplasmic domain and seems to be regulated by the beta4 integrin subunit | journal = The Journal of Cell Biology | volume = 136 | issue = 6 | pages = 1333–1347 | date = March 1997 | pmid = 9087447 | pmc = 2132520 | doi = 10.1083/jcb.136.6.1333 }} * {{cite journal | vauthors = Schumann H, Hammami-Hauasli N, Pulkkinen L, Mauviel A, Küster W, Lüthi U, Owaribe K, Uitto J, Bruckner-Tuderman L | title = Three novel homozygous point mutations and a new polymorphism in the COL17A1 gene: relation to biological and clinical phenotypes of junctional epidermolysis bullosa | journal = American Journal of Human Genetics | volume = 60 | issue = 6 | pages = 1344–1353 | date = June 1997 | pmid = 9199555 | pmc = 1716115 | doi = 10.1086/515463 }} * {{cite journal | vauthors = Chavanas S, Gache Y, Tadini G, Pulkkinen L, Uitto J, Ortonne JP, Meneguzzi G | title = A homozygous in-frame deletion in the collagenous domain of bullous pemphigoid antigen BP180 (type XVII collagen) causes generalized atrophic benign epidermolysis bullosa | journal = The Journal of Investigative Dermatology | volume = 109 | issue = 1 | pages = 74–78 | date = July 1997 | pmid = 9204958 | doi = 10.1111/1523-1747.ep12276614 | doi-access = free }} * {{cite journal | vauthors = Darling TN, Yee C, Koh B, McGrath JA, Bauer JW, Uitto J, Hintner H, Yancey KB | title = Cycloheximide facilitates the identification of aberrant transcripts resulting from a novel splice-site mutation in COL17A1 in a patient with generalized atrophic benign epidermolysis bullosa | journal = The Journal of Investigative Dermatology | volume = 110 | issue = 2 | pages = 165–169 | date = February 1998 | pmid = 9457913 | doi = 10.1046/j.1523-1747.1998.00103.x | doi-access = free }} * {{cite journal | vauthors = Aho S, Uitto J | title = Direct interaction between the intracellular domains of bullous pemphigoid antigen 2 (BP180) and beta 4 integrin, hemidesmosomal components of basal keratinocytes | journal = Biochemical and Biophysical Research Communications | volume = 243 | issue = 3 | pages = 694–699 | date = February 1998 | pmid = 9500991 | doi = 10.1006/bbrc.1998.8162 | bibcode = 1998BBRC..243..694A }} * {{cite journal | vauthors = Aho S, McLean WH, Li K, Uitto J | title = cDNA cloning, mRNA expression, and chromosomal mapping of human and mouse periplakin genes | journal = Genomics | volume = 48 | issue = 2 | pages = 242–247 | date = March 1998 | pmid = 9521878 | doi = 10.1006/geno.1997.5188 }} * {{cite journal | vauthors = Schaapveld RQ, Borradori L, Geerts D, van Leusden MR, Kuikman I, Nievers MG, Niessen CM, Steenbergen RD, Snijders PJ, Sonnenberg A | title = 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 | journal = The Journal of Cell Biology | volume = 142 | issue = 1 | pages = 271–284 | date = July 1998 | pmid = 9660880 | pmc = 2133016 | doi = 10.1083/jcb.142.1.271 }} * {{cite journal | vauthors = Ishiko A, Shimizu H, Masunaga T, Yancey KB, Giudice GJ, Zone JJ, Nishikawa T | title = 97 kDa linear IgA bullous dermatosis antigen localizes in the lamina lucida between the NC16A and carboxyl terminal domains of the 180 kDa bullous pemphigoid antigen | journal = The Journal of Investigative Dermatology | volume = 111 | issue = 1 | pages = 93–96 | date = July 1998 | pmid = 9665393 | doi = 10.1046/j.1523-1747.1998.00231.x | doi-access = free }} * {{cite journal | vauthors = Floeth M, Fiedorowicz J, Schäcke H, Hammami-Hausli N, Owaribe K, Trüeb RM, Bruckner-Tuderman L | title = Novel homozygous and compound heterozygous COL17A1 mutations associated with junctional epidermolysis bullosa | journal = The Journal of Investigative Dermatology | volume = 111 | issue = 3 | pages = 528–533 | date = September 1998 | pmid = 9740252 | doi = 10.1046/j.1523-1747.1998.00325.x | doi-access = free }} * {{cite journal | vauthors = Schäcke H, Schumann H, Hammami-Hauasli N, Raghunath M, Bruckner-Tuderman L | title = Two forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomain | journal = The Journal of Biological Chemistry | volume = 273 | issue = 40 | pages = 25937–25943 | date = October 1998 | pmid = 9748270 | doi = 10.1074/jbc.273.40.25937 | doi-access = free }} * {{cite journal | vauthors = Aho S, Uitto J | title = 180-kD bullous pemphigoid antigen/type XVII collagen: tissue-specific expression and molecular interactions with keratin 18 | journal = Journal of Cellular Biochemistry | volume = 72 | issue = 3 | pages = 356–367 | date = March 1999 | pmid = 10022517 | doi = 10.1002/(SICI)1097-4644(19990301)72:3<356::AID-JCB5>3.0.CO;2-M | s2cid = 30404639 }} {{refend}}
{{Fibrous proteins}}
Category:Collagens