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Volumn 28, Issue 1, 2010, Pages 61-66

Collagen XVII

Author keywords

Bullous pemphigoid; Collagen XVII; Dermal epidermal junction; Epidermal adhesion; Epidermolysis bullosa

Indexed keywords

COLLAGEN TYPE 17;

EID: 70450237245     PISSN: 07338635     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.det.2009.10.007     Document Type: Review
Times cited : (32)

References (42)
  • 1
    • 0019417455 scopus 로고
    • Characterization of bullous pemphigoid antigen: a unique basement membrane protein of stratified squamous epithelia
    • Stanley J.R., Hawley-Nelson P., Yuspa S.H., et al. Characterization of bullous pemphigoid antigen: a unique basement membrane protein of stratified squamous epithelia. Cell 24 3 (1981) 897-903
    • (1981) Cell , vol.24 , Issue.3 , pp. 897-903
    • Stanley, J.R.1    Hawley-Nelson, P.2    Yuspa, S.H.3
  • 2
    • 0029121987 scopus 로고
    • Mutations in the 180-kD bullous pemphigoid antigen (BPAG2), a hemidesmosomal transmembrane collagen (COL17A1), in generalized atrophic benign epidermolysis bullosa
    • McGrath J.A., Gatalica B., Christiano A.M., et al. Mutations in the 180-kD bullous pemphigoid antigen (BPAG2), a hemidesmosomal transmembrane collagen (COL17A1), in generalized atrophic benign epidermolysis bullosa. Nat Genet 11 1 (1995) 83-86
    • (1995) Nat Genet , vol.11 , Issue.1 , pp. 83-86
    • McGrath, J.A.1    Gatalica, B.2    Christiano, A.M.3
  • 3
    • 43449084027 scopus 로고    scopus 로고
    • The classification of inherited epidermolysis bullosa (EB): report of the Third International Consensus Meeting on Diagnosis and Classification of EB
    • Fine J.D., Eady R.A., Bauer E.A., et al. The classification of inherited epidermolysis bullosa (EB): report of the Third International Consensus Meeting on Diagnosis and Classification of EB. J Am Acad Dermatol 58 6 (2008) 931-950
    • (2008) J Am Acad Dermatol , vol.58 , Issue.6 , pp. 931-950
    • Fine, J.D.1    Eady, R.A.2    Bauer, E.A.3
  • 4
    • 0642368050 scopus 로고    scopus 로고
    • BP180 (type XVII collagen) and its role in cutaneous biology and disease
    • Van den Bergh F., and Giudice G.J. BP180 (type XVII collagen) and its role in cutaneous biology and disease. Adv Dermatol 19 (2003) 37-71
    • (2003) Adv Dermatol , vol.19 , pp. 37-71
    • Van den Bergh, F.1    Giudice, G.J.2
  • 5
    • 11944262997 scopus 로고    scopus 로고
    • Hemidesmosomes: molecular organization and their importance for cell adhesion and disease
    • Beissert T., and Nelson C.F. (Eds), Springer, Berlin
    • Koster J., Borradori L., and Sonnenberg A. Hemidesmosomes: molecular organization and their importance for cell adhesion and disease. In: Beissert T., and Nelson C.F. (Eds). Handbook of experimental pharmacology vol. 165 (2004), Springer, Berlin 245-267
    • (2004) Handbook of experimental pharmacology , vol.165 , pp. 245-267
    • Koster, J.1    Borradori, L.2    Sonnenberg, A.3
  • 6
    • 34447520444 scopus 로고    scopus 로고
    • Distribution of collagen XVII in the human brain
    • Seppanen A., Suuronen T., Hofmann S.C., et al. Distribution of collagen XVII in the human brain. Brain Res 1158 (2007) 50-56
    • (2007) Brain Res , vol.1158 , pp. 50-56
    • Seppanen, A.1    Suuronen, T.2    Hofmann, S.C.3
  • 7
    • 40649124485 scopus 로고    scopus 로고
    • Pemphigoid gestationis autoantigen, transmembrane collagen XVII, promotes the migration of cytotrophoblastic cells of placenta and is a structural component of fetal membranes
    • Huilaja L., Hurskainen T., Autio-Harmainen H., et al. Pemphigoid gestationis autoantigen, transmembrane collagen XVII, promotes the migration of cytotrophoblastic cells of placenta and is a structural component of fetal membranes. Matrix Biol 27 3 (2008) 190-200
    • (2008) Matrix Biol , vol.27 , Issue.3 , pp. 190-200
    • Huilaja, L.1    Hurskainen, T.2    Autio-Harmainen, H.3
  • 8
    • 6844265574 scopus 로고    scopus 로고
    • Expression of type XVII collagen alpha 1 chain mRNA in the mouse heart
    • Kondo J., Kusachi S., Ninomiya Y., et al. Expression of type XVII collagen alpha 1 chain mRNA in the mouse heart. Jpn Heart J 39 2 (1998) 211-220
    • (1998) Jpn Heart J , vol.39 , Issue.2 , pp. 211-220
    • Kondo, J.1    Kusachi, S.2    Ninomiya, Y.3
  • 9
    • 58249107829 scopus 로고    scopus 로고
    • Type XVII collagen is a key player in tooth enamel formation
    • Asaka T., Akiyama M., Domon T., et al. Type XVII collagen is a key player in tooth enamel formation. Am J Pathol 174 1 (2009) 91-100
    • (2009) Am J Pathol , vol.174 , Issue.1 , pp. 91-100
    • Asaka, T.1    Akiyama, M.2    Domon, T.3
  • 10
    • 0035847022 scopus 로고    scopus 로고
    • Properties of the collagen type XVII ectodomain. Evidence for N- to C-terminal triple helix folding
    • Areida S.K., Reinhardt D.P., Muller P.K., et al. Properties of the collagen type XVII ectodomain. Evidence for N- to C-terminal triple helix folding. J Biol Chem 276 2 (2001) 1594-1601
    • (2001) J Biol Chem , vol.276 , Issue.2 , pp. 1594-1601
    • Areida, S.K.1    Reinhardt, D.P.2    Muller, P.K.3
  • 11
    • 34547348003 scopus 로고    scopus 로고
    • Immunopathology and molecular diagnosis of autoimmune bullous diseases
    • Mihai S., and Sitaru C. Immunopathology and molecular diagnosis of autoimmune bullous diseases. J Cell Mol Med 11 3 (2007) 462-481
    • (2007) J Cell Mol Med , vol.11 , Issue.3 , pp. 462-481
    • Mihai, S.1    Sitaru, C.2
  • 12
    • 0042664095 scopus 로고    scopus 로고
    • Collagenous transmembrane proteins: collagen XVII as a prototype
    • Franzke C.W., Tasanen K., Schumann H., et al. Collagenous transmembrane proteins: collagen XVII as a prototype. Matrix Biol 22 4 (2003) 299-309
    • (2003) Matrix Biol , vol.22 , Issue.4 , pp. 299-309
    • Franzke, C.W.1    Tasanen, K.2    Schumann, H.3
  • 13
    • 2642578301 scopus 로고    scopus 로고
    • Shedding of collagen XVII/BP180: structural motifs influence cleavage from cell surface
    • Franzke C.W., Tasanen K., Borradori L., et al. Shedding of collagen XVII/BP180: structural motifs influence cleavage from cell surface. J Biol Chem 279 23 (2004) 24521-24529
    • (2004) J Biol Chem , vol.279 , Issue.23 , pp. 24521-24529
    • Franzke, C.W.1    Tasanen, K.2    Borradori, L.3
  • 14
    • 26644462168 scopus 로고    scopus 로고
    • Shedding of collagen XVII ectodomain depends on plasma membrane microenvironment
    • Zimina E.P., Bruckner-Tuderman L., and Franzke C.W. Shedding of collagen XVII ectodomain depends on plasma membrane microenvironment. J Biol Chem 280 40 (2005) 34019-34024
    • (2005) J Biol Chem , vol.280 , Issue.40 , pp. 34019-34024
    • Zimina, E.P.1    Bruckner-Tuderman, L.2    Franzke, C.W.3
  • 15
    • 34547928575 scopus 로고    scopus 로고
    • Extracellular phosphorylation of collagen XVII by ecto-casein kinase 2 inhibits ectodomain shedding
    • Zimina E.P., Fritsch A., Schermer B., et al. Extracellular phosphorylation of collagen XVII by ecto-casein kinase 2 inhibits ectodomain shedding. J Biol Chem 282 31 (2007) 22737-22746
    • (2007) J Biol Chem , vol.282 , Issue.31 , pp. 22737-22746
    • Zimina, E.P.1    Fritsch, A.2    Schermer, B.3
  • 16
    • 67449139105 scopus 로고    scopus 로고
    • Plasmin plays a role in the in vitro generation of the linear IgA dermatosis antigen LADB97
    • Hofmann S.C., Voith U., Schonau V., et al. Plasmin plays a role in the in vitro generation of the linear IgA dermatosis antigen LADB97. J Invest Dermatol 129 7 (2009) 1730-1739
    • (2009) J Invest Dermatol , vol.129 , Issue.7 , pp. 1730-1739
    • Hofmann, S.C.1    Voith, U.2    Schonau, V.3
  • 17
    • 2442701762 scopus 로고    scopus 로고
    • Keratinocytes from patients lacking collagen XVII display a migratory phenotype
    • Tasanen K., Tunggal L., Chometon G., et al. Keratinocytes from patients lacking collagen XVII display a migratory phenotype. Am J Pathol 164 6 (2004) 2027-2038
    • (2004) Am J Pathol , vol.164 , Issue.6 , pp. 2027-2038
    • Tasanen, K.1    Tunggal, L.2    Chometon, G.3
  • 18
    • 70349737907 scopus 로고    scopus 로고
    • Collagen XVII participates in keratinocyte adhesion to collagen IV, and in p38MAPK-dependent migration and cell signaling
    • Qiao H., Shibaki A., Long H.A., et al. Collagen XVII participates in keratinocyte adhesion to collagen IV, and in p38MAPK-dependent migration and cell signaling. J Invest Dermatol 129 9 (2009) 2288-2295
    • (2009) J Invest Dermatol , vol.129 , Issue.9 , pp. 2288-2295
    • Qiao, H.1    Shibaki, A.2    Long, H.A.3
  • 19
    • 34247359565 scopus 로고    scopus 로고
    • Localized and generalized forms of blistering in junctional epidermolysis bullosa due to COL17A1 mutations in the Netherlands
    • Pasmooij A.M., Pas H.H., Jansen G.H., et al. Localized and generalized forms of blistering in junctional epidermolysis bullosa due to COL17A1 mutations in the Netherlands. Br J Dermatol 156 5 (2007) 861-870
    • (2007) Br J Dermatol , vol.156 , Issue.5 , pp. 861-870
    • Pasmooij, A.M.1    Pas, H.H.2    Jansen, G.H.3
  • 20
    • 34250655712 scopus 로고    scopus 로고
    • Retrospective diagnosis of fatal BP180-deficient non-Herlitz junctional epidermolysis bullosa suggested by immunofluorescence (IF) antigen-mapping of parental carriers bearing enamel defects
    • Murrell D.F., Pasmooij A.M., Pas H.H., et al. Retrospective diagnosis of fatal BP180-deficient non-Herlitz junctional epidermolysis bullosa suggested by immunofluorescence (IF) antigen-mapping of parental carriers bearing enamel defects. J Invest Dermatol 127 7 (2007) 1772-1775
    • (2007) J Invest Dermatol , vol.127 , Issue.7 , pp. 1772-1775
    • Murrell, D.F.1    Pasmooij, A.M.2    Pas, H.H.3
  • 21
    • 33644830645 scopus 로고    scopus 로고
    • Molecular mechanisms of junctional epidermolysis bullosa: col 15 domain mutations decrease the thermal stability of collagen XVII
    • Vaisanen L., Has C., Franzke C., et al. Molecular mechanisms of junctional epidermolysis bullosa: col 15 domain mutations decrease the thermal stability of collagen XVII. J Invest Dermatol 125 6 (2005) 1112-1118
    • (2005) J Invest Dermatol , vol.125 , Issue.6 , pp. 1112-1118
    • Vaisanen, L.1    Has, C.2    Franzke, C.3
  • 22
    • 0033889376 scopus 로고    scopus 로고
    • Hemizygosity for a glycine substitution in collagen XVII: unfolding and degradation of the ectodomain
    • Tasanen K., Floeth M., Schumann H., et al. Hemizygosity for a glycine substitution in collagen XVII: unfolding and degradation of the ectodomain. J Invest Dermatol 115 2 (2000) 207-212
    • (2000) J Invest Dermatol , vol.115 , Issue.2 , pp. 207-212
    • Tasanen, K.1    Floeth, M.2    Schumann, H.3
  • 23
    • 0034602970 scopus 로고    scopus 로고
    • Collagen XVII is destabilized by a glycine substitution mutation in the cell adhesion domain Col15
    • Tasanen K., Eble J.A., Aumailley M., et al. Collagen XVII is destabilized by a glycine substitution mutation in the cell adhesion domain Col15. J Biol Chem 275 5 (2000) 3093-3099
    • (2000) J Biol Chem , vol.275 , Issue.5 , pp. 3093-3099
    • Tasanen, K.1    Eble, J.A.2    Aumailley, M.3
  • 24
    • 70349739358 scopus 로고    scopus 로고
    • Glycine substitution mutations cause intracellular accumulation of collagen XVII and affect its post-translational modifications
    • Huilaja L., Hurskainen T., Autio-Harmainen H., et al. Glycine substitution mutations cause intracellular accumulation of collagen XVII and affect its post-translational modifications. J Invest Dermatol 129 9 (2009) 2302-2306
    • (2009) J Invest Dermatol , vol.129 , Issue.9 , pp. 2302-2306
    • Huilaja, L.1    Hurskainen, T.2    Autio-Harmainen, H.3
  • 25
    • 33749568292 scopus 로고    scopus 로고
    • C-terminal truncation impairs glycosylation of transmembrane collagen XVII and leads to intracellular accumulation
    • Franzke C.W., Has C., Schulte C., et al. C-terminal truncation impairs glycosylation of transmembrane collagen XVII and leads to intracellular accumulation. J Biol Chem 281 40 (2006) 30260-30268
    • (2006) J Biol Chem , vol.281 , Issue.40 , pp. 30260-30268
    • Franzke, C.W.1    Has, C.2    Schulte, C.3
  • 26
    • 0030975365 scopus 로고    scopus 로고
    • Revertant mosaicism in epidermolysis bullosa caused by mitotic gene conversion
    • Jonkman M.F., Scheffer H., Stulp R., et al. Revertant mosaicism in epidermolysis bullosa caused by mitotic gene conversion. Cell 88 4 (1997) 543-551
    • (1997) Cell , vol.88 , Issue.4 , pp. 543-551
    • Jonkman, M.F.1    Scheffer, H.2    Stulp, R.3
  • 27
    • 27244452774 scopus 로고    scopus 로고
    • Multiple correcting COL17A1 mutations in patients with revertant mosaicism of epidermolysis bullosa
    • Pasmooij A.M., Pas H.H., Deviaene F.C., et al. Multiple correcting COL17A1 mutations in patients with revertant mosaicism of epidermolysis bullosa. Am J Hum Genet 77 5 (2005) 727-740
    • (2005) Am J Hum Genet , vol.77 , Issue.5 , pp. 727-740
    • Pasmooij, A.M.1    Pas, H.H.2    Deviaene, F.C.3
  • 28
    • 64749092605 scopus 로고    scopus 로고
    • Revertant mosaicism-patchwork in the skin
    • Jonkman M.F., and Pasmooij A.M. Revertant mosaicism-patchwork in the skin. N Engl J Med 360 16 (2009) 1680-1682
    • (2009) N Engl J Med , vol.360 , Issue.16 , pp. 1680-1682
    • Jonkman, M.F.1    Pasmooij, A.M.2
  • 29
    • 0035132809 scopus 로고    scopus 로고
    • A homozygous nonsense mutation in type XVII collagen gene (COL17A1) uncovers an alternatively spliced mRNA accounting for an unusually mild form of non-Herlitz junctional epidermolysis bullosa
    • Ruzzi L., Pas H., Posteraro P., et al. A homozygous nonsense mutation in type XVII collagen gene (COL17A1) uncovers an alternatively spliced mRNA accounting for an unusually mild form of non-Herlitz junctional epidermolysis bullosa. J Invest Dermatol 116 1 (2001) 182-187
    • (2001) J Invest Dermatol , vol.116 , Issue.1 , pp. 182-187
    • Ruzzi, L.1    Pas, H.2    Posteraro, P.3
  • 30
    • 1342305376 scopus 로고    scopus 로고
    • A very mild form of non-Herlitz junctional epidermolysis bullosa: BP180 rescue by outsplicing of mutated exon 30 coding for the COL15 domain
    • Pasmooij A.M., van Zalen S., Nijenhuis A.M., et al. A very mild form of non-Herlitz junctional epidermolysis bullosa: BP180 rescue by outsplicing of mutated exon 30 coding for the COL15 domain. Exp Dermatol 13 2 (2004) 125-128
    • (2004) Exp Dermatol , vol.13 , Issue.2 , pp. 125-128
    • Pasmooij, A.M.1    van Zalen, S.2    Nijenhuis, A.M.3
  • 31
    • 0029897474 scopus 로고    scopus 로고
    • 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
    • McGrath J.A., Gatalica B., Li K., et al. 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. Am J Pathol 148 6 (1996) 1787-1796
    • (1996) Am J Pathol , vol.148 , Issue.6 , pp. 1787-1796
    • McGrath, J.A.1    Gatalica, B.2    Li, K.3
  • 32
    • 0034233596 scopus 로고    scopus 로고
    • A disease-associated glycine substitution in BP180 (type XVII collagen) leads to a local destabilization of the major collagen triple helix
    • Olague-Marchan M., Twining S.S., Hacker M.K., et al. A disease-associated glycine substitution in BP180 (type XVII collagen) leads to a local destabilization of the major collagen triple helix. Matrix Biol 19 3 (2000) 223-233
    • (2000) Matrix Biol , vol.19 , Issue.3 , pp. 223-233
    • Olague-Marchan, M.1    Twining, S.S.2    Hacker, M.K.3
  • 33
    • 64849093040 scopus 로고    scopus 로고
    • Autosomal dominant junctional epidermolysis bullosa
    • Almaani N., Liu L., Dopping-Hepenstal P.J., et al. Autosomal dominant junctional epidermolysis bullosa. Br J Dermatol 160 5 (2009) 1094-1097
    • (2009) Br J Dermatol , vol.160 , Issue.5 , pp. 1094-1097
    • Almaani, N.1    Liu, L.2    Dopping-Hepenstal, P.J.3
  • 34
    • 1642452817 scopus 로고    scopus 로고
    • Molecular consequences of deletion of the cytoplasmic domain of bullous pemphigoid 180 in a patient with predominant features of epidermolysis bullosa simplex
    • Fontao L., Tasanen K., Huber M., et al. Molecular consequences of deletion of the cytoplasmic domain of bullous pemphigoid 180 in a patient with predominant features of epidermolysis bullosa simplex. J Invest Dermatol 122 1 (2004) 65-72
    • (2004) J Invest Dermatol , vol.122 , Issue.1 , pp. 65-72
    • Fontao, L.1    Tasanen, K.2    Huber, M.3
  • 35
    • 4944266746 scopus 로고    scopus 로고
    • Features of epidermolysis bullosa simplex due to mutations in the ectodomain of type XVII collagen
    • Pasmooij A.M., van der Steege G., Pas H.H., et al. Features of epidermolysis bullosa simplex due to mutations in the ectodomain of type XVII collagen. Br J Dermatol 151 3 (2004) 669-674
    • (2004) Br J Dermatol , vol.151 , Issue.3 , pp. 669-674
    • Pasmooij, A.M.1    van der Steege, G.2    Pas, H.H.3
  • 36
    • 69949112900 scopus 로고    scopus 로고
    • Adhesive stripping to remove epidermis in junctional epidermolysis bullosa for revertant cell therapy
    • Gostynski A., Deviaene F.C., Pasmooij A.M., et al. Adhesive stripping to remove epidermis in junctional epidermolysis bullosa for revertant cell therapy. Br J Dermatol 161 2 (2009) 444-447
    • (2009) Br J Dermatol , vol.161 , Issue.2 , pp. 444-447
    • Gostynski, A.1    Deviaene, F.C.2    Pasmooij, A.M.3
  • 37
    • 33847725511 scopus 로고    scopus 로고
    • Humanization of autoantigen
    • Nishie W., Sawamura D., Goto M., et al. Humanization of autoantigen. Nat Med 13 3 (2007) 378-383
    • (2007) Nat Med , vol.13 , Issue.3 , pp. 378-383
    • Nishie, W.1    Sawamura, D.2    Goto, M.3
  • 38
    • 9144233481 scopus 로고    scopus 로고
    • Characterization of the anti-BP180 autoantibody reactivity profile and epitope mapping in bullous pemphigoid patients
    • Di Zenzo G., Grosso F., Terracina M., et al. Characterization of the anti-BP180 autoantibody reactivity profile and epitope mapping in bullous pemphigoid patients. J Invest Dermatol 122 1 (2004) 103-110
    • (2004) J Invest Dermatol , vol.122 , Issue.1 , pp. 103-110
    • Di Zenzo, G.1    Grosso, F.2    Terracina, M.3
  • 39
    • 18644384411 scopus 로고    scopus 로고
    • Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs
    • Franzke C.W., Tasanen K., Schacke H., et al. Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs. EMBO J 21 19 (2002) 5026-5035
    • (2002) EMBO J , vol.21 , Issue.19 , pp. 5026-5035
    • Franzke, C.W.1    Tasanen, K.2    Schacke, H.3
  • 40
    • 33745640252 scopus 로고    scopus 로고
    • Generation and characterization of monoclonal antibodies against the intracellular domain of hemidesmosomal type XVII collagen
    • Olaru F., Mihai S., Petrescu I., et al. Generation and characterization of monoclonal antibodies against the intracellular domain of hemidesmosomal type XVII collagen. Hybridoma (Larchmt) 25 3 (2006) 158-162
    • (2006) Hybridoma (Larchmt) , vol.25 , Issue.3 , pp. 158-162
    • Olaru, F.1    Mihai, S.2    Petrescu, I.3
  • 41
    • 0033903442 scopus 로고    scopus 로고
    • The shed ectodomain of collagen XVII/BP180 is targeted by autoantibodies in different blistering skin diseases
    • Schumann H., Baetge J., Tasanen K., et al. The shed ectodomain of collagen XVII/BP180 is targeted by autoantibodies in different blistering skin diseases. Am J Pathol 156 2 (2000) 685-695
    • (2000) Am J Pathol , vol.156 , Issue.2 , pp. 685-695
    • Schumann, H.1    Baetge, J.2    Tasanen, K.3
  • 42
    • 0032476013 scopus 로고    scopus 로고
    • Two forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomain
    • Schacke H., Schumann H., Hammami-Hauasli N., et al. Two forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomain. J Biol Chem 273 40 (1998) 25937-25943
    • (1998) J Biol Chem , vol.273 , Issue.40 , pp. 25937-25943
    • Schacke, H.1    Schumann, H.2    Hammami-Hauasli, N.3


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