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Volumn 32, Issue 2, 2013, Pages 64-73

Collagen XVI in health and disease

Author keywords

Carcinogenesis; Collagen XVI; FACIT; Glioblastoma; Integrin; Myofibroblasts; Oral squamous cell carcinoma; Pathophysiology

Indexed keywords

COLLAGEN TYPE 16;

EID: 84875810865     PISSN: 0945053X     EISSN: 15691802     Source Type: Journal    
DOI: 10.1016/j.matbio.2012.11.001     Document Type: Review
Times cited : (45)

References (86)
  • 1
    • 0033513349 scopus 로고    scopus 로고
    • Expression of type XVI collagen in human skin fibroblasts: enhanced expression in fibrotic skin diseases
    • Akagi A., Tajima S., Ishibashi A., Yamaguchi N., Nagai Y. Expression of type XVI collagen in human skin fibroblasts: enhanced expression in fibrotic skin diseases. J. Invest. Dermatol. 1999, 113:246-250.
    • (1999) J. Invest. Dermatol. , vol.113 , pp. 246-250
    • Akagi, A.1    Tajima, S.2    Ishibashi, A.3    Yamaguchi, N.4    Nagai, Y.5
  • 2
    • 0036178616 scopus 로고    scopus 로고
    • Type XVI collagen is expressed in factor XIIIa+ monocyte-derived dermal dendrocytes and constitutes a potential substrate for factor XIIIa
    • Akagi A., Tajima S., Ishibashi A., Matsubara Y., Takehana M., Kobayashi S., Yamaguchi N. Type XVI collagen is expressed in factor XIIIa+ monocyte-derived dermal dendrocytes and constitutes a potential substrate for factor XIIIa. J. Invest. Dermatol. 2002, 118:267-274.
    • (2002) J. Invest. Dermatol. , vol.118 , pp. 267-274
    • Akagi, A.1    Tajima, S.2    Ishibashi, A.3    Matsubara, Y.4    Takehana, M.5    Kobayashi, S.6    Yamaguchi, N.7
  • 3
    • 0037371896 scopus 로고    scopus 로고
    • Loss of types XV and XIX collagen precedes basement membrane invasion in ductal carcinoma of the female breast
    • Amenta P.S., Hadad S., Lee M.T., Barnard N., Li D., Myers J.C. Loss of types XV and XIX collagen precedes basement membrane invasion in ductal carcinoma of the female breast. J. Pathol. 2003, 199:298-308.
    • (2003) J. Pathol. , vol.199 , pp. 298-308
    • Amenta, P.S.1    Hadad, S.2    Lee, M.T.3    Barnard, N.4    Li, D.5    Myers, J.C.6
  • 4
    • 0031908852 scopus 로고    scopus 로고
    • Structure and biological activity of the extracellular matrix
    • Aumailley M., Gayraud B. Structure and biological activity of the extracellular matrix. J. Mol. Med. (Berl) 1998, 76:253-265.
    • (1998) J. Mol. Med. (Berl) , vol.76 , pp. 253-265
    • Aumailley, M.1    Gayraud, B.2
  • 5
    • 34548080639 scopus 로고    scopus 로고
    • Cytoplasmic expression of type VII collagen is related to prognosis in patients with esophageal squamous cell carcinoma
    • Baba Y., Iyama K., Honda S., Ishikawa S., Miyanari N., Baba H. Cytoplasmic expression of type VII collagen is related to prognosis in patients with esophageal squamous cell carcinoma. Oncology 2006, 71:221-228.
    • (2006) Oncology , vol.71 , pp. 221-228
    • Baba, Y.1    Iyama, K.2    Honda, S.3    Ishikawa, S.4    Miyanari, N.5    Baba, H.6
  • 6
    • 0025733702 scopus 로고
    • Mammalian subtilisins: the long-sought dibasic processing endoproteases
    • Barr P.J. Mammalian subtilisins: the long-sought dibasic processing endoproteases. Cell 1991, 66:1-3.
    • (1991) Cell , vol.66 , pp. 1-3
    • Barr, P.J.1
  • 8
    • 0022475977 scopus 로고
    • Binding and covalent cross-linking of purified von Willebrand factor to native monomeric collagen
    • Bockenstedt P., McDonagh J., Handin R.I. Binding and covalent cross-linking of purified von Willebrand factor to native monomeric collagen. J. Clin. Invest. 1986, 78:551-556.
    • (1986) J. Clin. Invest. , vol.78 , pp. 551-556
    • Bockenstedt, P.1    McDonagh, J.2    Handin, R.I.3
  • 9
    • 72449155751 scopus 로고    scopus 로고
    • Suprastructures of extracellular matrices: paradigms of functions controlled by aggregates rather than molecules
    • Bruckner P. Suprastructures of extracellular matrices: paradigms of functions controlled by aggregates rather than molecules. Cell Tissue Res. 2010, 339:7-18.
    • (2010) Cell Tissue Res. , vol.339 , pp. 7-18
    • Bruckner, P.1
  • 11
    • 62849120016 scopus 로고    scopus 로고
    • Genetic and orthopedic aspects of collagen disorders
    • Carter E.M., Raggio C.L. Genetic and orthopedic aspects of collagen disorders. Curr. Opin. Pediatr. 2009, 21:46-54.
    • (2009) Curr. Opin. Pediatr. , vol.21 , pp. 46-54
    • Carter, E.M.1    Raggio, C.L.2
  • 12
    • 0024437561 scopus 로고
    • Characterization of factor XIIIa positive dermal dendritic cells in normal and inflamed skin
    • Cerio R., Griffiths C.E., Cooper K.D., Nickoloff B.J., Headington J.T. Characterization of factor XIIIa positive dermal dendritic cells in normal and inflamed skin. Br. J. Dermatol. 1989, 121:421-431.
    • (1989) Br. J. Dermatol. , vol.121 , pp. 421-431
    • Cerio, R.1    Griffiths, C.E.2    Cooper, K.D.3    Nickoloff, B.J.4    Headington, J.T.5
  • 13
    • 0020973415 scopus 로고
    • Elastin-associated microfibrils and microfibrillar proteins
    • Cleary E.G., Gibson M.A. Elastin-associated microfibrils and microfibrillar proteins. Int. Rev. Connect. Tissue Res. 1983, 10:97-209.
    • (1983) Int. Rev. Connect. Tissue Res. , vol.10 , pp. 97-209
    • Cleary, E.G.1    Gibson, M.A.2
  • 14
    • 0028851160 scopus 로고
    • Apoptosis mediates the decrease in cellularity during the transition between granulation tissue and scar
    • Desmouliere A., Redard M., Darby I., Gabbiani G. Apoptosis mediates the decrease in cellularity during the transition between granulation tissue and scar. Am. J. Pathol. 1995, 146:56-66.
    • (1995) Am. J. Pathol. , vol.146 , pp. 56-66
    • Desmouliere, A.1    Redard, M.2    Darby, I.3    Gabbiani, G.4
  • 15
    • 33748744382 scopus 로고    scopus 로고
    • Collagen XVI harbors an integrin alpha1 beta1 recognition site in its C-terminal domains
    • Eble J.A., Kassner A., Niland S., Morgelin M., Grifka J., Grassel S. Collagen XVI harbors an integrin alpha1 beta1 recognition site in its C-terminal domains. J. Biol. Chem. 2006, 281:25745-25756.
    • (2006) J. Biol. Chem. , vol.281 , pp. 25745-25756
    • Eble, J.A.1    Kassner, A.2    Niland, S.3    Morgelin, M.4    Grifka, J.5    Grassel, S.6
  • 18
    • 0027300061 scopus 로고
    • Type XIV collagen is encoded by alternative transcripts with distinct 5' regions and is a multidomain protein with homologies to von Willebrand's factor, fibronectin, and other matrix proteins
    • Gerecke D.R., Foley J.W., Castagnola P., Gennari M., Dublet B., Cancedda R., Linsenmayer T.F., van der R.M., Olsen B.R., Gordon M.K. Type XIV collagen is encoded by alternative transcripts with distinct 5' regions and is a multidomain protein with homologies to von Willebrand's factor, fibronectin, and other matrix proteins. J. Biol. Chem. 1993, 268:12177-12184.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12177-12184
    • Gerecke, D.R.1    Foley, J.W.2    Castagnola, P.3    Gennari, M.4    Dublet, B.5    Cancedda, R.6    Linsenmayer, T.F.7    van der, R.M.8    Olsen, B.R.9    Gordon, M.K.10
  • 20
    • 0023412468 scopus 로고
    • Type XII collagen: distinct extracellular matrix component discovered by cDNA cloning
    • Gordon M.K., Gerecke D.R., Olsen B.R. Type XII collagen: distinct extracellular matrix component discovered by cDNA cloning. Proc. Natl. Acad. Sci. U. S. A. 1987, 84:6040-6044.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 6040-6044
    • Gordon, M.K.1    Gerecke, D.R.2    Olsen, B.R.3
  • 21
    • 0030440410 scopus 로고    scopus 로고
    • Biosynthesis and processing of type XVI collagen in human fibroblasts and smooth muscle cells
    • Grassel S., Timpl R., Tan E.M., Chu M.L. Biosynthesis and processing of type XVI collagen in human fibroblasts and smooth muscle cells. Eur. J. Biochem. 1996, 242:576-584.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 576-584
    • Grassel, S.1    Timpl, R.2    Tan, E.M.3    Chu, M.L.4
  • 22
    • 0032475984 scopus 로고    scopus 로고
    • Collagen type XVI expression is modulated by basic fibroblast growth factor and transforming growth factor-beta
    • Grassel S., Tan E.M., Timpl R., Chu M.L. Collagen type XVI expression is modulated by basic fibroblast growth factor and transforming growth factor-beta. FEBS Lett. 1998, 436:197-201.
    • (1998) FEBS Lett. , vol.436 , pp. 197-201
    • Grassel, S.1    Tan, E.M.2    Timpl, R.3    Chu, M.L.4
  • 23
    • 0344848632 scopus 로고    scopus 로고
    • Collagen XVI is expressed by human dermal fibroblasts and keratinocytes and is associated with the microfibrillar apparatus in the upper papillary dermis
    • Grassel S., Unsold C., Schacke H., Bruckner-Tuderman L., Bruckner P. Collagen XVI is expressed by human dermal fibroblasts and keratinocytes and is associated with the microfibrillar apparatus in the upper papillary dermis. Matrix Biol. 1999, 18:309-317.
    • (1999) Matrix Biol. , vol.18 , pp. 309-317
    • Grassel, S.1    Unsold, C.2    Schacke, H.3    Bruckner-Tuderman, L.4    Bruckner, P.5
  • 24
    • 67649565425 scopus 로고    scopus 로고
    • Gene and protein expression profile of naive and osteo-chondrogenically differentiated rat bone marrow-derived mesenchymal progenitor cells
    • Grassel S., Ahmed N., Gottl C., Grifka J. Gene and protein expression profile of naive and osteo-chondrogenically differentiated rat bone marrow-derived mesenchymal progenitor cells. Int. J. Mol. Med. 2009, 23:745-755.
    • (2009) Int. J. Mol. Med. , vol.23 , pp. 745-755
    • Grassel, S.1    Ahmed, N.2    Gottl, C.3    Grifka, J.4
  • 25
    • 0006457649 scopus 로고
    • Identification of a third region of cell-specific alternative splicing in human fibronectin mRNA
    • Gutman A., Kornblihtt A.R. Identification of a third region of cell-specific alternative splicing in human fibronectin mRNA. Proc. Natl. Acad. Sci. U. S. A. 1987, 84:7179-7182.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 7179-7182
    • Gutman, A.1    Kornblihtt, A.R.2
  • 26
    • 0141621226 scopus 로고    scopus 로고
    • Macromolecular specificity of collagen fibrillogenesis: fibrils of collagens I and XI contain a heterotypic alloyed core and a collagen I sheath
    • Hansen U., Bruckner P. Macromolecular specificity of collagen fibrillogenesis: fibrils of collagens I and XI contain a heterotypic alloyed core and a collagen I sheath. J. Biol. Chem. 2003, 278:37352-37359.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37352-37359
    • Hansen, U.1    Bruckner, P.2
  • 27
    • 66449119343 scopus 로고    scopus 로고
    • Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects
    • Harburger D.S., Bouaouina M., Calderwood D.A. Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects. J. Biol. Chem. 2009, 284:11485-11497.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11485-11497
    • Harburger, D.S.1    Bouaouina, M.2    Calderwood, D.A.3
  • 28
    • 1342265613 scopus 로고    scopus 로고
    • Neurotrophins and extracellular matrix molecules modulate sensory axon outgrowth
    • Hari A., Djohar B., Skutella T., Montazeri S. Neurotrophins and extracellular matrix molecules modulate sensory axon outgrowth. Int. J. Dev. Neurosci. 2004, 22:113-117.
    • (2004) Int. J. Dev. Neurosci. , vol.22 , pp. 113-117
    • Hari, A.1    Djohar, B.2    Skutella, T.3    Montazeri, S.4
  • 29
    • 0036166823 scopus 로고    scopus 로고
    • Domain structure and organisation in extracellular matrix proteins
    • Hohenester E., Engel J. Domain structure and organisation in extracellular matrix proteins. Matrix Biol. 2002, 21:115-128.
    • (2002) Matrix Biol. , vol.21 , pp. 115-128
    • Hohenester, E.1    Engel, J.2
  • 30
    • 33947142997 scopus 로고    scopus 로고
    • Collagen XVI is a neural component of the developing and regenerating dorsal root ganglia extracellular matrix
    • Hubert T., Grimal S., Ratzinger S., Mechaly I., Grassel S., Fichard-Carroll A. Collagen XVI is a neural component of the developing and regenerating dorsal root ganglia extracellular matrix. Matrix Biol. 2007, 26:206-210.
    • (2007) Matrix Biol. , vol.26 , pp. 206-210
    • Hubert, T.1    Grimal, S.2    Ratzinger, S.3    Mechaly, I.4    Grassel, S.5    Fichard-Carroll, A.6
  • 31
    • 0032538562 scopus 로고    scopus 로고
    • Bone morphogenetic protein-1 processes the NH2-terminal propeptide, and a furin-like proprotein convertase processes the COOH-terminal propeptide of pro-alpha1(V) collagen
    • Imamura Y., Steiglitz B.M., Greenspan D.S. Bone morphogenetic protein-1 processes the NH2-terminal propeptide, and a furin-like proprotein convertase processes the COOH-terminal propeptide of pro-alpha1(V) collagen. J. Biol. Chem. 1998, 273:27511-27517.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27511-27517
    • Imamura, Y.1    Steiglitz, B.M.2    Greenspan, D.S.3
  • 32
    • 0028984327 scopus 로고
    • The mRNA for alpha 1(XIX) collagen chain, a new member of FACITs, contains a long unusual 3' untranslated region and displays many unique splicing variants
    • Inoguchi K., Yoshioka H., Khaleduzzaman M., Ninomiya Y. The mRNA for alpha 1(XIX) collagen chain, a new member of FACITs, contains a long unusual 3' untranslated region and displays many unique splicing variants. J. Biochem. 1995, 117:137-146.
    • (1995) J. Biochem. , vol.117 , pp. 137-146
    • Inoguchi, K.1    Yoshioka, H.2    Khaleduzzaman, M.3    Ninomiya, Y.4
  • 33
    • 0030038815 scopus 로고    scopus 로고
    • Ontogeny and characterization of factor XIIIa+ cells in developing human skin
    • Gibran N.S., Nickoloff B.J., Holbrook K.A. Ontogeny and characterization of factor XIIIa+ cells in developing human skin. Anat. Embryol. Berl 1996, 193(1):35-41.
    • (1996) Anat. Embryol. Berl , vol.193 , Issue.1 , pp. 35-41
    • Gibran, N.S.1    Nickoloff, B.J.2    Holbrook, K.A.3
  • 37
    • 33044503051 scopus 로고    scopus 로고
    • Type I collagen-mediated changes in gene expression and function of prostate cancer cells
    • Kiefer J., Alexander A., Farach-Carson M.C. Type I collagen-mediated changes in gene expression and function of prostate cancer cells. Cancer Treat. Res. 2004, 118:101-124.
    • (2004) Cancer Treat. Res. , vol.118 , pp. 101-124
    • Kiefer, J.1    Alexander, A.2    Farach-Carson, M.C.3
  • 38
    • 0029868132 scopus 로고    scopus 로고
    • Tissue distribution and developmental expression of type XVI collagen in the mouse
    • Lai C.H., Chu M.L. Tissue distribution and developmental expression of type XVI collagen in the mouse. Tissue Cell 1996, 28:155-164.
    • (1996) Tissue Cell , vol.28 , pp. 155-164
    • Lai, C.H.1    Chu, M.L.2
  • 39
    • 79959826381 scopus 로고    scopus 로고
    • Extracellular matrix dynamics in hepatocarcinogenesis: a comparative proteomics study of PDGFC transgenic and Pten null mouse models
    • Lai K.K., Shang S., Lohia N., Booth G.C., Masse D.J., Fausto N., Campbell J.S., Beretta L. Extracellular matrix dynamics in hepatocarcinogenesis: a comparative proteomics study of PDGFC transgenic and Pten null mouse models. PLoS Genet. 2011, 7:e1002147.
    • (2011) PLoS Genet. , vol.7
    • Lai, K.K.1    Shang, S.2    Lohia, N.3    Booth, G.C.4    Masse, D.J.5    Fausto, N.6    Campbell, J.S.7    Beretta, L.8
  • 40
    • 0029940986 scopus 로고    scopus 로고
    • Characterization of human type III collagen expressed in a baculovirus system. Production of a protein with a stable triple helix requires coexpression with the two types of recombinant prolyl 4-hydroxylase subunit
    • Lamberg A., Helaakoski T., Myllyharju J., Peltonen S., Notbohm H., Pihlajaniemi T., Kivirikko K.I. Characterization of human type III collagen expressed in a baculovirus system. Production of a protein with a stable triple helix requires coexpression with the two types of recombinant prolyl 4-hydroxylase subunit. J. Biol. Chem. 1996, 271:11988-11995.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11988-11995
    • Lamberg, A.1    Helaakoski, T.2    Myllyharju, J.3    Peltonen, S.4    Notbohm, H.5    Pihlajaniemi, T.6    Kivirikko, K.I.7
  • 41
    • 37249086640 scopus 로고    scopus 로고
    • Type I collagen is overexpressed in medulloblastoma as a component of tumor microenvironment
    • Liang Y., Diehn M., Bollen A.W., Israel M.A., Gupta N. Type I collagen is overexpressed in medulloblastoma as a component of tumor microenvironment. J. Neurooncol. 2008, 86:133-141.
    • (2008) J. Neurooncol. , vol.86 , pp. 133-141
    • Liang, Y.1    Diehn, M.2    Bollen, A.W.3    Israel, M.A.4    Gupta, N.5
  • 42
    • 84857657407 scopus 로고    scopus 로고
    • BMP activated Smad signaling strongly promotes migration and invasion of hepatocellular carcinoma cells
    • Maegdefrau U., Bosserhoff A.K. BMP activated Smad signaling strongly promotes migration and invasion of hepatocellular carcinoma cells. Exp. Mol. Pathol. 2012, 92:74-81.
    • (2012) Exp. Mol. Pathol. , vol.92 , pp. 74-81
    • Maegdefrau, U.1    Bosserhoff, A.K.2
  • 43
    • 0027682593 scopus 로고
    • New members of the collagen superfamily
    • Mayne R., Brewton R.G. New members of the collagen superfamily. Curr. Opin. Cell Biol. 1993, 5:883-890.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 883-890
    • Mayne, R.1    Brewton, R.G.2
  • 44
    • 33745749581 scopus 로고    scopus 로고
    • Gene profiling during development and after a peripheral nerve traumatism reveals genes specifically induced by injury in dorsal root ganglia
    • Mechaly I., Bourane S., Piquemal D., Al Jumaily M., Venteo S., Puech S., Scamps F., Valmier J., Carroll P. Gene profiling during development and after a peripheral nerve traumatism reveals genes specifically induced by injury in dorsal root ganglia. Mol. Cell. Neurosci. 2006, 32:217-229.
    • (2006) Mol. Cell. Neurosci. , vol.32 , pp. 217-229
    • Mechaly, I.1    Bourane, S.2    Piquemal, D.3    Al Jumaily, M.4    Venteo, S.5    Puech, S.6    Scamps, F.7    Valmier, J.8    Carroll, P.9
  • 45
    • 0021331433 scopus 로고
    • Cross-linking of fibronectin to collagenous proteins
    • Mosher D.F. Cross-linking of fibronectin to collagenous proteins. Mol. Cell. Biochem. 1984, 58:63-68.
    • (1984) Mol. Cell. Biochem. , vol.58 , pp. 63-68
    • Mosher, D.F.1
  • 46
    • 0019152373 scopus 로고
    • Cross-linking of collagen and fibronectin by factor XIIIa. Localization of participating glutaminyl residues to a tryptic fragment of fibronectin
    • Mosher D.F., Schad P.E., Vann J.M. Cross-linking of collagen and fibronectin by factor XIIIa. Localization of participating glutaminyl residues to a tryptic fragment of fibronectin. J. Biol. Chem. 1980, 255:1181-1188.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1181-1188
    • Mosher, D.F.1    Schad, P.E.2    Vann, J.M.3
  • 47
    • 0025074073 scopus 로고
    • The complete primary structure of two distinct forms of human alpha 1 (IX) collagen chains
    • Muragaki Y., Kimura T., Ninomiya Y., Olsen B.R. The complete primary structure of two distinct forms of human alpha 1 (IX) collagen chains. Eur. J. Biochem. 1990, 192:703-708.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 703-708
    • Muragaki, Y.1    Kimura, T.2    Ninomiya, Y.3    Olsen, B.R.4
  • 49
    • 0028238354 scopus 로고
    • The triple-helical region of human type XIX collagen consists of multiple collagenous subdomains and exhibits limited sequence homology to alpha 1(XVI)
    • Myers J.C., Yang H., D'Ippolito J.A., Presente A., Miller M.K., Dion A.S. The triple-helical region of human type XIX collagen consists of multiple collagenous subdomains and exhibits limited sequence homology to alpha 1(XVI). J. Biol. Chem. 1994, 269:18549-18557.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18549-18557
    • Myers, J.C.1    Yang, H.2    D'Ippolito, J.A.3    Presente, A.4    Miller, M.K.5    Dion, A.S.6
  • 50
    • 0033572689 scopus 로고    scopus 로고
    • Up-regulation of type XIX collagen in rhabdomyosarcoma cells accompanies myogenic differentiation
    • Myers J.C., Li D., Rubinstein N.A., Clark C.C. Up-regulation of type XIX collagen in rhabdomyosarcoma cells accompanies myogenic differentiation. Exp. Cell Res. 1999, 253:587-598.
    • (1999) Exp. Cell Res. , vol.253 , pp. 587-598
    • Myers, J.C.1    Li, D.2    Rubinstein, N.A.3    Clark, C.C.4
  • 51
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, flies and worms
    • Myllyharju J., Kivirikko K.I. Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet. 2004, 20:33-43.
    • (2004) Trends Genet. , vol.20 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 52
    • 0027432320 scopus 로고
    • Characterization of dermal dendritic cells obtained from normal human skin reveals phenotypic and functionally distinctive subsets
    • Nestle F.O., Zheng X.G., Thompson C.B., Turka L.A., Nickoloff B.J. Characterization of dermal dendritic cells obtained from normal human skin reveals phenotypic and functionally distinctive subsets. J. Immunol. 1993, 151:6535-6545.
    • (1993) J. Immunol. , vol.151 , pp. 6535-6545
    • Nestle, F.O.1    Zheng, X.G.2    Thompson, C.B.3    Turka, L.A.4    Nickoloff, B.J.5
  • 53
    • 0025904738 scopus 로고
    • The human progenitor cell antigen (CD34) is localized on endothelial cells, dermal dendritic cells, and perifollicular cells in formalin-fixed normal skin, and on proliferating endothelial cells and stromal spindle-shaped cells in Kaposi's sarcoma
    • Nickoloff B.J. The human progenitor cell antigen (CD34) is localized on endothelial cells, dermal dendritic cells, and perifollicular cells in formalin-fixed normal skin, and on proliferating endothelial cells and stromal spindle-shaped cells in Kaposi's sarcoma. Arch. Dermatol. 1991, 127:523-529.
    • (1991) Arch. Dermatol. , vol.127 , pp. 523-529
    • Nickoloff, B.J.1
  • 54
    • 0022397562 scopus 로고
    • Construction and characterization of cDNA encoding the alpha 2 chain of chicken type IX collagen
    • Ninomiya Y., van der R.M., Mayne R., Lozano G., Olsen B.R. Construction and characterization of cDNA encoding the alpha 2 chain of chicken type IX collagen. Biochemistry 1985, 24:4223-4229.
    • (1985) Biochemistry , vol.24 , pp. 4223-4229
    • Ninomiya, Y.1    van der, R.M.2    Mayne, R.3    Lozano, G.4    Olsen, B.R.5
  • 58
    • 22944454223 scopus 로고    scopus 로고
    • The tension mounts: mechanics meets morphogenesis and malignancy
    • Paszek M.J., Weaver V.M. The tension mounts: mechanics meets morphogenesis and malignancy. J. Mammary Gland Biol. Neoplasia 2004, 9:325-342.
    • (2004) J. Mammary Gland Biol. Neoplasia , vol.9 , pp. 325-342
    • Paszek, M.J.1    Weaver, V.M.2
  • 61
    • 0031691462 scopus 로고    scopus 로고
    • The cutaneous microfibrillar apparatus contains latent transforming growth factor-beta binding protein-1 (LTBP-1) and is a repository for latent TGF-beta1
    • Raghunath M., Unsold C., Kubitscheck U., Bruckner-Tuderman L., Peters R., Meuli M. The cutaneous microfibrillar apparatus contains latent transforming growth factor-beta binding protein-1 (LTBP-1) and is a repository for latent TGF-beta1. J. Invest. Dermatol. 1998, 111:559-564.
    • (1998) J. Invest. Dermatol. , vol.111 , pp. 559-564
    • Raghunath, M.1    Unsold, C.2    Kubitscheck, U.3    Bruckner-Tuderman, L.4    Peters, R.5    Meuli, M.6
  • 63
    • 77950863030 scopus 로고    scopus 로고
    • Collagen XVI induces formation of focal contacts on intestinal myofibroblasts isolated from the normal and inflamed intestinal tract
    • Ratzinger S., Eble J.A., Pasoldt A., Opolka A., Rogler G., Grifka J., Grassel S. Collagen XVI induces formation of focal contacts on intestinal myofibroblasts isolated from the normal and inflamed intestinal tract. Matrix Biol. 2010, 29:177-193.
    • (2010) Matrix Biol. , vol.29 , pp. 177-193
    • Ratzinger, S.1    Eble, J.A.2    Pasoldt, A.3    Opolka, A.4    Rogler, G.5    Grifka, J.6    Grassel, S.7
  • 64
    • 79952103916 scopus 로고    scopus 로고
    • Induction of type XVI collagen expression facilitates proliferation of oral cancer cells
    • Ratzinger S., Grassel S., Dowejko A., Reichert T.E., Bauer R.J. Induction of type XVI collagen expression facilitates proliferation of oral cancer cells. Matrix Biol. 2011, 30:118-125.
    • (2011) Matrix Biol. , vol.30 , pp. 118-125
    • Ratzinger, S.1    Grassel, S.2    Dowejko, A.3    Reichert, T.E.4    Bauer, R.J.5
  • 66
    • 79955044149 scopus 로고    scopus 로고
    • Matricryptins derived from collagens and proteoglycans
    • Ricard-Blum S., Ballut L. Matricryptins derived from collagens and proteoglycans. Front. Biosci. 2011, 16:674-697.
    • (2011) Front. Biosci. , vol.16 , pp. 674-697
    • Ricard-Blum, S.1    Ballut, L.2
  • 67
    • 23444447845 scopus 로고    scopus 로고
    • The collagen superfamily: from the extracellular matrix to the cell membrane
    • Ricard-Blum S., Ruggiero F. The collagen superfamily: from the extracellular matrix to the cell membrane. Pathol. Biol. (Paris) 2005, 53:430-442.
    • (2005) Pathol. Biol. (Paris) , vol.53 , pp. 430-442
    • Ricard-Blum, S.1    Ruggiero, F.2
  • 68
    • 0027422979 scopus 로고
    • Extracellular matrix 4: the elastic fiber
    • Rosenbloom J., Abrams W.R., Mecham R. Extracellular matrix 4: the elastic fiber. FASEB J. 1993, 7:1208-1218.
    • (1993) FASEB J. , vol.7 , pp. 1208-1218
    • Rosenbloom, J.1    Abrams, W.R.2    Mecham, R.3
  • 69
    • 0023002893 scopus 로고
    • Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils
    • Sakai L.Y., Keene D.R., Engvall E. Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils. J. Cell Biol. 1986, 103:2499-2509.
    • (1986) J. Cell Biol. , vol.103 , pp. 2499-2509
    • Sakai, L.Y.1    Keene, D.R.2    Engvall, E.3
  • 71
    • 33745031777 scopus 로고    scopus 로고
    • TGF-beta1 generates a specific multicomponent extracellular matrix in human coronary SMC
    • Schmidt A., Lorkowski S., Seidler D., Breithardt G., Buddecke E. TGF-beta1 generates a specific multicomponent extracellular matrix in human coronary SMC. Eur. J. Clin. Invest. 2006, 36:473-482.
    • (2006) Eur. J. Clin. Invest. , vol.36 , pp. 473-482
    • Schmidt, A.1    Lorkowski, S.2    Seidler, D.3    Breithardt, G.4    Buddecke, E.5
  • 72
    • 0023409308 scopus 로고
    • Multiple sites of alternative splicing of the rat fibronectin gene transcript
    • Schwarzbauer J.E., Patel R.S., Fonda D., Hynes R.O. Multiple sites of alternative splicing of the rat fibronectin gene transcript. EMBO J. 1987, 6:2573-2580.
    • (1987) EMBO J. , vol.6 , pp. 2573-2580
    • Schwarzbauer, J.E.1    Patel, R.S.2    Fonda, D.3    Hynes, R.O.4
  • 73
    • 53249121465 scopus 로고    scopus 로고
    • Collagen XVI expression is upregulated in glioblastomas and promotes tumor cell adhesion
    • Senner V., Ratzinger S., Mertsch S., Grassel S., Paulus W. Collagen XVI expression is upregulated in glioblastomas and promotes tumor cell adhesion. FEBS Lett. 2008, 582:3293-3300.
    • (2008) FEBS Lett. , vol.582 , pp. 3293-3300
    • Senner, V.1    Ratzinger, S.2    Mertsch, S.3    Grassel, S.4    Paulus, W.5
  • 74
    • 0037022008 scopus 로고    scopus 로고
    • Crohn's disease
    • Shanahan F. Crohn's disease. Lancet 2002, 359:62-69.
    • (2002) Lancet , vol.359 , pp. 62-69
    • Shanahan, F.1
  • 76
    • 0034598988 scopus 로고    scopus 로고
    • Expression of type XVI collagen in cultured skin fibroblasts is related to cell growth arrest
    • Tajima S., Akagi A., Tanaka N., Ishibashi A., Kawada A., Yamaguchi N. Expression of type XVI collagen in cultured skin fibroblasts is related to cell growth arrest. FEBS Lett. 2000, 469:1-4.
    • (2000) FEBS Lett. , vol.469 , pp. 1-4
    • Tajima, S.1    Akagi, A.2    Tanaka, N.3    Ishibashi, A.4    Kawada, A.5    Yamaguchi, N.6
  • 77
    • 1842587729 scopus 로고    scopus 로고
    • Activation of the protein kinase A pathway in human endometrial stromal cells reveals sequential categorical gene regulation
    • Tierney E.P., Tulac S., Huang S.T., Giudice L.C. Activation of the protein kinase A pathway in human endometrial stromal cells reveals sequential categorical gene regulation. Physiol. Genomics 2003, 16:47-66.
    • (2003) Physiol. Genomics , vol.16 , pp. 47-66
    • Tierney, E.P.1    Tulac, S.2    Huang, S.T.3    Giudice, L.C.4
  • 78
    • 0028798781 scopus 로고
    • Recombinant analysis of human alpha 1 (XVI) collagen. Evidence for processing of the N-terminal globular domain
    • Tillet E., Mann K., Nischt R., Pan T.C., Chu M.L., Timpl R. Recombinant analysis of human alpha 1 (XVI) collagen. Evidence for processing of the N-terminal globular domain. Eur. J. Biochem. 1995, 228:160-168.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 160-168
    • Tillet, E.1    Mann, K.2    Nischt, R.3    Pan, T.C.4    Chu, M.L.5    Timpl, R.6
  • 81
    • 0025792023 scopus 로고
    • Collagen family of proteins
    • van der Rest M., Garrone R. Collagen family of proteins. FASEB J. 1991, 5:2814-2823.
    • (1991) FASEB J. , vol.5 , pp. 2814-2823
    • van der Rest, M.1    Garrone, R.2
  • 82
    • 0242667573 scopus 로고    scopus 로고
    • Homeobox gene expression in adult dorsal root ganglia during sciatic nerve regeneration: is regeneration a recapitulation of development?
    • Vogelaar C.F., Hoekman M.F., Gispen W.H., Burbach J.P. Homeobox gene expression in adult dorsal root ganglia during sciatic nerve regeneration: is regeneration a recapitulation of development?. Eur. J. Pharmacol. 2003, 480(1-3):233-250.
    • (2003) Eur. J. Pharmacol. , vol.480 , Issue.1-3 , pp. 233-250
    • Vogelaar, C.F.1    Hoekman, M.F.2    Gispen, W.H.3    Burbach, J.P.4
  • 83
    • 0026451141 scopus 로고
    • Identification of cross-linking sites in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type IX bonding
    • Wu J.J., Woods P.E., Eyre D.R. Identification of cross-linking sites in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type IX bonding. J. Biol. Chem. 1992, 267:23007-23014.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23007-23014
    • Wu, J.J.1    Woods, P.E.2    Eyre, D.R.3
  • 84
    • 0026046510 scopus 로고
    • The complete primary structure of type XII collagen shows a chimeric molecule with reiterated fibronectin type III motifs, von Willebrand factor A motifs, a domain homologous to a noncollagenous region of type IX collagen, and short collagenous domains with an Arg-Gly-Asp site
    • Yamagata M., Yamada K.M., Yamada S.S., Shinomura T., Tanaka H., Nishida Y., Obara M., Kimata K. The complete primary structure of type XII collagen shows a chimeric molecule with reiterated fibronectin type III motifs, von Willebrand factor A motifs, a domain homologous to a noncollagenous region of type IX collagen, and short collagenous domains with an Arg-Gly-Asp site. J. Cell Biol. 1991, 115:209-221.
    • (1991) J. Cell Biol. , vol.115 , pp. 209-221
    • Yamagata, M.1    Yamada, K.M.2    Yamada, S.S.3    Shinomura, T.4    Tanaka, H.5    Nishida, Y.6    Obara, M.7    Kimata, K.8
  • 85
    • 0027096808 scopus 로고
    • Molecular cloning and partial characterization of a novel collagen chain, alpha 1(XVI), consisting of repetitive collagenous domains and cysteine-containing non-collagenous segments
    • Yamaguchi N., Kimura S., McBride O.W., Hori H., Yamada Y., Kanamori T., Yamakoshi H., Nagai Y. Molecular cloning and partial characterization of a novel collagen chain, alpha 1(XVI), consisting of repetitive collagenous domains and cysteine-containing non-collagenous segments. J. Biochem. (Tokyo) 1992, 112:856-863.
    • (1992) J. Biochem. (Tokyo) , vol.112 , pp. 856-863
    • Yamaguchi, N.1    Kimura, S.2    McBride, O.W.3    Hori, H.4    Yamada, Y.5    Kanamori, T.6    Yamakoshi, H.7    Nagai, Y.8
  • 86
    • 33746344387 scopus 로고    scopus 로고
    • The extracellular matrix in oral squamous cell carcinoma: friend or foe?
    • Ziober A.F., Falls E.M., Ziober B.L. The extracellular matrix in oral squamous cell carcinoma: friend or foe?. Head Neck 2006, 28:740-749.
    • (2006) Head Neck , vol.28 , pp. 740-749
    • Ziober, A.F.1    Falls, E.M.2    Ziober, B.L.3


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