메뉴 건너뛰기




Volumn 27, Issue 4, 2008, Pages 360-370

First molecular characterization and immunolocalization of keratoepithelin in adult human skeletal muscle

Author keywords

Extracellular matrix; FAS 1 domains; Immunolocalization; Skeletal muscle

Indexed keywords

COLLAGEN TYPE 6; KERATOEPITHELIN; POLYCLONAL ANTIBODY; PROTEIN ANTIBODY; RECOMBINANT PROTEIN; SCLEROPROTEIN; TISSUE EXTRACT;

EID: 43049101974     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.matbio.2007.12.003     Document Type: Article
Times cited : (7)

References (46)
  • 7
    • 33745203970 scopus 로고    scopus 로고
    • Transcriptional profiling reveals novel markers of liver fibrogenesis: gremlin and insulin-like growth factor-binding proteins
    • Boers W., Aarrass S., Linthorst C., Pinzani M., Elferink R.O., and Bosma P. Transcriptional profiling reveals novel markers of liver fibrogenesis: gremlin and insulin-like growth factor-binding proteins. J. Biol. Chem. 281 (2006) 16289-16295
    • (2006) J. Biol. Chem. , vol.281 , pp. 16289-16295
    • Boers, W.1    Aarrass, S.2    Linthorst, C.3    Pinzani, M.4    Elferink, R.O.5    Bosma, P.6
  • 10
    • 33748305676 scopus 로고    scopus 로고
    • Crosstalk between different adhesion molecules
    • Chen X., and Gumbiner B.M. Crosstalk between different adhesion molecules. Curr. Opin. Cell Biol. 18 (2006) 572-578
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 572-578
    • Chen, X.1    Gumbiner, B.M.2
  • 11
    • 0037317272 scopus 로고    scopus 로고
    • Novel fold revealed by the structure of a FAS1 domain pair from the insect cell adhesion molecule fasciclin I
    • Clout N.J., Tisi D., and Hohenester E. Novel fold revealed by the structure of a FAS1 domain pair from the insect cell adhesion molecule fasciclin I. Structure 11 (2003) 197-203
    • (2003) Structure , vol.11 , pp. 197-203
    • Clout, N.J.1    Tisi, D.2    Hohenester, E.3
  • 12
    • 0041328581 scopus 로고    scopus 로고
    • Developmental expression patterns of βig (βIG-H3) and its function as a cell adhesion protein
    • Ferguson J.W., Mikesh M.F., Wheeler E.F., and LeBaron R.G. Developmental expression patterns of βig (βIG-H3) and its function as a cell adhesion protein. Mech. Dev. 120 (2003) 851-864
    • (2003) Mech. Dev. , vol.120 , pp. 851-864
    • Ferguson, J.W.1    Mikesh, M.F.2    Wheeler, E.F.3    LeBaron, R.G.4
  • 14
    • 0030696781 scopus 로고    scopus 로고
    • Immunohistochemical and ultrastructural localization of MP78/70 (βig-h3) in extracellular matrix of developing and mature bovine tissues
    • Gibson M.A., Kumaratilake J.S., and Cleary E.G. Immunohistochemical and ultrastructural localization of MP78/70 (βig-h3) in extracellular matrix of developing and mature bovine tissues. J. Histochem. Cytochem. 45 (1997) 1683-1696
    • (1997) J. Histochem. Cytochem. , vol.45 , pp. 1683-1696
    • Gibson, M.A.1    Kumaratilake, J.S.2    Cleary, E.G.3
  • 15
    • 0042591181 scopus 로고    scopus 로고
    • Covalent and non-covalent interactions of βig-h3 with collagen VI. βig-h3 is covalently attached to the amino-terminal region of collagen VI in tissue microfibrils
    • Hanssen E., Reinboth B., and Gibson M.A. Covalent and non-covalent interactions of βig-h3 with collagen VI. βig-h3 is covalently attached to the amino-terminal region of collagen VI in tissue microfibrils. J. Biol. Chem. 278 (2003) 24334-24341
    • (2003) J. Biol. Chem. , vol.278 , pp. 24334-24341
    • Hanssen, E.1    Reinboth, B.2    Gibson, M.A.3
  • 16
    • 0032973197 scopus 로고    scopus 로고
    • Identification and characterization of a novel protein, periostin, with restricted expression to periosteum and periodontal ligament and increased expression by transforming growth factor β
    • Horiuchi K., Amizuka N., Takeshita S., Takamatsu H., Katsuura M., Ozawa H., Toyama Y., Bonewald L.F., and Kudo A. Identification and characterization of a novel protein, periostin, with restricted expression to periosteum and periodontal ligament and increased expression by transforming growth factor β. J. Bone Miner. Res. 14 (1999) 1239-1249
    • (1999) J. Bone Miner. Res. , vol.14 , pp. 1239-1249
    • Horiuchi, K.1    Amizuka, N.2    Takeshita, S.3    Takamatsu, H.4    Katsuura, M.5    Ozawa, H.6    Toyama, Y.7    Bonewald, L.F.8    Kudo, A.9
  • 17
    • 0031970797 scopus 로고    scopus 로고
    • Midline fasciclin: a Drosophila fasciclin-I-related membrane protein localized to the CNS midline cells and trachea
    • Hu S., Sonnenfeld M., Stahl S., and Crews S.T. Midline fasciclin: a Drosophila fasciclin-I-related membrane protein localized to the CNS midline cells and trachea. J. Neurobiol. 63 (1998) 77-93
    • (1998) J. Neurobiol. , vol.63 , pp. 77-93
    • Hu, S.1    Sonnenfeld, M.2    Stahl, S.3    Crews, S.T.4
  • 18
    • 0027980523 scopus 로고
    • Algal-CAMs: isoforms of a cell adhesion molecule in embryos of the alga Volvox with homology to Drosophila fasciclin I
    • Huber O., and Sumper M. Algal-CAMs: isoforms of a cell adhesion molecule in embryos of the alga Volvox with homology to Drosophila fasciclin I. EMBO J. 13 (1994) 4212-4222
    • (1994) EMBO J. , vol.13 , pp. 4212-4222
    • Huber, O.1    Sumper, M.2
  • 19
    • 0032562663 scopus 로고    scopus 로고
    • Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil α-helices
    • Kammerer R.A., Schulthess T., Landwehr R., Lustig A., and Fischer D Engel J. Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil α-helices. J. Biol. Chem. 273 (1998) 10602-10608
    • (1998) J. Biol. Chem. , vol.273 , pp. 10602-10608
    • Kammerer, R.A.1    Schulthess, T.2    Landwehr, R.3    Lustig, A.4    Fischer D Engel, J.5
  • 20
    • 33745365256 scopus 로고    scopus 로고
    • Delayed corneal epithelial wound healing after penetrating keratoplasty in individuals with lattice corneal dystrophy
    • Kawamoto K., Morishige N., Yamada N., Chikama T., and Nishida T. Delayed corneal epithelial wound healing after penetrating keratoplasty in individuals with lattice corneal dystrophy. Am. J. Ophthalmol. 142 (2006) 173-174
    • (2006) Am. J. Ophthalmol. , vol.142 , pp. 173-174
    • Kawamoto, K.1    Morishige, N.2    Yamada, N.3    Chikama, T.4    Nishida, T.5
  • 21
    • 0034613378 scopus 로고    scopus 로고
    • Identification of motifs for cell adhesion within the repeated domains of transforming growth factor-β-induced gene, βig-h3
    • Kim J.E., Kim S.J., Lee B.H., Park R.W., Kim K.S., and Kim I.S. Identification of motifs for cell adhesion within the repeated domains of transforming growth factor-β-induced gene, βig-h3. J. Biol. Chem. 275 (2000) 30907-30915
    • (2000) J. Biol. Chem. , vol.275 , pp. 30907-30915
    • Kim, J.E.1    Kim, S.J.2    Lee, B.H.3    Park, R.W.4    Kim, K.S.5    Kim, I.S.6
  • 22
    • 0037195797 scopus 로고    scopus 로고
    • Identification of motifs in the fasciclin domains of the transforming growth factor-β-induced matrix protein βig-h3 that interact with the αvβ5 integrin
    • Kim J.E., Jeong H.W., Nam J.O., Lee B.H., Choi J.Y., Park R.W., Park J.Y., and Kim I.S. Identification of motifs in the fasciclin domains of the transforming growth factor-β-induced matrix protein βig-h3 that interact with the αvβ5 integrin. J. Biol. Chem. 277 (2002) 46159-46165
    • (2002) J. Biol. Chem. , vol.277 , pp. 46159-46165
    • Kim, J.E.1    Jeong, H.W.2    Nam, J.O.3    Lee, B.H.4    Choi, J.Y.5    Park, R.W.6    Park, J.Y.7    Kim, I.S.8
  • 23
    • 33745199359 scopus 로고    scopus 로고
    • Urinary transforming growth factor-β-induced gene-bigh3 as a sensitive predictor in chronic cyclosporine nephrotoxicity
    • Kim C.D., Cho Y.J., Park S.H., Ha S.W., Lee E.G., Kim Y.J., Kwon T.H., Kim I.S., and Kim Y.L. Urinary transforming growth factor-β-induced gene-bigh3 as a sensitive predictor in chronic cyclosporine nephrotoxicity. Trasplant. Proc. 38 (2006) 1314-1319
    • (2006) Trasplant. Proc. , vol.38 , pp. 1314-1319
    • Kim, C.D.1    Cho, Y.J.2    Park, S.H.3    Ha, S.W.4    Lee, E.G.5    Kim, Y.J.6    Kwon, T.H.7    Kim, I.S.8    Kim, Y.L.9
  • 24
    • 33646560354 scopus 로고    scopus 로고
    • Systemic investigation of keratoepithelin deposits in TGFβI/βIGH3-related corneal dystrophy
    • Kochairi I., Letovanec I., Uffer S., Munier F.L., Chaubert P., and Schorderet D.F. Systemic investigation of keratoepithelin deposits in TGFβI/βIGH3-related corneal dystrophy. Mol. Vis. 12 (2006) 461-466
    • (2006) Mol. Vis. , vol.12 , pp. 461-466
    • Kochairi, I.1    Letovanec, I.2    Uffer, S.3    Munier, F.L.4    Chaubert, P.5    Schorderet, D.F.6
  • 25
    • 0034646599 scopus 로고    scopus 로고
    • Amyloid and non-amyloid forms of 5q31-linked corneal dystrophy resulting from kerato-epithelin mutations at Arg-124 are associated with abnormal turnover of the protein
    • Korvatska E., Henry H., Mashima Y., Yamada M., Bachmann C., Munier F.L., and Schorderet D.F. Amyloid and non-amyloid forms of 5q31-linked corneal dystrophy resulting from kerato-epithelin mutations at Arg-124 are associated with abnormal turnover of the protein. J. Biol. Chem. 275 (2000) 11465-11469
    • (2000) J. Biol. Chem. , vol.275 , pp. 11465-11469
    • Korvatska, E.1    Henry, H.2    Mashima, Y.3    Yamada, M.4    Bachmann, C.5    Munier, F.L.6    Schorderet, D.F.7
  • 26
    • 24944559356 scopus 로고    scopus 로고
    • Collagen VI related muscle disorders
    • Lampe A.K., and Bushby K.M. Collagen VI related muscle disorders. J. Med. Genet. 42 (2005) 673-685
    • (2005) J. Med. Genet. , vol.42 , pp. 673-685
    • Lampe, A.K.1    Bushby, K.M.2
  • 30
    • 20144384004 scopus 로고    scopus 로고
    • Regulation of tumor angiogenesis by fastatin, the fourth FAS1 domain of βig-h3, via αvβ3 integrin
    • Nam J.O., Jeong H.W., Lee B.H., Park R.W., and Kim I.S. Regulation of tumor angiogenesis by fastatin, the fourth FAS1 domain of βig-h3, via αvβ3 integrin. Cancer Res. 65 (2005) 4153-4161
    • (2005) Cancer Res. , vol.65 , pp. 4153-4161
    • Nam, J.O.1    Jeong, H.W.2    Lee, B.H.3    Park, R.W.4    Kim, I.S.5
  • 31
    • 20444430061 scopus 로고    scopus 로고
    • βig-h3 induces keratinocyte differentiation via modulation of involucrin and transglutaminase expression through the integrin α3β1 and the phosphatidylinositol 3-kinase/Akt signaling pathway
    • Oh J.E., Kook J.K., and Min B.M. βig-h3 induces keratinocyte differentiation via modulation of involucrin and transglutaminase expression through the integrin α3β1 and the phosphatidylinositol 3-kinase/Akt signaling pathway. J. Biol. Chem. 280 (2005) 21629-21637
    • (2005) J. Biol. Chem. , vol.280 , pp. 21629-21637
    • Oh, J.E.1    Kook, J.K.2    Min, B.M.3
  • 35
    • 43049096117 scopus 로고    scopus 로고
    • βig-h3 interacts directly with biglycan and decorin, promotes collagen VI aggregation, and participates in ternary complexing with these macromolecules
    • Reinboth B., Thomas J., Hanssen E., and Gibson M. βig-h3 interacts directly with biglycan and decorin, promotes collagen VI aggregation, and participates in ternary complexing with these macromolecules. J. Biol. Chem. 278 (2006) 12601-12604
    • (2006) J. Biol. Chem. , vol.278 , pp. 12601-12604
    • Reinboth, B.1    Thomas, J.2    Hanssen, E.3    Gibson, M.4
  • 38
    • 34248562605 scopus 로고    scopus 로고
    • Dystroglycan: a possible mediator for reducing congenital muscular dystrophy?
    • Sciandra F., Gawlik K., Brancaccio A., and Durbeej M. Dystroglycan: a possible mediator for reducing congenital muscular dystrophy?. Trends Biotechnol. 25 (2007) 262-268
    • (2007) Trends Biotechnol. , vol.25 , pp. 262-268
    • Sciandra, F.1    Gawlik, K.2    Brancaccio, A.3    Durbeej, M.4
  • 39
    • 0026783009 scopus 로고
    • cDNA cloning and sequence analysis of βig-h3, a novel gene induced in a human adenocarcinoma cell line after treatment with transforming growth factor-β
    • Skonier J., Neubauer M., Madisen L., Bennett K., Plowman G.D., and Purchio A.F. cDNA cloning and sequence analysis of βig-h3, a novel gene induced in a human adenocarcinoma cell line after treatment with transforming growth factor-β. DNA Cell Biol. 11 (1992) 511-522
    • (1992) DNA Cell Biol. , vol.11 , pp. 511-522
    • Skonier, J.1    Neubauer, M.2    Madisen, L.3    Bennett, K.4    Plowman, G.D.5    Purchio, A.F.6
  • 41
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 42
    • 33846218303 scopus 로고    scopus 로고
    • Identification of an amyloidogenic region on keratoepithelin via synthetic peptides
    • Yuan C., Berscheit H.L., and Huang A.J. Identification of an amyloidogenic region on keratoepithelin via synthetic peptides. FEBS Lett. 581 (2007) 241-247
    • (2007) FEBS Lett. , vol.581 , pp. 241-247
    • Yuan, C.1    Berscheit, H.L.2    Huang, A.J.3
  • 43
    • 0037202283 scopus 로고    scopus 로고
    • Induction of TGF-β-inducible gene-h3 (βig-h3) by TGF-β1 in astrocytes: implications for astrocyte response to brain injury
    • Yun S.J., Kim M.O., Kim S.O., Park J., Kwon Y.K., Kim I.S., and Lee E.H. Induction of TGF-β-inducible gene-h3 (βig-h3) by TGF-β1 in astrocytes: implications for astrocyte response to brain injury. Brain Res. Mol. 107 (2002) 57-64
    • (2002) Brain Res. Mol. , vol.107 , pp. 57-64
    • Yun, S.J.1    Kim, M.O.2    Kim, S.O.3    Park, J.4    Kwon, Y.K.5    Kim, I.S.6    Lee, E.H.7
  • 45
    • 32044440777 scopus 로고    scopus 로고
    • Loss of βig-h3 protein is frequent in primary lung carcinoma and related to tumorigenic phenotype in lung cancer cells
    • Zhao Y., El-Gabry M., and Hei T.K. Loss of βig-h3 protein is frequent in primary lung carcinoma and related to tumorigenic phenotype in lung cancer cells. Mol. Carcinog. 45 (2006) 84-92
    • (2006) Mol. Carcinog. , vol.45 , pp. 84-92
    • Zhao, Y.1    El-Gabry, M.2    Hei, T.K.3
  • 46
    • 0024292597 scopus 로고
    • Sequence analysis and neuronal expression of fasciclin I in grasshopper and Drosophila
    • Zinn K., McAllister L., and Goodman C.S. Sequence analysis and neuronal expression of fasciclin I in grasshopper and Drosophila. Cell 53 (1988) 577-587
    • (1988) Cell , vol.53 , pp. 577-587
    • Zinn, K.1    McAllister, L.2    Goodman, C.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.