메뉴 건너뛰기




Volumn 55, Issue , 2011, Pages 35-59

Laminin isoform profiles in salivary glands in Sjögren's syndrome

Author keywords

Basement membrane; Integrin; Labial salivary glands; Laminins; Sj gren's syndrome

Indexed keywords


EID: 80052648055     PISSN: 00652423     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-387042-1.00003-4     Document Type: Chapter
Times cited : (6)

References (87)
  • 4
    • 84855743576 scopus 로고    scopus 로고
    • Neurobiology and hormonal control of lacrimal and salivary gland function
    • Humana Press, New York, USA, R. Fox (Ed.)
    • Konttinen Y.T., Vivó Porcar A., Porola P., et al. Neurobiology and hormonal control of lacrimal and salivary gland function. Sjögren's Syndrome 2011, Humana Press, New York, USA. R. Fox (Ed.).
    • (2011) Sjögren's Syndrome
    • Konttinen, Y.T.1    Vivó Porcar, A.2    Porola, P.3
  • 6
    • 0019859454 scopus 로고
    • In situ characterization of the cellular infiltrate in labial and palatine glands in Sjögren's syndrome
    • Konttinen Y.T. In situ characterization of the cellular infiltrate in labial and palatine glands in Sjögren's syndrome. Scand. J. Rheumatol. 1981, 10(4):321-330.
    • (1981) Scand. J. Rheumatol. , vol.10 , Issue.4 , pp. 321-330
    • Konttinen, Y.T.1
  • 7
    • 0023178420 scopus 로고
    • T lymphocyte activation state in the minor salivary glands of patients with Sjögren's syndrome
    • Segerberg-Konttinen M., Bergroth V., Jungell P., et al. T lymphocyte activation state in the minor salivary glands of patients with Sjögren's syndrome. Ann. Rheum. Dis. 1987, 46(9):649-653.
    • (1987) Ann. Rheum. Dis. , vol.46 , Issue.9 , pp. 649-653
    • Segerberg-Konttinen, M.1    Bergroth, V.2    Jungell, P.3
  • 8
    • 0031661502 scopus 로고    scopus 로고
    • The role of the laminins in basement membrane function
    • Aumailley M., Smyth N. The role of the laminins in basement membrane function. J. Anat. 1998, 193:1-21.
    • (1998) J. Anat. , vol.193 , pp. 1-21
    • Aumailley, M.1    Smyth, N.2
  • 10
    • 1442310569 scopus 로고    scopus 로고
    • Basement membrane assembly, stability and activities observed through a developmental lens
    • Yurchenco P.D., Amenta P.S., Patton B.L. Basement membrane assembly, stability and activities observed through a developmental lens. Matrix Biol. 2004, 22(7):521-538.
    • (2004) Matrix Biol. , vol.22 , Issue.7 , pp. 521-538
    • Yurchenco, P.D.1    Amenta, P.S.2    Patton, B.L.3
  • 11
    • 0026006388 scopus 로고
    • Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV
    • Fox J.W., Mayer U., Nischt R., et al. Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV. EMBO J. 1991, 10(11):3137-3146.
    • (1991) EMBO J. , vol.10 , Issue.11 , pp. 3137-3146
    • Fox, J.W.1    Mayer, U.2    Nischt, R.3
  • 12
    • 0032508461 scopus 로고    scopus 로고
    • Nidogen-2: a new basement membrane protein with diverse binding properties
    • Kohfeldt E., Sasaki T., Gohring W., Timpl R. Nidogen-2: a new basement membrane protein with diverse binding properties. J. Mol. Biol. 1998, 282(1):99-109.
    • (1998) J. Mol. Biol. , vol.282 , Issue.1 , pp. 99-109
    • Kohfeldt, E.1    Sasaki, T.2    Gohring, W.3    Timpl, R.4
  • 13
    • 0032126693 scopus 로고    scopus 로고
    • Mapping of the binding of platelet-derived growth factor to distinct domains of the basement membrane proteins BM-40 and perlecan and distinction from the BM-40 collagen-binding epitope
    • Gohring W., Sasaki T., Heldin C.H., Timpl R. Mapping of the binding of platelet-derived growth factor to distinct domains of the basement membrane proteins BM-40 and perlecan and distinction from the BM-40 collagen-binding epitope. Eur. J. Biochem. 1998, 255(1):60-66.
    • (1998) Eur. J. Biochem. , vol.255 , Issue.1 , pp. 60-66
    • Gohring, W.1    Sasaki, T.2    Heldin, C.H.3    Timpl, R.4
  • 14
    • 10444278111 scopus 로고    scopus 로고
    • Segment-specific but pathologic laminin isoform profiles in human labial salivary glands of patients with Sjögren's. syndrome
    • Laine M., Virtanen I., Salo T., Konttinen Y.T. Segment-specific but pathologic laminin isoform profiles in human labial salivary glands of patients with Sjögren's. syndrome. Arthritis Rheum. 2004, 50(12):3968-3973.
    • (2004) Arthritis Rheum. , vol.50 , Issue.12 , pp. 3968-3973
    • Laine, M.1    Virtanen, I.2    Salo, T.3    Konttinen, Y.T.4
  • 17
    • 0035988822 scopus 로고    scopus 로고
    • Laminin isoforms in tumor invasion, angiogenesis and metastasis
    • Patarroyo M., Tryggvason K., Virtanen I. Laminin isoforms in tumor invasion, angiogenesis and metastasis. Semin. Cancer Biol. 2002, 12(3):197-207.
    • (2002) Semin. Cancer Biol. , vol.12 , Issue.3 , pp. 197-207
    • Patarroyo, M.1    Tryggvason, K.2    Virtanen, I.3
  • 18
    • 36249022091 scopus 로고    scopus 로고
    • Bridging structure with function: structural, regulatory, and developmental role of laminins
    • Tzu J., Marinkovich M.P. Bridging structure with function: structural, regulatory, and developmental role of laminins. Int. J. Biochem. Cell Biol. 2008, 40:199-214.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 199-214
    • Tzu, J.1    Marinkovich, M.P.2
  • 19
    • 72449128021 scopus 로고    scopus 로고
    • Laminins
    • Durbeej M. Laminins. Cell Tissue Res. 2010, 339(1):259-268.
    • (2010) Cell Tissue Res. , vol.339 , Issue.1 , pp. 259-268
    • Durbeej, M.1
  • 21
    • 0031920354 scopus 로고    scopus 로고
    • Differential expression of laminin chains in the human major salivary gland
    • Strassburger S., Berndt A., Hyckel P., Katenkamp D., Kosmehl H. Differential expression of laminin chains in the human major salivary gland. Histochem. J. 1998, 30(2):81-88.
    • (1998) Histochem. J. , vol.30 , Issue.2 , pp. 81-88
    • Strassburger, S.1    Berndt, A.2    Hyckel, P.3    Katenkamp, D.4    Kosmehl, H.5
  • 22
    • 0023033082 scopus 로고
    • Mapping of domains in human laminin using monoclonal antibodies: localization of the neurite-promoting site
    • Engvall E., Davis G.E., Dickerson K., Ruoslahti E., Varon S., Manthorpe M. Mapping of domains in human laminin using monoclonal antibodies: localization of the neurite-promoting site. J. Cell Biol. 1986, 103(6 pt 1):2457-2465.
    • (1986) J. Cell Biol. , vol.103 , Issue.6 PART 1 , pp. 2457-2465
    • Engvall, E.1    Davis, G.E.2    Dickerson, K.3    Ruoslahti, E.4    Varon, S.5    Manthorpe, M.6
  • 23
    • 0030612270 scopus 로고    scopus 로고
    • Presence of laminin α5 chain and lack of laminin α1 chain during human muscle development and in muscular dystrophies
    • Tiger C.F., Chapliaud M.F., Pedrosa-Domellof F., Thornell L.E., Ekblom P., Gullberg D. Presence of laminin α5 chain and lack of laminin α1 chain during human muscle development and in muscular dystrophies. J. Biol. Chem. 1997, 272(45):28590-28595.
    • (1997) J. Biol. Chem. , vol.272 , Issue.45 , pp. 28590-28595
    • Tiger, C.F.1    Chapliaud, M.F.2    Pedrosa-Domellof, F.3    Thornell, L.E.4    Ekblom, P.5    Gullberg, D.6
  • 24
    • 0034658727 scopus 로고    scopus 로고
    • Laminin α1-chain shows a restricted distribution in epithelial basement membranes of fetal and adult human tissues
    • Virtanen I., Gullberg D., Rissanen J., et al. Laminin α1-chain shows a restricted distribution in epithelial basement membranes of fetal and adult human tissues. Exp. Cell Res. 2000, 257(2):298-309.
    • (2000) Exp. Cell Res. , vol.257 , Issue.2 , pp. 298-309
    • Virtanen, I.1    Gullberg, D.2    Rissanen, J.3
  • 25
    • 29644443430 scopus 로고    scopus 로고
    • Clonal proliferation of multipotent stem/progenitor cells in the neonatal and adult salivary glands
    • Kishi T., Takao T., Fujita L., Taniguchi H. Clonal proliferation of multipotent stem/progenitor cells in the neonatal and adult salivary glands. Biochem. Biophys. Res. Commun. 2006, 340(2):544-552.
    • (2006) Biochem. Biophys. Res. Commun. , vol.340 , Issue.2 , pp. 544-552
    • Kishi, T.1    Takao, T.2    Fujita, L.3    Taniguchi, H.4
  • 26
    • 0027405147 scopus 로고
    • Human neoplastic submandibular intercalated duct cells express an acinar phenotype when cultured on a basement membrane matrix
    • Royce L.S., Kibbey M.C., Mertz P., Kleinman H.K., Baum B.J. Human neoplastic submandibular intercalated duct cells express an acinar phenotype when cultured on a basement membrane matrix. Differentiation 1993, 52(3):247-255.
    • (1993) Differentiation , vol.52 , Issue.3 , pp. 247-255
    • Royce, L.S.1    Kibbey, M.C.2    Mertz, P.3    Kleinman, H.K.4    Baum, B.J.5
  • 27
    • 0034075654 scopus 로고    scopus 로고
    • Form and function: the laminin family of heterotrimers
    • Colognato H., Yurchenco P.D. Form and function: the laminin family of heterotrimers. Dev. Dyn. 2000, 218(2):213-234.
    • (2000) Dev. Dyn. , vol.218 , Issue.2 , pp. 213-234
    • Colognato, H.1    Yurchenco, P.D.2
  • 28
    • 77950232123 scopus 로고    scopus 로고
    • Immigration check for neutrophils in RA lining: laminin α5 low expression regions act as exit points
    • Poduval P., Sillat T., Virtanen I., Dabagh-Meshin M., Konttinen Y.T. Immigration check for neutrophils in RA lining: laminin α5 low expression regions act as exit points. Scand. J. Rheumatol. 2010, 39(2):132-140.
    • (2010) Scand. J. Rheumatol. , vol.39 , Issue.2 , pp. 132-140
    • Poduval, P.1    Sillat, T.2    Virtanen, I.3    Dabagh-Meshin, M.4    Konttinen, Y.T.5
  • 29
    • 0027524641 scopus 로고
    • Monoclonal antibody detection of laminin in minor salivary glands of patients with Sjogren's syndrome
    • McArthur C.P., Fox N.W., Kragel P. Monoclonal antibody detection of laminin in minor salivary glands of patients with Sjogren's syndrome. J. Autoimmun. 1993, 6(5):649-661.
    • (1993) J. Autoimmun. , vol.6 , Issue.5 , pp. 649-661
    • McArthur, C.P.1    Fox, N.W.2    Kragel, P.3
  • 30
    • 0035984172 scopus 로고    scopus 로고
    • Localization of laminin α4-chain in developing and adult human tissues
    • Petäjäniemi N., Korhonen M., Kortesmaa J., et al. Localization of laminin α4-chain in developing and adult human tissues. J. Histochem. Cytochem. 2002, 50(8):1113-1130.
    • (2002) J. Histochem. Cytochem. , vol.50 , Issue.8 , pp. 1113-1130
    • Petäjäniemi, N.1    Korhonen, M.2    Kortesmaa, J.3
  • 31
    • 33750945342 scopus 로고    scopus 로고
    • Involvement of specific laminins and nidogens in the active remodeling of the basal lamina of labial salivary glands from patients with Sjögren's syndrome
    • Kwon Y.J., Pérez P., Aguilera S., et al. Involvement of specific laminins and nidogens in the active remodeling of the basal lamina of labial salivary glands from patients with Sjögren's syndrome. Arthritis Rheum. 2006, 54(11):3465-3475.
    • (2006) Arthritis Rheum. , vol.54 , Issue.11 , pp. 3465-3475
    • Kwon, Y.J.1    Pérez, P.2    Aguilera, S.3
  • 32
    • 67449164838 scopus 로고    scopus 로고
    • Severe alterations in expression and localisation of α6β4 integrin in salivary gland acini from patients with Sjogren syndrome
    • Velozo J., Aguilera S., Alliende C., et al. Severe alterations in expression and localisation of α6β4 integrin in salivary gland acini from patients with Sjogren syndrome. Ann. Rheum. Dis. 2009, 68(6):991-996.
    • (2009) Ann. Rheum. Dis. , vol.68 , Issue.6 , pp. 991-996
    • Velozo, J.1    Aguilera, S.2    Alliende, C.3
  • 33
    • 31144449900 scopus 로고    scopus 로고
    • Basal lamina disorganisation of the acini and ducts of labial salivary glands from patients with Sjogren's syndrome: association with mononuclear cell infiltration
    • Molina C., Alliende C., Aguilera S., et al. Basal lamina disorganisation of the acini and ducts of labial salivary glands from patients with Sjogren's syndrome: association with mononuclear cell infiltration. Ann. Rheum. Dis. 2006, 65(2):178-183.
    • (2006) Ann. Rheum. Dis. , vol.65 , Issue.2 , pp. 178-183
    • Molina, C.1    Alliende, C.2    Aguilera, S.3
  • 34
    • 68149154526 scopus 로고    scopus 로고
    • Healthy human salivary glands contain a DHEA-sulphate processing intracrine machinery, which is deranged in primary Sjögren's syndrome
    • Spaan M., Porola P., Laine M., Rozman B., Azuma M., Konttinen Y.T. Healthy human salivary glands contain a DHEA-sulphate processing intracrine machinery, which is deranged in primary Sjögren's syndrome. J. Cell. Mol. Med. 2009, 13(7):1261-1270.
    • (2009) J. Cell. Mol. Med. , vol.13 , Issue.7 , pp. 1261-1270
    • Spaan, M.1    Porola, P.2    Laine, M.3    Rozman, B.4    Azuma, M.5    Konttinen, Y.T.6
  • 35
    • 56449091590 scopus 로고    scopus 로고
    • Androgen deficiency and defective intracrine processing of DHEA in the salivary glands in Sjögren's syndrome
    • Porola P., Virkki L., Przybyla B.D., et al. Androgen deficiency and defective intracrine processing of DHEA in the salivary glands in Sjögren's syndrome. J. Rheumatol. 2008, 35(11):2229-2235.
    • (2008) J. Rheumatol. , vol.35 , Issue.11 , pp. 2229-2235
    • Porola, P.1    Virkki, L.2    Przybyla, B.D.3
  • 36
    • 33645380797 scopus 로고    scopus 로고
    • Ligand-binding specificities of laminin-binding integrins: a comprehensive survey of laminin-integrin interactions using recombinant alpha3beta1, alpha6beta1, alpha7beta1 and alpha6beta4 integrins
    • Nishiuchi R., Takagi J., Hayashi M., et al. Ligand-binding specificities of laminin-binding integrins: a comprehensive survey of laminin-integrin interactions using recombinant alpha3beta1, alpha6beta1, alpha7beta1 and alpha6beta4 integrins. Matrix Biol. 2006, 25(3):189-197.
    • (2006) Matrix Biol. , vol.25 , Issue.3 , pp. 189-197
    • Nishiuchi, R.1    Takagi, J.2    Hayashi, M.3
  • 37
    • 18844462417 scopus 로고    scopus 로고
    • Laminin-induced signaling in tumor cells
    • Givant-Horwitz V., Davidson B., Reich R. Laminin-induced signaling in tumor cells. Cancer Lett. 2005, 223(1):1-10.
    • (2005) Cancer Lett. , vol.223 , Issue.1 , pp. 1-10
    • Givant-Horwitz, V.1    Davidson, B.2    Reich, R.3
  • 39
    • 0035161468 scopus 로고    scopus 로고
    • Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity
    • Parsons S.F., Lee G., Spring F.A., et al. Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity. Blood 2001, 97(1):312-320.
    • (2001) Blood , vol.97 , Issue.1 , pp. 312-320
    • Parsons, S.F.1    Lee, G.2    Spring, F.A.3
  • 40
    • 0035252649 scopus 로고    scopus 로고
    • The complexities of dystroglycan
    • Winder S.J. The complexities of dystroglycan. Trends Biochem. Sci. 2001, 26(2):118-124.
    • (2001) Trends Biochem. Sci. , vol.26 , Issue.2 , pp. 118-124
    • Winder, S.J.1
  • 41
    • 33645113450 scopus 로고    scopus 로고
    • Review: Lutheran/B-CAM: a laminin receptor on red blood cells and various tissues
    • Kikkawa Y., Miner J.H. Review: Lutheran/B-CAM: a laminin receptor on red blood cells and various tissues. Connect. Tissue Res. 2005, 46(4-5):193-199.
    • (2005) Connect. Tissue Res. , vol.46 , Issue.4-5 , pp. 193-199
    • Kikkawa, Y.1    Miner, J.H.2
  • 42
    • 0035824835 scopus 로고    scopus 로고
    • Domain IVa of laminin alpha5 chain is cell-adhesive and binds beta1 and alphaVbeta3 integrins through Arg-Gly-Asp
    • Sasaki T., Timpl R. Domain IVa of laminin alpha5 chain is cell-adhesive and binds beta1 and alphaVbeta3 integrins through Arg-Gly-Asp. FEBS Lett. 2001, 509(2):181-185.
    • (2001) FEBS Lett. , vol.509 , Issue.2 , pp. 181-185
    • Sasaki, T.1    Timpl, R.2
  • 43
    • 57649121587 scopus 로고    scopus 로고
    • Laminin isoforms containing the gamma3 chain are unable to bind to integrins due to the absence of the glutamic acid residue conserved in the C-terminal regions of the gamma1 and gamma2 chains
    • Ido H., Ito S., Taniguchi Y., et al. Laminin isoforms containing the gamma3 chain are unable to bind to integrins due to the absence of the glutamic acid residue conserved in the C-terminal regions of the gamma1 and gamma2 chains. J. Biol. Chem. 2008, 283(42):28149-28157.
    • (2008) J. Biol. Chem. , vol.283 , Issue.42 , pp. 28149-28157
    • Ido, H.1    Ito, S.2    Taniguchi, Y.3
  • 44
    • 57249116222 scopus 로고    scopus 로고
    • Acinar epithelial cell laminin-receptors in labial salivary glands in Sjögren's syndrome
    • Laine M., Virtanen I., Porola P., et al. Acinar epithelial cell laminin-receptors in labial salivary glands in Sjögren's syndrome. Clin. Exp. Rheumatol. 2008, 26:807-813.
    • (2008) Clin. Exp. Rheumatol. , vol.26 , pp. 807-813
    • Laine, M.1    Virtanen, I.2    Porola, P.3
  • 45
    • 0029060919 scopus 로고
    • Overexpression of transforming growth factor-beta 1 mRNA is associated with up-regulation of glomerular tenascin and laminin gene expression in nonobese diabetic mice
    • Yang C.W., Hattori M., Vlassara H., et al. Overexpression of transforming growth factor-beta 1 mRNA is associated with up-regulation of glomerular tenascin and laminin gene expression in nonobese diabetic mice. J. Am. Soc. Nephrol. 1995, 5(8):1610-1617.
    • (1995) J. Am. Soc. Nephrol. , vol.5 , Issue.8 , pp. 1610-1617
    • Yang, C.W.1    Hattori, M.2    Vlassara, H.3
  • 46
    • 0029144650 scopus 로고
    • Transforming growth factor β2 in labial salivary glands in Sjögren's syndrome
    • Koski H., Konttinen Y.T., Xu-Hong G., Hietanen J., Malmström M. Transforming growth factor β2 in labial salivary glands in Sjögren's syndrome. Ann. Rheum. Dis. 1995, 54(9):744-747.
    • (1995) Ann. Rheum. Dis. , vol.54 , Issue.9 , pp. 744-747
    • Koski, H.1    Konttinen, Y.T.2    Xu-Hong, G.3    Hietanen, J.4    Malmström, M.5
  • 47
    • 70349975887 scopus 로고    scopus 로고
    • Cytokines in Sjögren's syndrome
    • Roescher N., Tak P.P., Illei G.G. Cytokines in Sjögren's syndrome. Oral Dis. 2009, 15(8):519-526.
    • (2009) Oral Dis. , vol.15 , Issue.8 , pp. 519-526
    • Roescher, N.1    Tak, P.P.2    Illei, G.G.3
  • 48
    • 0033168981 scopus 로고    scopus 로고
    • Cytokine-mediated stimulation of laminin expression and cell-growth arrest in a human submandibular gland duct-cell line (HSG)
    • Daniels P.J., McArthur C.P., Heruth D.P., Rothberg P.G., Pasztor L., Wang Y. Cytokine-mediated stimulation of laminin expression and cell-growth arrest in a human submandibular gland duct-cell line (HSG). Arch. Oral Biol. 1999, 44(7):603-615.
    • (1999) Arch. Oral Biol. , vol.44 , Issue.7 , pp. 603-615
    • Daniels, P.J.1    McArthur, C.P.2    Heruth, D.P.3    Rothberg, P.G.4    Pasztor, L.5    Wang, Y.6
  • 49
    • 35348912695 scopus 로고    scopus 로고
    • Chronic hyperglycaemia increases TGFbeta2 signaling and the expression of extracellular matrix proteins in the rat parotid gland
    • Lamers M.L., Gimenes F.A., Nogueira F.N., Nicolau J., Gama P., Santos M.F. Chronic hyperglycaemia increases TGFbeta2 signaling and the expression of extracellular matrix proteins in the rat parotid gland. Matrix Biol. 2007, 26(7):572-582.
    • (2007) Matrix Biol. , vol.26 , Issue.7 , pp. 572-582
    • Lamers, M.L.1    Gimenes, F.A.2    Nogueira, F.N.3    Nicolau, J.4    Gama, P.5    Santos, M.F.6
  • 50
    • 72749108194 scopus 로고    scopus 로고
    • Regulated laminin-332 expression in human islets of Langerhans
    • Armanet M., Wojtusciszyn A., Morel P., et al. Regulated laminin-332 expression in human islets of Langerhans. FASEB J. 2009, 23(12):4046-4055.
    • (2009) FASEB J. , vol.23 , Issue.12 , pp. 4046-4055
    • Armanet, M.1    Wojtusciszyn, A.2    Morel, P.3
  • 51
    • 0028940814 scopus 로고
    • IL-1 beta increases laminin B2 chain mRNA levels and activates NF-kappa B in rat glomerular epithelial cells
    • Richardson C.A., Gordon K.L., Couser W.G., Bomsztyk K. IL-1 beta increases laminin B2 chain mRNA levels and activates NF-kappa B in rat glomerular epithelial cells. Am. J. Physiol. 1995, 268(2 Pt. 2):F273-F278.
    • (1995) Am. J. Physiol. , vol.268 , Issue.2 PART 2
    • Richardson, C.A.1    Gordon, K.L.2    Couser, W.G.3    Bomsztyk, K.4
  • 52
    • 0029082448 scopus 로고
    • Differential cytokine modulation of the genes LAMA3, LAMB3, and LAMC2, encoding the constitutive polypeptides, alpha 3, beta 3, and gamma 2, of human laminin 5 in epidermal keratinocytes
    • Korang K., Christiano A.M., Uitto J., Mauviel A. Differential cytokine modulation of the genes LAMA3, LAMB3, and LAMC2, encoding the constitutive polypeptides, alpha 3, beta 3, and gamma 2, of human laminin 5 in epidermal keratinocytes. FEBS Lett. 1995, 368(3):556-558.
    • (1995) FEBS Lett. , vol.368 , Issue.3 , pp. 556-558
    • Korang, K.1    Christiano, A.M.2    Uitto, J.3    Mauviel, A.4
  • 53
    • 0033371904 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 regulates basement membrane formation by alveolar epithelial cells in vitro
    • Furuyama A., Iwata M., Hayashi T., Mochitate K. Transforming growth factor-beta1 regulates basement membrane formation by alveolar epithelial cells in vitro. Eur. J. Cell Biol. 1999, 78(12):867-875.
    • (1999) Eur. J. Cell Biol. , vol.78 , Issue.12 , pp. 867-875
    • Furuyama, A.1    Iwata, M.2    Hayashi, T.3    Mochitate, K.4
  • 54
    • 0345035511 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 stimulates the synthesis of basement membrane proteins laminin, collagen type IV and entactin in rat liver sinusoidal endothelial cells
    • Neubauer K., Krüger M., Quondamatteo F., Knittel T., Saile B., Ramadori G. Transforming growth factor-beta1 stimulates the synthesis of basement membrane proteins laminin, collagen type IV and entactin in rat liver sinusoidal endothelial cells. J. Hepatol. 1999, 31(4):692-702.
    • (1999) J. Hepatol. , vol.31 , Issue.4 , pp. 692-702
    • Neubauer, K.1    Krüger, M.2    Quondamatteo, F.3    Knittel, T.4    Saile, B.5    Ramadori, G.6
  • 55
    • 0242380798 scopus 로고    scopus 로고
    • Converging signals synergistically activate the LAMC2 promoter and lead to accumulation of the laminin gamma 2 chain in human colon carcinoma cells
    • Olsen J., Kirkeby L.T., Brorsson M.M., et al. Converging signals synergistically activate the LAMC2 promoter and lead to accumulation of the laminin gamma 2 chain in human colon carcinoma cells. Biochem. J. 2003, 371(Pt. 1):211-221.
    • (2003) Biochem. J. , vol.371 , Issue.PART 1 , pp. 211-221
    • Olsen, J.1    Kirkeby, L.T.2    Brorsson, M.M.3
  • 56
    • 45049085909 scopus 로고    scopus 로고
    • Interleukin-1beta and tumor necrosis factor-alpha have opposite effects on fibroblasts and epithelial cells during basement membrane formation
    • Furuyama A., Hosokawa T., Mochitate K. Interleukin-1beta and tumor necrosis factor-alpha have opposite effects on fibroblasts and epithelial cells during basement membrane formation. Matrix Biol. 2008, 27(5):429-440.
    • (2008) Matrix Biol. , vol.27 , Issue.5 , pp. 429-440
    • Furuyama, A.1    Hosokawa, T.2    Mochitate, K.3
  • 57
    • 0024351654 scopus 로고
    • A retinoic acid-responsive element is present in the 5' flanking region of the laminin B1 gene
    • Vasios G.W., Gold J.D., Petkovich M., Chambon P., Gudas L.J. A retinoic acid-responsive element is present in the 5' flanking region of the laminin B1 gene. Proc. Natl. Acad. Sci. USA 1989, 86(23):9099-9103.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , Issue.23 , pp. 9099-9103
    • Vasios, G.W.1    Gold, J.D.2    Petkovich, M.3    Chambon, P.4    Gudas, L.J.5
  • 58
    • 0029897993 scopus 로고    scopus 로고
    • Positive elements in the laminin γ1 gene synergize to activate high level transcription during cellular differentiation
    • Chang H.S., Kim N.B., Philips S.L. Positive elements in the laminin γ1 gene synergize to activate high level transcription during cellular differentiation. Nucleic Acids Res. 1996, 24(7):1360-1368.
    • (1996) Nucleic Acids Res. , vol.24 , Issue.7 , pp. 1360-1368
    • Chang, H.S.1    Kim, N.B.2    Philips, S.L.3
  • 59
    • 0031009862 scopus 로고    scopus 로고
    • Regulatory sequences for the transcription of the laminin B2 gene in astrocytes
    • Kedar V., Freese E., Hempel F.G. Regulatory sequences for the transcription of the laminin B2 gene in astrocytes. Brain Res. Mol. Brain Res. 1997, 47(1-2):87-98.
    • (1997) Brain Res. Mol. Brain Res. , vol.47 , Issue.1-2 , pp. 87-98
    • Kedar, V.1    Freese, E.2    Hempel, F.G.3
  • 60
    • 0036606463 scopus 로고    scopus 로고
    • Synergistic activation of the rat laminin gamma1 chain promoter by the gut-enriched Kruppel-like factor (GKLF/KLF4) and Sp1
    • Higaki Y., Schullery D., Kawata Y., Shnyreva M., Abrass C., Bomsztyk K. Synergistic activation of the rat laminin gamma1 chain promoter by the gut-enriched Kruppel-like factor (GKLF/KLF4) and Sp1. Nucleic Acids Res. 2002, 30(11):2270-2279.
    • (2002) Nucleic Acids Res. , vol.30 , Issue.11 , pp. 2270-2279
    • Higaki, Y.1    Schullery, D.2    Kawata, Y.3    Shnyreva, M.4    Abrass, C.5    Bomsztyk, K.6
  • 61
    • 0032502958 scopus 로고    scopus 로고
    • Structural analysis and proteolytic processing of recombinant G domain of mouse laminin alpha2 chain
    • Talts J.F., Mann K., Yamada Y., Timpl R. Structural analysis and proteolytic processing of recombinant G domain of mouse laminin alpha2 chain. FEBS Lett. 1998, 426(1):71-76.
    • (1998) FEBS Lett. , vol.426 , Issue.1 , pp. 71-76
    • Talts, J.F.1    Mann, K.2    Yamada, Y.3    Timpl, R.4
  • 63
    • 0037160514 scopus 로고    scopus 로고
    • Cell line-specific translation of two laminin 5 beta3 chain isoforms
    • Hao J., McDaniel K., Weyer C., Barrera J., Nagle R.B. Cell line-specific translation of two laminin 5 beta3 chain isoforms. Gene 2002, 283(1-2):237-244.
    • (2002) Gene , vol.283 , Issue.1-2 , pp. 237-244
    • Hao, J.1    McDaniel, K.2    Weyer, C.3    Barrera, J.4    Nagle, R.B.5
  • 64
    • 0036433237 scopus 로고    scopus 로고
    • Identification and recombinant production of human laminin alpha4 subunit splice variants
    • Hayashi Y., Kim K.H., Fujiwara H., et al. Identification and recombinant production of human laminin alpha4 subunit splice variants. Biochem. Biophys. Res. Commun. 2002, 299(3):498-504.
    • (2002) Biochem. Biophys. Res. Commun. , vol.299 , Issue.3 , pp. 498-504
    • Hayashi, Y.1    Kim, K.H.2    Fujiwara, H.3
  • 65
    • 0346963110 scopus 로고    scopus 로고
    • Aberrant promoter methylation and silencing of laminin-5-encoding genes in breast carcinoma
    • Sathyanarayana U.G., Padar A., Huang C.X., et al. Aberrant promoter methylation and silencing of laminin-5-encoding genes in breast carcinoma. Clin. Cancer Res. 2003, 9(17):6389-6394.
    • (2003) Clin. Cancer Res. , vol.9 , Issue.17 , pp. 6389-6394
    • Sathyanarayana, U.G.1    Padar, A.2    Huang, C.X.3
  • 66
    • 0346963111 scopus 로고    scopus 로고
    • Aberrant promoter methylation of laminin-5-encoding genes in prostate cancers and its relationship to clinicopathological features
    • Sathyanarayana U.G., Padar A., Suzuki M., et al. Aberrant promoter methylation of laminin-5-encoding genes in prostate cancers and its relationship to clinicopathological features. Clin. Cancer Res. 2003, 9(17):6395-6400.
    • (2003) Clin. Cancer Res. , vol.9 , Issue.17 , pp. 6395-6400
    • Sathyanarayana, U.G.1    Padar, A.2    Suzuki, M.3
  • 67
    • 34548205414 scopus 로고    scopus 로고
    • Binding of netrin-4 to laminin short arms regulates basement membrane assembly
    • Schneiders F.I., Maertens B., Böse K., et al. Binding of netrin-4 to laminin short arms regulates basement membrane assembly. J. Biol. Chem. 2007, 282(33):23750-23758.
    • (2007) J. Biol. Chem. , vol.282 , Issue.33 , pp. 23750-23758
    • Schneiders, F.I.1    Maertens, B.2    Böse, K.3
  • 68
    • 0034999541 scopus 로고    scopus 로고
    • Amplification of extracellular matrix and oncogenes in tat-transfected human salivary gland cell lines with expression of laminin, fibronectin, collagens I, III, IV, c-myc and p53
    • McArthur C.P., Wang Y., Heruth D., Gustafson S. Amplification of extracellular matrix and oncogenes in tat-transfected human salivary gland cell lines with expression of laminin, fibronectin, collagens I, III, IV, c-myc and p53. Arch. Oral Biol. 2001, 46(6):545-555.
    • (2001) Arch. Oral Biol. , vol.46 , Issue.6 , pp. 545-555
    • McArthur, C.P.1    Wang, Y.2    Heruth, D.3    Gustafson, S.4
  • 69
    • 0023389792 scopus 로고
    • Genes for basement membrane proteins are coordinately expressed in differentiating F9 cells but not in normal adult murine tissues
    • Kleinman H.K., Ebihara I., Killen P.D., et al. Genes for basement membrane proteins are coordinately expressed in differentiating F9 cells but not in normal adult murine tissues. Dev. Biol. 1987, 122(2):373-378.
    • (1987) Dev. Biol. , vol.122 , Issue.2 , pp. 373-378
    • Kleinman, H.K.1    Ebihara, I.2    Killen, P.D.3
  • 70
    • 64849092290 scopus 로고    scopus 로고
    • All-trans retinoic acid remodels extracellular matrix and suppresses laminin-enhanced contractility of cultured human retinal pigment epithelial cells
    • Chang Y.C., Kao Y.H., Hu D.N., Tsai L.Y., Wu W.C. All-trans retinoic acid remodels extracellular matrix and suppresses laminin-enhanced contractility of cultured human retinal pigment epithelial cells. Exp. Eye Res. 2009, 88(5):900-909.
    • (2009) Exp. Eye Res. , vol.88 , Issue.5 , pp. 900-909
    • Chang, Y.C.1    Kao, Y.H.2    Hu, D.N.3    Tsai, L.Y.4    Wu, W.C.5
  • 71
    • 0034982309 scopus 로고    scopus 로고
    • Low serum dehydroepiandrosterone sulfate in women with primary Sjögren's syndrome as an isolated sign of impaired HPA axis function
    • Valtysdóttir S.T., Wide L., Hällgren R. Low serum dehydroepiandrosterone sulfate in women with primary Sjögren's syndrome as an isolated sign of impaired HPA axis function. J. Rheumatol. 2001, 28(6):1259-1265.
    • (2001) J. Rheumatol. , vol.28 , Issue.6 , pp. 1259-1265
    • Valtysdóttir, S.T.1    Wide, L.2    Hällgren, R.3
  • 72
    • 36048988128 scopus 로고    scopus 로고
    • 17beta-Estradiol attenuates diabetic kidney disease by regulating extracellular matrix and transforming growth factor-beta protein expression and signaling
    • Dixon A., Maric C. 17beta-Estradiol attenuates diabetic kidney disease by regulating extracellular matrix and transforming growth factor-beta protein expression and signaling. Am. J. Physiol. Renal Physiol. 2007, 293(5):F1678-F1690.
    • (2007) Am. J. Physiol. Renal Physiol. , vol.293 , Issue.5
    • Dixon, A.1    Maric, C.2
  • 73
    • 77951248171 scopus 로고    scopus 로고
    • Effects of estrogens on extracellular matrix synthesis in cultures of human normal and scleroderma skin fibroblasts
    • Soldano S., Montagna P., Brizzolara R., et al. Effects of estrogens on extracellular matrix synthesis in cultures of human normal and scleroderma skin fibroblasts. Ann. N. Y. Acad. Sci. 2010, 1193(1):25-29.
    • (2010) Ann. N. Y. Acad. Sci. , vol.1193 , Issue.1 , pp. 25-29
    • Soldano, S.1    Montagna, P.2    Brizzolara, R.3
  • 74
    • 37049020899 scopus 로고    scopus 로고
    • Estradiol, tamoxifen and ICI 182,780 alter alpha3 and beta1 integrin expression and laminin-1 adhesion in oral squamous cell carcinoma cell cultures
    • Nelson K., Helmstaedter V., Moreau C., Lage H. Estradiol, tamoxifen and ICI 182,780 alter alpha3 and beta1 integrin expression and laminin-1 adhesion in oral squamous cell carcinoma cell cultures. Oral Oncol. 2008, 44(1):94-99.
    • (2008) Oral Oncol. , vol.44 , Issue.1 , pp. 94-99
    • Nelson, K.1    Helmstaedter, V.2    Moreau, C.3    Lage, H.4
  • 75
    • 0009733995 scopus 로고    scopus 로고
    • Estradiol enhances endothelial cell interactions with extracellular matrix proteins via an increase in integrin expression and function
    • Cid M.C., Esparza J., Schnaper H.W., et al. Estradiol enhances endothelial cell interactions with extracellular matrix proteins via an increase in integrin expression and function. Angiogenesis 1999, 3(3):271-280.
    • (1999) Angiogenesis , vol.3 , Issue.3 , pp. 271-280
    • Cid, M.C.1    Esparza, J.2    Schnaper, H.W.3
  • 76
    • 73949145188 scopus 로고    scopus 로고
    • Expression of estrogen receptor beta increases integrin alpha1 and integrin beta1 levels and enhances adhesion of breast cancer cells
    • Lindberg K., Ström A., Lock J.G., Gustafsson J.A., Haldosén L.A., Helguero L.A. Expression of estrogen receptor beta increases integrin alpha1 and integrin beta1 levels and enhances adhesion of breast cancer cells. J. Cell. Physiol. 2010, 222(1):156-167.
    • (2010) J. Cell. Physiol. , vol.222 , Issue.1 , pp. 156-167
    • Lindberg, K.1    Ström, A.2    Lock, J.G.3    Gustafsson, J.A.4    Haldosén, L.A.5    Helguero, L.A.6
  • 77
    • 0023274392 scopus 로고
    • Regulation of types I, III, and IV procollagen mRNA synthesis in glucocorticoid-mediated intestinal development
    • Walsh M.J., LeLeiko N.S., Sterling K.M. Regulation of types I, III, and IV procollagen mRNA synthesis in glucocorticoid-mediated intestinal development. J. Biol. Chem. 1987, 262(22):10814-10818.
    • (1987) J. Biol. Chem. , vol.262 , Issue.22 , pp. 10814-10818
    • Walsh, M.J.1    LeLeiko, N.S.2    Sterling, K.M.3
  • 78
    • 3543098725 scopus 로고    scopus 로고
    • Increase in laminin expression in allergic airway remodelling and decrease by dexamethasone
    • Christie P.E., Jonas M., Tsai C.H., Chi E.Y., Henderson W.R. Increase in laminin expression in allergic airway remodelling and decrease by dexamethasone. Eur. Respir. J. 2004, 24(1):107-115.
    • (2004) Eur. Respir. J. , vol.24 , Issue.1 , pp. 107-115
    • Christie, P.E.1    Jonas, M.2    Tsai, C.H.3    Chi, E.Y.4    Henderson, W.R.5
  • 79
    • 0030922879 scopus 로고    scopus 로고
    • The alpha chain of laminin-1 is independently secreted and drives secretion of its beta- and gamma-chain partners
    • Yurchenco P.D., Quan Y., Colognato H., et al. The alpha chain of laminin-1 is independently secreted and drives secretion of its beta- and gamma-chain partners. Proc. Natl. Acad. Sci. USA 1997, 94(19):10189-10194.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.19 , pp. 10189-10194
    • Yurchenco, P.D.1    Quan, Y.2    Colognato, H.3
  • 81
    • 13144250206 scopus 로고    scopus 로고
    • Matrix metalloproteinase (MMP)-9 type IV collagenase/gelatinase implicated in the pathogenesis of Sjögren's syndrome
    • Konttinen Y.T., Halinen S., Hanemaaijer R., et al. Matrix metalloproteinase (MMP)-9 type IV collagenase/gelatinase implicated in the pathogenesis of Sjögren's syndrome. Matrix Biol. 1998, 17(5):335-347.
    • (1998) Matrix Biol. , vol.17 , Issue.5 , pp. 335-347
    • Konttinen, Y.T.1    Halinen, S.2    Hanemaaijer, R.3
  • 82
    • 0032428256 scopus 로고    scopus 로고
    • A novel and simple immunocapture assay for determination of gelatinase-B (MMP-9) activities in biological fluids: saliva from patients with Sjögren's syndrome contain increased latent and active gelatinase-B levels
    • Hanemaaijer R., Visser H., Konttinen Y.T., Koolwijk P., Verheijen J.H. A novel and simple immunocapture assay for determination of gelatinase-B (MMP-9) activities in biological fluids: saliva from patients with Sjögren's syndrome contain increased latent and active gelatinase-B levels. Matrix Biol. 1998, 17(8-9):657-665.
    • (1998) Matrix Biol. , vol.17 , Issue.8-9 , pp. 657-665
    • Hanemaaijer, R.1    Visser, H.2    Konttinen, Y.T.3    Koolwijk, P.4    Verheijen, J.H.5
  • 83
    • 0034538381 scopus 로고    scopus 로고
    • Differential expression of matrix metalloproteinases in labial salivary glands of patients with primary Sjögren's syndrome
    • Pérez P., Goicovich E., Alliende C., et al. Differential expression of matrix metalloproteinases in labial salivary glands of patients with primary Sjögren's syndrome. Arthritis Rheum. 2000, 43(12):2807-2817.
    • (2000) Arthritis Rheum. , vol.43 , Issue.12 , pp. 2807-2817
    • Pérez, P.1    Goicovich, E.2    Alliende, C.3
  • 84
    • 25444431697 scopus 로고    scopus 로고
    • Increased acinar damage of salivary glands of patients with Sjögren's syndrome is paralleled by simultaneous imbalance of matrix metalloproteinase 3/tissue inhibitor of metalloproteinases 1 and matrix metalloproteinase 9/tissue inhibitor of metalloproteinases 1 ratios
    • Pérez P., Kwon Y.J., Alliende C., et al. Increased acinar damage of salivary glands of patients with Sjögren's syndrome is paralleled by simultaneous imbalance of matrix metalloproteinase 3/tissue inhibitor of metalloproteinases 1 and matrix metalloproteinase 9/tissue inhibitor of metalloproteinases 1 ratios. Arthritis Rheum. 2005, 52(9):2751-2760.
    • (2005) Arthritis Rheum. , vol.52 , Issue.9 , pp. 2751-2760
    • Pérez, P.1    Kwon, Y.J.2    Alliende, C.3
  • 85
    • 0141564937 scopus 로고    scopus 로고
    • Enhanced degradation of proteins of the basal lamina and stroma by matrix metalloproteinases from the salivary glands of Sjögren's syndrome patients: correlation with reduced structural integrity of acini and ducts
    • Goicovich E., Molina C., Pérez P., et al. Enhanced degradation of proteins of the basal lamina and stroma by matrix metalloproteinases from the salivary glands of Sjögren's syndrome patients: correlation with reduced structural integrity of acini and ducts. Arthritis Rheum. 2003, 48(9):2573-2584.
    • (2003) Arthritis Rheum. , vol.48 , Issue.9 , pp. 2573-2584
    • Goicovich, E.1    Molina, C.2    Pérez, P.3
  • 86
    • 0032489876 scopus 로고    scopus 로고
    • Processing of laminin-5 and its functional consequences: role of plasmin and tissue-type plasminogen activator
    • Goldfinger L.E., Stack M.S., Jones J.C. Processing of laminin-5 and its functional consequences: role of plasmin and tissue-type plasminogen activator. J. Cell Biol. 1998, 141(1):255-265.
    • (1998) J. Cell Biol. , vol.141 , Issue.1 , pp. 255-265
    • Goldfinger, L.E.1    Stack, M.S.2    Jones, J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.