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Volumn 8, Issue 8, 2013, Pages

Laminin Receptor 37/67LR Regulates Adhesion and Proliferation of Normal Human Intestinal Epithelial Cells

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; INTEGRIN RECEPTOR; LAMININ; LAMININ RECEPTOR; MEMBRANE PROTEIN; SMALL INTERFERING RNA;

EID: 84882738953     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0074337     Document Type: Article
Times cited : (19)

References (83)
  • 1
    • 0030087944 scopus 로고    scopus 로고
    • Supramolecular assembly of basement membranes
    • doi:10.1002/bies.950180208
    • Timpl R, Brown JC, (1996) Supramolecular assembly of basement membranes. Bioessays 18: 123-132. doi:10.1002/bies.950180208. PubMed: 8851045.
    • (1996) Bioessays , vol.18 , pp. 123-132
    • Timpl, R.1    Brown, J.C.2
  • 2
    • 72449128021 scopus 로고    scopus 로고
    • Laminins
    • doi:10.1007/s00441-009-0838-2
    • Durbeej M, (2010) Laminins. Cell Tissue Res 339: 259-268. doi:10.1007/s00441-009-0838-2. PubMed: 19693542.
    • (2010) Cell Tissue Res , vol.339 , pp. 259-268
    • Durbeej, M.1
  • 3
    • 0035988822 scopus 로고    scopus 로고
    • Laminin isoforms in tumor invasion, angiogenesis and metastasis
    • doi:10.1016/S1044-579X(02)00023-8
    • Patarroyo M, Tryggvason K, Virtanen I, (2002) Laminin isoforms in tumor invasion, angiogenesis and metastasis. Semin Cancer Biol 12: 197-207. doi:10.1016/S1044-579X(02)00023-8. PubMed: 12083850.
    • (2002) Semin Cancer Biol , vol.12 , pp. 197-207
    • Patarroyo, M.1    Tryggvason, K.2    Virtanen, I.3
  • 4
    • 8444247525 scopus 로고    scopus 로고
    • Laminin functions in tissue morphogenesis
    • doi:10.1146/annurev.cellbio.20.010403.094555
    • Miner JH, Yurchenco PD, (2004) Laminin functions in tissue morphogenesis. Annu Rev Cell Dev Biol 20: 255-284. doi:10.1146/annurev.cellbio.20.010403.094555. PubMed: 15473841.
    • (2004) Annu Rev Cell Dev Biol , vol.20 , pp. 255-284
    • Miner, J.H.1    Yurchenco, P.D.2
  • 5
    • 84870183095 scopus 로고    scopus 로고
    • Functional diversity of laminins
    • doi:10.1146/annurev-cellbio-101011-155750
    • Domogatskaya A, Rodin S, Tryggvason K, (2012) Functional diversity of laminins. Annu Rev Cell Dev Biol 28: 523-553. doi:10.1146/annurev-cellbio-101011-155750. PubMed: 23057746.
    • (2012) Annu Rev Cell Dev Biol , vol.28 , pp. 523-553
    • Domogatskaya, A.1    Rodin, S.2    Tryggvason, K.3
  • 6
    • 84865726671 scopus 로고    scopus 로고
    • Integrin alpha6beta4 in colorectal cancer
    • doi:10.4239/wjd.v1.i1.3
    • Beaulieu JF, (2010) Integrin alpha6beta4 in colorectal cancer. World J Gastrointest Pathophysiol 1: 3-11. doi:10.4239/wjd.v1.i1.3. PubMed: 21607137.
    • (2010) World J Gastrointest Pathophysiol , vol.1 , pp. 3-11
    • Beaulieu, J.F.1
  • 7
    • 0034333146 scopus 로고    scopus 로고
    • Integrins as receptors for laminins
    • doi:10.1002/1097-0029(20001101)51:3
    • Belkin AM, Stepp MA, (2000) Integrins as receptors for laminins. Microsc Res Tech 51: 280-301. doi:10.1002/1097-0029(20001101)51:3. PubMed: 11054877.
    • (2000) Microsc Res Tech , vol.51 , pp. 280-301
    • Belkin, A.M.1    Stepp, M.A.2
  • 8
    • 84863257178 scopus 로고    scopus 로고
    • beta1D chain increases alpha7beta1 integrin and laminin and protects against sarcolemmal damage in mdx mice
    • doi:10.1093/hmg/ddr596
    • Liu J, Milner DJ, Boppart MD, Ross RS, Kaufman SJ, (2012) beta1D chain increases alpha7beta1 integrin and laminin and protects against sarcolemmal damage in mdx mice. Hum Mol Genet 21: 1592-1603. doi:10.1093/hmg/ddr596. PubMed: 22180459.
    • (2012) Hum Mol Genet , vol.21 , pp. 1592-1603
    • Liu, J.1    Milner, D.J.2    Boppart, M.D.3    Ross, R.S.4    Kaufman, S.J.5
  • 9
    • 67349170307 scopus 로고    scopus 로고
    • Functional diversity of dystroglycan
    • doi:10.1016/j.matbio.2009.03.003
    • Bozzi M, Morlacchi S, Bigotti MG, Sciandra F, Brancaccio A, (2009) Functional diversity of dystroglycan. Matrix Biol 28: 179-187. doi:10.1016/j.matbio.2009.03.003. PubMed: 19303439.
    • (2009) Matrix Biol , vol.28 , pp. 179-187
    • Bozzi, M.1    Morlacchi, S.2    Bigotti, M.G.3    Sciandra, F.4    Brancaccio, A.5
  • 10
    • 33645113450 scopus 로고    scopus 로고
    • Review: Lutheran/B-CAM: a laminin receptor on red blood cells and in various tissues
    • doi:10.1080/03008200500344074
    • Kikkawa Y, Miner JH, (2005) Review: Lutheran/B-CAM: a laminin receptor on red blood cells and in various tissues. Connect Tissue Res 46: 193-199. doi:10.1080/03008200500344074. PubMed: 16546822.
    • (2005) Connect Tissue Res , vol.46 , pp. 193-199
    • Kikkawa, Y.1    Miner, J.H.2
  • 11
    • 46249105332 scopus 로고    scopus 로고
    • The 67 kDa laminin receptor: structure, function and role in disease
    • doi:10.1042/BSR20070004
    • Nelson J, McFerran NV, Pivato G, Chambers E, Doherty C, et al. (2008) The 67 kDa laminin receptor: structure, function and role in disease. Biosci Rep 28: 33-48. doi:10.1042/BSR20070004. PubMed: 18269348.
    • (2008) Biosci Rep , vol.28 , pp. 33-48
    • Nelson, J.1    McFerran, N.V.2    Pivato, G.3    Chambers, E.4    Doherty, C.5
  • 12
    • 78650501836 scopus 로고    scopus 로고
    • Patented biological approaches for the therapeutic modulation of the 37 kDa/67 kDa laminin receptor
    • doi:10.1517/13543776.2011.539203
    • Omar A, Jovanovic K, Da Costa Dias B, Gonsalves D, Moodley K, et al. (2011) Patented biological approaches for the therapeutic modulation of the 37 kDa/67 kDa laminin receptor. Expert Opin Ther Pat 21: 35-53. doi:10.1517/13543776.2011.539203. PubMed: 21110766.
    • (2011) Expert Opin Ther Pat , vol.21 , pp. 35-53
    • Omar, A.1    Jovanovic, K.2    Da Costa Dias, B.3    Gonsalves, D.4    Moodley, K.5
  • 13
    • 0020618286 scopus 로고
    • Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells
    • doi:10.1083/jcb.96.5.1475
    • Malinoff HL, Wicha MS, (1983) Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells. J Cell Biol 96: 1475-1479. doi:10.1083/jcb.96.5.1475. PubMed: 6302102.
    • (1983) J Cell Biol , vol.96 , pp. 1475-1479
    • Malinoff, H.L.1    Wicha, M.S.2
  • 14
    • 0020561107 scopus 로고
    • Isolation of a tumor cell laminin receptor
    • doi:10.1016/0006-291X(83)91370-0
    • Rao NC, Barsky SH, Terranova VP, Liotta LA, (1983) Isolation of a tumor cell laminin receptor. Biochem Biophys Res Commun 111: 804-808. doi:10.1016/0006-291X(83)91370-0. PubMed: 6301485.
    • (1983) Biochem Biophys Res Commun , vol.111 , pp. 804-808
    • Rao, N.C.1    Barsky, S.H.2    Terranova, V.P.3    Liotta, L.A.4
  • 15
    • 0031880124 scopus 로고    scopus 로고
    • The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution
    • doi:10.1093/oxfordjournals.molbev.a026000
    • Ardini E, Pesole G, Tagliabue E, Magnifico A, Castronovo V, et al. (1998) The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution. Mol Biol Evol 15: 1017-1025. doi:10.1093/oxfordjournals.molbev.a026000. PubMed: 9718729.
    • (1998) Mol Biol Evol , vol.15 , pp. 1017-1025
    • Ardini, E.1    Pesole, G.2    Tagliabue, E.3    Magnifico, A.4    Castronovo, V.5
  • 16
    • 0036139519 scopus 로고    scopus 로고
    • Differential expression of genes coding for ribosomal proteins in different human tissues
    • doi:10.1093/bioinformatics/17.12.1152
    • Bortoluzzi S, d'Alessi F, Romualdi C, Danieli GA, (2001) Differential expression of genes coding for ribosomal proteins in different human tissues. Bioinformatics 17: 1152-1157. doi:10.1093/bioinformatics/17.12.1152. PubMed: 11751223.
    • (2001) Bioinformatics , vol.17 , pp. 1152-1157
    • Bortoluzzi, S.1    d'Alessi, F.2    Romualdi, C.3    Danieli, G.A.4
  • 17
    • 74149090508 scopus 로고    scopus 로고
    • Multiple functions of the 37/67-kd laminin receptor make it a suitable target for novel cancer gene therapy
    • doi:10.1038/mt.2009.199
    • Scheiman J, Tseng JC, Zheng Y, Meruelo D, (2010) Multiple functions of the 37/67-kd laminin receptor make it a suitable target for novel cancer gene therapy. Mol Ther 18: 63-74. doi:10.1038/mt.2009.199. PubMed: 19724263.
    • (2010) Mol Ther , vol.18 , pp. 63-74
    • Scheiman, J.1    Tseng, J.C.2    Zheng, Y.3    Meruelo, D.4
  • 18
    • 0035886968 scopus 로고    scopus 로고
    • Midkine binds to 37-kDa laminin binding protein precursor, leading to nuclear transport of the complex
    • doi:10.1006/excr.2001.5341
    • Salama RH, Muramatsu H, Zou K, Inui T, Kimura T, et al. (2001) Midkine binds to 37-kDa laminin binding protein precursor, leading to nuclear transport of the complex. Exp Cell Res 270: 13-20. doi:10.1006/excr.2001.5341. PubMed: 11597123.
    • (2001) Exp Cell Res , vol.270 , pp. 13-20
    • Salama, R.H.1    Muramatsu, H.2    Zou, K.3    Inui, T.4    Kimura, T.5
  • 19
    • 0030600537 scopus 로고    scopus 로고
    • Analysis of nuclear localization of laminin binding protein precursor p40 (LBP/p40)
    • doi:10.1006/bbrc.1996.1899
    • Sato M, Kinoshita K, Kaneda Y, Saeki Y, Iwamatsu A, et al. (1996) Analysis of nuclear localization of laminin binding protein precursor p40 (LBP/p40). Biochem Biophys Res Commun 229: 896-901. doi:10.1006/bbrc.1996.1899. PubMed: 8954992.
    • (1996) Biochem Biophys Res Commun , vol.229 , pp. 896-901
    • Sato, M.1    Kinoshita, K.2    Kaneda, Y.3    Saeki, Y.4    Iwamatsu, A.5
  • 20
    • 0032545335 scopus 로고    scopus 로고
    • LBP-p40 binds DNA tightly through associations with histones H2A, H2B, and H4
    • doi:10.1006/bbrc.1998.9699
    • Kinoshita K, Kaneda Y, Sato M, Saeki Y, Wataya-Kaneda M, et al. (1998) LBP-p40 binds DNA tightly through associations with histones H2A, H2B, and H4. Biochem Biophys Res Commun 253: 277-282. doi:10.1006/bbrc.1998.9699. PubMed: 9878528.
    • (1998) Biochem Biophys Res Commun , vol.253 , pp. 277-282
    • Kinoshita, K.1    Kaneda, Y.2    Sato, M.3    Saeki, Y.4    Wataya-Kaneda, M.5
  • 21
    • 77956630769 scopus 로고    scopus 로고
    • Interactions between PrP(c) and other ligands with the 37-kDa/67-kDa laminin receptor
    • doi:10.2741/3667
    • Mbazima V, Da Costa Dias B, Omar A, Jovanovic K, Weiss SF, (2010) Interactions between PrP(c) and other ligands with the 37-kDa/67-kDa laminin receptor. Front Biosci 15: 1150-1163. doi:10.2741/3667. PubMed: 20515747.
    • (2010) Front Biosci , vol.15 , pp. 1150-1163
    • Mbazima, V.1    Da Costa Dias, B.2    Omar, A.3    Jovanovic, K.4    Weiss, S.F.5
  • 22
    • 15444338707 scopus 로고    scopus 로고
    • Formation of the 67-kDa laminin receptor by acylation of the precursor
    • doi:10.1002/(SICI)1097-4644(19980601)69:3
    • Butò S, Tagliabue E, Ardini E, Magnifico A, Ghirelli C, et al. (1998) Formation of the 67-kDa laminin receptor by acylation of the precursor. J Cell Biochem 69: 244-251. doi:10.1002/(SICI)1097-4644(19980601)69:3. PubMed: 9581863.
    • (1998) J Cell Biochem , vol.69 , pp. 244-251
    • Butò, S.1    Tagliabue, E.2    Ardini, E.3    Magnifico, A.4    Ghirelli, C.5
  • 23
    • 0029144232 scopus 로고
    • Control pathways of the 67 kDa laminin binding protein: surface expression and activity of a new ligand binding domain
    • Landowski TH, Uthayakumar S, Starkey JR, (1995) Control pathways of the 67 kDa laminin binding protein: surface expression and activity of a new ligand binding domain. Clin Exp Metastasis 13: 357-372. PubMed: 7641420.
    • (1995) Clin Exp Metastasis , vol.13 , pp. 357-372
    • Landowski, T.H.1    Uthayakumar, S.2    Starkey, J.R.3
  • 24
    • 0013504830 scopus 로고    scopus 로고
    • The role of the non-integrin 67kDa laminin receptor in enterocyte proliferation, and adhesion, and motility
    • Dordrecht: Kluwer Publishing House Academic Publishers
    • Weiser MM, Sykes DE, Piscatelli JJ, Rao M, (1997) The role of the non-integrin 67kDa laminin receptor in enterocyte proliferation, and adhesion, and motility. In: Halter F, Winton D, Wright NA, eds. The Gut as a Model in Cell and Molecular Biology. Dordrecht: Kluwer Publishing House Academic Publishers. pp. pp. 149-164.
    • (1997) The Gut as a Model in Cell and Molecular Biology , pp. 149-164
    • Halter, F.1    Winton, D.2    Wright, N.A.3
  • 25
    • 0025841906 scopus 로고
    • Functional domains of the 67-kDa laminin receptor precursor
    • Castronovo V, Taraboletti G, Sobel ME, (1991) Functional domains of the 67-kDa laminin receptor precursor. J Biol Chem 266: 20440-20446. PubMed: 1834645.
    • (1991) J Biol Chem , vol.266 , pp. 20440-20446
    • Castronovo, V.1    Taraboletti, G.2    Sobel, M.E.3
  • 26
    • 17944363361 scopus 로고    scopus 로고
    • The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein
    • doi:10.1093/emboj/20.21.5863
    • Gauczynski S, Peyrin JM, Haïk S, Leucht C, Hundt C, et al. (2001) The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein. EMBO J 20: 5863-5875. doi:10.1093/emboj/20.21.5863. PubMed: 11689427.
    • (2001) EMBO J , vol.20 , pp. 5863-5875
    • Gauczynski, S.1    Peyrin, J.M.2    Haïk, S.3    Leucht, C.4    Hundt, C.5
  • 27
    • 42449160941 scopus 로고    scopus 로고
    • Invasion of tumorigenic HT1080 cells is impeded by blocking or downregulating the 37-kDa/67-kDa laminin receptor
    • doi:10.1016/j.jmb.2008.02.004
    • Zuber C, Knackmuss S, Zemora G, Reusch U, Vlasova E, et al. (2008) Invasion of tumorigenic HT1080 cells is impeded by blocking or downregulating the 37-kDa/67-kDa laminin receptor. J Mol Biol 378: 530-539. doi:10.1016/j.jmb.2008.02.004. PubMed: 18387633.
    • (2008) J Mol Biol , vol.378 , pp. 530-539
    • Zuber, C.1    Knackmuss, S.2    Zemora, G.3    Reusch, U.4    Vlasova, E.5
  • 29
    • 0000596059 scopus 로고
    • Isolation of a laminin-binding protein from muscle cell membranes
    • Lesot H, Kühl U, Mark K, (1983) Isolation of a laminin-binding protein from muscle cell membranes. EMBO J 2: 861-865. PubMed: 16453457.
    • (1983) EMBO J , vol.2 , pp. 861-865
    • Lesot, H.1    Kühl, U.2    Mark, K.3
  • 30
    • 0344247741 scopus 로고    scopus 로고
    • New insights into the metastasis-associated 67 kD laminin receptor
    • doi:10.1002/(SICI)1097-4644(19971101)67:2
    • Ménard S, Castronovo V, Tagliabue E, Sobel ME, (1997) New insights into the metastasis-associated 67 kD laminin receptor. J Cell Biochem 67: 155-165. doi:10.1002/(SICI)1097-4644(19971101)67:2. PubMed: 9328821.
    • (1997) J Cell Biochem , vol.67 , pp. 155-165
    • Ménard, S.1    Castronovo, V.2    Tagliabue, E.3    Sobel, M.E.4
  • 31
    • 0027516662 scopus 로고
    • Prognostic significance of the 67-kilodalton laminin receptor expression in human breast carcinomas
    • doi:10.1093/jnci/85.5.398
    • Martignone S, Ménard S, Bufalino R, Cascinelli N, Pellegrini R, et al. (1993) Prognostic significance of the 67-kilodalton laminin receptor expression in human breast carcinomas. J Natl Cancer Inst 85: 398-402. doi:10.1093/jnci/85.5.398. PubMed: 8433393.
    • (1993) J Natl Cancer Inst , vol.85 , pp. 398-402
    • Martignone, S.1    Ménard, S.2    Bufalino, R.3    Cascinelli, N.4    Pellegrini, R.5
  • 32
    • 0027672251 scopus 로고
    • Differential expression of the 67 kDa laminin receptor in cancer
    • Sobel ME, (1993) Differential expression of the 67 kDa laminin receptor in cancer. Semin Cancer Biol 4: 311-317. PubMed: 8257781.
    • (1993) Semin Cancer Biol , vol.4 , pp. 311-317
    • Sobel, M.E.1
  • 33
    • 0028017481 scopus 로고
    • Laminin receptor expression in rat intestine and liver during development and differentiation
    • doi:10.1016/0016-5085(94)90125-2
    • Rao M, Manishen WJ, Maheshwari Y, Sykes DE, Siyanova EY, et al. (1994) Laminin receptor expression in rat intestine and liver during development and differentiation. Gastroenterology 107: 764-772. doi:10.1016/0016-5085(94)90125-2. PubMed: 8076763.
    • (1994) Gastroenterology , vol.107 , pp. 764-772
    • Rao, M.1    Manishen, W.J.2    Maheshwari, Y.3    Sykes, D.E.4    Siyanova, E.Y.5
  • 34
    • 0031946192 scopus 로고    scopus 로고
    • The 67-kd laminin receptor is preferentially expressed by proliferating retinal vessels in a murine model of ischemic retinopathy
    • Stitt AW, McKenna D, Simpson DA, Gardiner TA, Harriott P, et al. (1998) The 67-kd laminin receptor is preferentially expressed by proliferating retinal vessels in a murine model of ischemic retinopathy. Am J Pathol 152: 1359-1365. PubMed: 9588904.
    • (1998) Am J Pathol , vol.152 , pp. 1359-1365
    • Stitt, A.W.1    McKenna, D.2    Simpson, D.A.3    Gardiner, T.A.4    Harriott, P.5
  • 35
    • 78650414544 scopus 로고    scopus 로고
    • Extraribosomal functions associated with the C terminus of the 37/67 kDa laminin receptor are required for maintaining cell viability
    • doi:10.1038/cddis.2010.19
    • Scheiman J, Jamieson KV, Ziello J, Tseng JC, Meruelo D, (2010) Extraribosomal functions associated with the C terminus of the 37/67 kDa laminin receptor are required for maintaining cell viability. Cell Death Dis 1: e42. doi:10.1038/cddis.2010.19. PubMed: 21243100.
    • (2010) Cell Death Dis , vol.1
    • Scheiman, J.1    Jamieson, K.V.2    Ziello, J.3    Tseng, J.C.4    Meruelo, D.5
  • 36
    • 56349171792 scopus 로고    scopus 로고
    • siRNA-mediated silencing of the 37/67-kDa high affinity laminin receptor in Hep3B cells induces apoptosis
    • doi:10.2478/s11658-008-0017-6
    • Susantad T, Smith DR, (2008) siRNA-mediated silencing of the 37/67-kDa high affinity laminin receptor in Hep3B cells induces apoptosis. Cell Mol Biol Lett 13: 452-464. doi:10.2478/s11658-008-0017-6. PubMed: 18425431.
    • (2008) Cell Mol Biol Lett , vol.13 , pp. 452-464
    • Susantad, T.1    Smith, D.R.2
  • 37
    • 1842525199 scopus 로고    scopus 로고
    • A receptor for green tea polyphenol EGCG
    • doi:10.1038/nsmb743
    • Tachibana H, Koga K, Fujimura Y, Yamada K, (2004) A receptor for green tea polyphenol EGCG. Nat Struct Mol Biol 11: 380-381. doi:10.1038/nsmb743. PubMed: 15024383.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 380-381
    • Tachibana, H.1    Koga, K.2    Fujimura, Y.3    Yamada, K.4
  • 38
    • 43049159573 scopus 로고    scopus 로고
    • Involvement of 67-kDa laminin receptor-mediated myosin phosphatase activation in antiproliferative effect of epigallocatechin-3-O-gallate at a physiological concentration on Caco-2 colon cancer cells
    • doi:10.1016/j.bbrc.2008.04.041
    • Umeda D, Yano S, Yamada K, Tachibana H, (2008) Involvement of 67-kDa laminin receptor-mediated myosin phosphatase activation in antiproliferative effect of epigallocatechin-3-O-gallate at a physiological concentration on Caco-2 colon cancer cells. Biochem Biophys Res Commun 371: 172-176. doi:10.1016/j.bbrc.2008.04.041. PubMed: 18423375.
    • (2008) Biochem Biophys Res Commun , vol.371 , pp. 172-176
    • Umeda, D.1    Yano, S.2    Yamada, K.3    Tachibana, H.4
  • 39
    • 79952315602 scopus 로고    scopus 로고
    • Green tea polyphenol epigallocatechin-3-gallate inhibits TLR2 signaling induced by peptidoglycan through the polyphenol sensing molecule 67-kDa laminin receptor
    • doi:10.1016/j.febslet.2011.02.010
    • Byun EH, Omura T, Yamada K, Tachibana H, (2011) Green tea polyphenol epigallocatechin-3-gallate inhibits TLR2 signaling induced by peptidoglycan through the polyphenol sensing molecule 67-kDa laminin receptor. FEBS Lett 585: 814-820. doi:10.1016/j.febslet.2011.02.010. PubMed: 21320497.
    • (2011) FEBS Lett , vol.585 , pp. 814-820
    • Byun, E.H.1    Omura, T.2    Yamada, K.3    Tachibana, H.4
  • 40
    • 0002398919 scopus 로고    scopus 로고
    • Growth and development of the gastrointestinal tract
    • Babyatsky MW, Podolsky DK, (1999) Growth and development of the gastrointestinal tract. In: Yamada T, eds., editor. Textbook of gastroenterology. 3rd ed. ed. Philadelphia: J. B Lippincott Publishing House. pp. 547-584.
    • (1999) Textbook of gastroenterology , pp. 547-584
    • Yamada, T.1
  • 42
    • 84873654484 scopus 로고    scopus 로고
    • Intestinal mucosal atrophy and adaptation
    • doi:10.3748/wjg.v18.i44.6357
    • Shaw D, Gohil K, Basson MD, (2012) Intestinal mucosal atrophy and adaptation. World J Gastroenterol 18: 6357-6375. doi:10.3748/wjg.v18.i44.6357. PubMed: 23197881.
    • (2012) World J Gastroenterol , vol.18 , pp. 6357-6375
    • Shaw, D.1    Gohil, K.2    Basson, M.D.3
  • 43
    • 0030629297 scopus 로고    scopus 로고
    • Extracellular matrix components and integrins in relationship to human intestinal epithelial cell differentiation
    • Beaulieu JF, (1997) Extracellular matrix components and integrins in relationship to human intestinal epithelial cell differentiation. Prog Histochem Cytochem 31: 1-78. PubMed: 9088045.
    • (1997) Prog Histochem Cytochem , vol.31 , pp. 1-78
    • Beaulieu, J.F.1
  • 44
    • 0037351409 scopus 로고    scopus 로고
    • Invited research review: Cell-matrix interactions in the gut epithelium
    • doi:10.1067/msy.2003.24
    • Basson MD, (2003) Invited research review: Cell-matrix interactions in the gut epithelium. Surgery 133: 263-267. doi:10.1067/msy.2003.24. PubMed: 12660637.
    • (2003) Surgery , vol.133 , pp. 263-267
    • Basson, M.D.1
  • 45
    • 85012563489 scopus 로고    scopus 로고
    • Interactions between laminin and epithelial cells in intestinal health and disease
    • Accessed
    • Teller IC, Beaulieu JF, (2001) Interactions between laminin and epithelial cells in intestinal health and disease. Expert Rev Mol Med 3: 1-18. Accessed 2013 July 30. doi:10.1017/S1462399401002575. PubMed: 14585148.
    • (2001) Expert Rev Mol Med , vol.3 , pp. 1-18
    • Teller, I.C.1    Beaulieu, J.F.2
  • 46
    • 73349115588 scopus 로고    scopus 로고
    • Integrin-linked kinase regulates migration and proliferation of human intestinal cells under a fibronectin-dependent mechanism
    • doi:10.1002/jcp.21963
    • Gagné D, Groulx JF, Benoit YD, Basora N, Herring E, et al. (2010) Integrin-linked kinase regulates migration and proliferation of human intestinal cells under a fibronectin-dependent mechanism. J Cell Physiol 222: 387-400. doi:10.1002/jcp.21963. PubMed: 19885839.
    • (2010) J Cell Physiol , vol.222 , pp. 387-400
    • Gagné, D.1    Groulx, J.F.2    Benoit, Y.D.3    Basora, N.4    Herring, E.5
  • 47
    • 79955549388 scopus 로고    scopus 로고
    • Collagen VI is a basement membrane component that regulates epithelial cell-fibronectin interactions
    • doi:10.1016/j.matbio.2011.03.002
    • Groulx JF, Gagné D, Benoit YD, Martel D, Basora N, et al. (2011) Collagen VI is a basement membrane component that regulates epithelial cell-fibronectin interactions. Matrix Biol 30: 195-206. doi:10.1016/j.matbio.2011.03.002. PubMed: 21406227.
    • (2011) Matrix Biol , vol.30 , pp. 195-206
    • Groulx, J.F.1    Gagné, D.2    Benoit, Y.D.3    Martel, D.4    Basora, N.5
  • 48
    • 34447499028 scopus 로고    scopus 로고
    • Laminins in the developing and adult human small intestine: relation with the functional absorptive unit
    • doi:10.1002/dvdy.21186
    • Teller IC, Auclair J, Herring E, Gauthier R, Ménard D, et al. (2007) Laminins in the developing and adult human small intestine: relation with the functional absorptive unit. Dev Dyn 236: 1980-1990. doi:10.1002/dvdy.21186. PubMed: 17503455.
    • (2007) Dev Dyn , vol.236 , pp. 1980-1990
    • Teller, I.C.1    Auclair, J.2    Herring, E.3    Gauthier, R.4    Ménard, D.5
  • 49
    • 0029074141 scopus 로고
    • Extracellular heterotrimeric laminin promotes differentiation in human enterocytes
    • Vachon PH, Beaulieu JF, (1995) Extracellular heterotrimeric laminin promotes differentiation in human enterocytes. Am J Physiol 268: G857-G867. PubMed: 7539221.
    • (1995) Am J Physiol , vol.268
    • Vachon, P.H.1    Beaulieu, J.F.2
  • 50
    • 74549214303 scopus 로고    scopus 로고
    • Intestinal epithelial wound healing assay in an epithelial-mesenchymal co-culture system
    • doi:10.1111/j.1524-475X.2009.00554.x
    • Seltana A, Basora N, Beaulieu JF, (2010) Intestinal epithelial wound healing assay in an epithelial-mesenchymal co-culture system. Wound Repair Regen 18: 114-122. doi:10.1111/j.1524-475X.2009.00554.x. PubMed: 20082684.
    • (2010) Wound Repair Regen , vol.18 , pp. 114-122
    • Seltana, A.1    Basora, N.2    Beaulieu, J.F.3
  • 51
    • 0026629491 scopus 로고
    • Human enterocyte (Caco-2) migration is modulated in vitro by extracellular matrix composition and epidermal growth factor
    • doi:10.1172/JCI115828
    • Basson MD, Modlin IM, Madri JA, (1992) Human enterocyte (Caco-2) migration is modulated in vitro by extracellular matrix composition and epidermal growth factor. J Clin Invest 90: 15-23. doi:10.1172/JCI115828. PubMed: 1634605.
    • (1992) J Clin Invest , vol.90 , pp. 15-23
    • Basson, M.D.1    Modlin, I.M.2    Madri, J.A.3
  • 52
    • 34547993706 scopus 로고    scopus 로고
    • Fak/Src signaling in human intestinal epithelial cell survival and anoikis: differentiation state-specific uncoupling with the PI3-K/Akt-1 and MEK/Erk pathways
    • doi:10.1002/jcp.21096
    • Bouchard V, Demers MJ, Thibodeau S, Laquerre V, Fujita N, et al. (2007) Fak/Src signaling in human intestinal epithelial cell survival and anoikis: differentiation state-specific uncoupling with the PI3-K/Akt-1 and MEK/Erk pathways. J Cell Physiol 212: 717-728. doi:10.1002/jcp.21096. PubMed: 17443665.
    • (2007) J Cell Physiol , vol.212 , pp. 717-728
    • Bouchard, V.1    Demers, M.J.2    Thibodeau, S.3    Laquerre, V.4    Fujita, N.5
  • 53
    • 0029793401 scopus 로고    scopus 로고
    • Overexpression of the 67-kD laminin receptor correlates with tumour progression in human colorectal carcinoma
    • doi:10.1002/(SICI)1096-9896(199608)179:4
    • Sanjuán X, Fernández PL, Miquel R, Muñoz J, Castronovo V, et al. (1996) Overexpression of the 67-kD laminin receptor correlates with tumour progression in human colorectal carcinoma. J Pathol 179: 376-380. doi:10.1002/(SICI)1096-9896(199608)179:4. PubMed: 8869283.
    • (1996) J Pathol , vol.179 , pp. 376-380
    • Sanjuán, X.1    Fernández, P.L.2    Miquel, R.3    Muñoz, J.4    Castronovo, V.5
  • 54
    • 0033921739 scopus 로고    scopus 로고
    • Diverse patterns of expression of the 67-kD laminin receptor in human small intestinal mucosa: potential binding sites for prion proteins?
    • doi:10.1002/1096-9896(2000)9999:9999
    • Shmakov AN, Bode J, Kilshaw PJ, Ghosh S, (2000) Diverse patterns of expression of the 67-kD laminin receptor in human small intestinal mucosa: potential binding sites for prion proteins? J Pathol 191: 318-322. doi:10.1002/1096-9896(2000)9999:9999. PubMed: 10878555.
    • (2000) J Pathol , vol.191 , pp. 318-322
    • Shmakov, A.N.1    Bode, J.2    Kilshaw, P.J.3    Ghosh, S.4
  • 55
    • 0025088501 scopus 로고
    • Laminin-cell membrane binding proteins in small intestinal epithelial cells
    • doi:10.1159/000200364
    • Stallmach A, Riecken EO, (1990) Laminin-cell membrane binding proteins in small intestinal epithelial cells. Digestion 46 (Suppl 2):: 31-39. doi:10.1159/000200364. PubMed: 2148161.
    • (1990) Digestion , vol.46 , Issue.SUPPL. 2 , pp. 31-39
    • Stallmach, A.1    Riecken, E.O.2
  • 56
    • 0032499898 scopus 로고    scopus 로고
    • Epithelial vs mesenchymal contribution to the extracellular matrix in the human intestine
    • doi:10.1006/bbrc.1998.8919
    • Perreault N, Herring-Gillam FE, Desloges N, Bélanger I, Pageot LP, et al. (1998) Epithelial vs mesenchymal contribution to the extracellular matrix in the human intestine. Biochem Biophys Res Commun 248: 121-126. doi:10.1006/bbrc.1998.8919. PubMed: 9675097.
    • (1998) Biochem Biophys Res Commun , vol.248 , pp. 121-126
    • Perreault, N.1    Herring-Gillam, F.E.2    Desloges, N.3    Bélanger, I.4    Pageot, L.P.5
  • 57
    • 0026742145 scopus 로고
    • Differential expression of the VLA family of integrins along the crypt-villus axis in the human small intestine
    • Beaulieu JF, (1992) Differential expression of the VLA family of integrins along the crypt-villus axis in the human small intestine. J Cell Sci 102(3):: 427-436. PubMed: 1506425.
    • (1992) J Cell Sci , vol.102 , pp. 427-436
    • Beaulieu, J.F.1
  • 58
    • 0034658190 scopus 로고    scopus 로고
    • Human cell models to study small intestinal functions: recapitulation of the crypt-villus axis
    • doi:10.1002/(SICI)1097-0029(20000515)49:4
    • Pageot LP, Perreault N, Basora N, Francoeur C, Magny P, et al. (2000) Human cell models to study small intestinal functions: recapitulation of the crypt-villus axis. Microsc Res Tech 49: 394-406. doi:10.1002/(SICI)1097-0029(20000515)49:4. PubMed: 10820523.
    • (2000) Microsc Res Tech , vol.49 , pp. 394-406
    • Pageot, L.P.1    Perreault, N.2    Basora, N.3    Francoeur, C.4    Magny, P.5
  • 59
    • 0030010377 scopus 로고    scopus 로고
    • Use of the dissociating enzyme thermolysin to generate viable human normal intestinal epithelial cell cultures
    • doi:10.1006/excr.1996.0145
    • Perreault N, Beaulieu JF, (1996) Use of the dissociating enzyme thermolysin to generate viable human normal intestinal epithelial cell cultures. Exp Cell Res 224: 354-364. doi:10.1006/excr.1996.0145. PubMed: 8612712.
    • (1996) Exp Cell Res , vol.224 , pp. 354-364
    • Perreault, N.1    Beaulieu, J.F.2
  • 60
    • 82355190802 scopus 로고    scopus 로고
    • Isolation, characterization, and culture of normal human intestinal crypt and villus cells
    • doi:10.1007/978-1-61779-367-7_11
    • Beaulieu JF, Ménard D, (2012) Isolation, characterization, and culture of normal human intestinal crypt and villus cells. Methods Mol Biol 806: 157-173. doi:10.1007/978-1-61779-367-7_11. PubMed: 22057451.
    • (2012) Methods Mol Biol , vol.806 , pp. 157-173
    • Beaulieu, J.F.1    Ménard, D.2
  • 61
    • 0030870173 scopus 로고    scopus 로고
    • Cell dynamics and differentiation of conditionally immortalized human intestinal epithelial cells
    • doi:10.1053/gast.1997.v113.pm
    • Quaroni A, Beaulieu JF, (1997) Cell dynamics and differentiation of conditionally immortalized human intestinal epithelial cells. Gastroenterology 113: 1198-1213. doi:10.1053/gast.1997.v113.pm9322515. PubMed: 9322515.
    • (1997) Gastroenterology , vol.113 , pp. 1198-1213
    • Quaroni, A.1    Beaulieu, J.F.2
  • 62
    • 84877921898 scopus 로고    scopus 로고
    • RGD-Dependent Epithelial Cell-Matrix Interactions in the Human Intestinal Crypt
    • Benoit YD, Groulx JF, Gagné D, Beaulieu JF, (2012) RGD-Dependent Epithelial Cell-Matrix Interactions in the Human Intestinal Crypt. Signal Transduct, 2012(2012): 248759. PubMed: 22988499.
    • (2012) Signal Transduct , vol.2012
    • Benoit, Y.D.1    Groulx, J.F.2    Gagné, D.3    Beaulieu, J.F.4
  • 63
    • 0033569721 scopus 로고    scopus 로고
    • Expression of functionally distinct variants of the beta(4)A integrin subunit in relation to the differentiation state in human intestinal cells
    • doi:10.1074/jbc.274.42.29819
    • Basora N, Herring-Gillam FE, Boudreau F, Perreault N, Pageot LP, et al. (1999) Expression of functionally distinct variants of the beta(4)A integrin subunit in relation to the differentiation state in human intestinal cells. J Biol Chem 274: 29819-29825. doi:10.1074/jbc.274.42.29819. PubMed: 10514460.
    • (1999) J Biol Chem , vol.274 , pp. 29819-29825
    • Basora, N.1    Herring-Gillam, F.E.2    Boudreau, F.3    Perreault, N.4    Pageot, L.P.5
  • 64
    • 0033971765 scopus 로고    scopus 로고
    • Human crypt intestinal epithelial cells are capable of lipid production, apolipoprotein synthesis, and lipoprotein assembly
    • Levy E, Beaulieu JF, Delvin E, Seidman E, Yotov W, et al. (2000) Human crypt intestinal epithelial cells are capable of lipid production, apolipoprotein synthesis, and lipoprotein assembly. J Lipid Res 41: 12-22. PubMed: 10627497.
    • (2000) J Lipid Res , vol.41 , pp. 12-22
    • Levy, E.1    Beaulieu, J.F.2    Delvin, E.3    Seidman, E.4    Yotov, W.5
  • 65
    • 33744546642 scopus 로고    scopus 로고
    • Implication of TNF-related apoptosis-inducing ligand in inflammatory intestinal epithelial lesions
    • doi:10.1053/j.gastro.2006.03.022
    • Begue B, Wajant H, Bambou JC, Dubuquoy L, Siegmund D, et al. (2006) Implication of TNF-related apoptosis-inducing ligand in inflammatory intestinal epithelial lesions. Gastroenterology 130: 1962-1974. doi:10.1053/j.gastro.2006.03.022. PubMed: 16762619.
    • (2006) Gastroenterology , vol.130 , pp. 1962-1974
    • Begue, B.1    Wajant, H.2    Bambou, J.C.3    Dubuquoy, L.4    Siegmund, D.5
  • 66
    • 4143053542 scopus 로고    scopus 로고
    • Proinflammatory cytokines TNF-alpha and IFN-gamma alter laminin expression under an apoptosis-independent mechanism in human intestinal epithelial cells
    • doi:10.1152/ajpgi.00535.2003
    • Francoeur C, Escaffit F, Vachon PH, Beaulieu JF, (2004) Proinflammatory cytokines TNF-alpha and IFN-gamma alter laminin expression under an apoptosis-independent mechanism in human intestinal epithelial cells. Am J Physiol Gastrointest Liver Physiol 287: G592-G598. doi:10.1152/ajpgi.00535.2003. PubMed: 15087281.
    • (2004) Am J Physiol Gastrointest Liver Physiol , vol.287
    • Francoeur, C.1    Escaffit, F.2    Vachon, P.H.3    Beaulieu, J.F.4
  • 67
    • 84862117297 scopus 로고    scopus 로고
    • Polycomb repressive complex 2 impedes intestinal cell terminal differentiation
    • doi:10.1242/jcs.102061
    • Benoit YD, Lepage MB, Khalfaoui T, Tremblay E, Basora N, et al. (2012) Polycomb repressive complex 2 impedes intestinal cell terminal differentiation. J Cell Sci 125: 3454-3463. doi:10.1242/jcs.102061. PubMed: 22467857.
    • (2012) J Cell Sci , vol.125 , pp. 3454-3463
    • Benoit, Y.D.1    Lepage, M.B.2    Khalfaoui, T.3    Tremblay, E.4    Basora, N.5
  • 68
    • 77950260505 scopus 로고    scopus 로고
    • Cooperation between HNF-1alpha, Cdx2, and GATA-4 in initiating an enterocytic differentiation program in a normal human intestinal epithelial progenitor cell line
    • doi:10.1152/ajpgi.00265.2009
    • Benoit YD, Paré F, Francoeur C, Jean D, Tremblay E, et al. (2010) Cooperation between HNF-1alpha, Cdx2, and GATA-4 in initiating an enterocytic differentiation program in a normal human intestinal epithelial progenitor cell line. Am J Physiol Gastrointest Liver Physiol 298: G504-G517. doi:10.1152/ajpgi.00265.2009. PubMed: 20133952.
    • (2010) Am J Physiol Gastrointest Liver Physiol , vol.298
    • Benoit, Y.D.1    Paré, F.2    Francoeur, C.3    Jean, D.4    Tremblay, E.5
  • 69
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • doi:10.1093/nar/29.9.e45
    • Pfaffl MW, (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29: e45. doi:10.1093/nar/29.9.e45. PubMed: 11328886.
    • (2001) Nucleic Acids Res , vol.29
    • Pfaffl, M.W.1
  • 70
    • 33645837045 scopus 로고    scopus 로고
    • Normalizing genes for quantitative RT-PCR in differentiating human intestinal epithelial cells and adenocarcinomas of the colon
    • Dydensborg AB, Herring E, Auclair J, Tremblay E, Beaulieu JF, (2006) Normalizing genes for quantitative RT-PCR in differentiating human intestinal epithelial cells and adenocarcinomas of the colon. Am J Physiol Gastrointest Liver Physiol 290: G1067-G1074. PubMed: 16399877.
    • (2006) Am J Physiol Gastrointest Liver Physiol , vol.290
    • Dydensborg, A.B.1    Herring, E.2    Auclair, J.3    Tremblay, E.4    Beaulieu, J.F.5
  • 71
    • 70350088536 scopus 로고    scopus 로고
    • Integrin alpha8beta1 regulates adhesion, migration and proliferation of human intestinal crypt cells via a predominant RhoA/ROCK-dependent mechanism
    • doi:10.1042/BC20090060
    • Benoit YD, Lussier C, Ducharme PA, Sivret S, Schnapp LM, et al. (2009) Integrin alpha8beta1 regulates adhesion, migration and proliferation of human intestinal crypt cells via a predominant RhoA/ROCK-dependent mechanism. Biol Cell 101: 695-708. doi:10.1042/BC20090060. PubMed: 19527220.
    • (2009) Biol Cell , vol.101 , pp. 695-708
    • Benoit, Y.D.1    Lussier, C.2    Ducharme, P.A.3    Sivret, S.4    Schnapp, L.M.5
  • 72
    • 36649036320 scopus 로고    scopus 로고
    • Bioactive microarrays immobilized on low-fouling surfaces to study specific endothelial cell adhesion
    • doi:10.1021/bm7007907
    • Monchaux E, Vermette P, (2007) Bioactive microarrays immobilized on low-fouling surfaces to study specific endothelial cell adhesion. Biomacromolecules 8: 3668-3673. doi:10.1021/bm7007907. PubMed: 17939716.
    • (2007) Biomacromolecules , vol.8 , pp. 3668-3673
    • Monchaux, E.1    Vermette, P.2
  • 73
    • 84855462974 scopus 로고    scopus 로고
    • Culturing INS-1 cells on CDPGYIGSR-, RGD- and fibronectin surfaces improves insulin secretion and cell proliferation
    • doi:10.1016/j.actbio.2011.10.036
    • Kuehn C, Dubiel EA, Sabra G, Vermette P, (2012) Culturing INS-1 cells on CDPGYIGSR-, RGD- and fibronectin surfaces improves insulin secretion and cell proliferation. Acta Biomater 8: 619-626. doi:10.1016/j.actbio.2011.10.036. PubMed: 22085924.
    • (2012) Acta Biomater , vol.8 , pp. 619-626
    • Kuehn, C.1    Dubiel, E.A.2    Sabra, G.3    Vermette, P.4
  • 74
    • 33750542545 scopus 로고    scopus 로고
    • Gene expression profiles of normal proliferating and differentiating human intestinal epithelial cells: a comparison with the Caco-2 cell model
    • doi:10.1002/jcb.21015
    • Tremblay E, Auclair J, Delvin E, Levy E, Ménard D, et al. (2006) Gene expression profiles of normal proliferating and differentiating human intestinal epithelial cells: a comparison with the Caco-2 cell model. J Cell Biochem 99: 1175-1186. doi:10.1002/jcb.21015. PubMed: 16795037.
    • (2006) J Cell Biochem , vol.99 , pp. 1175-1186
    • Tremblay, E.1    Auclair, J.2    Delvin, E.3    Levy, E.4    Ménard, D.5
  • 75
    • 0028213826 scopus 로고
    • Reciprocal expression of laminin A-chain isoforms along the crypt-villus axis in the human small intestine
    • Beaulieu JF, Vachon PH, (1994) Reciprocal expression of laminin A-chain isoforms along the crypt-villus axis in the human small intestine. Gastroenterology 106: 829-839. PubMed: 8143989.
    • (1994) Gastroenterology , vol.106 , pp. 829-839
    • Beaulieu, J.F.1    Vachon, P.H.2
  • 76
    • 0033876170 scopus 로고    scopus 로고
    • Altered expression of laminins in Crohn's disease small intestinal mucosa
    • doi:10.1016/S0002-9440(10)64704-9
    • Bouatrouss Y, Herring-Gillam FE, Gosselin J, Poisson J, Beaulieu JF, (2000) Altered expression of laminins in Crohn's disease small intestinal mucosa. Am J Pathol 156: 45-50. doi:10.1016/S0002-9440(10)64704-9. PubMed: 10623652.
    • (2000) Am J Pathol , vol.156 , pp. 45-50
    • Bouatrouss, Y.1    Herring-Gillam, F.E.2    Gosselin, J.3    Poisson, J.4    Beaulieu, J.F.5
  • 77
    • 0026412560 scopus 로고
    • Increased expression of the laminin receptor in human colon cancer
    • doi:10.1093/jnci/83.1.29
    • Cioce V, Castronovo V, Shmookler BM, Garbisa S, Grigioni WF, et al. (1991) Increased expression of the laminin receptor in human colon cancer. J Natl Cancer Inst 83: 29-36. doi:10.1093/jnci/83.1.29. PubMed: 1824600.
    • (1991) J Natl Cancer Inst , vol.83 , pp. 29-36
    • Cioce, V.1    Castronovo, V.2    Shmookler, B.M.3    Garbisa, S.4    Grigioni, W.F.5
  • 78
    • 0021992851 scopus 로고
    • Influence of spatial configuration of carcinoma cell populations on the expression of a tumor-associated glycoprotein
    • Horan Hand P, Colcher D, Salomon D, Ridge J, Noguchi P, et al. (1985) Influence of spatial configuration of carcinoma cell populations on the expression of a tumor-associated glycoprotein. Cancer Res 45: 833-840. PubMed: 3881173.
    • (1985) Cancer Res , vol.45 , pp. 833-840
    • Horan Hand, P.1    Colcher, D.2    Salomon, D.3    Ridge, J.4    Noguchi, P.5
  • 79
    • 0026131489 scopus 로고
    • Augmentation of type IV collagenase, laminin receptor, and Ki67 proliferation antigen associated with human colon, gastric, and breast carcinoma progression
    • D'Errico A, Garbisa S, Liotta LA, Castronovo V, Stetler-Stevenson WG, et al. (1991) Augmentation of type IV collagenase, laminin receptor, and Ki67 proliferation antigen associated with human colon, gastric, and breast carcinoma progression. Mod Pathol 4: 239-246. PubMed: 1646457.
    • (1991) Mod Pathol , vol.4 , pp. 239-246
    • D'Errico, A.1    Garbisa, S.2    Liotta, L.A.3    Castronovo, V.4    Stetler-Stevenson, W.G.5
  • 80
    • 0034125483 scopus 로고    scopus 로고
    • The expression of membrane-associated 67-kDa laminin receptor (67LR) is modulated in vitro by cell-contact inhibition
    • doi:10.1006/mcbr.2000.0191
    • Donaldson EA, McKenna DJ, McMullen CB, Scott WN, Stitt AW, et al. (2000) The expression of membrane-associated 67-kDa laminin receptor (67LR) is modulated in vitro by cell-contact inhibition. Mol Cell Biol Res Commun 3: 53-59. doi:10.1006/mcbr.2000.0191. PubMed: 10683318.
    • (2000) Mol Cell Biol Res Commun , vol.3 , pp. 53-59
    • Donaldson, E.A.1    McKenna, D.J.2    McMullen, C.B.3    Scott, W.N.4    Stitt, A.W.5
  • 81
    • 0023518505 scopus 로고
    • A pentapeptide from the laminin B1 chain mediates cell adhesion and binds the 67,000 laminin receptor
    • doi:10.1021/bi00396a004
    • Graf J, Ogle RC, Robey FA, Sasaki M, Martin GR, et al. (1987) A pentapeptide from the laminin B1 chain mediates cell adhesion and binds the 67,000 laminin receptor. Biochemistry 26: 6896-6900. doi:10.1021/bi00396a004. PubMed: 2962631.
    • (1987) Biochemistry , vol.26 , pp. 6896-6900
    • Graf, J.1    Ogle, R.C.2    Robey, F.A.3    Sasaki, M.4    Martin, G.R.5
  • 82
    • 0034607550 scopus 로고    scopus 로고
    • Phage display mapping for peptide 11 sensitive sequences binding to laminin-1
    • doi:10.1006/jmbi.2000.3680
    • Kazmin DA, Hoyt TR, Taubner L, Teintze M, Starkey JR, (2000) Phage display mapping for peptide 11 sensitive sequences binding to laminin-1. J Mol Biol 298: 431-445. doi:10.1006/jmbi.2000.3680. PubMed: 10772861.
    • (2000) J Mol Biol , vol.298 , pp. 431-445
    • Kazmin, D.A.1    Hoyt, T.R.2    Taubner, L.3    Teintze, M.4    Starkey, J.R.5
  • 83
    • 0031030316 scopus 로고    scopus 로고
    • Co-regulation and physical association of the 67-kDa monomeric laminin receptor and the alpha6beta4 integrin
    • doi:10.1074/jbc.272.4.2342
    • Ardini E, Tagliabue E, Magnifico A, Butò S, Castronovo V, et al. (1997) Co-regulation and physical association of the 67-kDa monomeric laminin receptor and the alpha6beta4 integrin. J Biol Chem 272: 2342-2345. doi:10.1074/jbc.272.4.2342. PubMed: 8999943.
    • (1997) J Biol Chem , vol.272 , pp. 2342-2345
    • Ardini, E.1    Tagliabue, E.2    Magnifico, A.3    Butò, S.4    Castronovo, V.5


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