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Volumn 76, Issue 4, 1998, Pages 251-264

Phenotypical changes of a human pancreatic adenocarcinoma cell line after selection on laminin-1/nidogen (LM/Ng) substratum

Author keywords

Cell polarity; Human pancreatic tumour cell lines; Laminin 1; Nidogen; Vacuolar apical compartment

Indexed keywords

5' NUCLEOTIDASE; ENTACTIN; LAMININ; PLASMINOGEN ACTIVATOR; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; REPETITIVE DNA;

EID: 0031687477     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0171-9335(98)80003-4     Document Type: Article
Times cited : (5)

References (62)
  • 1
    • 0024370276 scopus 로고
    • Role of microtubules in polarized delivery of apical membrane proteins to the brush border of intestinal epithelium
    • Achler, C., D. Filmer, C. Merte, D. Drenckhahn: Role of microtubules in polarized delivery of apical membrane proteins to the brush border of intestinal epithelium. J. Cell Biol. 109, 179-189 (1989).
    • (1989) J. Cell Biol. , vol.109 , pp. 179-189
    • Achler, C.1    Filmer, D.2    Merte, C.3    Drenckhahn, D.4
  • 2
    • 0027397539 scopus 로고
    • Tumour necrosis factor alpha (TNF alpha) and transforming growth factor-beta 1 (TGF beta 1) stimulate fibronectin synthesis and transdifferentiation of fat-storing cells in the rat liver into myofibroblasts
    • Bachem, M. G., K. M. Sell, R. Melchior, J. Kropf, T. Eller, A. M. Gressner: Tumour necrosis factor alpha (TNF alpha) and transforming growth factor-beta 1 (TGF beta 1) stimulate fibronectin synthesis and transdifferentiation of fat-storing cells in the rat liver into myofibroblasts. Virchows Arch. B Cell Pathol. Incl. Mol. Pathol. 63, 123-130 (1993).
    • (1993) Virchows Arch. B Cell Pathol. Incl. Mol. Pathol. , vol.63 , pp. 123-130
    • Bachem, M.G.1    Sell, K.M.2    Melchior, R.3    Kropf, J.4    Eller, T.5    Gressner, A.M.6
  • 3
    • 0029899741 scopus 로고    scopus 로고
    • Regulation of human (Caco-2) intestinal epithelial cell differentiation by extracellular matrix proteins
    • Basson, M. D., G. Turowski, N. Emenacker: Regulation of human (Caco-2) intestinal epithelial cell differentiation by extracellular matrix proteins. Exp. Cell Res. 225, 301-305 (1996).
    • (1996) Exp. Cell Res. , vol.225 , pp. 301-305
    • Basson, M.D.1    Turowski, G.2    Emenacker, N.3
  • 4
    • 0024383791 scopus 로고
    • Dissecting tumour cell invasion. Epithelial cells acquire invasive properties after the loss of uvomorulin-mediated cell-cell adhesion
    • Behrens, J., M. M. Mareel, P. M. van Roy, W. Birchmeier: Dissecting tumour cell invasion. Epithelial cells acquire invasive properties after the loss of uvomorulin-mediated cell-cell adhesion. J. Cell Biol. 108, 2435-2448 (1989).
    • (1989) J. Cell Biol. , vol.108 , pp. 2435-2448
    • Behrens, J.1    Mareel, M.M.2    Van Roy, P.M.3    Birchmeier, W.4
  • 5
    • 0023197175 scopus 로고
    • Urokinase-type plasminogen activators: Proenzyme, receptor, and inhibitors
    • Blasi, F., J.-D. Vassalli, K. Dano: Urokinase-type plasminogen activators: Proenzyme, receptor, and inhibitors. J. Cell Biol. 104, 801-804 (1987).
    • (1987) J. Cell Biol. , vol.104 , pp. 801-804
    • Blasi, F.1    Vassalli, J.-D.2    Dano, K.3
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein dye binding
    • Bradford, M. M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein dye binding. Anal. Biochem. 72, 495-502 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 495-502
    • Bradford, M.M.1
  • 7
    • 0344975376 scopus 로고
    • Villin: The major microfilament-associated protein of the intestinal microvillus
    • Bretscher, A., K. Weber: Villin: The major microfilament-associated protein of the intestinal microvillus. Proc. Natl. Acad. Sci. USA 76, 2321-2325 (1979).
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2321-2325
    • Bretscher, A.1    Weber, K.2
  • 8
    • 0023463846 scopus 로고
    • Cell surface receptors for the extracellular matrix molecules
    • Buck, C. A., A. F. Horwitz: Cell surface receptors for the extracellular matrix molecules. Annu. Rev. Cell Biol. 3, 179-205 (1987).
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 179-205
    • Buck, C.A.1    Horwitz, A.F.2
  • 9
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeletal-extracellular matrix linkage
    • Campbell, K. P.: Three muscular dystrophies: Loss of cytoskeletal-extracellular matrix linkage. Cell 80, 675-679 (1995).
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 10
    • 0030842795 scopus 로고    scopus 로고
    • Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration
    • Chapman, H. A.: Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration. Curr. Opin. Cell Biol. 9, 714-724 (1997).
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 714-724
    • Chapman, H.A.1
  • 11
    • 0018178824 scopus 로고
    • Familial enteropathy: A syndrome of protracted diarrhea from birth, failure to thrive, and hypoplastic villus atrophy
    • Davidson, G. P., E. Cutz, J. R. Hamilton, J. D. Gall: Familial enteropathy: a syndrome of protracted diarrhea from birth, failure to thrive, and hypoplastic villus atrophy. Gastroenterology 75, 783-790 (1978).
    • (1978) Gastroenterology , vol.75 , pp. 783-790
    • Davidson, G.P.1    Cutz, E.2    Hamilton, J.R.3    Gall, J.D.4
  • 12
    • 0030272735 scopus 로고    scopus 로고
    • Integrin-cytoplasmic interactions and bidirectional transmembrane signalling
    • Dedhar, S., G. E. Hannigan: Integrin-cytoplasmic interactions and bidirectional transmembrane signalling. Curr. Opin. Cell Biol. 8, 657-669 (1996).
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 657-669
    • Dedhar, S.1    Hannigan, G.E.2
  • 13
    • 0022466757 scopus 로고
    • The extracellular matrix proteins laminin and fibronectin modify the AMPase activity of 5′-nucleotidase from chicken gizzard smooth muscle
    • Dieckhoff, J., J. Mollenhauer, B. Niggemeyer, K. von der Mark, H. G. Mannherz: The extracellular matrix proteins laminin and fibronectin modify the AMPase activity of 5′-nucleotidase from chicken gizzard smooth muscle. FEBS Lett. 195, 82-86 (1986).
    • (1986) FEBS Lett. , vol.195 , pp. 82-86
    • Dieckhoff, J.1    Mollenhauer, J.2    Niggemeyer, B.3    Von Der Mark, K.4    Mannherz, H.G.5
  • 14
    • 0020619223 scopus 로고
    • Distribution of actin and the actin-associated proteins myosin, tropomyosin, alpha-actinin, vinculin, and villin in rat and bovine exocrine glands
    • Drenckhahn, D., H. G. Mannherz: Distribution of actin and the actin-associated proteins myosin, tropomyosin, alpha-actinin, vinculin, and villin in rat and bovine exocrine glands. Eur. J. Cell Biol. 30, 167-176 (1983).
    • (1983) Eur. J. Cell Biol. , vol.30 , pp. 167-176
    • Drenckhahn, D.1    Mannherz, H.G.2
  • 17
    • 0026073422 scopus 로고
    • Immunohistochemical demonstration of villin in the normal and in chronic pancreatitis
    • Elsässer, H.-P., G. Klöppel, H. G. Mannherz, K. Flocke, H. F. Kern: Immunohistochemical demonstration of villin in the normal and in chronic pancreatitis. Histochemistry 95, 383-390 (1991).
    • (1991) Histochemistry , vol.95 , pp. 383-390
    • Elsässer, H.-P.1    Klöppel, G.2    Mannherz, H.G.3    Flocke, K.4    Kern, H.F.5
  • 18
    • 0026569866 scopus 로고
    • Establishment and characterisation of two cell lines with different grade of differentiation derived from one primary human pancreatic adenocarcinoma
    • Elsässer, H.-P., U. Lehr, B. Agricola, H. F. Kern: Establishment and characterisation of two cell lines with different grade of differentiation derived from one primary human pancreatic adenocarcinoma. Virchows Arch. B Cell Pathol. Incl. Mol. Pathol. 61, 295-305 (1992).
    • (1992) Virchows Arch. b Cell Pathol. Incl. Mol. Pathol. , vol.61 , pp. 295-305
    • Elsässer, H.-P.1    Lehr, U.2    Agricola, B.3    Kern, H.F.4
  • 19
    • 0027486540 scopus 로고
    • Structural analysis of a new highly metastatic cell line PaTu 8902 from a primary human pancreatic adenocarcinoma
    • Elsässer, H.-P., U. Lehr, B. Agricola, H. F. Kern: Structural analysis of a new highly metastatic cell line PaTu 8902 from a primary human pancreatic adenocarcinoma. Virchows Arch. B Cell Pathol. Incl. Mol. Pathol. 64, 201-207 (1993).
    • (1993) Virchows Arch. b Cell Pathol. Incl. Mol. Pathol. , vol.64 , pp. 201-207
    • Elsässer, H.-P.1    Lehr, U.2    Agricola, B.3    Kern, H.F.4
  • 20
    • 0027504892 scopus 로고
    • Characterization of a transglutaminase expressed in human pancreatic adenocarcinoma cells
    • Elsässer, H.-P., R. MacDonald, M. Dienst, H. F. Kern: Characterization of a transglutaminase expressed in human pancreatic adenocarcinoma cells. Eur. J. Cell Biol. 61, 321-328 (1993).
    • (1993) Eur. J. Cell Biol. , vol.61 , pp. 321-328
    • Elsässer, H.-P.1    MacDonald, R.2    Dienst, M.3    Kern, H.F.4
  • 22
    • 0025174871 scopus 로고
    • Genetic control of cancer metastasis
    • Fidler, I. J., R. Radinsky: Genetic control of cancer metastasis. J. Natl. Cancer Inst. 82, 166-168 (1990).
    • (1990) J. Natl. Cancer Inst. , vol.82 , pp. 166-168
    • Fidler, I.J.1    Radinsky, R.2
  • 23
    • 0025964127 scopus 로고
    • Isolation and characterization of 5′-nucleotidase of a human pancreatic tumour cell line
    • Flocke, K., H. G. Mannherz: Isolation and characterization of 5′-nucleotidase of a human pancreatic tumour cell line. Biochim. Biophys. Acta 1076, 273-281 (1991).
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 273-281
    • Flocke, K.1    Mannherz, H.G.2
  • 24
    • 0026711079 scopus 로고
    • Monoclonal antibodies against 5′-nucleotidase from a human pancreatic tumour cell line: Their characterization and inhibitory capacity on tumour cell adhesion to fibronectin substratum
    • Flocke, K., G. Lesch, H.-P. Elsässer, K. Bosslet, H. G. Mannherz: Monoclonal antibodies against 5′-nucleotidase from a human pancreatic tumour cell line: Their characterization and inhibitory capacity on tumour cell adhesion to fibronectin substratum. Eur. J. Cell Biol. 58, 62-70 (1992).
    • (1992) Eur. J. Cell Biol. , vol.58 , pp. 62-70
    • Flocke, K.1    Lesch, G.2    Elsässer, H.-P.3    Bosslet, K.4    Mannherz, H.G.5
  • 25
    • 0025992052 scopus 로고
    • Induction of vacuolar apical compartments in the Caco-2 intestinal epithelial cell line
    • Gilbert, T., E. Rodriguez-Boulan: Induction of vacuolar apical compartments in the Caco-2 intestinal epithelial cell line. J. Cell Sci. 100, 451-458 (1991).
    • (1991) J. Cell Sci. , vol.100 , pp. 451-458
    • Gilbert, T.1    Rodriguez-Boulan, E.2
  • 26
    • 0018193854 scopus 로고
    • A study of proteases and protease-inhibitor complexes in biological fluids
    • Granelli-Piperno, A., E. Reich: A study of proteases and protease-inhibitor complexes in biological fluids. J. Exp. Med. 148, 223-234 (1978).
    • (1978) J. Exp. Med. , vol.148 , pp. 223-234
    • Granelli-Piperno, A.1    Reich, E.2
  • 27
    • 0026608889 scopus 로고
    • Rapid acinar to ductual transdifferentiation in cultured human exocrine pancreas
    • Hall, P. A., N. R. Lemoine: Rapid acinar to ductual transdifferentiation in cultured human exocrine pancreas. J. Pathol. 166, 97-103 (1992).
    • (1992) J. Pathol. , vol.166 , pp. 97-103
    • Hall, P.A.1    Lemoine, N.R.2
  • 28
    • 0027507910 scopus 로고
    • Extracellular matrix alters epithelial differentiation
    • Hay, E. D.: Extracellular matrix alters epithelial differentiation. Curr. Opin. Cell Biol. 5, 1029-1035 (1993).
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 1029-1035
    • Hay, E.D.1
  • 29
    • 0021893217 scopus 로고
    • Isolation of 5′-nucleotidase from chicken gizzard, its properties, and subcellular localization in chicken tissues using monospecific antibodies
    • Heidemann, M., J. Dieckhoff, C. Hlavsa, H. G. Mannherz: Isolation of 5′-nucleotidase from chicken gizzard, its properties, and subcellular localization in chicken tissues using monospecific antibodies. Eur. J. Cell Biol. 37, 122-129 (1985).
    • (1985) Eur. J. Cell Biol. , vol.37 , pp. 122-129
    • Heidemann, M.1    Dieckhoff, J.2    Hlavsa, C.3    Mannherz, H.G.4
  • 30
    • 0024787046 scopus 로고
    • Synthesis and secretion of plasminogen activators and plasminogen activator inhibitors in cell lines derived from different groups of human lung tumours
    • Heidtmann, H. H., M. Hofmann, E. Jacob, K. Havemann, R. Schwartz-Albiez: Synthesis and secretion of plasminogen activators and plasminogen activator inhibitors in cell lines derived from different groups of human lung tumours. Cancer Res. 49, 6960-6965 (1989).
    • (1989) Cancer Res. , vol.49 , pp. 6960-6965
    • Heidtmann, H.H.1    Hofmann, M.2    Jacob, E.3    Havemann, K.4    Schwartz-Albiez, R.5
  • 31
    • 0027861133 scopus 로고
    • Secretion of a latent, acid activatable cathepsin L precursor by human non-small lung cancer cell lines
    • Heidtmann, H.-H., U. Salge, K. Havemann, H. Kirschke, B. Wiederanders: Secretion of a latent, acid activatable cathepsin L precursor by human non-small lung cancer cell lines. Oncol. Res. 5, 41-451 (1993).
    • (1993) Oncol. Res. , vol.5 , pp. 41-451
    • Heidtmann, H.-H.1    Salge, U.2    Havemann, K.3    Kirschke, H.4    Wiederanders, B.5
  • 33
    • 85030345644 scopus 로고
    • Signal transduction from the extracellular matrix
    • Juliano, R, L., S. Haskill; Signal transduction from the extracellular matrix. J. Cell Biol. 4, 943-961 (1993).
    • (1993) J. Cell Biol. , vol.4 , pp. 943-961
    • Juliano1    Ravi, L.2    Haskill, S.3
  • 34
    • 0023626543 scopus 로고
    • Biochemical analysis of two cell surface glycoprotein complexes, very common antigen 1 and very common antigen 2
    • Kantor, R. R. S., M. J. Mattes, K. O. Lloyd, L. J. Old, A. P. Albino: Biochemical analysis of two cell surface glycoprotein complexes, very common antigen 1 and very common antigen 2. J. Biol. Chem. 262, 15158-15165 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 15158-15165
    • Kantor, R.R.S.1    Mattes, M.J.2    Lloyd, K.O.3    Old, L.J.4    Albino, A.P.5
  • 35
    • 0025145392 scopus 로고
    • Integrins of normal human epidermis: Differential expression, synthesis and molecular structure
    • Klein, C. E., T. Steinmayer, J. M. Mattes, R. Kaufmann, L.Weber: Integrins of normal human epidermis: differential expression, synthesis and molecular structure. Br. J. Dermatol. 123, 171-178 (1990).
    • (1990) Br. J. Dermatol. , vol.123 , pp. 171-178
    • Klein, C.E.1    Steinmayer, T.2    Mattes, J.M.3    Kaufmann, R.4    LWeber5
  • 36
    • 0021891243 scopus 로고
    • Histological and fine structural features of pancreatic ductal adenocarcinomas in relation to growth and prognosis. Studies in xenografted tumours and clinicohistopathologic correlation in a series of 75 cases
    • Klöppel, G., G. Lingenthal, M.von Bülow, H. F. Kern: Histological and fine structural features of pancreatic ductal adenocarcinomas in relation to growth and prognosis. Studies in xenografted tumours and clinicohistopathologic correlation in a series of 75 cases. Histopathology 9, 841-856 (1985).
    • (1985) Histopathology , vol.9 , pp. 841-856
    • Klöppel, G.1    Lingenthal, G.2    Bülow, M.V.3    Kern, H.F.4
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 0000596059 scopus 로고
    • Isolation of a laminin-binding protein from muscle cell membranes
    • Lesot, H., U. Kühl, K. von der Mark: Isolation of a laminin-binding protein from muscle cell membranes. EMBO J. 2, 861-865 (1983).
    • (1983) EMBO J. , vol.2 , pp. 861-865
    • Lesot, H.1    Kühl, U.2    Von Der Mark, K.3
  • 39
    • 0022656975 scopus 로고
    • Tumour invasion and metastases-role of the extracellular matrix
    • Liotta, L. A.: Tumour invasion and metastases-role of the extracellular matrix. Cancer Res. 46, 1-7 (1986).
    • (1986) Cancer Res. , vol.46 , pp. 1-7
    • Liotta, L.A.1
  • 40
    • 0000441994 scopus 로고
    • Polarized apical distribution of glycosyl-phosphatidylinositol-anchored proteins in a renal epithelial line
    • Lisanti, M., M. Sargiacomo, L. Graeve, A. Saltiel, E. Rodriguez-Boulan: Polarized apical distribution of glycosyl-phosphatidylinositol-anchored proteins in a renal epithelial line. Proc. Natl. Acad. Sci. USA 85, 9557-9561 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9557-9561
    • Lisanti, M.1    Sargiacomo, M.2    Graeve, L.3    Saltiel, A.4    Rodriguez-Boulan, E.5
  • 41
    • 0002748308 scopus 로고    scopus 로고
    • Structure of laminins and their chain assembly
    • P. Ekblom, R. Timpl (eds.) Harwood Academic Publishers. Amsterdam, The Netherlands
    • Maurer, P., J. Engel: Structure of laminins and their chain assembly. In: P. Ekblom, R. Timpl (eds.): The Laminins. pp. 27-49. Harwood Academic Publishers. Amsterdam, The Netherlands, 1996.
    • (1996) The Laminins , pp. 27-49
    • Maurer, P.1    Engel, J.2
  • 42
    • 0027286695 scopus 로고
    • A single EGF-like motif of laminin is responsible for high affinity nidogen binding
    • Mayer, U, R. Nischt, E. Pöschl, K. Mann, K. Fukuda, M. Gerl, Y. Yamada, R. Timpl: A single EGF-like motif of laminin is responsible for high affinity nidogen binding. EMBO J. 12, 1879-1885 (1993).
    • (1993) EMBO J. , vol.12 , pp. 1879-1885
    • Mayer, U.1    Nischt, R.2    Pöschl, E.3    Mann, K.4    Fukuda, K.5    Gerl, M.6    Yamada, Y.7    Timpl, R.8
  • 44
    • 0027164777 scopus 로고
    • Dual mechanism of laminin modulation of ecto-5′-nucleotidase activity
    • Mehul, B., M. Aubery, H. G. Mannherz, P. Codogno: Dual mechanism of laminin modulation of ecto-5′-nucleotidase activity. J. Cell. Biochem. 52, 2166-274 (1993).
    • (1993) J. Cell. Biochem. , vol.52 , pp. 2166-2274
    • Mehul, B.1    Aubery, M.2    Mannherz, H.G.3    Codogno, P.4
  • 45
    • 0023890834 scopus 로고
    • Biosynthesis of lysosomal cathepsins B and H in cultured rat hepatocytes
    • Nishimura, Y: Biosynthesis of lysosomal cathepsins B and H in cultured rat hepatocytes. Arch. Biochem. Biophys. 262, 159-170 (1988).
    • (1988) Arch. Biochem. Biophys. , vol.262 , pp. 159-170
    • Nishimura, Y.1
  • 46
    • 0023377705 scopus 로고
    • Laminin-nidogen complex: Extraction with chelating agents and structural characterization
    • Paulsson, M., M. Aumailley, R. Deutzmann, R. Timpl, K. Beek, J. Engel: Laminin-nidogen complex: Extraction with chelating agents and structural characterization. Eur. J. Biochem. 166, 11-19 (1987).
    • (1987) Eur. J. Biochem. , vol.166 , pp. 11-19
    • Paulsson, M.1    Aumailley, M.2    Deutzmann, R.3    Timpl, R.4    Beek, K.5    Engel, J.6
  • 47
    • 0022513621 scopus 로고
    • Ornithine decarboxylase, transglutaminase, diamine oxidase and total diamine and polyamines in maternal liver and kidney throughout rat pregnancy
    • Piacentini, M., C. Sartori, S. Beninati, A. M. Bargagli, M. P. Argento-Ceru: Ornithine decarboxylase, transglutaminase, diamine oxidase and total diamine and polyamines in maternal liver and kidney throughout rat pregnancy. Biochem. J. 234, 435-440 (1986).
    • (1986) Biochem. J. , vol.234 , pp. 435-440
    • Piacentini, M.1    Sartori, C.2    Beninati, S.3    Bargagli, A.M.4    Argento-Ceru, M.P.5
  • 49
    • 0023201461 scopus 로고
    • Retinal pigmented epithelial cells induced to transdifferentiate to neurons by laminin
    • Reh, T. A., T. Nagy, H. Gretton: Retinal pigmented epithelial cells induced to transdifferentiate to neurons by laminin. Nature 330, 68-71 (1987).
    • (1987) Nature , vol.330 , pp. 68-71
    • Reh, T.A.1    Nagy, T.2    Gretton, H.3
  • 51
    • 0024315423 scopus 로고
    • Morphogenesis of the polarized epithelial cell phenotype
    • Rodriguez-Boulan, E., W. J. Nelson: Morphogenesis of the polarized epithelial cell phenotype. Science 245, 718-725 (1989).
    • (1989) Science , vol.245 , pp. 718-725
    • Rodriguez-Boulan, E.1    Nelson, W.J.2
  • 52
    • 0025331728 scopus 로고
    • Differentiation capacity of human non-small-cell lung cancer cell lines after exposure to phorbol ester
    • Salge, U., P. Kilian, K. Neumann, H.-P. Elsässer, K. Havemann, H. H. Heidtmann: Differentiation capacity of human non-small-cell lung cancer cell lines after exposure to phorbol ester. Int. J. Cancer 45, 1143-1150 (1990).
    • (1990) Int. J. Cancer , vol.45 , pp. 1143-1150
    • Salge, U.1    Kilian, P.2    Neumann, K.3    Elsässer, H.-P.4    Havemann, K.5    Heidtmann, H.H.6
  • 53
    • 0029161155 scopus 로고
    • Differential expression of urokinase-type plasminogen activator (uPA), its receptor (uPA-R), and inhibitor type-2 (PAI-2) during differentiation of keratinocytes in an organotypic coculture system
    • Schaefer, B. M., H. J. Stark, N. E. Fusenig, R. F. Todd, M. D. Kramer: Differential expression of urokinase-type plasminogen activator (uPA), its receptor (uPA-R), and inhibitor type-2 (PAI-2) during differentiation of keratinocytes in an organotypic coculture system. Exp. Cell Res. 220, 415-423 (1995).
    • (1995) Exp. Cell Res. , vol.220 , pp. 415-423
    • Schaefer, B.M.1    Stark, H.J.2    Fusenig, N.E.3    Todd, R.F.4    Kramer, M.D.5
  • 54
    • 0027333411 scopus 로고
    • Tumour cell interactions with the extracellular matrix during invasion and metastasis
    • Stetler-Stevenson, W. G., S. Aznavoorian, L. A. Liotta: Tumour cell interactions with the extracellular matrix during invasion and metastasis. Annu. Rev. Cell Biol. 9, 541-573 (1993).
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 541-573
    • Stetler-Stevenson, W.G.1    Aznavoorian, S.2    Liotta, L.A.3
  • 55
    • 0024458171 scopus 로고
    • Evidence for the direct interaction of chicken gizzard 5′-nucleotidase with laminin and fibronectin
    • Stochaj, U., J. Dieckhoff, J. Mollenhauer, M. Cramer, H. G. Mannherz: Evidence for the direct interaction of chicken gizzard 5′-nucleotidase with laminin and fibronectin. Biochim. Biophys. Acta 992, 385-392 (1989).
    • (1989) Biochim. Biophys. Acta , vol.992 , pp. 385-392
    • Stochaj, U.1    Dieckhoff, J.2    Mollenhauer, J.3    Cramer, M.4    Mannherz, H.G.5
  • 56
    • 0024453115 scopus 로고
    • 5′-Nucleotidases of chicken gizzard and human adenocarcinoma cells are anchored to the plasma membrane via a phosphatidylinositolglycan
    • Stochaj, U., K. Flocke, W. Mathes, H. G. Mannherz: 5′-Nucleotidases of chicken gizzard and human adenocarcinoma cells are anchored to the plasma membrane via a phosphatidylinositolglycan. Biochem. J. 262, 33-40 (1989).
    • (1989) Biochem. J. , vol.262 , pp. 33-40
    • Stochaj, U.1    Flocke, K.2    Mathes, W.3    Mannherz, H.G.4
  • 57
    • 0027056735 scopus 로고
    • Chicken gizzard 5′-nucleotidase functions as a binding protein for the laminin/nidogen complex
    • Stochaj, U., H. G. Mannherz: Chicken gizzard 5′-nucleotidase functions as a binding protein for the laminin/nidogen complex. Eur. J. Cell Biol. 59, 364-372 (1992).
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 364-372
    • Stochaj, U.1    Mannherz, H.G.2
  • 58
    • 0025218067 scopus 로고
    • Chicken gizzard 5′-nucleotidase is a receptor for the extracellular matrix component fibronectin
    • Stochaj, U., H. Richter, H. G. Mannherz: Chicken gizzard 5′-nucleotidase is a receptor for the extracellular matrix component fibronectin. Eur. J. Cell Biol. 51, 335-338 (1990).
    • (1990) Eur. J. Cell Biol. , vol.51 , pp. 335-338
    • Stochaj, U.1    Richter, H.2    Mannherz, H.G.3
  • 59
    • 0023227996 scopus 로고
    • Purification of 5′-nucleotidase from human placenta after release from plasma membranes by phosphatidylinositol-specific phospholipase C
    • Thompson, L. F., J. M. Ruedi, M. G. Low: Purification of 5′-nucleotidase from human placenta after release from plasma membranes by phosphatidylinositol-specific phospholipase C. Biochem. Biophys. Res. Commun. 145, 118-125 (1987).
    • (1987) Biochem. Biophys. Res. Commun. , vol.145 , pp. 118-125
    • Thompson, L.F.1    Ruedi, J.M.2    Low, M.G.3
  • 60
    • 0024558106 scopus 로고
    • Structure and biological activity of basement membrane proteins
    • Timpl, R.: Structure and biological activity of basement membrane proteins. Eur. J. Biochem. 180, 487-502 (1989).
    • (1989) Eur. J. Biochem. , vol.180 , pp. 487-502
    • Timpl, R.1
  • 61
    • 0024582686 scopus 로고
    • Abundant class of human DNA polymorphisms which can be typed using the polymerase chain reaction
    • Weber, J. L., P. E. May: Abundant class of human DNA polymorphisms which can be typed using the polymerase chain reaction. Am. J. Hum. Genet. 44, 388-396 (1989).
    • (1989) Am. J. Hum. Genet. , vol.44 , pp. 388-396
    • Weber, J.L.1    May, P.E.2


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