메뉴 건너뛰기




Volumn 20, Issue 2, 2000, Pages 129-137

β1 Integrins play an essential role in adhesion and invasion of pancreatic carcinoma cells

Author keywords

1 integrin; Cell adhesion; Cell invasion; Pancreatic carcinoma

Indexed keywords

BETA1 INTEGRIN; COLLAGEN; FIBRONECTIN; INTEGRIN; LAMININ; MONOCLONAL ANTIBODY;

EID: 0033621847     PISSN: 08853177     EISSN: None     Source Type: Journal    
DOI: 10.1097/00006676-200003000-00004     Document Type: Article
Times cited : (60)

References (41)
  • 1
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes RO. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 1992;69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 2
    • 0029997916 scopus 로고    scopus 로고
    • Adhesion receptors in malignant transformation and dissemination of gastrointestinal tumors
    • Streit M, Schmidt R, Hilgenfeld RU, Thiel E, Kreuser ED. Adhesion receptors in malignant transformation and dissemination of gastrointestinal tumors. J Mol Med 1996;74:253-68.
    • (1996) J Mol Med , vol.74 , pp. 253-268
    • Streit, M.1    Schmidt, R.2    Hilgenfeld, R.U.3    Thiel, E.4    Kreuser, E.D.5
  • 3
    • 0030272735 scopus 로고    scopus 로고
    • Integrin cytoplasmic interactions and bidirectional transmembrane signalling
    • Dedhar S, Hannigan GE. Integrin cytoplasmic interactions and bidirectional transmembrane signalling. Curr Opin Cell Biol 1996; 8:657-69.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 657-669
    • Dedhar, S.1    Hannigan, G.E.2
  • 4
    • 0029895788 scopus 로고    scopus 로고
    • Association of TM4SF proteins with integrins: Relevance to cancer
    • Hemler ME, Mannion BA, Berditchevski F. Association of TM4SF proteins with integrins: relevance to cancer. Biochim Biophys Acta 1996;1287:67-71.
    • (1996) Biochim Biophys Acta , vol.1287 , pp. 67-71
    • Hemler, M.E.1    Mannion, B.A.2    Berditchevski, F.3
  • 5
    • 0028813315 scopus 로고
    • High expression level of α6 integrin in human breast carcinoma is correlated with reduced survival
    • Friedrichs K, Ruiz P, Franke F, Gille I, Terpe HJ, Imhof BA. High expression level of α6 integrin in human breast carcinoma is correlated with reduced survival. Cancer Res 1995;55:901-6.
    • (1995) Cancer Res , vol.55 , pp. 901-906
    • Friedrichs, K.1    Ruiz, P.2    Franke, F.3    Gille, I.4    Terpe, H.J.5    Imhof, B.A.6
  • 6
    • 0028978457 scopus 로고
    • Re-expression of the α2β1 integrin abrogates the malignant phenotype of breast carcinoma cells
    • Zutter MM, Santoro SA, Staatz WD, Tsung YL. Re-expression of the α2β1 integrin abrogates the malignant phenotype of breast carcinoma cells. Proc Natl Acad Sci USA 1995;92:7411-5.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7411-7415
    • Zutter, M.M.1    Santoro, S.A.2    Staatz, W.D.3    Tsung, Y.L.4
  • 7
    • 0026446816 scopus 로고
    • Expression and function of VLA-α2. -α3. -α5 and -α6 integrin receptors in pancreatic carcinoma
    • Weinel RJ, Rosendahl A, Neumann K, et al. Expression and function of VLA-α2. -α3. -α5 and -α6 integrin receptors in pancreatic carcinoma. Int J Cancer 1992;52:827-33.
    • (1992) Int J Cancer , vol.52 , pp. 827-833
    • Weinel, R.J.1    Rosendahl, A.2    Neumann, K.3
  • 9
    • 0029916875 scopus 로고    scopus 로고
    • Outside-in integrin signal transduction. AIIbb3 (GPIIbIIIa)-tyrosine phosphorylation induced by platelet aggregation
    • Law DA, Nannizzi AL, Phillips DR. Outside-in integrin signal transduction. aIIbb3 (GPIIbIIIa)-tyrosine phosphorylation induced by platelet aggregation. J Biol Chem 1996;271:10811-5.
    • (1996) J Biol Chem , vol.271 , pp. 10811-10815
    • Law, D.A.1    Nannizzi, A.L.2    Phillips, D.R.3
  • 10
    • 0031018338 scopus 로고    scopus 로고
    • Dual role of the actin cytoskeleton in regulating cell adhesion mediated by the integrin lymphocyte function-associated molecule-1
    • Lub M, van Kooyk Y, van Vliet S, Figdor CG. Dual role of the actin cytoskeleton in regulating cell adhesion mediated by the integrin lymphocyte function-associated molecule-1. Mol Biol Cell 1997;8:341-51.
    • (1997) Mol Biol Cell , vol.8 , pp. 341-351
    • Lub, M.1    Van Kooyk, Y.2    Van Vliet, S.3    Figdor, C.G.4
  • 11
    • 0027497502 scopus 로고
    • Multiple functional forms of the integrin VLA-2 can be derived from a single α2 cDNA clone: Interconversion of forms induced by an anti-β1 antibody
    • Chan BMC, Hemler ME. Multiple functional forms of the integrin VLA-2 can be derived from a single α2 cDNA clone: interconversion of forms induced by an anti-β1 antibody. J Cell Biol 1993; 120:537-43.
    • (1993) J Cell Biol , vol.120 , pp. 537-543
    • Chan, B.M.C.1    Hemler, M.E.2
  • 12
    • 0027398570 scopus 로고
    • Multiple activation states of VLA-4: Mechanistic differences between adhesion to CS1/fibronectin and to vascular cell adhesion molecule-1
    • Masumoto A, Hemler ME. Multiple activation states of VLA-4: mechanistic differences between adhesion to CS1/fibronectin and to vascular cell adhesion molecule-1. J Biol Chem 1993;268:228-34.
    • (1993) J Biol Chem , vol.268 , pp. 228-234
    • Masumoto, A.1    Hemler, M.E.2
  • 13
    • 0032590002 scopus 로고    scopus 로고
    • Role of β1 integrins in adhesion and invasion of hepatocellular carcinoma cells
    • Masumoto A, Arao S, Otsuki M. Role of β1 integrins in adhesion and invasion of hepatocellular carcinoma cells. Hepatology 1999; 29:68-74.
    • (1999) Hepatology , vol.29 , pp. 68-74
    • Masumoto, A.1    Arao, S.2    Otsuki, M.3
  • 14
    • 0027169160 scopus 로고
    • Interchangeable a chain cytoplasmic domains play a positive role in control of cell adhesion mediated by VLA-4, a β1 integrin
    • Kassner PD, Hemler ME. Interchangeable a chain cytoplasmic domains play a positive role in control of cell adhesion mediated by VLA-4, a β1 integrin. J Exp Med 1993;178:649-60.
    • (1993) J Exp Med , vol.178 , pp. 649-660
    • Kassner, P.D.1    Hemler, M.E.2
  • 15
    • 0027327104 scopus 로고
    • Role of the a subunit cytoplasmic domain in regulation of adhesive activity mediated by the integrin VLA-2
    • Kawaguchi S, Hemler ME. Role of the a subunit cytoplasmic domain in regulation of adhesive activity mediated by the integrin VLA-2. J Biol Chem 1993;268:16279-85.
    • (1993) J Biol Chem , vol.268 , pp. 16279-16285
    • Kawaguchi, S.1    Hemler, M.E.2
  • 16
    • 0027496638 scopus 로고
    • Mutation of putative divalent cation sites in the α4 subunit of the integrin VLA-4: Distinct effects on adhesion to CS1/fibronectin, VCAM-1. and invasin
    • Masumoto A, Hemler ME. Mutation of putative divalent cation sites in the α4 subunit of the integrin VLA-4: distinct effects on adhesion to CS1/fibronectin, VCAM-1. and invasin. J Cell Biol 1993;123:245-53.
    • (1993) J Cell Biol , vol.123 , pp. 245-253
    • Masumoto, A.1    Hemler, M.E.2
  • 17
    • 0025037032 scopus 로고
    • Establishment and characterization of human pancreatic cancer cell lines in tissue culture and in nude mice
    • Ikeda Y, Ezaki M, Hayashi I, Yasuda D, Nakayama K, Kono A. Establishment and characterization of human pancreatic cancer cell lines in tissue culture and in nude mice. Jpn J Cancer Res 1990; 81:987-93.
    • (1990) Jpn J Cancer Res , vol.81 , pp. 987-993
    • Ikeda, Y.1    Ezaki, M.2    Hayashi, I.3    Yasuda, D.4    Nakayama, K.5    Kono, A.6
  • 18
    • 0023187867 scopus 로고
    • A rapid in vitro assay for quantitating the invasive potential of tumor cells
    • Albini A, Iwamoto Y, Kleinman HK, et al. A rapid in vitro assay for quantitating the invasive potential of tumor cells. Cancer Res 1987;47:3239-45.
    • (1987) Cancer Res , vol.47 , pp. 3239-3245
    • Albini, A.1    Iwamoto, Y.2    Kleinman, H.K.3
  • 19
    • 0029965070 scopus 로고    scopus 로고
    • Cholecystokinin receptor antagonist, loxiglumide, inhibits invasiveness of human pancreatic cancer cell lines
    • Hirata M, Itoh M, Tsuchida A. Ooishi H, Hanada K, Kajiyama G. Cholecystokinin receptor antagonist, loxiglumide, inhibits invasiveness of human pancreatic cancer cell lines. FEBS Lett 1996; 383:241-4.
    • (1996) FEBS Lett , vol.383 , pp. 241-244
    • Hirata, M.1    Itoh, M.2    Tsuchida, A.3    Ooishi, H.4    Hanada, K.5    Kajiyama, G.6
  • 20
    • 0028879643 scopus 로고
    • The novel structural motif G1n795-G1n802 in the integrin β1C cytoplasmic domain regulates cell proliferation
    • Fornaro M, Zheng DQ, Languino LR. The novel structural motif G1n795-G1n802 in the integrin β1C cytoplasmic domain regulates cell proliferation. J Biol Chem 1995;270:24666-9.
    • (1995) J Biol Chem , vol.270 , pp. 24666-24669
    • Fornaro, M.1    Zheng, D.Q.2    Languino, L.R.3
  • 21
    • 0030026679 scopus 로고    scopus 로고
    • Regulation of cell adhesion and anchorage-dependent growth by a new β1-integrin-linked protein kinase
    • Hannigan GE, Leung-Hagesteijn C, Fitz-Gibbon L, et al. Regulation of cell adhesion and anchorage-dependent growth by a new β1-integrin-linked protein kinase. Nature 1996;379:91-6.
    • (1996) Nature , vol.379 , pp. 91-96
    • Hannigan, G.E.1    Leung-Hagesteijn, C.2    Fitz-Gibbon, L.3
  • 24
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark EA, Brugge JS. Integrins and signal transduction pathways: the road taken. Science 1995;268:233-9.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 25
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger DA, Horwitz AF. Cell migration: a physically integrated molecular process. Cell 1996;84:359-69.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 26
    • 0031022629 scopus 로고    scopus 로고
    • Functional relevance during lymphocyte migration and cellular localization of activated β1 integrins
    • Gomez M, Luque A, del Pozo MA, Hogg N, Sanchez-Madrid F, Cabanas C. Functional relevance during lymphocyte migration and cellular localization of activated β1 integrins. Eur J Immunol 1997; 27:8-16.
    • (1997) Eur J Immunol , vol.27 , pp. 8-16
    • Gomez, M.1    Luque, A.2    Del Pozo, M.A.3    Hogg, N.4    Sanchez-Madrid, F.5    Cabanas, C.6
  • 27
    • 0031034352 scopus 로고    scopus 로고
    • Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness
    • Palecek SP, Loftus JC, Ginsberg MH, Lauffenburger DA, Horwitz AF. Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness. Nature 1997;385:537-40.
    • (1997) Nature , vol.385 , pp. 537-540
    • Palecek, S.P.1    Loftus, J.C.2    Ginsberg, M.H.3    Lauffenburger, D.A.4    Horwitz, A.F.5
  • 28
    • 0026581198 scopus 로고
    • Interaction of leukocyte integrins with ligand is necessary but not sufficient for function
    • Dransfield I, Cabanas C, Barrett J, Hogg N. Interaction of leukocyte integrins with ligand is necessary but not sufficient for function. J Cell Biol 1992;116:1527-35.
    • (1992) J Cell Biol , vol.116 , pp. 1527-1535
    • Dransfield, I.1    Cabanas, C.2    Barrett, J.3    Hogg, N.4
  • 29
    • 0029150795 scopus 로고
    • Proteolytic remodeling of extracellular matrix
    • Birkedal-Hansen H. Proteolytic remodeling of extracellular matrix. Curr Opin Cell Biol 1995;7:728-35.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 728-735
    • Birkedal-Hansen, H.1
  • 30
    • 0030882679 scopus 로고    scopus 로고
    • Production of extracellular matrix-degrading proteinases by primary cultures of human epithelial ovarian carcinoma cells
    • Fishman DA, Bafetti LM, Banionis S, Kearns AS, Chilukuri K, Stack MS. Production of extracellular matrix-degrading proteinases by primary cultures of human epithelial ovarian carcinoma cells. Cancer 1997;80:1457-63.
    • (1997) Cancer , vol.80 , pp. 1457-1463
    • Fishman, D.A.1    Bafetti, L.M.2    Banionis, S.3    Kearns, A.S.4    Chilukuri, K.5    Stack, M.S.6
  • 31
    • 0030951910 scopus 로고    scopus 로고
    • Expression and tissue localization of membrane-types 1, 2, and 3 matrix metalloproteinases in human invasive breast carcinomas
    • Ueno H, Nakamura H, Inoue M, et al. Expression and tissue localization of membrane-types 1, 2, and 3 matrix metalloproteinases in human invasive breast carcinomas. Cancer Res 1997;57:2055-60.
    • (1997) Cancer Res , vol.57 , pp. 2055-2060
    • Ueno, H.1    Nakamura, H.2    Inoue, M.3
  • 32
    • 0028067549 scopus 로고
    • Activation of 72-kDa type IV collagenase/gelatinase by normal fibroblasts in collagen lattices is mediated by integrin receptors but is not related to lattice contraction
    • Seltzer JL, Lee AY, Akers KT, et al. Activation of 72-kDa type IV collagenase/gelatinase by normal fibroblasts in collagen lattices is mediated by integrin receptors but is not related to lattice contraction. Exp Cell Res 1994;213:365-74.
    • (1994) Exp Cell Res , vol.213 , pp. 365-374
    • Seltzer, J.L.1    Lee, A.Y.2    Akers, K.T.3
  • 33
    • 0028987190 scopus 로고
    • Cooperative signaling by α5β1 and α4β1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin
    • Huhtala P, Humphries MJ, McCarthy JB, Tremble PM, Werb Z, Damsky CH. Cooperative signaling by α5β1 and α4β1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin. J Cell Biol 1995;129:867-79.
    • (1995) J Cell Biol , vol.129 , pp. 867-879
    • Huhtala, P.1    Humphries, M.J.2    McCarthy, J.B.3    Tremble, P.M.4    Werb, Z.5    Damsky, C.H.6
  • 34
    • 0030578932 scopus 로고    scopus 로고
    • Integrin α2β1-dependent contraction of floating collagen gels and induction of collagenase are inhibited by tyrosine kinase inhibitors
    • Broberg A, Heino J. Integrin α2β1-dependent contraction of floating collagen gels and induction of collagenase are inhibited by tyrosine kinase inhibitors. Exp Cell Res 1996;228:29-35.
    • (1996) Exp Cell Res , vol.228 , pp. 29-35
    • Broberg, A.1    Heino, J.2
  • 35
    • 0030954151 scopus 로고    scopus 로고
    • Localization and activation of type IV collagenase/gelatinase at endothelial focal contacts
    • Partridge CA, Phillips PG, Niedbala MJ, Jeffrey JJ. Localization and activation of type IV collagenase/gelatinase at endothelial focal contacts. Am J Physiol 1997;272:L813-22.
    • (1997) Am J Physiol , vol.272
    • Partridge, C.A.1    Phillips, P.G.2    Niedbala, M.J.3    Jeffrey, J.J.4
  • 36
    • 0027373782 scopus 로고
    • Activation of protein kinase C precedes α5β1 integrin-mediated cell spreading on fibronectin
    • Vuori K, Ruoslahti E. Activation of protein kinase C precedes α5β1 integrin-mediated cell spreading on fibronectin. J Biol Chem 1993;268:21459-62.
    • (1993) J Biol Chem , vol.268 , pp. 21459-21462
    • Vuori, K.1    Ruoslahti, E.2
  • 37
    • 0025745212 scopus 로고
    • Insoluble fibronectin activates the Na+/H+ antiporter by clustering and immobilizing integrin α5β1, independent of cell shape
    • Schwartz MA, Lechene C, Ingber DE. Insoluble fibronectin activates the Na+/H+ antiporter by clustering and immobilizing integrin α5β1, independent of cell shape. Proc Natl Acad Sci USA 1991;88:7849-53.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7849-7853
    • Schwartz, M.A.1    Lechene, C.2    Ingber, D.E.3
  • 38
    • 0030976110 scopus 로고    scopus 로고
    • Clustering the adhesion molecules VLA-4 (CD49d/CD29) in Jurkat T cells or VCAM-1 (CD106) in endothelial (ECV 304) cells activates the phosphoinositide pathway and triggers Cα2+ mobilization
    • Ricard I, Payet MD, Dupuis G. Clustering the adhesion molecules VLA-4 (CD49d/CD29) in Jurkat T cells or VCAM-1 (CD106) in endothelial (ECV 304) cells activates the phosphoinositide pathway and triggers Cα2+ mobilization. Eur J Immunol 1997;27: 1530-8.
    • (1997) Eur J Immunol , vol.27 , pp. 1530-1538
    • Ricard, I.1    Payet, M.D.2    Dupuis, G.3
  • 39
    • 0027397549 scopus 로고
    • Spreading of human endothelial cells on fibronectin or vitronectin triggers elevetion of intracellular free calcium
    • Schwartz MA. Spreading of human endothelial cells on fibronectin or vitronectin triggers elevetion of intracellular free calcium. J Cell Biol 1993;120:1003-10.
    • (1993) J Cell Biol , vol.120 , pp. 1003-1010
    • Schwartz, M.A.1
  • 40
    • 0027452326 scopus 로고
    • Stimulation of tyrosine phosphorylation and accumulation of GTP-bound p21ras upon antibody-mediated α2β1 integrin activation in T-lymphoblastic cells
    • Kapron-Bras C, FitzGibbon L, Jeevaratnam P, Wilkins J, Dedhar S. Stimulation of tyrosine phosphorylation and accumulation of GTP-bound p21ras upon antibody-mediated α2β1 integrin activation in T-lymphoblastic cells. J Biol Chem 1993;268:20701-4.
    • (1993) J Biol Chem , vol.268 , pp. 20701-20704
    • Kapron-Bras, C.1    FitzGibbon, L.2    Jeevaratnam, P.3    Wilkins, J.4    Dedhar, S.5
  • 41
    • 0030874021 scopus 로고    scopus 로고
    • Integrin-mediated activation of MAP kinase is independent of FAK: Evidence for dual integrin signaling pathways in fibroblasts
    • Lin TH, Aplin AE, Shen Y, et al. Integrin-mediated activation of MAP kinase is independent of FAK: evidence for dual integrin signaling pathways in fibroblasts. J Cell Biol 1997;136:1385-95.
    • (1997) J Cell Biol , vol.136 , pp. 1385-1395
    • Lin, T.H.1    Aplin, A.E.2    Shen, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.