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Volumn 64, Issue 17, 2004, Pages 6065-6070

Adhesion of gastric carcinoma cells to peritoneum mediated by α3β1 integrin (VLA-3)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA2 INTEGRIN; ALPHA3 INTEGRIN; KALININ; LAMININ; LAMININ 10; LAMININ 11; MESSENGER RNA; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 3;

EID: 4344628872     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-04-0321     Document Type: Article
Times cited : (76)

References (42)
  • 2
    • 0032926793 scopus 로고    scopus 로고
    • Fibronectin and its integrin receptors in cancer
    • Ruoslahti E. Fibronectin and its integrin receptors in cancer. Adv Cancer Res 1999;76:1-20.
    • (1999) Adv Cancer Res , vol.76 , pp. 1-20
    • Ruoslahti, E.1
  • 3
  • 4
    • 0034715891 scopus 로고    scopus 로고
    • Multiple roles of integrins in cell motility
    • Holly SP, Larson MK, Parise LV. Multiple roles of integrins in cell motility. Exp Cell Res 2000;261:69-74.
    • (2000) Exp Cell Res , vol.261 , pp. 69-74
    • Holly, S.P.1    Larson, M.K.2    Parise, L.V.3
  • 5
    • 0037278885 scopus 로고    scopus 로고
    • Integrin adhesion receptors in tumor metastasis
    • Felding-Habermann B. Integrin adhesion receptors in tumor metastasis. Clin Exp Metastasis 2003;20:203-13.
    • (2003) Clin Exp Metastasis , vol.20 , pp. 203-213
    • Felding-Habermann, B.1
  • 6
    • 0030028717 scopus 로고    scopus 로고
    • Peritoneal metastatic model for human scirrhous gastric carcinoma in nude mice
    • Yashiro M, Chung YS, Nishimura S, Inoue T, Sowa M. Peritoneal metastatic model for human scirrhous gastric carcinoma in nude mice. Clin Exp Metastasis 1996;14: 43-54.
    • (1996) Clin Exp Metastasis , vol.14 , pp. 43-54
    • Yashiro, M.1    Chung, Y.S.2    Nishimura, S.3    Inoue, T.4    Sowa, M.5
  • 7
    • 0030945387 scopus 로고    scopus 로고
    • Adhesion molecules and TGF-β1 are involved in the peritoneal dissemination of NUGC-4 human gastric cancer cells
    • Nakashio T, Narita T, Akiyama S, et al. Adhesion molecules and TGF-β1 are involved in the peritoneal dissemination of NUGC-4 human gastric cancer cells. Int J Cancer 1997;70:612-8.
    • (1997) Int J Cancer , vol.70 , pp. 612-618
    • Nakashio, T.1    Narita, T.2    Akiyama, S.3
  • 8
    • 0031595984 scopus 로고    scopus 로고
    • Separate-functions of σ2β1 and α3β1 integrins in the metastatic process of human gastric carcinoma
    • Ura H, Denno R, Hirata K, Yamaguchi K, Yasoshima T. Separate-functions of σ2β1 and α3β1 integrins in the metastatic process of human gastric carcinoma. Surg Today 1998;28:1001-6.
    • (1998) Surg Today , vol.28 , pp. 1001-1006
    • Ura, H.1    Denno, R.2    Hirata, K.3    Yamaguchi, K.4    Yasoshima, T.5
  • 9
    • 0033629622 scopus 로고    scopus 로고
    • Increased expression of α2/β1 integrin in the peritoneal dissemination of human gastric carcinoma
    • Matsuoka T, Yashiro M, Nishimura S, et al. Increased expression of α2/β1 integrin in the peritoneal dissemination of human gastric carcinoma. Int J Mol Med 2000;5:21-5.
    • (2000) Int J Mol Med , vol.5 , pp. 21-25
    • Matsuoka, T.1    Yashiro, M.2    Nishimura, S.3
  • 10
    • 0028364318 scopus 로고
    • Intercellular adhesion induced by anti-α3 integrin (VLA-3) antibodies
    • Takeuchi K, Tsuji T, Hakomori S, Irimura T. Intercellular adhesion induced by anti-α3 integrin (VLA-3) antibodies. Exp Cell Res 1994;211:133-41.
    • (1994) Exp Cell Res , vol.211 , pp. 133-141
    • Takeuchi, K.1    Tsuji, T.2    Hakomori, S.3    Irimura, T.4
  • 11
    • 0036204641 scopus 로고    scopus 로고
    • Regulation of melanoma cell migration and invasion by laminin-5 and α3/β1 integrin (VLA-3)
    • Tsuji T, Kawada Y, Kai-Murozono M, et al. Regulation of melanoma cell migration and invasion by laminin-5 and α3/β1 integrin (VLA-3). Clin Exp Metastasis 2002; 19:127-34.
    • (2002) Clin Exp Metastasis , vol.19 , pp. 127-134
    • Tsuji, T.1    Kawada, Y.2    Kai-Murozono, M.3
  • 12
    • 0024382716 scopus 로고
    • The primary structure of the VLA-2/collagen receptor α2 subunit (platelet GPIa): Homology to other integrins and the presence of a possible collagen-binding domain
    • Takada Y, Hemler ME. The primary structure of the VLA-2/collagen receptor α2 subunit (platelet GPIa): homology to other integrins and the presence of a possible collagen-binding domain. J Cell Biol 1989;109:397-407.
    • (1989) J Cell Biol , vol.109 , pp. 397-407
    • Takada, Y.1    Hemler, M.E.2
  • 13
    • 0028963272 scopus 로고
    • x carbohydrate antigen: Liver colonization and adhesion to vascular endothelial cells
    • x carbohydrate antigen: liver colonization and adhesion to vascular endothelial cells. Exp Cell Res 1995;216:215-21.
    • (1995) Exp Cell Res , vol.216 , pp. 215-221
    • Izumi, Y.1    Taniuchi, Y.2    Tsuji, T.3
  • 14
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987;162:156-9.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 15
    • 0029143930 scopus 로고
    • Cloning and complete primary structure of the mouse laminin α3 chain. Distinct expression pattern of the laminin α3A and α3B chain isoforms
    • Galliano MF, Aberdam D, Aguzzi A, Ortonne JP, Menehguzzi G. Cloning and complete primary structure of the mouse laminin α3 chain. Distinct expression pattern of the laminin α3A and α3B chain isoforms. J Biol Chem 1995;270:21820-6.
    • (1995) J Biol Chem , vol.270 , pp. 21820-21826
    • Galliano, M.F.1    Aberdam, D.2    Aguzzi, A.3    Ortonne, J.P.4    Menehguzzi, G.5
  • 16
    • 0028860732 scopus 로고
    • Molecular cloning of a novel laminin chain, α5, and widespread expression in adult mouse tissues
    • Miner JH, Lewis RM, Sanes JR. Molecular cloning of a novel laminin chain, α5, and widespread expression in adult mouse tissues. J Biol Chem 1995:270:28523-6.
    • (1995) J Biol Chem , vol.270 , pp. 28523-28526
    • Miner, J.H.1    Lewis, R.M.2    Sanes, J.R.3
  • 17
    • 0025887362 scopus 로고
    • Epiligrin, a new cell adhesion ligand for integrin α3β1 in epithelial basement membranes
    • Carter WG, Ryan MC, Gahr PJ. Epiligrin, a new cell adhesion ligand for integrin α3β1 in epithelial basement membranes. Cell 1991;65:599-610.
    • (1991) Cell , vol.65 , pp. 599-610
    • Carter, W.G.1    Ryan, M.C.2    Gahr, P.J.3
  • 18
    • 0027420876 scopus 로고
    • Basement membrane proteins kalinin and nicein are structurally and immunologically identical
    • Marinkovitch MP, Verrando P, Keene DR, et al. Basement membrane proteins kalinin and nicein are structurally and immunologically identical. Lab Invest 1993;69:295-9.
    • (1993) Lab Invest , vol.69 , pp. 295-299
    • Marinkovitch, M.P.1    Verrando, P.2    Keene, D.R.3
  • 19
    • 0027938248 scopus 로고
    • Marked stimulation of cell adhesion and motility by ladsin, a laminin-like scatter factor
    • Kikkawa Y, Umeda M, Miyazaki K. Marked stimulation of cell adhesion and motility by ladsin, a laminin-like scatter factor. J Biochem (Tokyo) 1994;116:862-9.
    • (1994) J Biochem (Tokyo) , vol.116 , pp. 862-869
    • Kikkawa, Y.1    Umeda, M.2    Miyazaki, K.3
  • 20
    • 0032546780 scopus 로고    scopus 로고
    • Isolation and characterization of laminin-10/11 secreted by human lung carcinoma cells. Laminin-10/11 mediates cell adhesion through integrin α3β1
    • Kikkawa Y, Sanzen N, Sekiguchi K. Isolation and characterization of laminin-10/11 secreted by human lung carcinoma cells. Laminin-10/11 mediates cell adhesion through integrin α3β1. J Biol Chem 1998;273:15854-9.
    • (1998) J Biol Chem , vol.273 , pp. 15854-15859
    • Kikkawa, Y.1    Sanzen, N.2    Sekiguchi, K.3
  • 21
    • 0029847196 scopus 로고    scopus 로고
    • Role of α2β1- and α3β1-integrin in the peritoneal implantation of scirrhous gastric carcinoma
    • Nishimura S, Chung YS, Yashiro M, Inoue T, Sowa M. Role of α2β1- and α3β1-integrin in the peritoneal implantation of scirrhous gastric carcinoma. Br J Cancer 1996;74:1406-12.
    • (1996) Br J Cancer , vol.74 , pp. 1406-1412
    • Nishimura, S.1    Chung, Y.S.2    Yashiro, M.3    Inoue, T.4    Sowa, M.5
  • 22
    • 0035315763 scopus 로고    scopus 로고
    • Significance of integrin α2/β1 in peritoneal dissemination of a human gastric cancer xenograft model
    • Kawamura T, Endo Y, Yonemura Y, et al. Significance of integrin α2/β1 in peritoneal dissemination of a human gastric cancer xenograft model. Int J Oncol 2001;18: 809-15.
    • (2001) Int J Oncol , vol.18 , pp. 809-815
    • Kawamura, T.1    Endo, Y.2    Yonemura, Y.3
  • 23
    • 0033621823 scopus 로고    scopus 로고
    • Integrin α6β4 as a suppressor and a predictive marker for peritoneal dissemination in human gastric cancer
    • Ishii Y, Ochiai A, Yamada T, et al. Integrin α6β4 as a suppressor and a predictive marker for peritoneal dissemination in human gastric cancer. Gastroenterology 2000; 118:497-506.
    • (2000) Gastroenterology , vol.118 , pp. 497-506
    • Ishii, Y.1    Ochiai, A.2    Yamada, T.3
  • 24
    • 0025246152 scopus 로고
    • Characterization through cDNA cloning of galactoprotein b3 (Gap b3), a cell surface membrane glycoprotein showing enhanced expression on oncogenic transformation. Identification of Gap b3 as a member of the integrin superfamily
    • Tsuji T, Yamamoto F, Miura Y, et al. Characterization through cDNA cloning of galactoprotein b3 (Gap b3), a cell surface membrane glycoprotein showing enhanced expression on oncogenic transformation. Identification of Gap b3 as a member of the integrin superfamily. J Biol Chem 1990;265:7016-21.
    • (1990) J Biol Chem , vol.265 , pp. 7016-7021
    • Tsuji, T.1    Yamamoto, F.2    Miura, Y.3
  • 25
    • 0025756936 scopus 로고
    • Identification of human galactoprotein b3, an oncogenic transformation-induced membrane glycoprotein, as VLA-3 α subunit: The primary structure of human integrin α3
    • Tsuji T, Hakomori S, Osawa T. Identification of human galactoprotein b3, an oncogenic transformation-induced membrane glycoprotein, as VLA-3 α subunit: the primary structure of human integrin α3. J Biochem (Tokyo) 1991;109:659-65.
    • (1991) J Biochem (Tokyo) , vol.109 , pp. 659-665
    • Tsuji, T.1    Hakomori, S.2    Osawa, T.3
  • 26
    • 0028982785 scopus 로고
    • The α3β1 integrin is involved in melanoma cell migration and invasion
    • Melchiori A, Mortarini R, Carlone S, et al. The α3β1 integrin is involved in melanoma cell migration and invasion. Exp Cell Res 1995;219:233-42.
    • (1995) Exp Cell Res , vol.219 , pp. 233-242
    • Melchiori, A.1    Mortarini, R.2    Carlone, S.3
  • 27
    • 0027933266 scopus 로고
    • Transformation and tumor progression are frequently associated with expression of the α3/β1 heterodimer in solid tumors
    • Bartolazzi A, Cerboni C, Nicotra MR, Mottolese M, Bigotti A, Natali PG. Transformation and tumor progression are frequently associated with expression of the α3/β1 heterodimer in solid tumors. Int J Cancer 1994;58:488-91.
    • (1994) Int J Cancer , vol.58 , pp. 488-491
    • Bartolazzi, A.1    Cerboni, C.2    Nicotra, M.R.3    Mottolese, M.4    Bigotti, A.5    Natali, P.G.6
  • 28
    • 0028810270 scopus 로고
    • Increase in suprabasilar integrin adhesion molecule expression in human epidermal neoplasms accompanies increased proliferation occurring with immortalization and tumor progression
    • Van Waes C, Surh DM, Chen Z, et al. Increase in suprabasilar integrin adhesion molecule expression in human epidermal neoplasms accompanies increased proliferation occurring with immortalization and tumor progression. Cancer Res 1995;55: 5434-44.
    • (1995) Cancer Res , vol.55 , pp. 5434-5444
    • Van Waes, C.1    Surh, D.M.2    Chen, Z.3
  • 29
    • 0029664423 scopus 로고    scopus 로고
    • Integrin α3β1 can promote adhesion and spreading of metastatic breast carcinoma cells on the lymph node stroma
    • Tawil NJ, Gowri V, Djoneidi M, Nip J, Carbonetto S, Brodt P. Integrin α3β1 can promote adhesion and spreading of metastatic breast carcinoma cells on the lymph node stroma. Int J Cancer 1996;66:703-10.
    • (1996) Int J Cancer , vol.66 , pp. 703-710
    • Tawil, N.J.1    Gowri, V.2    Djoneidi, M.3    Nip, J.4    Carbonetto, S.5    Brodt, P.6
  • 30
    • 0032814982 scopus 로고    scopus 로고
    • Ultrastructural localization of α-3 integrin subunit in malignant melanoma and adjacent epidermis
    • Schumacher D, Schaumburg-Lever G. Ultrastructural localization of α-3 integrin subunit in malignant melanoma and adjacent epidermis. J Cutan Pathol 1999;26: 321-6.
    • (1999) J Cutan Pathol , vol.26 , pp. 321-326
    • Schumacher, D.1    Schaumburg-Lever, G.2
  • 31
    • 0032896208 scopus 로고    scopus 로고
    • Monoclonal antibody ONS-M21 recognizes integrin α3 in gliomas and medulloblastomas
    • Kishima H, Shimizu K, Tamura K, et al. Monoclonal antibody ONS-M21 recognizes integrin α3 in gliomas and medulloblastomas. Br J Cancer 1999;79:333-9.
    • (1999) Br J Cancer , vol.79 , pp. 333-339
    • Kishima, H.1    Shimizu, K.2    Tamura, K.3
  • 32
    • 0033624331 scopus 로고    scopus 로고
    • Functions of α3β1 integrin
    • Kreidberg JA. Functions of α3β1 integrin. Curr Opin Cell Biol 2000;12:548-53.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 548-553
    • Kreidberg, J.A.1
  • 33
    • 0031594731 scopus 로고    scopus 로고
    • Integrin α3β1-mediated interaction with laminin-5 stimulates adhesion, migration and invasion of malignant glioma cells
    • Fukushima Y, Ohnishi T, Arita N, Hayakawa T, Sekiguchi K. Integrin α3β1-mediated interaction with laminin-5 stimulates adhesion, migration and invasion of malignant glioma cells. Int J Cancer 1998;76:63-72.
    • (1998) Int J Cancer , vol.76 , pp. 63-72
    • Fukushima, Y.1    Ohnishi, T.2    Arita, N.3    Hayakawa, T.4    Sekiguchi, K.5
  • 34
    • 0034256088 scopus 로고    scopus 로고
    • The α3β1 integrin is associated with mammary carcinoma cell metastasis, invasion, and gelatinase B (MMP-9) activity
    • Morini M, Mottolese M, Ferrari N, et al. The α3β1 integrin is associated with mammary carcinoma cell metastasis, invasion, and gelatinase B (MMP-9) activity. Int J Cancer 2000;87:336-42.
    • (2000) Int J Cancer , vol.87 , pp. 336-342
    • Morini, M.1    Mottolese, M.2    Ferrari, N.3
  • 35
    • 0029932456 scopus 로고    scopus 로고
    • Modulation of matrix metalloprotease-2 and invasion in human glioma cells by α3β1 integrin
    • Chintala SK, Sawaya R, Gokaslan ZL, Rao JS. Modulation of matrix metalloprotease-2 and invasion in human glioma cells by α3β1 integrin. Cancer Lett 1996;103: 201-8.
    • (1996) Cancer Lett , vol.103 , pp. 201-208
    • Chintala, S.K.1    Sawaya, R.2    Gokaslan, Z.L.3    Rao, J.S.4
  • 36
    • 0030614727 scopus 로고    scopus 로고
    • Anti-α3 integrin antibody induces the activated form of matrix metalloprotease-2 (MMP-2) with concomitant stimulation of invasion through Matrigel by human rhabdomyosarcoma cells
    • Kubota S, Ito H, Ishibashi Y, Seyama Y. Anti-α3 integrin antibody induces the activated form of matrix metalloprotease-2 (MMP-2) with concomitant stimulation of invasion through Matrigel by human rhabdomyosarcoma cells. Int J Cancer 1997;70: 106-11.
    • (1997) Int J Cancer , vol.70 , pp. 106-111
    • Kubota, S.1    Ito, H.2    Ishibashi, Y.3    Seyama, Y.4
  • 38
    • 0034614939 scopus 로고    scopus 로고
    • Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5
    • Koshikawa N, Giannelli G, Cirulli V, Miyazaki K, Quaranta V. Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5. J Cell Biol 2000;148:615-24.
    • (2000) J Cell Biol , vol.148 , pp. 615-624
    • Koshikawa, N.1    Giannelli, G.2    Cirulli, V.3    Miyazaki, K.4    Quaranta, V.5
  • 39
    • 0036380643 scopus 로고    scopus 로고
    • Characterization of the promoter for the mouse α3 integrin gene. Involvement of the Ets-family of transcription factors in the promoter activity
    • Kato T, Katabami K, Takatsuki H, et al. Characterization of the promoter for the mouse α3 integrin gene. Involvement of the Ets-family of transcription factors in the promoter activity. Eur J Biochem 2002;269:4524-32.
    • (2002) Eur J Biochem , vol.269 , pp. 4524-4532
    • Kato, T.1    Katabami, K.2    Takatsuki, H.3
  • 40
    • 0034684619 scopus 로고    scopus 로고
    • Ets target genes: Past, present and future
    • Sementchenko VI, Watson DK. Ets target genes: past, present and future. Oncogene 2000;19:6533-48.
    • (2000) Oncogene , vol.19 , pp. 6533-6548
    • Sementchenko, V.I.1    Watson, D.K.2
  • 41
    • 0030071143 scopus 로고    scopus 로고
    • A single ets-related transcription factor, E1AF, confers invasive phenotype on human cancer cells
    • Kaya M, Yoshida K, Higashino F, Mitaka T, Ishii S, Fujinaga K. A single ets-related transcription factor, E1AF, confers invasive phenotype on human cancer cells. Oncogene 1996;12:221-7.
    • (1996) Oncogene , vol.12 , pp. 221-227
    • Kaya, M.1    Yoshida, K.2    Higashino, F.3    Mitaka, T.4    Ishii, S.5    Fujinaga, K.6
  • 42
    • 0033522242 scopus 로고    scopus 로고
    • Increased E1AF expression in mouse fibrosarcoma promotes metastasis through induction of MT1-MMP expression
    • Habelhah H, Okada F, Kobayashi M, et al. Increased E1AF expression in mouse fibrosarcoma promotes metastasis through induction of MT1-MMP expression. Oncogene 1999;18:1771-6.
    • (1999) Oncogene , vol.18 , pp. 1771-1776
    • Habelhah, H.1    Okada, F.2    Kobayashi, M.3


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