메뉴 건너뛰기




Volumn 248, Issue 1, 1999, Pages 260-271

Activation of protein kinase C by phorbol esters modulates α2β1 integrin on MCF-7 breast cancer cells

Author keywords

Adhesion; Breast carcinoma; Collagen; Integrin; PKC; Rho

Indexed keywords

BOTULINUM TOXIN; CALPHOSTIN C; COLLAGEN; GUANOSINE TRIPHOSPHATASE; INTEGRIN; LAMININ; MESSENGER RNA; PHORBOL 13 ACETATE 12 MYRISTATE; PHORBOL ESTER; PROTEIN KINASE C; PROTEIN KINASE C INHIBITOR; RHO FACTOR;

EID: 0033541446     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1998.4390     Document Type: Article
Times cited : (21)

References (76)
  • 1
    • 0023917498 scopus 로고
    • Patterns of tumor metastasis: Organ selectivity in the spread of cancer cells
    • Auerbach R. Patterns of tumor metastasis: Organ selectivity in the spread of cancer cells. Lab. Invest. 58:1988;361-364.
    • (1988) Lab. Invest. , vol.58 , pp. 361-364
    • Auerbach, R.1
  • 2
    • 0025286753 scopus 로고
    • Tumor interactions with the vasculature: Angiogenesis and tumor metastasis
    • Blood C. H., Zetter B. R. Tumor interactions with the vasculature: Angiogenesis and tumor metastasis. Biochim. Biophys. Acta. 1032:1990;89-118.
    • (1990) Biochim. Biophys. Acta , vol.1032 , pp. 89-118
    • Blood, C.H.1    Zetter, B.R.2
  • 3
    • 0026027556 scopus 로고
    • Cancer metastasis and angiogenesis: An imbalance of positive and negative regulation
    • Liotta L. A., Steeg P. S., Stetler-Stevenson W. G. Cancer metastasis and angiogenesis: An imbalance of positive and negative regulation. Cell. 64:1991;327-336.
    • (1991) Cell , vol.64 , pp. 327-336
    • Liotta, L.A.1    Steeg, P.S.2    Stetler-Stevenson, W.G.3
  • 4
    • 0026712934 scopus 로고
    • Adhesive interactions in angiogenesis and metastasis
    • McCormick B. A., Zetter B. R. Adhesive interactions in angiogenesis and metastasis. Pharmacol. Ther. 53:1992;239-260.
    • (1992) Pharmacol. Ther. , vol.53 , pp. 239-260
    • McCormick, B.A.1    Zetter, B.R.2
  • 5
    • 0027395858 scopus 로고
    • Role of integrins and other cell adhesion molecules in tumor progression and metastasis
    • Albelda S. M. Role of integrins and other cell adhesion molecules in tumor progression and metastasis. Lab. Invest. 6:1993;4-17.
    • (1993) Lab. Invest. , vol.6 , pp. 4-17
    • Albelda, S.M.1
  • 6
    • 0027946954 scopus 로고
    • Are cellular adhesion molecules involved in the metastasis of breast cancer?
    • Maemura M., Dickson R. B. Are cellular adhesion molecules involved in the metastasis of breast cancer? Breast Cancer Res. Treat. 32:1994;239-260.
    • (1994) Breast Cancer Res. Treat. , vol.32 , pp. 239-260
    • Maemura, M.1    Dickson, R.B.2
  • 7
    • 0028808210 scopus 로고
    • Fibronectin and integrins in invasion and metastasis
    • Akiyama S. K., Olden K., Yamada K. M. Fibronectin and integrins in invasion and metastasis. Cancer Metast. Rev. 14:1995;173-189.
    • (1995) Cancer Metast. Rev. , vol.14 , pp. 173-189
    • Akiyama, S.K.1    Olden, K.2    Yamada, K.M.3
  • 9
    • 0025138216 scopus 로고
    • Alterations in integrin receptor expression on chemically transformed human cells: Specific enhancement of laminin and collagen receptor complexes
    • Dedhar S., Saulnier R. Alterations in integrin receptor expression on chemically transformed human cells: Specific enhancement of laminin and collagen receptor complexes. J. Cell Biol. 110:1990;481-489.
    • (1990) J. Cell Biol. , vol.110 , pp. 481-489
    • Dedhar, S.1    Saulnier, R.2
  • 10
    • 0027361344 scopus 로고
    • Specific alterations in the expression of α3 β1 and α6β4 integrins in highly invasive and metastatic variants of human prostate carcinoma cells selected byin vitro
    • Dedhar S., Saulnier R., Nagle R., Overall C. M. Specific alterations in the expression of α3 β1 and α6β4 integrins in highly invasive and metastatic variants of human prostate carcinoma cells selected byin vitro. Clin. Exp. Metast. 11:1993;391-400.
    • (1993) Clin. Exp. Metast. , vol.11 , pp. 391-400
    • Dedhar, S.1    Saulnier, R.2    Nagle, R.3    Overall, C.M.4
  • 11
    • 0027167020 scopus 로고
    • Regulation of integrin-mediated adhesion to laminin and collagen in human melanocytes and in non-metastatic and highly metastatic human melanoma cells
    • Danen E. H. J., van Muijen G. N. P., van de Wiel-van Kemenade E., Jansen K. F. J., Ruiter D. J., Figdor C. G. Regulation of integrin-mediated adhesion to laminin and collagen in human melanocytes and in non-metastatic and highly metastatic human melanoma cells. Int. J. Cancer. 54:1993;315-321.
    • (1993) Int. J. Cancer , vol.54 , pp. 315-321
    • Danen, E.H.J.1    Van Muijen, G.N.P.2    Van De Wiel-Van Kemenade, E.3    Jansen, K.F.J.4    Ruiter, D.J.5    Figdor, C.G.6
  • 12
    • 0024534377 scopus 로고
    • Changes in integrin receptors on oncogenically transformed cells
    • Plantefaber L. C., Hynes R. O. Changes in integrin receptors on oncogenically transformed cells. Cell. 56:1989;281-290.
    • (1989) Cell , vol.56 , pp. 281-290
    • Plantefaber, L.C.1    Hynes, R.O.2
  • 13
    • 0024816259 scopus 로고
    • Localization of integrin receptors for fibronectin, collagen, and laminin in human skin variable expression in basal and squamous cell carcinomas
    • Peltonen J. P., Larjava H., Jaakola S., Gralnick H., Akiyama S. K., Yamada S. S., Yamada K. M., Uitto J. Localization of integrin receptors for fibronectin, collagen, and laminin in human skin variable expression in basal and squamous cell carcinomas. J. Clin. Invest. 84:1989;1916-1923.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1916-1923
    • Peltonen, J.P.1    Larjava, H.2    Jaakola, S.3    Gralnick, H.4    Akiyama, S.K.5    Yamada, S.S.6    Yamada, K.M.7    Uitto, J.8
  • 14
    • 0025213155 scopus 로고
    • Low expression of collagen receptors in moderate and poorly differentiated colorectal adenocarcinomas
    • Pignatelli M., Smith M. E. F., Bodmer W. F. Low expression of collagen receptors in moderate and poorly differentiated colorectal adenocarcinomas. Br. J. Cancer. 61:1990;636-638.
    • (1990) Br. J. Cancer , vol.61 , pp. 636-638
    • Pignatelli, M.1    Smith, M.E.F.2    Bodmer, W.F.3
  • 16
    • 0027475345 scopus 로고
    • Integrin expression in normal, hyperplastic, dysplastic, and malignant oral epithelium
    • Jones J., Sugiyama M., Watt F. M., Speight P. M. Integrin expression in normal, hyperplastic, dysplastic, and malignant oral epithelium. J. Pathol. 169:1993;235-243.
    • (1993) J. Pathol. , vol.169 , pp. 235-243
    • Jones, J.1    Sugiyama, M.2    Watt, F.M.3    Speight, P.M.4
  • 17
    • 0025037292 scopus 로고
    • Decreased expression of integrin adhesive protein receptors in adenocarcinoma of the breast
    • Zutter M. M., Mazoujian G., Santoro S. A. Decreased expression of integrin adhesive protein receptors in adenocarcinoma of the breast. Am. J. Pathol. 137:1990;863-870.
    • (1990) Am. J. Pathol. , vol.137 , pp. 863-870
    • Zutter, M.M.1    Mazoujian, G.2    Santoro, S.A.3
  • 18
    • 0027772194 scopus 로고
    • Altered integrin expression in adenocarcinoma of the breast. Analysis byin situ
    • Zutter M. M., Krigman H. R., Santoro S. A. Altered integrin expression in adenocarcinoma of the breast. Analysis byin situ. Am. J. Pathol. 142:1993;1439-1448.
    • (1993) Am. J. Pathol. , vol.142 , pp. 1439-1448
    • Zutter, M.M.1    Krigman, H.R.2    Santoro, S.A.3
  • 20
    • 0026644051 scopus 로고
    • Integrins and their accessory adhesion molecules in mammary carcinomas: Loss of polarization in poorly differentiated tumors
    • Pignatelli M., Cardillo M. R., Hanby A., Stamp G. W. Integrins and their accessory adhesion molecules in mammary carcinomas: Loss of polarization in poorly differentiated tumors. Hum. Pathol. 23:1992;1159-1166.
    • (1992) Hum. Pathol. , vol.23 , pp. 1159-1166
    • Pignatelli, M.1    Cardillo, M.R.2    Hanby, A.3    Stamp, G.W.4
  • 21
    • 0027324966 scopus 로고
    • Expression of βl integrins in non-neoplastic mammary epithelium, fibroadenoma and carcinoma of the breast
    • Mechtersheimer G., Munk M., Barth T., Koretz K., Moller P. Expression of βl integrins in non-neoplastic mammary epithelium, fibroadenoma and carcinoma of the breast. Virchow's Arch. A. 422:1993;203-210.
    • (1993) Virchow's Arch. A , vol.422 , pp. 203-210
    • Mechtersheimer, G.1    Munk, M.2    Barth, T.3    Koretz, K.4    Moller, P.5
  • 22
    • 0026730017 scopus 로고
    • Alteration of stromal protein and integrin expression in breast - A marker of premalignant change?
    • Jones J. L., Critchley D. R., Walker R. A. Alteration of stromal protein and integrin expression in breast - A marker of premalignant change? J. Pathol. 167:1992;399-406.
    • (1992) J. Pathol. , vol.167 , pp. 399-406
    • Jones, J.L.1    Critchley, D.R.2    Walker, R.A.3
  • 26
    • 0028092237 scopus 로고
    • Selective involvement of protein kinase C isozymes in differentiation and neoplastic transformation
    • Goodnight J., Mischak H., Mushinski J. F. Selective involvement of protein kinase C isozymes in differentiation and neoplastic transformation. Adv. Cancer Res. 64:1994;159-209.
    • (1994) Adv. Cancer Res. , vol.64 , pp. 159-209
    • Goodnight, J.1    Mischak, H.2    Mushinski, J.F.3
  • 27
    • 0030584097 scopus 로고    scopus 로고
    • Protein kinase C and its substrates
    • Liu J. P. Protein kinase C and its substrates. Mol. Cell Endocrinol. 116:1996;1-29.
    • (1996) Mol. Cell Endocrinol. , vol.116 , pp. 1-29
    • Liu, J.P.1
  • 29
    • 0018771246 scopus 로고
    • Induction of differentiation in human promyelocytic leukemia cells by tumor promoters
    • Rovera G., O'Brien T. G., Diamond L. Induction of differentiation in human promyelocytic leukemia cells by tumor promoters. Science. 204:1979;868-869.
    • (1979) Science , vol.204 , pp. 868-869
    • Rovera, G.1    O'Brien, T.G.2    Diamond, L.3
  • 30
    • 0024323584 scopus 로고
    • Elevated protein kinase C expression in human breast tumor biopsies relative to normal breast tissue
    • O'Brian C. A., Vogel V. G., Singletary S. E., Ward N. E. Elevated protein kinase C expression in human breast tumor biopsies relative to normal breast tissue. Cancer Res. 49:1989;3215-3217.
    • (1989) Cancer Res. , vol.49 , pp. 3215-3217
    • O'Brian, C.A.1    Vogel, V.G.2    Singletary, S.E.3    Ward, N.E.4
  • 33
    • 0028903545 scopus 로고
    • MCF-7 breast cancer cells transfected with protein kinase C-alpha exhibit altered expression of other protein kinase C isoforms and display a more aggressive neoplastic phenotype
    • Ways D. K., Kukoly C. A., de Vente J., Hooker J. L., Bryant W. O., Posekany K. J., Fletcher D. J., Cook P. P., Parker P. J. MCF-7 breast cancer cells transfected with protein kinase C-alpha exhibit altered expression of other protein kinase C isoforms and display a more aggressive neoplastic phenotype. J. Clin. Invest. 95:1995;1906-1915.
    • (1995) J. Clin. Invest. , vol.95 , pp. 1906-1915
    • Ways, D.K.1    Kukoly, C.A.2    De Vente, J.3    Hooker, J.L.4    Bryant, W.O.5    Posekany, K.J.6    Fletcher, D.J.7    Cook, P.P.8    Parker, P.J.9
  • 34
    • 0029968827 scopus 로고    scopus 로고
    • Rho family GTPases: The cytoskeleton and beyond
    • Symons M. Rho family GTPases: The cytoskeleton and beyond. Trends Biol. Sci. 21:1996;178-181.
    • (1996) Trends Biol. Sci. , vol.21 , pp. 178-181
    • Symons, M.1
  • 36
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley A. J., Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:1992;369-399.
    • (1992) Cell , vol.70 , pp. 369-399
    • Ridley, A.J.1    Hall, A.2
  • 38
    • 0023882163 scopus 로고
    • Botulinum ADP-ribosyltransferase C3. Purification of the enzyme and characterization of the ADP-ribosylation reaction in platelet membranes
    • Aktories K., Rosener S., Blaschke U., Chhatwal G. S. Botulinum ADP-ribosyltransferase C3. Purification of the enzyme and characterization of the ADP-ribosylation reaction in platelet membranes. Eur. J. Biochem. 172:1988;445-450.
    • (1988) Eur. J. Biochem. , vol.172 , pp. 445-450
    • Aktories, K.1    Rosener, S.2    Blaschke, U.3    Chhatwal, G.S.4
  • 39
    • 0024353843 scopus 로고
    • Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase
    • Sekine A., Fujiwara M., Narumiya S. Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. J. Biol. Chem. 264:1989;8602-8605.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8602-8605
    • Sekine, A.1    Fujiwara, M.2    Narumiya, S.3
  • 40
    • 0025602433 scopus 로고
    • ADP-ribosylation of the rho/rac gene products by botulinum ADP-ribosyltransferase: Identity of the enzyme and effects on protein and cell functions
    • Narumiya S., Morii N., Sekine A., Kozaki S. ADP-ribosylation of the rho/rac gene products by botulinum ADP-ribosyltransferase: Identity of the enzyme and effects on protein and cell functions. J. Physiol. 84:1990;267-272.
    • (1990) J. Physiol. , vol.84 , pp. 267-272
    • Narumiya, S.1    Morii, N.2    Sekine, A.3    Kozaki, S.4
  • 41
    • 0028258943 scopus 로고
    • Rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor- And 12-O
    • Nishiyama T., Sasaki T., Takaishi K., Kato M., Yaku H., Araki K., Matsuura Y., Takai Y. rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor- and 12-O. Mol. Cell. Biol. 14:1994;2447-2456.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2447-2456
    • Nishiyama, T.1    Sasaki, T.2    Takaishi, K.3    Kato, M.4    Yaku, H.5    Araki, K.6    Matsuura, Y.7    Takai, Y.8
  • 42
    • 0029131982 scopus 로고
    • Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows
    • Takaishi K., Sasaki T., Kameyama T., Tsukita S., Tsukita S., Takai Y. Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows. Oncogene. 11:1995;39-48.
    • (1995) Oncogene , vol.11 , pp. 39-48
    • Takaishi, K.1    Sasaki, T.2    Kameyama, T.3    Tsukita, S.4    Tsukita, S.5    Takai, Y.6
  • 43
    • 0024359871 scopus 로고
    • Analysis of fibronectin receptor function with monoclonal antibodies: Roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization
    • Akiyama S. K., Yamada S. S., Chen W.-T., Yamada K. M. Analysis of fibronectin receptor function with monoclonal antibodies: Roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization. J. Cell Biol. 109:1989;863-875.
    • (1989) J. Cell Biol. , vol.109 , pp. 863-875
    • Akiyama, S.K.1    Yamada, S.S.2    Chen, W.-T.3    Yamada, K.M.4
  • 44
    • 0023280134 scopus 로고
    • Use of the monoclonal antibody 12F1 to characterize the differentiation antigen VLA-2
    • Pischel K. D., Hemler M. E., Huang C., Bluestein H. G., Woods V. L. Jr. Use of the monoclonal antibody 12F1 to characterize the differentiation antigen VLA-2. J. Immunol. 138:1987;226-233.
    • (1987) J. Immunol. , vol.138 , pp. 226-233
    • Pischel, K.D.1    Hemler, M.E.2    Huang, C.3    Bluestein, H.G.4    Woods V.L., Jr.5
  • 45
    • 0024321318 scopus 로고
    • Collagen-platelet interactions: Evidence for a direct interaction of collagen with platelet GPIa/IIa and an indirect interaction with platelet GPIIb/IIIa mediated by adhesive proteins
    • Coller B. S., Beer J. H., Scudder L. E., Steinberg M. H. Collagen-platelet interactions: Evidence for a direct interaction of collagen with platelet GPIa/IIa and an indirect interaction with platelet GPIIb/IIIa mediated by adhesive proteins. Blood. 74:1989;182-192.
    • (1989) Blood , vol.74 , pp. 182-192
    • Coller, B.S.1    Beer, J.H.2    Scudder, L.E.3    Steinberg, M.H.4
  • 47
    • 0029151366 scopus 로고
    • Purification and assay of recombinant C3 transferase
    • Dillon S. T., Feig L. A. Purification and assay of recombinant C3 transferase. Methods Enzymol. 256:1995;174-184.
    • (1995) Methods Enzymol. , vol.256 , pp. 174-184
    • Dillon, S.T.1    Feig, L.A.2
  • 48
    • 0023277545 scopus 로고
    • A rapid single step method for preparing RNA
    • Chomczynski P., Sacchi N. A rapid single step method for preparing RNA. Anal. Biochem. 162:1987;156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 49
    • 0024336285 scopus 로고
    • Oestrogenic activity of tamoxifen and its metabolites on gene regulation and cell proliferation in MCF-7 breast cancer cells
    • Johnson M. D., Westley B. R., May F. E. B. Oestrogenic activity of tamoxifen and its metabolites on gene regulation and cell proliferation in MCF-7 breast cancer cells. Br. J. Cancer. 59:1989;727-738.
    • (1989) Br. J. Cancer , vol.59 , pp. 727-738
    • Johnson, M.D.1    Westley, B.R.2    May, F.E.B.3
  • 50
    • 0020488029 scopus 로고
    • Cloning of cDNA sequences of hormone-regulated genes from the MCF-7 human breast cancer cell line
    • Masiakowski P., Breathnach R., Bloch J., Gannon F., Krust A., Chambon P. Cloning of cDNA sequences of hormone-regulated genes from the MCF-7 human breast cancer cell line. Nucleic Acids Res. 10:1982;7895-7903.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 7895-7903
    • Masiakowski, P.1    Breathnach, R.2    Bloch, J.3    Gannon, F.4    Krust, A.5    Chambon, P.6
  • 51
    • 0025778925 scopus 로고
    • 36B4 cDNA used as an estradiol-independent mRNA control is the cDNA for human acidic ribosomal phosphoprotein PO
    • Laborda, J. 1991, 36B4 cDNA used as an estradiol-independent mRNA control is the cDNA for human acidic ribosomal phosphoprotein PO, Nucleic Acids Res. 19, 3998.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3998
    • Laborda, J.1
  • 54
    • 0022492043 scopus 로고
    • Protein kinase C desensitization by phorbol esters and its impact on growth of human breast cancer cells
    • Fabbro D., Regazzi R., Costa S. D., Borner C., Eppenberger U. Protein kinase C desensitization by phorbol esters and its impact on growth of human breast cancer cells. Biochem. Biophys. Res. Commun. 135:1986;65-73.
    • (1986) Biochem. Biophys. Res. Commun. , vol.135 , pp. 65-73
    • Fabbro, D.1    Regazzi, R.2    Costa, S.D.3    Borner, C.4    Eppenberger, U.5
  • 55
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase C
    • Nishizuka Y. Studies and perspectives of protein kinase C. Science. 233:1986;305-312.
    • (1986) Science , vol.233 , pp. 305-312
    • Nishizuka, Y.1
  • 56
    • 0024550448 scopus 로고
    • Calphostin C (UCN-1028C), a novel microbial compound, is a highly potent and specific inhibitor of protein kinase C
    • Kobayashi E., Nakano H., Morimoto M., Tamaoki T. Calphostin C (UCN-1028C), a novel microbial compound, is a highly potent and specific inhibitor of protein kinase C. Biochem. Biophys. Res. Commun. 159:1989;548-553.
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 548-553
    • Kobayashi, E.1    Nakano, H.2    Morimoto, M.3    Tamaoki, T.4
  • 57
    • 0023673928 scopus 로고
    • Tumor promoter-induced membrane-bound protein kinase C regulates hematogenous metastasis
    • Gopalakrishna R., Barsky S. H. Tumor promoter-induced membrane-bound protein kinase C regulates hematogenous metastasis. Proc. Natl. Acad. Sci. USA. 85:1988;612-616.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 612-616
    • Gopalakrishna, R.1    Barsky, S.H.2
  • 58
    • 0025203931 scopus 로고
    • Protein kinase C inhibitors block the enhanced expression of intercellular adhesion molecule-l, lipopolysaccharide and tumor necrosis factor
    • Lane T. A., Lamkin G. E., Wancewicz E. V. Protein kinase C inhibitors block the enhanced expression of intercellular adhesion molecule-l, lipopolysaccharide and tumor necrosis factor. Biochem. Biophys. Res. Commun. 172:1990;1273-1281.
    • (1990) Biochem. Biophys. Res. Commun. , vol.172 , pp. 1273-1281
    • Lane, T.A.1    Lamkin, G.E.2    Wancewicz, E.V.3
  • 59
    • 0021879854 scopus 로고
    • Interleukin-2 stimulates association of protein kinase C with plasma membrane
    • Farrar W. L., Anderson W. B. Interleukin-2 stimulates association of protein kinase C with plasma membrane. Nature. 315:1985;233-235.
    • (1985) Nature , vol.315 , pp. 233-235
    • Farrar, W.L.1    Anderson, W.B.2
  • 60
    • 0021812451 scopus 로고
    • Altered cytosol/membrane enzyme redistribution on interleukin-3 activation of protein kinase C
    • Farrar W. L., Thomas T. P., Anderson W. B. Altered cytosol/membrane enzyme redistribution on interleukin-3 activation of protein kinase C. Nature. 315:1985;235-237.
    • (1985) Nature , vol.315 , pp. 235-237
    • Farrar, W.L.1    Thomas, T.P.2    Anderson, W.B.3
  • 61
    • 0023754049 scopus 로고
    • Interferon-γ And interleukin-l α induce transient translocation of protein kinase C activity to membranes in a B lymphoid cell line. Evidence for a protein kinase C-independent pathway in lymphokine-induced cytoplasmic alkalinization
    • Ostrowski J., Meier K. E., Stanton T. H., Smith L. L., Bomsztyk K. Interferon-γ and interleukin-l α induce transient translocation of protein kinase C activity to membranes in a B lymphoid cell line. Evidence for a protein kinase C-independent pathway in lymphokine-induced cytoplasmic alkalinization. J. Biol. Chem. 263:1988;13786-13790.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13786-13790
    • Ostrowski, J.1    Meier, K.E.2    Stanton, T.H.3    Smith, L.L.4    Bomsztyk, K.5
  • 62
    • 0025807704 scopus 로고
    • Tumor necrosis factor α and interferon γ modulate the expression of the vitronectin receptor (integrin β3) in human endothelial cells
    • Deflippi P., Truffa G., Stefanuto G., Altruda F., Silengo L., Tarone G. Tumor necrosis factor α and interferon γ modulate the expression of the vitronectin receptor (integrin β3) in human endothelial cells. J. Biol. Chem. 266:1991;7638-7645.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7638-7645
    • Deflippi, P.1    Truffa, G.2    Stefanuto, G.3    Altruda, F.4    Silengo, L.5    Tarone, G.6
  • 63
    • 0026343904 scopus 로고
    • Regulation of integrin-type cell adhesion receptors by cytokines
    • Santala P., Heino J. Regulation of integrin-type cell adhesion receptors by cytokines. J. Biol. Chem. 266:1991;23505-23509.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23505-23509
    • Santala, P.1    Heino, J.2
  • 64
    • 0027164724 scopus 로고
    • Tumor necrosis factor-α increased the integrin α2β1 expression and cell attachment to type I collagen in human dermal fibroblasts
    • Ezoe K., Horikoshi T. Tumor necrosis factor-α increased the integrin α2β1 expression and cell attachment to type I collagen in human dermal fibroblasts. Biochem. Biophys. Res. Commun. 192:1993;281-287.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 281-287
    • Ezoe, K.1    Horikoshi, T.2
  • 65
    • 0026611378 scopus 로고
    • α6βl integrin (laminin receptor) is down-regulated by tumor necrosis factor α and interleukin-l β in human endothelial cells
    • Deflippi P., Silengo L., Tarone G. α6βl integrin (laminin receptor) is down-regulated by tumor necrosis factor α and interleukin-l β in human endothelial cells. J. Biol. Chem. 267:1992;18303-18307.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18303-18307
    • Deflippi, P.1    Silengo, L.2    Tarone, G.3
  • 66
    • 0024506757 scopus 로고
    • Phorbol ester modulation of integrin-mediated cell adhesion: A postreceptor event
    • Danilov Y. N., Juliano R. L. Phorbol ester modulation of integrin-mediated cell adhesion: A postreceptor event. J. Cell Biol. 10:1989;1925-1933.
    • (1989) J. Cell Biol. , vol.10 , pp. 1925-1933
    • Danilov, Y.N.1    Juliano, R.L.2
  • 67
    • 0024398939 scopus 로고
    • Phorbol ester induces increased expression, altered glycosylation, and reduced adhesion of K562 erythroleukemia cell fibronectin receptors
    • Symington B. E., Symington F. W., Rohrschneider L. R. Phorbol ester induces increased expression, altered glycosylation, and reduced adhesion of K562 erythroleukemia cell fibronectin receptors. J. Biol. Chem. 264:1989;13258-13266.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13258-13266
    • Symington, B.E.1    Symington, F.W.2    Rohrschneider, L.R.3
  • 69
    • 0026756152 scopus 로고
    • Triggering through CD16 or phorbol esters enhances adhesion of NK cells to laminin via very late antigen 6
    • Gismondi A., Mainiero F., Morrone S., Palmieri G., Piccoli M., Frati L., Santoni A. Triggering through CD16 or phorbol esters enhances adhesion of NK cells to laminin via very late antigen 6. J. Exp. Med. 176:1992;1251-1257.
    • (1992) J. Exp. Med. , vol.176 , pp. 1251-1257
    • Gismondi, A.1    Mainiero, F.2    Morrone, S.3    Palmieri, G.4    Piccoli, M.5    Frati, L.6    Santoni, A.7
  • 70
    • 0029090122 scopus 로고
    • Inducible interaction of integrin alpha 2 beta 1 with calreticulin. Dependence on the activation state of the integrin
    • Coppolino M., Leung-Hagesteijn C., Dedhar S., Wilkins J. Inducible interaction of integrin alpha 2 beta 1 with calreticulin. Dependence on the activation state of the integrin. J. Biol. Chem. 270:1995;23132-23138.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23132-23138
    • Coppolino, M.1    Leung-Hagesteijn, C.2    Dedhar, S.3    Wilkins, J.4
  • 71
    • 0025666501 scopus 로고
    • Integrin-associated protein: A 50-kD plasma membrane antigen physically and functionally associated with integrins
    • Brown E., Hooper L., Ho T., Gresham H. Integrin-associated protein: A 50-kD plasma membrane antigen physically and functionally associated with integrins. J. Cell Biol. 111:1990;2785-2794.
    • (1990) J. Cell Biol. , vol.111 , pp. 2785-2794
    • Brown, E.1    Hooper, L.2    Ho, T.3    Gresham, H.4
  • 72
    • 0030694459 scopus 로고    scopus 로고
    • Cholecystokinin-stimulated tyrosine phosphorylation of p125FAK and paxillin is mediated by phospholipase C-dependent and -independent mechanisms and requires the integrity of the actin cytoskeleton and participation of p21Rho
    • Garcia L. J., Rosado J. A., Gonzalez A., Jensen R. T. Cholecystokinin-stimulated tyrosine phosphorylation of p125FAK and paxillin is mediated by phospholipase C-dependent and -independent mechanisms and requires the integrity of the actin cytoskeleton and participation of p21Rho. Biochem. J. 327:1997;461-472.
    • (1997) Biochem. J. , vol.327 , pp. 461-472
    • Garcia, L.J.1    Rosado, J.A.2    Gonzalez, A.3    Jensen, R.T.4
  • 74
    • 0023759172 scopus 로고
    • Induction of proto-oncogene JUN/AP-1 by serum and TPA
    • Lamph W. W., Wamsley P., Sassone-Corsi P., Verma I. M. Induction of proto-oncogene JUN/AP-1 by serum and TPA. Nature. 334:1988;629-631.
    • (1988) Nature , vol.334 , pp. 629-631
    • Lamph, W.W.1    Wamsley, P.2    Sassone-Corsi, P.3    Verma, I.M.4
  • 75
    • 0023663116 scopus 로고
    • Transcription factor AP-2 mediates induction by two different signal-transduction pathways: Protein kinase C and cAMP
    • Imagawa M., Chiu R., Karin M. Transcription factor AP-2 mediates induction by two different signal-transduction pathways: Protein kinase C and cAMP. Cell. 51:1987;251-260.
    • (1987) Cell , vol.51 , pp. 251-260
    • Imagawa, M.1    Chiu, R.2    Karin, M.3
  • 76
    • 0026667736 scopus 로고
    • Induced cell surface expression of functional alpha 2 beta 1 integrin during megakaryocytic differentiation of K562 leukemic cells
    • Burger S. R., Zutter M. M., Sturgill-Koszycki S., Santoro S. A. Induced cell surface expression of functional alpha 2 beta 1 integrin during megakaryocytic differentiation of K562 leukemic cells. Exp. Cell Res. 202:1992;28-35.
    • (1992) Exp. Cell Res. , vol.202 , pp. 28-35
    • Burger, S.R.1    Zutter, M.M.2    Sturgill-Koszycki, S.3    Santoro, S.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.