메뉴 건너뛰기




Volumn 15, Issue 5, 2009, Pages 651-660

The effect of tunicamycin on embryonic and newborn murine spleen tissues;Tunikamisinin embriyonik ve yenidoǧan fare dalak dokularına etkisi

Author keywords

Apoptosis; Glycosaminoglycan; Laminin; Spleen; Tunicamycin

Indexed keywords

MURINAE;

EID: 70449130836     PISSN: 13006045     EISSN: None     Source Type: Journal    
DOI: 10.9775/kvfd.2009.064-a     Document Type: Article
Times cited : (3)

References (75)
  • 1
    • 0027490178 scopus 로고
    • Extracellular matrix 5: Adhesive interactions in early mammalian embryogenesis, implantation, and placentation
    • Damsky C, Sutherland A, Fisher S: Extracellular matrix 5: adhesive interactions in early mammalian embryogenesis, implantation, and placentation. FASEB J, 7 (14): 1320-1329, 1993.
    • (1993) FASEB J , vol.7 , Issue.14 , pp. 1320-1329
    • Damsky, C.1    Sutherland, A.2    Fisher, S.3
  • 2
    • 0031908852 scopus 로고    scopus 로고
    • Structure and biological activity of the extracellular matrix
    • Aumailley M, Gayraud B: Structure and biological activity of the extracellular matrix. J Mol Med, 76 (3-4): 253-265, 1998.
    • (1998) J Mol Med , vol.76 , Issue.3-4 , pp. 253-265
    • Aumailley, M.1    Gayraud, B.2
  • 3
    • 40549131272 scopus 로고    scopus 로고
    • Extracellular matrix dynamics in development and regenerative medicine
    • Daley WP, Peters SB, Larsen M: Extracellular matrix dynamics in development and regenerative medicine. J Cell Sci, 121, 255-264, 2008.
    • (2008) J Cell Sci , vol.121 , pp. 255-264
    • Daley, W.P.1    Peters, S.B.2    Larsen, M.3
  • 4
    • 0142122297 scopus 로고    scopus 로고
    • Role of the extracellular matrix in morphogenesis
    • Kleinman HK, Philp D, Hoffman MP: Role of the extracellular matrix in morphogenesis. Curr Opin Biotechnol, 14 (5): 526-532, 2003.
    • (2003) Curr Opin Biotechnol , vol.14 , Issue.5 , pp. 526-532
    • Kleinman, H.K.1    Philp, D.2    Hoffman, M.P.3
  • 5
    • 0032842777 scopus 로고    scopus 로고
    • Extracellular matrix remodelling and cellular differentiation
    • Streuli C: Extracellular matrix remodelling and cellular differentiation. Curr Opin Cell Biol, 11 (5): 634-640, 1999.
    • (1999) Curr Opin Cell Biol , vol.11 , Issue.5 , pp. 634-640
    • Streuli, C.1
  • 6
    • 0032262399 scopus 로고    scopus 로고
    • Laminins and their ligands: Involvement of carbohydrates in formation of the extracellular matrix and in cell adhesion
    • Hall H, Schachner M: Laminins and their ligands: involvement of carbohydrates in formation of the extracellular matrix and in cell adhesion. Trends Glycosci Glycotechnol, 10 (55): 361-382, 1998.
    • (1998) Trends Glycosci Glycotechnol , vol.10 , Issue.55 , pp. 361-382
    • Hall, H.1    Schachner, M.2
  • 8
    • 0025289776 scopus 로고
    • A biological role of the carbohydrate moieties of laminin
    • Dean JW 3rd, Chandrasekaran S, Tanzer ML: A biological role of the carbohydrate moieties of laminin. J Biol Chem, 265 (21): 12553-12562, 1990.
    • (1990) J Biol Chem , vol.265 , Issue.21 , pp. 12553-12562
    • Dean III, J.W.1    Chandrasekaran, S.2    Tanzer, M.L.3
  • 9
    • 0028802948 scopus 로고
    • Laminin receptors: Achieving specificity through cooperation
    • Mercurio AM: Laminin receptors: Achieving specificity through cooperation. Trends Cell Biol, 5 (11): 419-423 1995.
    • (1995) Trends Cell Biol , vol.5 , Issue.11 , pp. 419-423
    • Mercurio, A.M.1
  • 10
    • 0034075654 scopus 로고    scopus 로고
    • Form and function: The laminin family of heterotrimers
    • Colognato H, Yurchenco PD: Form and function: the laminin family of heterotrimers. Dev Dyn, 218 (2): 213-234, 2000.
    • (2000) Dev Dyn , vol.218 , Issue.2 , pp. 213-234
    • Colognato, H.1    Yurchenco, P.D.2
  • 11
    • 0034956546 scopus 로고    scopus 로고
    • Glycosaminoglycans in the study of mammalian organ development
    • Davies JA, Fisher CE, Barnett MW: Glycosaminoglycans in the study of mammalian organ development. Biochem Soc Trans, 29, 166-171, 2001.
    • (2001) Biochem Soc Trans , vol.29 , pp. 166-171
    • Davies, J.A.1    Fisher, C.E.2    Barnett, M.W.3
  • 12
    • 0026507880 scopus 로고
    • Proteoglycans: Many forms and many functions
    • Hardingham TE, Fosang AJ: Proteoglycans: Many forms and many functions. FASEB J, 6 (3): 861-870, 1992.
    • (1992) FASEB J , vol.6 , Issue.3 , pp. 861-870
    • Hardingham, T.E.1    Fosang, A.J.2
  • 13
    • 0027267162 scopus 로고
    • Function of proteoglycans in the extracellular matrix
    • Yanagishita M: Function of proteoglycans in the extracellular matrix. Acta Pathol Jpn, 43 (6): 283-293, 1993
    • (1993) Acta Pathol Jpn , vol.43 , Issue.6 , pp. 283-293
    • Yanagishita, M.1
  • 14
    • 0027204045 scopus 로고
    • Extracellular matrix. 3: Evolution of the extracellular matrix in invertebrates
    • Har-el R, Tanzer ML: Extracellular matrix. 3: Evolution of the extracellular matrix in invertebrates. FASEB J, 7 (12): 1115-1123, 1993.
    • (1993) FASEB J , vol.7 , Issue.12 , pp. 1115-1123
    • Har-El, R.1    Tanzer, M.L.2
  • 15
    • 0024958386 scopus 로고
    • The extracellular matrix and cell surface, mediators of cell interactions in chicken gastrulation
    • Harrisson F: The extracellular matrix and cell surface, mediators of cell interactions in chicken gastrulation. Int J Dev Biol, 33 (4): 417-438, 1989.
    • (1989) Int J Dev Biol , vol.33 , Issue.4 , pp. 417-438
    • Harrisson, F.1
  • 16
    • 0035182105 scopus 로고    scopus 로고
    • Extracellular matrix in development of the early embryo
    • Zagris N: Extracellular matrix in development of the early embryo. Micron, 32 (4): 427-438, 2001.
    • (2001) Micron , vol.32 , Issue.4 , pp. 427-438
    • Zagris, N.1
  • 17
    • 0025648150 scopus 로고
    • Proteoglycans in haemopoietic cells
    • Kolset SO, Gallagher JT: Proteoglycans in haemopoietic cells. Biochim Biophys Acta, 1032 (2-3): 191-211, 1990.
    • (1990) Biochim Biophys Acta , vol.1032 , Issue.2-3 , pp. 191-211
    • Kolset, S.O.1    Gallagher, J.T.2
  • 18
  • 19
    • 0030010512 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular environment: Clues from the gene and protein side offer novel perspectives in molecular diversity and function
    • Iozzo RV, Murdoch AD: Proteoglycans of the extracellular environment: Clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J, 10 (5): 598-614, 1996.
    • (1996) FASEB J , vol.10 , Issue.5 , pp. 598-614
    • Iozzo, R.V.1    Murdoch, A.D.2
  • 20
    • 0023856875 scopus 로고
    • Mouse mammary epithelial cells produce basement membrane and cell surface heparan sulfate proteoglycans containing distinct core proteins
    • Jalkanen M, Rapraeger A, Bernfield M: Mouse mammary epithelial cells produce basement membrane and cell surface heparan sulfate proteoglycans containing distinct core proteins. J Cell Biol, 106 (3): 953-962, 1988.
    • (1988) J Cell Biol , vol.106 , Issue.3 , pp. 953-962
    • Jalkanen, M.1    Rapraeger, A.2    Bernfield, M.3
  • 21
    • 0003880161 scopus 로고    scopus 로고
    • Cell junctions, cell adhesions, and the extracellular matrix
    • In, Gibbs S (Ed), 5th ed, Garland Science, New York
    • Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P: Cell junctions, cell adhesions, and the extracellular matrix. In, Gibbs S (Ed): Molecular Biology of the Cell. 5th ed. pp. 1131-1204, Garland Science, New York, 2008.
    • (2008) Molecular Biology of the Cell , pp. 1131-1204
    • Alberts, B.1    Johnson, A.2    Lewis, J.3    Raff, M.4    Roberts, K.5    Walter, P.6
  • 22
    • 0033975514 scopus 로고    scopus 로고
    • Synthesis and sorting of proteoglycans
    • Prydz K, Dalen KT: Synthesis and sorting of proteoglycans. J Cell Sci, 113, 193-205, 2000.
    • (2000) J Cell Sci , vol.113 , pp. 193-205
    • Prydz, K.1    Dalen, K.T.2
  • 23
    • 0004110428 scopus 로고
    • Carbohydrates
    • Nelson DL, Cox MM (Eds), 2nd ed, Worth Publishers, New York
    • Lehninger AL, Nelson DL, Cox MM: Carbohydrates. In, Nelson DL, Cox MM (Eds): Principles of Biochemistry. 2nd ed. pp. 298-323, Worth Publishers, New York, 1993.
    • (1993) Principles of Biochemistry , pp. 298-323
    • Lehninger, A.L.1    Nelson, D.L.2    Cox, M.M.3
  • 25
    • 0035783042 scopus 로고    scopus 로고
    • Hyaluronan in morphogenesis
    • Toole BP: Hyaluronan in morphogenesis. Semin Cell Dev Biol, 12 (2): 79-87, 2001.
    • (2001) Semin Cell Dev Biol , vol.12 , Issue.2 , pp. 79-87
    • Toole, B.P.1
  • 26
    • 0019819542 scopus 로고
    • Effect of tunicamycin on epidermal glycoprotein and glycosaminoglycan synthesis in vitro
    • King IA, Tabiowo A: Effect of tunicamycin on epidermal glycoprotein and glycosaminoglycan synthesis in vitro. Biochem J, 198 (2): 331-338, 1981.
    • (1981) Biochem J , vol.198 , Issue.2 , pp. 331-338
    • King, I.A.1    Tabiowo, A.2
  • 27
    • 0016616517 scopus 로고
    • Inhibition of biosynthesis of polyisoprenol sugars in chick embryo microsomes by tunicamycin
    • Takatsuki A, Kohno K, Tamura G: Inhibition of biosynthesis of polyisoprenol sugars in chick embryo microsomes by tunicamycin. Agric Biol Chem, 39, 2089-2091, 1975.
    • (1975) Agric Biol Chem , vol.39 , pp. 2089-2091
    • Takatsuki, A.1    Kohno, K.2    Tamura, G.3
  • 28
    • 0016757289 scopus 로고
    • Tunicamycin inhibition of polyisoprenyl N-acetylglucosaminyl pyrophosphate formation in calf-liver microsomes
    • Tkacz JS, Lampen O: Tunicamycin inhibition of polyisoprenyl N-acetylglucosaminyl pyrophosphate formation in calf-liver microsomes. Biochem Biophys Res Commun, 65, 248-257, 1975.
    • (1975) Biochem Biophys Res Commun , vol.65 , pp. 248-257
    • Tkacz, J.S.1    Lampen, O.2
  • 29
    • 0017181626 scopus 로고
    • The specific site of tunicamycin inhibition in the formation of dolichol-bound N- acetylglucosamine derivatives
    • Lehle L, Tanner W: The specific site of tunicamycin inhibition in the formation of dolichol-bound N- acetylglucosamine derivatives. FEBS Lett, 72 (1): 167-170, 1976.
    • (1976) FEBS Lett , vol.72 , Issue.1 , pp. 167-170
    • Lehle, L.1    Tanner, W.2
  • 30
    • 0037144487 scopus 로고    scopus 로고
    • Biosynthesis of tunicamycin and metabolic origin of the 11-carbon dialdose sugar, tunicamine
    • Tsvetanova BC, Kiemle DJ, Price NP: Biosynthesis of tunicamycin and metabolic origin of the 11-carbon dialdose sugar, tunicamine. J Biol Chem, 277 (38): 35289-35296, 2002.
    • (2002) J Biol Chem , vol.277 , Issue.38 , pp. 35289-35296
    • Tsvetanova, B.C.1    Kiemle, D.J.2    Price, N.P.3
  • 31
    • 0013808926 scopus 로고
    • Differential staining of acid glycosaminoglycans (mucopolysaccharides) by alcian blue in salt solutions
    • Scott JE, Dorling J: Differential staining of acid glycosaminoglycans (mucopolysaccharides) by alcian blue in salt solutions. Histochimie, 5 (3): 221-233, 1965.
    • (1965) Histochimie , vol.5 , Issue.3 , pp. 221-233
    • Scott, J.E.1    Dorling, J.2
  • 32
    • 84982385493 scopus 로고
    • The special value of methods that color both acidic and vicinal hydroxyl groups in the histochemical study of mucins. With revised directions for the colloidal iron stain, the use of alcian blue 8GX, and their combination with the periodic-acid-Schiff reaction
    • Mowry RW: The special value of methods that color both acidic and vicinal hydroxyl groups in the histochemical study of mucins. With revised directions for the colloidal iron stain, the use of alcian blue 8GX, and their combination with the periodic-acid-Schiff reaction. Ann N Y Acad Sci, 106, 402-423, 1963.
    • (1963) Ann N Y Acad Sci , vol.106 , pp. 402-423
    • Mowry, R.W.1
  • 33
    • 0001770807 scopus 로고
    • Histochemistry of connective tissue mucopolysaccharides
    • Wagner BM, Smith DE (Eds), Williams and Wilkins Co, Baltimore
    • Spicer SS, Horn RG, Leppi TJ: Histochemistry of connective tissue mucopolysaccharides. In, Wagner BM, Smith DE (Eds): The Connective Tissue. pp. 251-303, Williams and Wilkins Co, Baltimore, 1967.
    • (1967) The Connective Tissue , pp. 251-303
    • Spicer, S.S.1    Horn, R.G.2    Leppi, T.J.3
  • 34
    • 0023626113 scopus 로고
    • Periodic acid-Schiff-alcian blue: A method for the differential staining of glycoproteins
    • Yamabayashi S: Periodic acid-Schiff-alcian blue: A method for the differential staining of glycoproteins. Histochem J, 19 (10-11): 565-571, 1987.
    • (1987) Histochem J , vol.19 , Issue.10-11 , pp. 565-571
    • Yamabayashi, S.1
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227 (5259): 680-685, 1970.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA, 76 (9): 4350-4354, 1979.
    • (1979) Proc Natl Acad Sci USA , vol.76 , Issue.9 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 37
    • 0031859097 scopus 로고    scopus 로고
    • Characterization of beta-D-xyloside-initiated glycosaminoglycan synthesized by human skin fibroblasts in the presence of tunicamycin
    • Takagaki K, Tazawa T, Munakata H, Nakamura T, Endo M: Characterization of beta-D-xyloside-initiated glycosaminoglycan synthesized by human skin fibroblasts in the presence of tunicamycin. Glycoconj J, 15 (5): 483-489, 1998.
    • (1998) Glycoconj J , vol.15 , Issue.5 , pp. 483-489
    • Takagaki, K.1    Tazawa, T.2    Munakata, H.3    Nakamura, T.4    Endo, M.5
  • 38
    • 0017857653 scopus 로고
    • Effects of tunicamycin on the biosynthesis of glycosaminoglycans by embryonic chick cornea
    • Hart GW, Lennarz WJ: Effects of tunicamycin on the biosynthesis of glycosaminoglycans by embryonic chick cornea. J Biol Chem, 253 (16): 5795-5801, 1978.
    • (1978) J Biol Chem , vol.253 , Issue.16 , pp. 5795-5801
    • Hart, G.W.1    Lennarz, W.J.2
  • 39
    • 0020457316 scopus 로고
    • Absence of heparin or heparin-like compounds in mast-cell-free tissues and animals
    • Straus AH, Nader HB, Dietrich CP: Absence of heparin or heparin-like compounds in mast-cell-free tissues and animals. Biochim Biophys Acta, 717 (3): 478-485, 1982.
    • (1982) Biochim Biophys Acta , vol.717 , Issue.3 , pp. 478-485
    • Straus, A.H.1    Nader, H.B.2    Dietrich, C.P.3
  • 40
    • 0025976979 scopus 로고
    • Distribution of laminin and types IV and III collagen in fetal, infant and adult human spleens
    • Liakka A, Apaja-Sarkkinen M, Karttunen T, Autio-Harmainen H: Distribution of laminin and types IV and III collagen in fetal, infant and adult human spleens. Cell Tissue Res, 263 (2): 245-252, 1991.
    • (1991) Cell Tissue Res , vol.263 , Issue.2 , pp. 245-252
    • Liakka, A.1    Apaja-Sarkkinen, M.2    Karttunen, T.3    Autio-Harmainen, H.4
  • 41
    • 0027878064 scopus 로고
    • Localization of beta 1 integrins and their extracellular ligands in human lymphoid tissues
    • van den Berg TK, van der Ende M, Döpp EA, Kraal G, Dijkstra CD: Localization of beta 1 integrins and their extracellular ligands in human lymphoid tissues. Am J Pathol, 143 (4): 1098-1110, 1993.
    • (1993) Am J Pathol , vol.143 , Issue.4 , pp. 1098-1110
    • van den Berg, T.K.1    van der Ende, M.2    Döpp, E.A.3    Kraal, G.4    Dijkstra, C.D.5
  • 42
    • 0028181059 scopus 로고
    • The integrin subunits alpha 2, alpha 3, alpha 4, alpha 5, alpha 6, alpha V, beta 1 and beta 3 in fetal, infant and adult human spleen as detected by immunohisto- chemistry
    • Liakka KA: The integrin subunits alpha 2, alpha 3, alpha 4, alpha 5, alpha 6, alpha V, beta 1 and beta 3 in fetal, infant and adult human spleen as detected by immunohisto- chemistry. Differentiation, 56 (3): 183-190, 1994.
    • (1994) Differentiation , vol.56 , Issue.3 , pp. 183-190
    • Liakka, K.A.1
  • 43
    • 0030467092 scopus 로고    scopus 로고
    • Distribution of laminin variants and their integrin receptors in human secondary lymphoid tissue. Colocalization suggests that the alpha 6 beta 4-integrin is a receptor for laminin-5 in lymphoid follicles
    • Jaspars LH, De Melker AA, Bonnet P, Sonnenberg A, Meijer CJ: Distribution of laminin variants and their integrin receptors in human secondary lymphoid tissue. Colocalization suggests that the alpha 6 beta 4-integrin is a receptor for laminin-5 in lymphoid follicles. Cell Adhes Commun, 4 (4-5): 269-279, 1996.
    • (1996) Cell Adhes Commun , vol.4 , Issue.4-5 , pp. 269-279
    • Jaspars, L.H.1    de Melker, A.A.2    Bonnet, P.3    Sonnenberg, A.4    Meijer, C.J.5
  • 44
    • 0033545239 scopus 로고    scopus 로고
    • Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation
    • Smyth N, Vatansever HS, Murray P, Meyer M, Frie C, Paulsson M, Edgar D: Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation. J Cell Biol, 144 (1): 151-160, 1999.
    • (1999) J Cell Biol , vol.144 , Issue.1 , pp. 151-160
    • Smyth, N.1    Vatansever, H.S.2    Murray, P.3    Meyer, M.4    Frie, C.5    Paulsson, M.6    Edgar, D.7
  • 45
    • 3042790010 scopus 로고    scopus 로고
    • Compositional and structural requirements for laminin and basement membranes during mouse embryo implantation and gastrulation
    • Miner JH, Li C, Mudd JL, Go G, Sutherland AE: Compositional and structural requirements for laminin and basement membranes during mouse embryo implantation and gastrulation. Development, 131 (10): 2247-2256, 2004.
    • (2004) Development , vol.131 , Issue.10 , pp. 2247-2256
    • Miner, J.H.1    Li, C.2    Mudd, J.L.3    Go, G.4    Sutherland, A.E.5
  • 49
    • 39649094291 scopus 로고    scopus 로고
    • The extracellular matrix of the spleen as a potential organizer of immune cell compartments
    • Lokmic Z, Lämmermann T, Sixt M, Cardell S, Hallmann R, Sorokin L: The extracellular matrix of the spleen as a potential organizer of immune cell compartments. Semin Immunol, 20 (1): 4-13, 2008.
    • (2008) Semin Immunol , vol.20 , Issue.1 , pp. 4-13
    • Lokmic, Z.1    Lämmermann, T.2    Sixt, M.3    Cardell, S.4    Hallmann, R.5    Sorokin, L.6
  • 51
    • 0021336701 scopus 로고
    • Functional role of laminin carbohydrate
    • Howe CC: Functional role of laminin carbohydrate. Mol Cell Biol, 4 (1): 1-7, 1984.
    • (1984) Mol Cell Biol , vol.4 , Issue.1 , pp. 1-7
    • Howe, C.C.1
  • 52
    • 0026513844 scopus 로고
    • Functional and morphological changes induced by tunicamycin in dividing and confluent endothelial cells
    • Tiganis T, Leaver DD, Ham K, Friedhuber A, Stewart P, Dziadek M: Functional and morphological changes induced by tunicamycin in dividing and confluent endothelial cells. Exp Cell Res, 198 (2): 191-200, 1992.
    • (1992) Exp Cell Res , vol.198 , Issue.2 , pp. 191-200
    • Tiganis, T.1    Leaver, D.D.2    Ham, K.3    Friedhuber, A.4    Stewart, P.5    Dziadek, M.6
  • 53
    • 0034320568 scopus 로고    scopus 로고
    • Mechanisms of apoptosis
    • Reed JC: Mechanisms of apoptosis. Am J Pathol, 157 (5): 1415-1430, 2000.
    • (2000) Am J Pathol , vol.157 , Issue.5 , pp. 1415-1430
    • Reed, J.C.1
  • 54
    • 0026504147 scopus 로고
    • Social controls of cell survival and cell death
    • Raff MC: Social controls of cell survival and cell death. Nature, 356 (6368): 397-400, 1992.
    • (1992) Nature , vol.356 , Issue.6368 , pp. 397-400
    • Raff, M.C.1
  • 55
    • 0029965136 scopus 로고    scopus 로고
    • The molecular biology of apoptosis
    • Vaux DL, Strasser A: The molecular biology of apoptosis. Proc Natl Acad Sci U S A, 93 (6): 2239-2244, 1996.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.6 , pp. 2239-2244
    • Vaux, D.L.1    Strasser, A.2
  • 56
    • 0035938924 scopus 로고    scopus 로고
    • What is apoptosis, and why is it important?
    • Renehan AG, Booth C, Potten CS: What is apoptosis, and why is it important? BMJ, 322 (7301): 1536-1538, 2001.
    • (2001) BMJ , vol.322 , Issue.7301 , pp. 1536-1538
    • Renehan, A.G.1    Booth, C.2    Potten, C.S.3
  • 57
    • 0042266400 scopus 로고    scopus 로고
    • Death from within: Apoptosis and the secretory pathway
    • Maag RS, Hicks SW, Machamer CE: Death from within: apoptosis and the secretory pathway. Curr Opin Cell Biol, 15 (14): 456-461, 2003.
    • (2003) Curr Opin Cell Biol , vol.15 , Issue.14 , pp. 456-461
    • Maag, R.S.1    Hicks, S.W.2    Machamer, C.E.3
  • 59
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • Nakagawa T, Yuan J: Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol, 150 (4): 887-94, 2000.
    • (2000) J Cell Biol , vol.150 , Issue.4 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 60
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum- specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T, Zhu H, Morishima N, Li E, Xu J, Yankner BA, Yuan J: Caspase-12 mediates endoplasmic-reticulum- specific apoptosis and cytotoxicity by amyloid-beta. Nature, 403 (6765): 98-103, 2000.
    • (2000) Nature , vol.403 , Issue.6765 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 61
    • 33745242294 scopus 로고    scopus 로고
    • Involvement of caspase-2 and caspase-9 in endoplasmic reticulum stress-induced apoptosis: A role for the IAPs
    • Cheung HH, Lynn Kelly N, Liston P, Korneluk RG: Involvement of caspase-2 and caspase-9 in endoplasmic reticulum stress-induced apoptosis: A role for the IAPs. Exp Cell Res, 312 (12): 2347-2357, 2006.
    • (2006) Exp Cell Res , vol.312 , Issue.12 , pp. 2347-2357
    • Cheung, H.H.1    Lynn Kelly, N.2    Liston, P.3    Korneluk, R.G.4
  • 62
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding HP, Zhang Y, Bertolotti A, Zeng H, Ron D: Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell, 5 (5): 897-904, 2000.
    • (2000) Mol Cell , vol.5 , Issue.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 63
    • 0032544573 scopus 로고    scopus 로고
    • A functional link between N- linked glycosylation and apoptosis in Chinese hamster ovary cells
    • Walker BK, Lei H, Krag SS: A functional link between N- linked glycosylation and apoptosis in Chinese hamster ovary cells. Biochem Biophys Res Commun, 250 (2): 264-270, 1998.
    • (1998) Biochem Biophys Res Commun , vol.250 , Issue.2 , pp. 264-270
    • Walker, B.K.1    Lei, H.2    Krag, S.S.3
  • 64
    • 0034610057 scopus 로고    scopus 로고
    • Inhibition of N-linked glycosylation causes apoptosis in hamster BHK21 cells
    • Yoshimi M, Sekiguchi T, Hara N, Nishimoto T: Inhibition of N-linked glycosylation causes apoptosis in hamster BHK21 cells. Biochem Biophys Res Commun, 276 (3): 965-969, 2000.
    • (2000) Biochem Biophys Res Commun , vol.276 , Issue.3 , pp. 965-969
    • Yoshimi, M.1    Sekiguchi, T.2    Hara, N.3    Nishimoto, T.4
  • 65
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch SM, Francis H: Disruption of epithelial cell-matrix interactions induces apoptosis. J Cell Biol, 124 (4): 619-626, 1994.
    • (1994) J Cell Biol , vol.124 , Issue.4 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 66
    • 0030913673 scopus 로고    scopus 로고
    • Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway
    • Khwaja A, Rodriguez-Viciana P, Wennström S, Warne PH, Downward J: Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway. EMBO J, 16 (10): 2783-2793, 1997.
    • (1997) EMBO J , vol.16 , Issue.10 , pp. 2783-2793
    • Khwaja, A.1    Rodriguez-Viciana, P.2    Wennström, S.3    Warne, P.H.4    Downward, J.5
  • 68
  • 69
    • 0029794008 scopus 로고    scopus 로고
    • Merosin and laminin in myogenesis; specific requirement for merosin in myotube stability and survival
    • Vachon PH, Loechel F, Xu H, Wewer UM, Engvall E: Merosin and laminin in myogenesis; specific requirement for merosin in myotube stability and survival. J Cell Biol, 134 (6): 1483-1497, 1996.
    • (1996) J Cell Biol , vol.134 , Issue.6 , pp. 1483-1497
    • Vachon, P.H.1    Loechel, F.2    Xu, H.3    Wewer, U.M.4    Engvall, E.5
  • 70
    • 0026768210 scopus 로고
    • Coordinated expression of extracellular matrix-degrading proteinases and their inhibitors regulates mammary epithelial function during involution
    • Talhouk RS, Bissell MJ, Werb Z: Coordinated expression of extracellular matrix-degrading proteinases and their inhibitors regulates mammary epithelial function during involution. J Cell Biol, 118 (5): 1271-1282, 1992.
    • (1992) J Cell Biol , vol.118 , Issue.5 , pp. 1271-1282
    • Talhouk, R.S.1    Bissell, M.J.2    Werb, Z.3
  • 71
    • 0028927484 scopus 로고
    • Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix
    • Boudreau N, Sympson CJ, Werb Z, Bissell MJ: Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix. Sci, 267 (5199): 891-893, 1995.
    • (1995) Sci , vol.267 , Issue.5199 , pp. 891-893
    • Boudreau, N.1    Sympson, C.J.2    Werb, Z.3    Bissell, M.J.4
  • 72
    • 0028962198 scopus 로고
    • Tenascin-C inhibits extracellular matrix-dependent gene expression in mammary epithelial cells. Localization of active regions using recombinant tenascin fragments
    • Jones PL, Boudreau N, Myers CA, Erickson HP, Bissell MJ: Tenascin-C inhibits extracellular matrix-dependent gene expression in mammary epithelial cells. Localization of active regions using recombinant tenascin fragments. J Cell Sci, 108: 519-527, 1995.
    • (1995) J Cell Sci , vol.108 , pp. 519-527
    • Jones, P.L.1    Boudreau, N.2    Myers, C.A.3    Erickson, H.P.4    Bissell, M.J.5
  • 73
    • 0030030021 scopus 로고    scopus 로고
    • Two distinct phases of apoptosis in mammary gland involution: Proteinase-independent and - dependent pathways
    • Lund LR, Rømer J, Thomasset N, Solberg H, Pyke C, Bissell MJ, Danø K, Werb Z: Two distinct phases of apoptosis in mammary gland involution: Proteinase-independent and - dependent pathways. Development, 122 (1): 181-193, 1996.
    • (1996) Development , vol.122 , Issue.1 , pp. 181-193
    • Lund, L.R.1    Rømer, J.2    Thomasset, N.3    Solberg, H.4    Pyke, C.5    Bissell, M.J.6    Danø, K.7    Werb, Z.8
  • 74
    • 0032521857 scopus 로고    scopus 로고
    • Perturbation of beta1-integrin function alters the development of murine mammary gland
    • Faraldo MM, Deugnier MA, Lukashev M, Thiery JP, Glukhova MA: Perturbation of beta1-integrin function alters the development of murine mammary gland. EMBO J, 17 (8): 2139-2147, 1998.
    • (1998) EMBO J , vol.17 , Issue.8 , pp. 2139-2147
    • Faraldo, M.M.1    Deugnier, M.A.2    Lukashev, M.3    Thiery, J.P.4    Glukhova, M.A.5
  • 75
    • 0033867148 scopus 로고    scopus 로고
    • Tissue architecture and breast cancer: The role of extracellular matrix and steroid hormones
    • Hansen RK, Bissell MJ: Tissue architecture and breast cancer: The role of extracellular matrix and steroid hormones. Endocr Relat Cancer, 7 (2): 95-113, 2000.
    • (2000) Endocr Relat Cancer , vol.7 , Issue.2 , pp. 95-113
    • Hansen, R.K.1    Bissell, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.