메뉴 건너뛰기




Volumn 44, Issue 2, 1999, Pages 133-142

Progressive association of a 'soluble' glycolytic enzyme with the detergent-insoluble cytoskeleton during in vitro morphogenesis of MDCK epithelial cells

Author keywords

Actin; ATP; Cytokeratins; Epithelium; GAPDH

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE; DETERGENT; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCOLYTIC ENZYME; LACTATE DEHYDROGENASE; PHOSPHOGLYCERATE MUTASE; PROTEIN;

EID: 0032882048     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0169(199910)44:2<133::AID-CM5>3.0.CO;2-9     Document Type: Article
Times cited : (21)

References (27)
  • 1
    • 0030464473 scopus 로고    scopus 로고
    • Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion
    • Adams CL, Nelson WJ, Smith SJ. 1996. Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion. J Cell Biol 135:1899-1911.
    • (1996) J Cell Biol , vol.135 , pp. 1899-1911
    • Adams, C.L.1    Nelson, W.J.2    Smith, S.J.3
  • 2
    • 0023098484 scopus 로고
    • Identification of the 37-kDa protein displaying a variable interaction with the erythroid cell membrane as glyceraldehyde-3-phosphate dehydrogenase
    • Allen RW, Trach KA, Hoch JA. 1987. Identification of the 37-kDa protein displaying a variable interaction with the erythroid cell membrane as glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 262:649-653.
    • (1987) J Biol Chem , vol.262 , pp. 649-653
    • Allen, R.W.1    Trach, K.A.2    Hoch, J.A.3
  • 3
    • 0025957990 scopus 로고
    • Where is the glycolytic complex? A critical evaluation of present data from muscle tissue
    • Brooks SPJ, Storey KB. 1991. Where is the glycolytic complex? A critical evaluation of present data from muscle tissue. FEBS Lett 278:135-1380.
    • (1991) FEBS Lett , vol.278 , pp. 135-1380
    • Brooks, S.P.J.1    Storey, K.B.2
  • 4
    • 0031589971 scopus 로고    scopus 로고
    • Protein insolubility and late-stage morphogenesis in long-term postconfluent cultures of MDCK epithelial cells
    • Cao F, Burke JM. 1997. Protein insolubility and late-stage morphogenesis in long-term postconfluent cultures of MDCK epithelial cells. Biochem. Biophys Res Commun 234:719-728.
    • (1997) Biochem. Biophys Res Commun , vol.234 , pp. 719-728
    • Cao, F.1    Burke, J.M.2
  • 5
    • 0021804407 scopus 로고
    • Interaction of glyceraldehyde-3-phosphate dehydrogenase with isolated microsomal subfractions of skeletal muscle
    • Caswell AH, Corbett AM. 1985. Interaction of glyceraldehyde-3-phosphate dehydrogenase with isolated microsomal subfractions of skeletal muscle. J Biol Chem 260:6892-6898.
    • (1985) J Biol Chem , vol.260 , pp. 6892-6898
    • Caswell, A.H.1    Corbett, A.M.2
  • 6
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper JA. 1987. Effects of cytochalasin and phalloidin on actin. J Cell Biol 105:1473-1478.
    • (1987) J Cell Biol , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 7
    • 0023099854 scopus 로고
    • Microtubules bind glyceraldehyde-3-phosphate dehydrogenase and modulate its enzyme activity and quaternary structure
    • Durrieu C, Bernier-Valentin F, Rousset B. 1987. Microtubules bind glyceraldehyde-3-phosphate dehydrogenase and modulate its enzyme activity and quaternary structure. Arch Biochem Biophys 252:32-40.
    • (1987) Arch Biochem Biophys , vol.252 , pp. 32-40
    • Durrieu, C.1    Bernier-Valentin, F.2    Rousset, B.3
  • 8
    • 0021893224 scopus 로고
    • Alteration of intermediate filament distribution in Ptk1 cells by acrylamide
    • Eckert BS. 1985. Alteration of intermediate filament distribution in Ptk1 cells by acrylamide. Eur J Cell Biol 37:169-174.
    • (1985) Eur J Cell Biol , vol.37 , pp. 169-174
    • Eckert, B.S.1
  • 9
    • 0025269824 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is a major protein associated with the plasma membrane of retinal photoreceptor outer segments
    • Hsu S-C, Molday RS. 1990. Glyceraldehyde-3-phosphate dehydrogenase is a major protein associated with the plasma membrane of retinal photoreceptor outer segments. J Biol Chem 265:13308-13313.
    • (1990) J Biol Chem , vol.265 , pp. 13308-13313
    • Hsu, S.-C.1    Molday, R.S.2
  • 10
    • 0022359757 scopus 로고
    • Bundling of microtubules by glyceraldehyde-3-phosphate dehydrogenase and its modulation by ATP
    • Huitorel P, Pantaloni P. 1985. Bundling of microtubules by glyceraldehyde-3-phosphate dehydrogenase and its modulation by ATP. Eur J Biochem 150:265-269.
    • (1985) Eur J Biochem , vol.150 , pp. 265-269
    • Huitorel, P.1    Pantaloni, P.2
  • 11
    • 0030045251 scopus 로고    scopus 로고
    • Evidence that glyceraldehyde-3-phosphate dehydrogenase is involved in age-induced apoptosis in mature cerebellar neurons in culture
    • Ishitani R, Sunaga K, Hirano A, Saunders P, Katsube N, Chuang D-M. 1996. Evidence that glyceraldehyde-3-phosphate dehydrogenase is involved in age-induced apoptosis in mature cerebellar neurons in culture. J Neurochem 66:928-935.
    • (1996) J Neurochem , vol.66 , pp. 928-935
    • Ishitani, R.1    Sunaga, K.2    Hirano, A.3    Saunders, P.4    Katsube, N.5    Chuang, D.-M.6
  • 12
    • 0031968628 scopus 로고    scopus 로고
    • Nuclear localization of overexpressed glyceraldehyde-3-phosphate dehydrogenase in cultured cerebellar neurons undergoing apoptosis
    • Ishitani R, Tanaka M, Sunaga K, Katsube N, Chuang DM. 1998. Nuclear localization of overexpressed glyceraldehyde-3-phosphate dehydrogenase in cultured cerebellar neurons undergoing apoptosis. Mol Pharmacol 53:701-707.
    • (1998) Mol Pharmacol , vol.53 , pp. 701-707
    • Ishitani, R.1    Tanaka, M.2    Sunaga, K.3    Katsube, N.4    Chuang, D.M.5
  • 13
    • 0022477471 scopus 로고
    • Autophosphorylation of glyceraldehyde phosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes
    • Kawamoto RM, Caswell AH. 1986. Autophosphorylation of glyceraldehyde phosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes. Biochemistry 25:657-661.
    • (1986) Biochemistry , vol.25 , pp. 657-661
    • Kawamoto, R.M.1    Caswell, A.H.2
  • 14
    • 0026489887 scopus 로고
    • Association of glycolytic enzymes with the cytoskeleton
    • Knull HR, Walsh JL. 1992. Association of glycolytic enzymes with the cytoskeleton. Curr Top Cell Regul 33:15-30.
    • (1992) Curr Top Cell Regul , vol.33 , pp. 15-30
    • Knull, H.R.1    Walsh, J.L.2
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 17
    • 0027398589 scopus 로고
    • Spatial and temporal dissection of immediate and early events following cadherin-mediated epithelial cell adhesion
    • McNeill H, Ryan TA, Smith SJ, Nelson WJ. 1993. Spatial and temporal dissection of immediate and early events following cadherin-mediated epithelial cell adhesion. J Cell Biol 120:1217-1226.
    • (1993) J Cell Biol , vol.120 , pp. 1217-1226
    • McNeill, H.1    Ryan, T.A.2    Smith, S.J.3    Nelson, W.J.4
  • 18
    • 0023001826 scopus 로고
    • Dynamics of membrane-skeleton (fodrin) organization during development of polarity in Madin-Darby Canine Kidney epithelial cells
    • Nelson WJ, Veshnock PJ. 1986. Dynamics of membrane-skeleton (fodrin) organization during development of polarity in Madin-Darby Canine Kidney epithelial cells. J Cell Biol 103:1751-1765.
    • (1986) J Cell Biol , vol.103 , pp. 1751-1765
    • Nelson, W.J.1    Veshnock, P.J.2
  • 19
    • 0029095105 scopus 로고
    • A mutation in glyceraldehyde-3-phosphate dehydrogenase alters endocytosis in CHO cells
    • Robbins AR, Ward RD, Oliver C. 1995. A mutation in glyceraldehyde-3-phosphate dehydrogenase alters endocytosis in CHO cells. J Cell Biol 130:1093-1104.
    • (1995) J Cell Biol , vol.130 , pp. 1093-1104
    • Robbins, A.R.1    Ward, R.D.2    Oliver, C.3
  • 20
    • 0030868934 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase: Nuclear translocation participates in neuronal and nonneuronal cell death
    • Sawa A, Khan AA, Hester LD, Snyder SH. 1997. Glyceraldehyde-3-phosphate dehydrogenase: nuclear translocation participates in neuronal and nonneuronal cell death. Proc Natl Acad Sci USA 94:11669-11674.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11669-11674
    • Sawa, A.1    Khan, A.A.2    Hester, L.D.3    Snyder, S.H.4
  • 21
    • 0026070055 scopus 로고
    • A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase
    • Siegler KM, Mauro DJ, Seal G, Wurzer J, deRiel JK, Sirover MA. 1991. A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase. Proc Natl Acad Sci USA 88:8460-8464.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8460-8464
    • Siegler, K.M.1    Mauro, D.J.2    Seal, G.3    Wurzer, J.4    DeRiel, J.K.5    Sirover, M.A.6
  • 22
    • 0027518424 scopus 로고
    • Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase
    • Singh R, Green MR. 1993. Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase. Science 259: 365-368.
    • (1993) Science , vol.259 , pp. 365-368
    • Singh, R.1    Green, M.R.2
  • 23
    • 0030746213 scopus 로고    scopus 로고
    • Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology
    • Sirover MA. 1997. Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology. J Cell Biochem 66:133-140.
    • (1997) J Cell Biochem , vol.66 , pp. 133-140
    • Sirover, M.A.1
  • 24
    • 0030035970 scopus 로고    scopus 로고
    • Proteins in unexpected locations
    • Smalheiser NR. 1996. Proteins in unexpected locations. Mol Biol Cell 7:1003-1014.
    • (1996) Mol Biol Cell , vol.7 , pp. 1003-1014
    • Smalheiser, N.R.1
  • 25
    • 0025083511 scopus 로고
    • Analysis of the binding of glyceraldehyde-3-phosphate dehydrogenase to microtubules, the mechanism of bundle formation and the linkage effect
    • Somers M, Engelborghs Y, Beart J. 1990. Analysis of the binding of glyceraldehyde-3-phosphate dehydrogenase to microtubules, the mechanism of bundle formation and the linkage effect. Eur J Biochem 193:437-444.
    • (1990) Eur J Biochem , vol.193 , pp. 437-444
    • Somers, M.1    Engelborghs, Y.2    Beart, J.3
  • 26
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 27
    • 0020478636 scopus 로고
    • Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase
    • Tsai I-H, Murthy SNP, Stack TL. 1982. Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 257:1438-1442.
    • (1982) J Biol Chem , vol.257 , pp. 1438-1442
    • Tsai, I.-H.1    Murthy, S.N.P.2    Stack, T.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.