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Volumn 2, Issue 1, 2003, Pages 24-36

A novel method of imaging lysosomes in living human mammary epithelial cells

Author keywords

Breast cancer; Fluorescence microscopy; Fluorescent probe; Lysosomes; Trafficking

Indexed keywords

AMINO ACIDS; ANTIBODIES; CELLS; ENZYME KINETICS; ENZYMES; FLUORESCENCE; NONINVASIVE MEDICAL PROCEDURES; ONCOLOGY; PATHOLOGY; PROBES; TUMORS;

EID: 0042975439     PISSN: 15353508     EISSN: None     Source Type: Journal    
DOI: 10.1162/153535003765276264     Document Type: Article
Times cited : (8)

References (65)
  • 1
    • 0027535914 scopus 로고
    • Biology and biochemistry of proteinases in tumor invasion
    • Mignatti P, Rifkin DB (1993). Biology and biochemistry of proteinases in tumor invasion. Physiol Rev. 73:161-195.
    • (1993) Physiol Rev. , vol.73 , pp. 161-195
    • Mignatti, P.1    Rifkin, D.B.2
  • 2
    • 0031774869 scopus 로고    scopus 로고
    • Inhibition of tumour cell invasion by protease inhibitors: Correlation with the protease profile
    • Kolkhorst V, Sturzebecher J, Wiederanders B (1998). Inhibition of tumour cell invasion by protease inhibitors: Correlation with the protease profile. J Cancer Res Clin Oncol. 124:598-606.
    • (1998) J Cancer Res Clin Oncol. , vol.124 , pp. 598-606
    • Kolkhorst, V.1    Sturzebecher, J.2    Wiederanders, B.3
  • 3
    • 0026522287 scopus 로고
    • The role of proteolytic enzymes in cancer invasion and metastasis
    • Duffy MJ (1992). The role of proteolytic enzymes in cancer invasion and metastasis. Clin Exp Metastasis. 10:145-155.
    • (1992) Clin Exp Metastasis , vol.10 , pp. 145-155
    • Duffy, M.J.1
  • 4
    • 0345643514 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase expression in tumor invasion
    • Westermarck J, Kahari VM (1999). Regulation of matrix metalloproteinase expression in tumor invasion. FASEB J. 13:781-792.
    • (1999) FASEB J. , vol.13 , pp. 781-792
    • Westermarck, J.1    Kahari, V.M.2
  • 5
    • 0025610853 scopus 로고
    • The role of urokinase-type plasminogen activator in aggressive tumor cell behavior
    • Testa JE, Quigley JP (1999). The role of urokinase-type plasminogen activator in aggressive tumor cell behavior. Cancer Metastasis Rev. 9:353-367.
    • (1990) Cancer Metastasis Rev. , vol.9 , pp. 353-367
    • Testa, J.E.1    Quigley, J.P.2
  • 7
    • 0025676568 scopus 로고
    • Cathepsin B and its endogenous inhibitors: The role in tumor malignancy
    • Sloan BF, Moin K, Krepela E, Rozhin J (1990). Cathepsin B and its endogenous inhibitors: The role in tumor malignancy. Cancer Metastasis Rev. 9:333-352.
    • (1990) Cancer Metastasis Rev. , vol.9 , pp. 333-352
    • Sloan, B.F.1    Moin, K.2    Krepela, E.3    Rozhin, J.4
  • 8
    • 0025413403 scopus 로고
    • The role of cathepsin L in malignant transformation
    • Kane SE, Gottesman MM (1990). The role of cathepsin L in malignant transformation. Semin Cancer Biol. 1:127-136.
    • (1990) Semin Cancer Biol. , vol.1 , pp. 127-136
    • Kane, S.E.1    Gottesman, M.M.2
  • 10
    • 0025423520 scopus 로고
    • "In vitro" digestion of intact bovine lens capsules by four human lysosomal cysteine-proteinases
    • Guinec N, Pagano M, Dalet-Fumeron V, Engler R (1990). "In vitro" digestion of intact bovine lens capsules by four human lysosomal cysteine-proteinases. Biol Chem Hoppe-Seyler. 371:239-254.
    • (1990) Biol Chem Hoppe-Seyler , vol.371 , pp. 239-254
    • Guinec, N.1    Pagano, M.2    Dalet-Fumeron, V.3    Engler, R.4
  • 11
    • 0027329828 scopus 로고
    • "In vitro" study of basement membrane degradation by the cysteine proteinases, cathepsins B, B-like and L. Digestion of collagen IV, laminin, fibronectin, and release of gelatinase activities from basement membrane fibronectin
    • Guinec N, Dalet-Fumeron V, Pagano M (1993). "In vitro" study of basement membrane degradation by the cysteine proteinases, cathepsins B, B-like and L. Digestion of collagen IV, laminin, fibronectin, and release of gelatinase activities from basement membrane fibronectin. Biol Chem Hoppe-Seyler. 374:1135-1146.
    • (1993) Biol Chem Hoppe-Seyler , vol.374 , pp. 1135-1146
    • Guinec, N.1    Dalet-Fumeron, V.2    Pagano, M.3
  • 12
    • 0026575258 scopus 로고
    • Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumour tissues
    • Buck MR, Karustis DG, Day NA, Honn KV, Sloane BF (1992). Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumour tissues. Biochem J. 282:273-278.
    • (1992) Biochem J. , vol.282 , pp. 273-278
    • Buck, M.R.1    Karustis, D.G.2    Day, N.A.3    Honn, K.V.4    Sloane, B.F.5
  • 13
    • 0025845425 scopus 로고
    • Cathepsin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinase-type plasminogen activator (Pro-uPA)
    • Kobayashi H, Schmitt M, Goretzki L, Chucholowski N, Calvete J, Kramer M, Gunzler WA, Janicke F, Graeff H (1991). Cathepsin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinase-type plasminogen activator (Pro-uPA). J Biol Chem. 266:5147-5152.
    • (1991) J Biol Chem. , vol.266 , pp. 5147-5152
    • Kobayashi, H.1    Schmitt, M.2    Goretzki, L.3    Chucholowski, N.4    Calvete, J.5    Kramer, M.6    Gunzler, W.A.7    Janicke, F.8    Graeff, H.9
  • 14
    • 0026734254 scopus 로고
    • Inhibition of in vitro ovarian cancer cell invasion by modulation of urokinase-type plasminogen activator and cathepsin B
    • Kobayashi H, Ohi H, Sugimura M, Shinohara H, Fujii T, Terao T (1992). Inhibition of in vitro ovarian cancer cell invasion by modulation of urokinase-type plasminogen activator and cathepsin B. Cancer Res. 52:3610-3614.
    • (1992) Cancer Res. , vol.52 , pp. 3610-3614
    • Kobayashi, H.1    Ohi, H.2    Sugimura, M.3    Shinohara, H.4    Fujii, T.5    Terao, T.6
  • 15
    • 0027015335 scopus 로고
    • Physiological mechanisms for metalloproteinase activation
    • Murphy G, Ward R, Gavrilovic J, Atkinson S (1992). Physiological mechanisms for metalloproteinase activation. Matrix Suppl. 1:224-230.
    • (1992) Matrix Suppl. , vol.1 , pp. 224-230
    • Murphy, G.1    Ward, R.2    Gavrilovic, J.3    Atkinson, S.4
  • 16
    • 0028618307 scopus 로고
    • Pericellular pH affects distribution and secretion of cathepsin B in malignant cells
    • Rozhin J, Sameni M, Ziegler G, Sloane BF (1994). Pericellular pH affects distribution and secretion of cathepsin B in malignant cells. Cancer Res. 54:6517-6525.
    • (1994) Cancer Res. , vol.54 , pp. 6517-6525
    • Rozhin, J.1    Sameni, M.2    Ziegler, G.3    Sloane, B.F.4
  • 17
    • 0031059664 scopus 로고    scopus 로고
    • Exposure to hypoxia, glucose starvation and acidosis: Effect on invasive capacity of murine tumor cells and correlation with cathepsin (L + B) secretion
    • Cuvier C, Jang A, Hill RP (1997). Exposure to hypoxia, glucose starvation and acidosis: Effect on invasive capacity of murine tumor cells and correlation with cathepsin (L + B) secretion. Clin Exp Metastasis. 15:19-25.
    • (1997) Clin Exp Metastasis , vol.15 , pp. 19-25
    • Cuvier, C.1    Jang, A.2    Hill, R.P.3
  • 18
    • 0028820625 scopus 로고
    • A lysosomal targeting signal in the cytoplasmic tail of the beta chain directs HIA-DM to MHC class II compartments
    • Marks MS, Roche PA, van Donselaar E, Woodruff L, Peters PJ, Bonifacino JS (1995). A lysosomal targeting signal in the cytoplasmic tail of the beta chain directs HIA-DM to MHC class II compartments. J Cell Biol. 131:351-369.
    • (1995) J Cell Biol. , vol.131 , pp. 351-369
    • Marks, M.S.1    Roche, P.A.2    Van Donselaar, E.3    Woodruff, L.4    Peters, P.J.5    Bonifacino, J.S.6
  • 19
    • 0024429248 scopus 로고
    • Osteoclast biology: Lessons from mammalian mutations
    • Marks SC, Jr. (1989). Osteoclast biology: Lessons from mammalian mutations. Am J Med Genet. 34:43-54.
    • (1989) Am J Med Genet. , vol.34 , pp. 43-54
    • Marks S.C., Jr.1
  • 20
    • 0025888871 scopus 로고
    • Degradation of epidermal growth factor receptor in rat liver. Membrane topology through the lysosomal pathway
    • Renfrew CA, Hubbard AL (1991). Degradation of epidermal growth factor receptor in rat liver. Membrane topology through the lysosomal pathway. J Biol Chem. 266:21265-21273.
    • (1991) J Biol Chem. , vol.266 , pp. 21265-21273
    • Renfrew, C.A.1    Hubbard, A.L.2
  • 21
    • 0015223736 scopus 로고
    • Lysosomal changes and enhanced metastatic growth: An experimental study of the effects of some non-ionic surfactants
    • Carter RL, Birbeck MS, Stock JA (1971). Lysosomal changes and enhanced metastatic growth: An experimental study of the effects of some non-ionic surfactants. Int J Cancer. 7:34-49.
    • (1971) Int J Cancer. , vol.7 , pp. 34-49
    • Carter, R.L.1    Birbeck, M.S.2    Stock, J.A.3
  • 22
    • 0018950699 scopus 로고
    • Elevation of lysosomal enzymes in primary Lewis lung tumor correlated with the initiation of metastasis
    • Dobrossy L, Pavelic ZP, Vaughan M, Porter N, Bernacki RJ (1980). Elevation of lysosomal enzymes in primary Lewis lung tumor correlated with the initiation of metastasis. Cancer Res. 40:3281-3285.
    • (1980) Cancer Res. , vol.40 , pp. 3281-3285
    • Dobrossy, L.1    Pavelic, Z.P.2    Vaughan, M.3    Porter, N.4    Bernacki, R.J.5
  • 23
    • 0019797924 scopus 로고
    • Lysosomal cathepsin B: Correlation with metastatic potential
    • Sloane BF, Dunn JR, Honn KV (1981). Lysosomal cathepsin B: Correlation with metastatic potential. Science. 212:1151-1153.
    • (1981) Science , vol.212 , pp. 1151-1153
    • Sloane, B.F.1    Dunn, J.R.2    Honn, K.V.3
  • 24
    • 0028287546 scopus 로고
    • Estrogen receptor-Sp1 complexes mediate estrogen-induced cathepsin D gene expression in MCF-7 human breast cancer cells
    • Krishnan V, Wang X, Safe S (1994). Estrogen receptor-Sp1 complexes mediate estrogen-induced cathepsin D gene expression in MCF-7 human breast cancer cells. J Biol Chem. 269:15912-15917.
    • (1994) J Biol Chem. , vol.269 , pp. 15912-15917
    • Krishnan, V.1    Wang, X.2    Safe, S.3
  • 25
    • 0026001074 scopus 로고
    • Estradiol down-regulates the mannose-6-phosphate/insulin-like growth factor-II receptor gene and induces cathepsin-D in breast cancer cells: A receptor saturation mechanism to increase the secretion of lysosomal proenzymes
    • Mathieu M, Vignon F, Capony F, Rochefort H (1991). Estradiol down-regulates the mannose-6-phosphate/insulin-like growth factor-II receptor gene and induces cathepsin-D in breast cancer cells: A receptor saturation mechanism to increase the secretion of lysosomal proenzymes. Mol Endocrinol. 5:815-822.
    • (1991) Mol Endocrinol. , vol.5 , pp. 815-822
    • Mathieu, M.1    Vignon, F.2    Capony, F.3    Rochefort, H.4
  • 28
    • 0024238385 scopus 로고
    • Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences
    • Fukuda M, Viitala J, Matteson J, Carlsson SR (1988). Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences. J Biol Chem. 263:18920-18928.
    • (1988) J Biol Chem. , vol.263 , pp. 18920-18928
    • Fukuda, M.1    Viitala, J.2    Matteson, J.3    Carlsson, S.R.4
  • 30
    • 0033134175 scopus 로고    scopus 로고
    • Differential expression of the lysosome-associated membrane proteins in normal human tissues
    • Furuta K, Yang XL, Chen JS, Hamilton SR, August JT (1999). Differential expression of the lysosome-associated membrane proteins in normal human tissues. Arch Biochem Biophys. 365:75-82.
    • (1999) Arch Biochem Biophys. , vol.365 , pp. 75-82
    • Furuta, K.1    Yang, X.L.2    Chen, J.S.3    Hamilton, S.R.4    August, J.T.5
  • 31
    • 0021738226 scopus 로고
    • Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes
    • Twining SS (1984). Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes. Anal Biochem. 143:30-34.
    • (1984) Anal Biochem. , vol.143 , pp. 30-34
    • Twining, S.S.1
  • 32
    • 0031554927 scopus 로고    scopus 로고
    • Quenched BODIPY dye-labeled casein substrates for the assay of protease activity by direct fluorescence measurement
    • Jones LJ, Upson RH, Haugland RP, Panchuk-Voloshina N, Zhou M (1997). Quenched BODIPY dye-labeled casein substrates for the assay of protease activity by direct fluorescence measurement. Anal Biochem. 251:144-152.
    • (1997) Anal Biochem. , vol.251 , pp. 144-152
    • Jones, L.J.1    Upson, R.H.2    Haugland, R.P.3    Panchuk-Voloshina, N.4    Zhou, M.5
  • 33
    • 0000086787 scopus 로고
    • Vital staining and fluorescence microscopy of lysosomes
    • In Dingle JT, Fell HB (Eds.); North-Holland, Amsterdam
    • Allison AC, Young MR (1969). Vital staining and fluorescence microscopy of lysosomes. In Dingle JT, Fell HB (Eds.), Lysosomes in Biology and Pathology. North-Holland, Amsterdam. pp. 600-628.
    • (1969) Lysosomes in Biology and Pathology , pp. 600-628
    • Allison, A.C.1    Young, M.R.2
  • 34
    • 0018861183 scopus 로고
    • Lysosomal acridine orange uptake in fibroblasts transformed by SV40 or human cytomegalovirus
    • Redai I, Halmy M (1980). Lysosomal acridine orange uptake in fibroblasts transformed by SV40 or human cytomegalovirus. Acta Microbiol Acad Sci Hung. 27:41-45.
    • (1980) Acta Microbiol Acad Sci Hung. , vol.27 , pp. 41-45
    • Redai, I.1    Halmy, M.2
  • 35
    • 0242509380 scopus 로고    scopus 로고
    • Rhodamine B, a fluorescent probe for acidic organelles in denervated skeletal muscle
    • Vult von Steyern F, Josefsson JO, Tagerud S (1996). Rhodamine B, a fluorescent probe for acidic organelles in denervated skeletal muscle. J Histochem Cytochem. 44:267-274.
    • (1996) J Histochem Cytochem. , vol.44 , pp. 267-274
    • Vult Von Steyern, F.1    Josefsson, J.O.2    Tagerud, S.3
  • 36
    • 0033169080 scopus 로고    scopus 로고
    • A novel acidotropic pH indicator and its potential application in labeling acidic organelles of live cells
    • Diwu Z, Chen CS, Zhang C, Klaubert DH, Haugland RP (1999). A novel acidotropic pH indicator and its potential application in labeling acidic organelles of live cells. Chem Biol. 6:411-418.
    • (1999) Chem Biol. , vol.6 , pp. 411-418
    • Diwu, Z.1    Chen, C.S.2    Zhang, C.3    Klaubert, D.H.4    Haugland, R.P.5
  • 37
    • 0022555867 scopus 로고
    • Acidification of the endocytic and exocytic pathways
    • Mellman I, Fuchs R, Helenius A (1986). Acidification of the endocytic and exocytic pathways. Annu Rev Biochem. 55:663-700.
    • (1986) Annu Rev Biochem. , vol.55 , pp. 663-700
    • Mellman, I.1    Fuchs, R.2    Helenius, A.3
  • 38
    • 0031704477 scopus 로고    scopus 로고
    • Diverse roles of single membrane organelles: Factors establishing the acid lumenal pH
    • Futai M, Oka T, Moriyama Y, Wada Y (1998). Diverse roles of single membrane organelles: Factors establishing the acid lumenal pH. J Biochem (Tokyo). 124:259-267.
    • (1998) J Biochem (Tokyo) , vol.124 , pp. 259-267
    • Futai, M.1    Oka, T.2    Moriyama, Y.3    Wada, Y.4
  • 39
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma S, Poole B (1978). Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc Natl Acad Sci USA. 75:3327-3331.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 40
    • 0025250045 scopus 로고
    • The cDNA sequence of mouse LAMP-2. Evidence for two classes of lysosomal membrane glycoproteins
    • Cha Y, Holland SM, August JT (1990). The cDNA sequence of mouse LAMP-2. Evidence for two classes of lysosomal membrane glycoproteins. J Biol Chem. 265:5008-5013.
    • (1990) J Biol Chem. , vol.265 , pp. 5008-5013
    • Cha, Y.1    Holland, S.M.2    August, J.T.3
  • 41
    • 0025287536 scopus 로고
    • Characterization and cloning of lgp110, a lysosomal membrane glycoprotein from mouse and rat cells
    • Granger BL, Green SA, Gabel CA, Howe CL, Mellman I, Helenius A (1990). Characterization and cloning of lgp110, a lysosomal membrane glycoprotein from mouse and rat cells. J Biol Chem. 265:12036-12043.
    • (1990) J Biol Chem. , vol.265 , pp. 12036-12043
    • Granger, B.L.1    Green, S.A.2    Gabel, C.A.3    Howe, C.L.4    Mellman, I.5    Helenius, A.6
  • 42
    • 0023881180 scopus 로고
    • Structure of LEP100, a glycoprotein that shuttles between lysosomes and the plasma membrane, deduced from the nucleotide sequence of the encoding cDNA
    • Fambrough DM, Takeyasu K, Lippincott-Schwarz J, Siegel NR (1988). Structure of LEP100, a glycoprotein that shuttles between lysosomes and the plasma membrane, deduced from the nucleotide sequence of the encoding cDNA. J Cell Biol. 106:61-67.
    • (1988) J Cell Biol. , vol.106 , pp. 61-67
    • Fambrough, D.M.1    Takeyasu, K.2    Lippincott-Schwarz, J.3    Siegel, N.R.4
  • 43
    • 0032742816 scopus 로고    scopus 로고
    • Asparagine-linked oligosaccharides protect Lamp-1 and Lamp-2 from intracellular proteolysis
    • Kundra R, Kornfeld S (1999). Asparagine-linked oligosaccharides protect Lamp-1 and Lamp-2 from intracellular proteolysis. J Biol Chem. 274:31039-31046.
    • (1999) J Biol Chem. , vol.274 , pp. 31039-31046
    • Kundra, R.1    Kornfeld, S.2
  • 44
    • 0026557242 scopus 로고
    • Characterization of epithelial phenotypes in mortal and immortal human breast cells
    • Paine T.M., Soule H.D., Pauley R.J. Dawson P.J. (1992). Characterization of epithelial phenotypes in mortal and immortal human breast cells. Int J Cancer. 50:463-473.
    • (1992) Int J Cancer. , vol.50 , pp. 463-473
    • Paine, T.M.1    Soule, H.D.2    Pauley, R.J.3    Dawson, P.J.4
  • 45
    • 0015762456 scopus 로고
    • A human cell line from a pleural effusion derived from a breast carcinoma
    • Soule H.D., Varguez J., Long A., Albert S., Brennan M. (1973). A human cell line from a pleural effusion derived from a breast carcinoma. J Natl Cancer Inst. 51:1409-1416.
    • (1973) J Natl Cancer Inst. , vol.51 , pp. 1409-1416
    • Soule, H.D.1    Varguez, J.2    Long, A.3    Albert, S.4    Brennan, M.5
  • 46
    • 0030888196 scopus 로고    scopus 로고
    • Dansyl N-acetyl glucosamine as a precursor of fluorescent chitin: A method to detect fungal cell wall inhibitors
    • Carrano L., Tavecchia P., Sponga F., Spreafico F. (1997). Dansyl N-acetyl glucosamine as a precursor of fluorescent chitin: A method to detect fungal cell wall inhibitors. J Antibiot (Tokyo). 50:177-179.
    • (1997) J Antibiot (Tokyo) , vol.50 , pp. 177-179
    • Carrano, L.1    Tavecchia, P.2    Sponga, F.3    Spreafico, F.4
  • 47
    • 0029799743 scopus 로고    scopus 로고
    • Protecting group strategies in organic synthesis
    • Schelhaas M., Waldmann H. (1996). Protecting group strategies in organic synthesis. Angew Chem Int Ed Engl. 35:2056-2083.
    • (1996) Angew Chem Int Ed Engl. , vol.35 , pp. 2056-2083
    • Schelhaas, M.1    Waldmann, H.2
  • 48
    • 0028167730 scopus 로고
    • Iodixanol: A nonionic iso-osmotic centrifugation medium for the formation of self-generated gradients
    • Ford T., Graham J., Rickwood D. (1994). Iodixanol: A nonionic iso-osmotic centrifugation medium for the formation of self-generated gradients. Anal Biochem. 220:360-366.
    • (1994) Anal Biochem. , vol.220 , pp. 360-366
    • Ford, T.1    Graham, J.2    Rickwood, D.3
  • 49
    • 0028167731 scopus 로고
    • The preparation of subcellular organelles from mouse liver in self-generated gradients of iodixanol
    • Graham J., Ford T., Rickwood D. (1994). The preparation of subcellular organelles from mouse liver in self-generated gradients of iodixanol. Anal Biochem. 220:367-373.
    • (1994) Anal Biochem. , vol.220 , pp. 367-373
    • Graham, J.1    Ford, T.2    Rickwood, D.3
  • 50
    • 0027352793 scopus 로고
    • The identification of subcellular fractions from mammalian cells
    • In Graham JM, Higgins JA (Eds.); Humana Press, Totowa, NJ
    • Graham J.M. (1993). The identification of subcellular fractions from mammalian cells. In Graham JM, Higgins JA (Eds.), Biomembrane Protocols: Methods in Molecular Biology. Humana Press, Totowa, NJ. pp. 1-18.
    • (1993) Biomembrane Protocols: Methods in Molecular Biology , pp. 1-18
    • Graham, J.M.1
  • 51
    • 0016369243 scopus 로고
    • Isolation of rat liver peroxisomes
    • Baudhuin P. (1974). Isolation of rat liver peroxisomes. Methods Enzymol. 31:356-368.
    • (1974) Methods Enzymol. , vol.31 , pp. 356-368
    • Baudhuin, P.1
  • 52
    • 0032893756 scopus 로고    scopus 로고
    • Malignant transformation alters membrane choline phospholipid metabolism of human mammary epithelial cells
    • Aboagye E.O., Bhujwalla Z.M. (1999). Malignant transformation alters membrane choline phospholipid metabolism of human mammary epithelial cells. Cancer Res. 59:80-84.
    • (1999) Cancer Res. , vol.59 , pp. 80-84
    • Aboagye, E.O.1    Bhujwalla, Z.M.2
  • 53
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius A., Aebi M. (2001). Intracellular functions of N-linked glycans. Science. 291:2364-2369.
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 54
    • 0032712592 scopus 로고    scopus 로고
    • Trafficking of oligomannosides released during N-glycosylation: A clearing mechanism of the rough endoplasmic reticulum
    • Verbert A., Cacan R. (1999). Trafficking of oligomannosides released during N-glycosylation: A clearing mechanism of the rough endoplasmic reticulum. Biochim Biophys Acta. 1473:137-146.
    • (1999) Biochim Biophys Acta. , vol.1473 , pp. 137-146
    • Verbert, A.1    Cacan, R.2
  • 55
    • 0036247196 scopus 로고    scopus 로고
    • New prospects for the treatment of lysosomal storage diseases
    • Schiffmann R., Brady R.O. (2002). New prospects for the treatment of lysosomal storage diseases. Drugs. 62:733-742.
    • (2002) Drugs , vol.62 , pp. 733-742
    • Schiffmann, R.1    Brady, R.O.2
  • 56
    • 0036242349 scopus 로고    scopus 로고
    • Gaucher disease: Perspectives on a prototype lysosomal disease
    • Zhao H., Grabowski G.A. (2002). Gaucher disease: Perspectives on a prototype lysosomal disease. Cell Mol Life Sci. 59:694-707.
    • (2002) Cell Mol Life Sci. , vol.59 , pp. 694-707
    • Zhao, H.1    Grabowski, G.A.2
  • 57
    • 0034304390 scopus 로고    scopus 로고
    • The endosomal-lysosomal system of neurons in Alzheimer's disease pathogenesis: A review
    • Nixon R.A., Cataldo A.M., Mathews P.M. (2000). The endosomal-lysosomal system of neurons in Alzheimer's disease pathogenesis: A review. Neurochem Res. 25:1161-1172.
    • (2000) Neurochem Res. , vol.25 , pp. 1161-1172
    • Nixon, R.A.1    Cataldo, A.M.2    Mathews, P.M.3
  • 58
    • 0035159785 scopus 로고    scopus 로고
    • Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease
    • Glabe C. (2001). Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease. J Mol Neurosci. 17:137-145.
    • (2001) J Mol Neurosci. , vol.17 , pp. 137-145
    • Glabe, C.1
  • 59
    • 0034519967 scopus 로고    scopus 로고
    • Surface-targeted lysosomal membrane glycoprotein-1 (Lamp-1) enhances lysosome exocytosis and cell invasion by trypanosoma cruzi
    • Kima P.E., Burleigh B., Andrews N.W. (2000). Surface-targeted lysosomal membrane glycoprotein-1 (Lamp-1) enhances lysosome exocytosis and cell invasion by Trypanosoma cruzi. Cell Microbiol. 2:477-486.
    • (2000) Cell Microbiol. , vol.2 , pp. 477-486
    • Kima, P.E.1    Burleigh, B.2    Andrews, N.W.3
  • 60
    • 0036606805 scopus 로고    scopus 로고
    • When cell biology meets development: Endocytic regulation of signaling pathways
    • Seto E.S., Bellen H.J., Lloyd T.E. (2002). When cell biology meets development: Endocytic regulation of signaling pathways. Genes Dev. 16:1314-1336.
    • (2002) Genes Dev. , vol.16 , pp. 1314-1336
    • Seto, E.S.1    Bellen, H.J.2    Lloyd, T.E.3
  • 61
    • 0037155686 scopus 로고    scopus 로고
    • Fusion and fission: Membrane trafficking in animal cytokinesis
    • Finger F.P., White J.G. (2002). Fusion and fission: Membrane trafficking in animal cytokinesis. Cell. 108:727-730.
    • (2002) Cell , vol.108 , pp. 727-730
    • Finger, F.P.1    White, J.G.2
  • 62
    • 0035074341 scopus 로고    scopus 로고
    • The molecular machinery for lysosome biogenesis
    • Mullins C., Bonifacino J.S. (2001) The molecular machinery for lysosome biogenesis. Bioessays. 23:333-343.
    • (2001) Bioessays , vol.23 , pp. 333-343
    • Mullins, C.1    Bonifacino, J.S.2
  • 63
    • 0035658298 scopus 로고    scopus 로고
    • Actin filaments and myosin I alpha cooperate with microtubules for the movement of lysosomes
    • Cordonnier MN, Dauzonne D, Louvard D, Coudrier E (2001). Actin filaments and myosin I alpha cooperate with microtubules for the movement of lysosomes. Mol Biol Cell. 12: 4013-4029.
    • (2001) Mol Biol Cell , vol.12 , pp. 4013-4029
    • Cordonnier, M.N.1    Dauzonne, D.2    Louvard, D.3    Coudrier, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.