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Volumn 393, Issue 9, 2012, Pages 959-970

Characterisation and metabolism of astroglia-rich primary cultures from cathepsin K-deficient mice

Author keywords

Astrocytes; Cysteine cathepsins; Energy metabolism; Glutathione metabolism; Oligodendrocytes

Indexed keywords

CATHEPSIN B; CATHEPSIN K; CATHEPSIN L; GAMMA GLUTAMYLTRANSFERASE; GLUTATHIONE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; LACTIC ACID; MYELIN ASSOCIATED GLYCOPROTEIN; MYELIN BASIC PROTEIN;

EID: 84869411676     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2012-0145     Document Type: Conference Paper
Times cited : (11)

References (59)
  • 1
    • 84860389887 scopus 로고    scopus 로고
    • Imaging of protease functions - Current guide to spotting cysteine cathepsins in classical and novel scenes of action in mammalian epithelial cells and tissues
    • Arampatzidou, M., Rehders, M., Dauth, S., Yu, D.M., Tedelind, S., and Brix, K. (2011). Imaging of protease functions - current guide to spotting cysteine cathepsins in classical and novel scenes of action in mammalian epithelial cells and tissues. Ital. J. Anat. Embryol. 116, 1-19.
    • (2011) Ital. J. Anat. Embryol. , vol.116 , pp. 1-19
    • Arampatzidou, M.1    Rehders, M.2    Dauth, S.3    Yu, D.M.4    Tedelind, S.5    Brix, K.6
  • 3
    • 77952394341 scopus 로고    scopus 로고
    • Glucose and lactate supply to the synapse
    • Barros, L.F. and Deitmer, J.W. (2010). Glucose and lactate supply to the synapse. Brain Res. Rev. 63, 149-159.
    • (2010) Brain Res. Rev. , vol.63 , pp. 149-159
    • Barros, L.F.1    Deitmer, J.W.2
  • 4
    • 0035066639 scopus 로고    scopus 로고
    • Biology of oligodendrocyte and myelin in the mammalian central nervous system
    • Baumann, N. and Pham-Dinh, D. (2001). Biology of oligodendrocyte and myelin in the mammalian central nervous system. Physiol. Rev. 81, 871-927.
    • (2001) Physiol. Rev. , vol.81 , pp. 871-927
    • Baumann, N.1    Pham-Dinh, D.2
  • 5
    • 34249674580 scopus 로고    scopus 로고
    • Binding and inhibition assays for Siglecs
    • Bock, N. and Kelm, S. (2006). Binding and inhibition assays for Siglecs. Methods Mol. Biol. 347, 359-375.
    • (2006) Methods Mol. Biol. , vol.347 , pp. 359-375
    • Bock, N.1    Kelm, S.2
  • 6
    • 83855162737 scopus 로고    scopus 로고
    • The antiretroviral protease inhibitors indinavir and nelfi - Navir stimulate Mrp1-mediated GSH export from cultured brain astrocytes
    • Brandmann, M., Tulpule, K., Schmidt, M.M., and Dringen, R. (2012). The antiretroviral protease inhibitors indinavir and nelfi - navir stimulate Mrp1-mediated GSH export from cultured brain astrocytes. J. Neurochem. 120, 78-92.
    • (2012) J. Neurochem. , vol.120 , pp. 78-92
    • Brandmann, M.1    Tulpule, K.2    Schmidt, M.M.3    Dringen, R.4
  • 7
    • 38649111363 scopus 로고    scopus 로고
    • Cysteine cathepsins: Cellular roadmap to different functions
    • Brix, K., Dunkhorst, A., Mayer, K., and Jordans, S. (2008). Cysteine cathepsins: cellular roadmap to different functions. Biochimie 90, 194-207.
    • (2008) Biochimie , vol.90 , pp. 194-207
    • Brix, K.1    Dunkhorst, A.2    Mayer, K.3    Jordans, S.4
  • 8
    • 0029310512 scopus 로고
    • Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution
    • Bromme, D. and Okamoto, K. (1995). Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution. Biol. Chem. Hoppe Seyler 376, 379-384.
    • (1995) Biol. Chem. Hoppe Seyler , vol.376 , pp. 379-384
    • Bromme, D.1    Okamoto, K.2
  • 12
    • 79960666941 scopus 로고    scopus 로고
    • Cathepsin K defi ciency in mice induces structural and metabolic changes in the central nervous system that are associated with learning and memory defi cits
    • Dauth, S., Sirbulescu, R.F., Jordans, S., Rehders, M., Avena, L., Oswald, J., Lerchl, A., Saftig, P., and Brix, K. (2011b). Cathepsin K defi ciency in mice induces structural and metabolic changes in the central nervous system that are associated with learning and memory defi cits. BMC. Neurosci. 12, 74.
    • (2011) BMC. Neurosci. , vol.12 , pp. 74
    • Dauth, S.1    Sirbulescu, R.F.2    Jordans, S.3    Rehders, M.4    Avena, L.5    Oswald, J.6    Lerchl, A.7    Saftig, P.8    Brix, K.9
  • 13
    • 0034672943 scopus 로고    scopus 로고
    • Metabolism and functions of glutathione in brain
    • Dringen, R. (2000). Metabolism and functions of glutathione in brain. Prog. Neurobiol. 62, 649-671.
    • (2000) Prog. Neurobiol. , vol.62 , pp. 649-671
    • Dringen, R.1
  • 14
    • 0029836312 scopus 로고    scopus 로고
    • Glutathione content as an indicator for the presence of metabolic pathways of amino acids in astroglial cultures
    • Dringen, R. and Hamprecht B. (1996). Glutathione content as an indicator for the presence of metabolic pathways of amino acids in astroglial cultures. J. Neurochem. 67, 1375-1382.
    • (1996) J. Neurochem. , vol.67 , pp. 1375-1382
    • Dringen, R.1    Hamprecht, B.2
  • 15
    • 0038636003 scopus 로고    scopus 로고
    • Glutathione pathways in the brain
    • Dringen, R. and Hirrlinger, J. (2003). Glutathione pathways in the brain. Biol. Chem. 384, 505-516.
    • (2003) Biol. Chem. , vol.384 , pp. 505-516
    • Dringen, R.1    Hirrlinger, J.2
  • 16
    • 0027216810 scopus 로고
    • Glycogen in astrocytes: Possible function as lactate supply for neighboring cells
    • Dringen, R., Gebhardt, R., and Hamprecht, B. (1993). Glycogen in astrocytes: possible function as lactate supply for neighboring cells. Brain Res. 623, 208-214.
    • (1993) Brain Res. , vol.623 , pp. 208-214
    • Dringen, R.1    Gebhardt, R.2    Hamprecht, B.3
  • 17
    • 0031004608 scopus 로고    scopus 로고
    • The gammaglutamyl transpeptidase inhibitor acivicin preserves glutathione released by astroglial cells in culture
    • Dringen, R., Kranich, O. and Hamprecht, B. (1997). The gammaglutamyl transpeptidase inhibitor acivicin preserves glutathione released by astroglial cells in culture. Neurochem. Res. 22, 727-733.
    • (1997) Neurochem. Res. , vol.22 , pp. 727-733
    • Dringen, R.1    Kranich, O.2    Hamprecht, B.3
  • 18
    • 0031808935 scopus 로고    scopus 로고
    • Detoxifi cation of exogenous hydrogen peroxide and organic hydroperoxides by cultured astroglial cells assessed by microtiter plate assay
    • Dringen, R., Kussmaul, L., and Hamprecht, B. (1998). Detoxifi cation of exogenous hydrogen peroxide and organic hydroperoxides by cultured astroglial cells assessed by microtiter plate assay. Brain Res. Protoc. 2, 223-228.
    • (1998) Brain Res. Protoc. , vol.2 , pp. 223-228
    • Dringen, R.1    Kussmaul, L.2    Hamprecht, B.3
  • 19
    • 0033555806 scopus 로고    scopus 로고
    • Synthesis of the antioxidant glutathione in neurons: Supply by astrocytes of CysGly as precursor for neuronal glutathione
    • Dringen, R., Pfeiffer, B., and Hamprecht, B. (1999). Synthesis of the antioxidant glutathione in neurons: supply by astrocytes of CysGly as precursor for neuronal glutathione. J. Neurosci. 19, 562-569.
    • (1999) J. Neurosci. , vol.19 , pp. 562-569
    • Dringen, R.1    Pfeiffer, B.2    Hamprecht, B.3
  • 20
    • 42549146494 scopus 로고    scopus 로고
    • Glutamate induces release of glutathione from cultured rat astrocytes - A possible neuroprotective mechanism?
    • Frade, J., Pope, S., Schmidt, M., Dringen, R., Barbosa, R., Pocock, J., Laranjinha, J., and Heales, S. (2008). Glutamate induces release of glutathione from cultured rat astrocytes - a possible neuroprotective mechanism? J. Neurochem. 105, 1144-1152.
    • (2008) J Neurochem. , vol.105 , pp. 1144-1152
    • Frade, J.1    Pope, S.2    Schmidt, M.3    Dringen, R.4    Barbosa, R.5    Pocock, J.6    Laranjinha, J.7    Heales, S.8
  • 22
    • 4043110513 scopus 로고    scopus 로고
    • Lactate metabolism: A new paradigm for the third millennium
    • Gladden, L.B. (2004). Lactate metabolism: a new paradigm for the third millennium. J. Physiol. 558, 5-30.
    • (2004) J. Physiol. , vol.558 , pp. 5-30
    • Gladden, L.B.1
  • 23
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The fi rst enzymatic step in mercapturic acid formation
    • Habig, W.H., Pabst, M.J., and Jakoby, W.B. (1974). Glutathione S-transferases. The fi rst enzymatic step in mercapturic acid formation. J. Biol. Chem. 249, 7130-7139.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 25
    • 0021893839 scopus 로고
    • Primary glial cultures as a model for studying hormone action
    • Hamprecht, B. and Loffl er, F. (1985). Primary glial cultures as a model for studying hormone action. Methods Enzymol. 109, 341-345.
    • (1985) Methods Enzymol. , vol.109 , pp. 341-345
    • Hamprecht, B.1    Loffl Er, F.2
  • 26
    • 77952356102 scopus 로고    scopus 로고
    • The cytosolic redox state of astrocytes: Maintenance, regulation and functional implications for metabolite traffi cking
    • Hirrlinger, J. and Dringen, R. (2010). The cytosolic redox state of astrocytes: Maintenance, regulation and functional implications for metabolite traffi cking. Brain Res. Rev. 63, 177-188.
    • (2010) Brain Res. Rev. , vol.63 , pp. 177-188
    • Hirrlinger, J.1    Dringen, R.2
  • 27
    • 0036328365 scopus 로고    scopus 로고
    • Oligodendroglial cells in culture effectively dispose of exogenous hydrogen peroxide: Comparison with cultured neurones, astroglial and microglial cells
    • Hirrlinger, J., Resch, A., Gutterer, J.M., and Dringen, R. (2002). Oligodendroglial cells in culture effectively dispose of exogenous hydrogen peroxide: comparison with cultured neurones, astroglial and microglial cells. J. Neurochem. 82, 635-644.
    • (2002) J. Neurochem. , vol.82 , pp. 635-644
    • Hirrlinger, J.1    Resch, A.2    Gutterer, J.M.3    Dringen, R.4
  • 28
    • 71049188177 scopus 로고    scopus 로고
    • Monitoring compartment- specifi c substrate cleavage by cathepsins B, K, L, and S at physiological pH and redox conditions
    • Jordans, S., Jenko-Kokalj, S., Kuhl, N.M., Tedelind, S., Sendt, W., Bromme, D., Turk, D., and Brix, K. (2009). Monitoring compartment- specifi c substrate cleavage by cathepsins B, K, L, and S at physiological pH and redox conditions. BMC Biochem. 10, 23.
    • (2009) BMC Biochem. , vol.10 , pp. 23
    • Jordans, S.1    Jenko-Kokalj, S.2    Kuhl, N.M.3    Tedelind, S.4    Sendt, W.5    Bromme, D.6    Turk, D.7    Brix, K.8
  • 29
  • 31
    • 77956602111 scopus 로고    scopus 로고
    • Astrocytes retain their antioxidant capacity into advanced old age
    • Liddell, J.R., Robinson, S.R., Dringen, R., and Bishop, G.M. (2010). Astrocytes retain their antioxidant capacity into advanced old age. Glia 58, 1500-1509.
    • (2010) Glia , vol.58 , pp. 1500-1509
    • Liddell, J.R.1    Robinson, S.R.2    Dringen, R.3    Bishop, G.M.4
  • 33
    • 79951786397 scopus 로고    scopus 로고
    • GFAP in health and disease
    • Middeldorp, J. and Hol, E.M. (2011). GFAP in health and disease. Prog. Neurobiol. 93, 421-443.
    • (2011) Prog. Neurobiol. , vol.93 , pp. 421-443
    • Middeldorp, J.1    Hol, E.M.2
  • 34
    • 33645304045 scopus 로고    scopus 로고
    • The multidrug resistance protein 1 (Mrp1), but not Mrp5, mediates export of glutathione and glutathione disulfi de from brain astrocytes
    • Minich, T., Riemer, J., Schulz, J.B., Wielinga, P., Wijnholds J., and Dringen, R. (2006). The multidrug resistance protein 1 (Mrp1), but not Mrp5, mediates export of glutathione and glutathione disulfi de from brain astrocytes. J. Neurochem. 97, 373-384.
    • (2006) J. Neurochem. , vol.97 , pp. 373-384
    • Minich, T.1    Riemer, J.2    Schulz, J.B.3    Wielinga, P.4    Wijnholds, J.5    Dringen, R.6
  • 35
    • 0018609721 scopus 로고
    • A simple, versatile, sensitive and volume-independent method for quantitative protein determination which is independent of other external infl uences
    • Neuhoff, V., Philipp, K., Zimmer, H.G., and Mesecke, S. (1979). A simple, versatile, sensitive and volume-independent method for quantitative protein determination which is independent of other external infl uences. Hoppe Seylers Z. Physiol. Chem. 360, 1657-1670.
    • (1979) Hoppe Seylers Z. Physiol. Chem. , vol.360 , pp. 1657-1670
    • Neuhoff, V.1    Philipp, K.2    Zimmer, H.G.3    Mesecke, S.4
  • 38
    • 0033802292 scopus 로고    scopus 로고
    • Regulation of elastinolytic cysteine proteinase activity in normal and cathepsin K-defi cient human macrophages
    • Punturieri, A., Filippov, S., Allen, E., Caras, I., Murray, R., Reddy, V., and Weiss S.J. (2000). Regulation of elastinolytic cysteine proteinase activity in normal and cathepsin K-defi cient human macrophages. J. Exp. Med. 192, 789-799.
    • (2000) J. Exp. Med. , vol.192 , pp. 789-799
    • Punturieri, A.1    Filippov, S.2    Allen, E.3    Caras, I.4    Murray, R.5    Reddy, V.6    Weiss, S.J.7
  • 39
    • 0742322783 scopus 로고    scopus 로고
    • TNF alpha increases activity of gamma-glutamyl transpeptidase in cultured rat astroglial cells
    • Ruedig, C. and Dringen, R. (2004). TNF alpha increases activity of gamma-glutamyl transpeptidase in cultured rat astroglial cells. J. Neurosci. Res. 75, 536-543.
    • (2004) J. Neurosci. Res. , vol.75 , pp. 536-543
    • Ruedig, C.1    Dringen, R.2
  • 41
    • 0029988384 scopus 로고    scopus 로고
    • Glutathione effl ux from cultured astrocytes
    • Sagara, J., Makino, N., and Bannai, S. (1996). Glutathione effl ux from cultured astrocytes. J. Neurochem. 66, 1876-1881.
    • (1996) J. Neurochem. , vol.66 , pp. 1876-1881
    • Sagara, J.1    Makino, N.2    Bannai, S.3
  • 42
    • 79958083851 scopus 로고    scopus 로고
    • Copper-treatment increases the cellular GSH content and accelerates GSH export from cultured rat astrocytes
    • Scheiber, I.F., and Dringen, R. (2011). Copper-treatment increases the cellular GSH content and accelerates GSH export from cultured rat astrocytes. Neurosci. Lett. 498, 42-46.
    • (2011) Neurosci. Lett. , vol.498 , pp. 42-46
    • Scheiber, I.F.1    Dringen, R.2
  • 43
    • 77952327640 scopus 로고    scopus 로고
    • Differential effects of iodoacetamide and iodoacetate on glycolysis and glutathione metabolism of cultured astrocytes
    • Schmidt, M.M. and Dringen, R. (2009). Differential effects of iodoacetamide and iodoacetate on glycolysis and glutathione metabolism of cultured astrocytes. Front. Neuroenergetics 1, 1.
    • (2009) Front. Neuroenergetics , vol.1 , pp. 1
    • Schmidt, M.M.1    Dringen, R.2
  • 44
    • 77956228055 scopus 로고    scopus 로고
    • Fumaric acid diesters deprive cultured primary astrocytes rapidly of glutathione
    • Schmidt, M.M. and Dringen, R. (2010). Fumaric acid diesters deprive cultured primary astrocytes rapidly of glutathione. Neurochem. Int. 57, 460-467.
    • (2010) Neurochem. Int. , vol.57 , pp. 460-467
    • Schmidt, M.M.1    Dringen, R.2
  • 47
    • 79958150830 scopus 로고    scopus 로고
    • Effects of chlorinated acetates on the glutathione metabolism and on glycolysis of cultured astrocytes
    • Schmidt, M.M., Rohwedder A., and Dringen, R. (2011). Effects of chlorinated acetates on the glutathione metabolism and on glycolysis of cultured astrocytes. Neurotox. Res. 19, 628-637.
    • (2011) Neurotox. Res. , vol.19 , pp. 628-637
    • Schmidt, M.M.1    Rohwedder, A.2    Dringen, R.3
  • 48
    • 0019420888 scopus 로고
    • A fl uorometric assay for gamma-glutamyl transpeptidase: Demonstration enzymatic activity in cultured cells of neural origin
    • Shine, H.D., Hertz, L., De Vellis, J. and Haber, B. (1981). A fl uorometric assay for gamma-glutamyl transpeptidase: demonstration enzymatic activity in cultured cells of neural origin. Neurochem. Res. 6, 453-463.
    • (1981) Neurochem. Res. , vol.6 , pp. 453-463
    • Shine, H.D.1    Hertz, L.2    De Vellis, J.3    Haber, B.4
  • 49
    • 33751514940 scopus 로고    scopus 로고
    • Neuron-glia communication in the control of oligodendrocyte function and myelin biogenesis
    • Simons, M. and Trajkovic, K. (2006). Neuron-glia communication in the control of oligodendrocyte function and myelin biogenesis. J. Cell Sci. 119, 4381-4389.
    • (2006) J. Cell Sci. , vol.119 , pp. 4381-4389
    • Simons, M.1    Trajkovic, K.2
  • 51
    • 84869483088 scopus 로고    scopus 로고
    • Effect of reduced glutathione (GSH) on activity of lysosomal system in subcellular fractions of mouse kidney
    • Sliwa-Jozwik, A., Jozwik, A., Fronczyk, Guszkiewicz, W.A., and Kolataj, A. (2004). Effect of reduced glutathione (GSH) on activity of lysosomal system in subcellular fractions of mouse kidney. Anim. Sci. Pap. and Rep. 22, 237-245.
    • (2004) Anim. Sci. Pap. and Rep. , vol.22 , pp. 237-245
    • Sliwa-Jozwik, A.1    Jozwik, A.2    Fronczyk Guszkiewicz, W.A.3    Kolataj, A.4
  • 52
  • 53
    • 0023831025 scopus 로고
    • Changes in the activity of gamma-glutamyl transpeptidase in brain microvessels, astroglial cells and synaptosomes derived from rats with hepatic encephalopathy
    • Stastny, F., Hilgier, W., Albrecht, J., and Lisy, V. (1988). Changes in the activity of gamma-glutamyl transpeptidase in brain microvessels, astroglial cells and synaptosomes derived from rats with hepatic encephalopathy. Neurosci. Lett. 84, 323-328.
    • (1988) Neurosci. Lett. , vol.84 , pp. 323-328
    • Stastny, F.1    Hilgier, W.2    Albrecht, J.3    Lisy, V.4
  • 54
    • 0034502852 scopus 로고    scopus 로고
    • Cathepsin K in thyroid epithelial cells: Sequence, localization and possible function in extracellular proteolysis of thyroglobulin
    • Tepel, C., Bromme, D., Herzog, V., and Brix, K. (2000). Cathepsin K in thyroid epithelial cells: sequence, localization and possible function in extracellular proteolysis of thyroglobulin. J. Cell Sci. 113, 4487-4498.
    • (2000) J. Cell Sci. , vol.113 , pp. 4487-4498
    • Tepel, C.1    Bromme, D.2    Herzog, V.3    Brix, K.4
  • 55
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • Tietze, F. (1969). Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal. Biochem. 27, 502-522.
    • (1969) Anal. Biochem. , vol.27 , pp. 502-522
    • Tietze, F.1
  • 57
  • 59
    • 77956187502 scopus 로고    scopus 로고
    • Neuronal activity in vitro and the in vivo reality: The role of energy homeostasis
    • Zilberter, Y., Zilberter, T., and Bregestovski, P. (2010). Neuronal activity in vitro and the in vivo reality: the role of energy homeostasis. Trends Pharmacol. Sci. 31, 394-401.
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 394-401
    • Zilberter, Y.1    Zilberter, T.2    Bregestovski, P.3


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