메뉴 건너뛰기




Volumn 144, Issue 2, 2006, Pages 117-126

Effects of phospholipase A2 on the lysosomal ion permeability and osmotic sensitivity

Author keywords

Lysosome; Osmotic sensitivity; Permeability; Phospholipase A2; Potassium ion; Proton

Indexed keywords

BETA N ACETYLHEXOSAMINIDASE; HYDROGEN; PHOSPHOLIPASE A2; POTASSIUM ION; PROTON; SUCROSE; PHOSPHOLIPASE A; POTASSIUM;

EID: 33750957800     PISSN: 00093084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2006.08.003     Document Type: Article
Times cited : (6)

References (62)
  • 1
    • 0023388106 scopus 로고
    • Translocation of sugars into rat liver lysosomes. Evidence against a common carrier for d-glucose and d-ribose
    • Bird S.J., Forster S., and Lloyd J.B. Translocation of sugars into rat liver lysosomes. Evidence against a common carrier for d-glucose and d-ribose. Biochem. J. 245 (1987) 929-931
    • (1987) Biochem. J. , vol.245 , pp. 929-931
    • Bird, S.J.1    Forster, S.2    Lloyd, J.B.3
  • 2
    • 0017280348 scopus 로고
    • Analysis of the pinocytic process in rat kidney. II. Biochemical composition of pinocytic vesicles compared to brush border microvilli, lysosomes and basolateral plasma membranes
    • Bode F., Baumann K., and Kinne R. Analysis of the pinocytic process in rat kidney. II. Biochemical composition of pinocytic vesicles compared to brush border microvilli, lysosomes and basolateral plasma membranes. Biochim. Biophys. Acta 433 (1976) 294-310
    • (1976) Biochim. Biophys. Acta , vol.433 , pp. 294-310
    • Bode, F.1    Baumann, K.2    Kinne, R.3
  • 3
    • 0030757986 scopus 로고    scopus 로고
    • Photo-oxidative disruption of lysosomal membranes causes apoptosis of cultured human fibroblasts
    • Brunk U.T., Dalen H., Roberg K., and Hellquist H.B. Photo-oxidative disruption of lysosomal membranes causes apoptosis of cultured human fibroblasts. Free Radic. Biol. Med. 23 (1997) 616-626
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 616-626
    • Brunk, U.T.1    Dalen, H.2    Roberg, K.3    Hellquist, H.B.4
  • 5
    • 0017891387 scopus 로고
    • The permeability of the lysosomal membrane to small ions
    • Casey R.P., Hollemans M., and Tager J.M. The permeability of the lysosomal membrane to small ions. Biochim. Biophys. Acta. 508 (1978) 15-26
    • (1978) Biochim. Biophys. Acta. , vol.508 , pp. 15-26
    • Casey, R.P.1    Hollemans, M.2    Tager, J.M.3
  • 7
    • 0942265544 scopus 로고    scopus 로고
    • Selective disruption of lysosomes in HeLa cells triggers apoptosis mediated by cleavage of Bid by multiple papain-like lysosomal cathepsins
    • Cirman T., Oresic K., Mazovec G.D., Turk V., Reed J.C., Myers R.M., Salvesen G.S., and Turk B. Selective disruption of lysosomes in HeLa cells triggers apoptosis mediated by cleavage of Bid by multiple papain-like lysosomal cathepsins. J. Biol. Chem. 279 (2004) 3578-3587
    • (2004) J. Biol. Chem. , vol.279 , pp. 3578-3587
    • Cirman, T.1    Oresic, K.2    Mazovec, G.D.3    Turk, V.4    Reed, J.C.5    Myers, R.M.6    Salvesen, G.S.7    Turk, B.8
  • 8
    • 0003319796 scopus 로고
    • Effects of fat-soluble compounds on lysosomes in vitro
    • de Duve C., Wattiaux R., and Wibo M. Effects of fat-soluble compounds on lysosomes in vitro. Biochem. Pharmacol. 9 (1962) 97-116
    • (1962) Biochem. Pharmacol. , vol.9 , pp. 97-116
    • de Duve, C.1    Wattiaux, R.2    Wibo, M.3
  • 10
    • 0018832583 scopus 로고
    • Distribution of lysosomal cathepsin D in normal, ischemic, and starved rabbit cardiac myocytes
    • Decker R.S., Poole A.R., and Wildenthal K. Distribution of lysosomal cathepsin D in normal, ischemic, and starved rabbit cardiac myocytes. Circ. Res. 46 (1980) 485-494
    • (1980) Circ. Res. , vol.46 , pp. 485-494
    • Decker, R.S.1    Poole, A.R.2    Wildenthal, K.3
  • 11
    • 0000194142 scopus 로고
    • Peroxidative and radiation damage to isolated lysosomes
    • Desai I.D., Sawant P.L., and Tappel A.L. Peroxidative and radiation damage to isolated lysosomes. Biochim. Biophys. Acta 86 (1964) 277-285
    • (1964) Biochim. Biophys. Acta , vol.86 , pp. 277-285
    • Desai, I.D.1    Sawant, P.L.2    Tappel, A.L.3
  • 12
    • 0018597788 scopus 로고
    • Characterization of an 11,000-dalton beta-bungarotoxin: binding and enzyme activity on rat brain synaptosomal membranes
    • Donlon M., Shain W., Tobias G.S., and Marinetti G.V. Characterization of an 11,000-dalton beta-bungarotoxin: binding and enzyme activity on rat brain synaptosomal membranes. Membr. Biochem. 2 (1979) 367-391
    • (1979) Membr. Biochem. , vol.2 , pp. 367-391
    • Donlon, M.1    Shain, W.2    Tobias, G.S.3    Marinetti, G.V.4
  • 13
    • 11844294713 scopus 로고    scopus 로고
    • Induction of lysosomal membrane permeabilization by compounds that activate p53-independent apoptosis
    • Erdal H., Berndtsson M., Castro J., Brunk U.T., Shoshan M.C., and Linder S. Induction of lysosomal membrane permeabilization by compounds that activate p53-independent apoptosis. Proc. Natl. Acad. Sci. USA 102 (2005) 192-197
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 192-197
    • Erdal, H.1    Berndtsson, M.2    Castro, J.3    Brunk, U.T.4    Shoshan, M.C.5    Linder, S.6
  • 15
    • 0007263402 scopus 로고
    • Studies on the mode of action of excess of vitamin A. 6. Lysosomal protease and the degradation of cartilage matrix
    • Fell H.B., and Dingle J.T. Studies on the mode of action of excess of vitamin A. 6. Lysosomal protease and the degradation of cartilage matrix. Biochem. J. 87 (1963) 403-408
    • (1963) Biochem. J. , vol.87 , pp. 403-408
    • Fell, H.B.1    Dingle, J.T.2
  • 16
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri K.F., and Kroemer G. Organelle-specific initiation of cell death pathways. Nat. Cell Biol. 3 (2001) E255-E263
    • (2001) Nat. Cell Biol. , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 17
    • 0015715404 scopus 로고
    • Evidence that peroxidation of lysosomal membranes is initiated by hydroxyl free radicals produced during flavin enzyme activity
    • Fong K.L., McCay P.B., and Poyer L.J. Evidence that peroxidation of lysosomal membranes is initiated by hydroxyl free radicals produced during flavin enzyme activity. J. Biol. Chem. 248 (1973) 7792-7797
    • (1973) J. Biol. Chem. , vol.248 , pp. 7792-7797
    • Fong, K.L.1    McCay, P.B.2    Poyer, L.J.3
  • 18
    • 0023714439 scopus 로고
    • Solute translocation across the mammalian lysosome membrane
    • Forster S., and Lloyd J.B. Solute translocation across the mammalian lysosome membrane. Biochim. Biophys. Acta 947 (1988) 465-491
    • (1988) Biochim. Biophys. Acta , vol.947 , pp. 465-491
    • Forster, S.1    Lloyd, J.B.2
  • 19
    • 2942687937 scopus 로고    scopus 로고
    • The cell biology of lysosomal storage disorders
    • Futerman A.H., and van Meer G. The cell biology of lysosomal storage disorders. Nat. Rev. Mol. Cell Biol. 5 (2004) 554-565
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 554-565
    • Futerman, A.H.1    van Meer, G.2
  • 20
    • 33750935347 scopus 로고
    • Lysosomal transport of amino acids
    • Thoene J.G. (Ed), CRC Press, Boca Raton
    • Gahl W. Lysosomal transport of amino acids. In: Thoene J.G. (Ed). Pathophoysiology of Lysosomal Transport (1992), CRC Press, Boca Raton 45-68
    • (1992) Pathophoysiology of Lysosomal Transport , pp. 45-68
    • Gahl, W.1
  • 22
    • 0002042774 scopus 로고
    • Approaches to the study of lysosomal transport
    • Thoene J.G. (Ed), CRC Press, Boca Raton
    • Greene A.A., and Schneider J.S. Approaches to the study of lysosomal transport. In: Thoene J.G. (Ed). Pathophoysiology of Lysosomal Transport (1992), CRC Press, Boca Raton 7-44
    • (1992) Pathophoysiology of Lysosomal Transport , pp. 7-44
    • Greene, A.A.1    Schneider, J.S.2
  • 23
    • 0014707149 scopus 로고
    • Patterns of cytopathology and lysosomal enzyme release in poliovirus-infected HEp-2 cells treated with either 2-(alpha-hydroxybenzyl)-benzimidazole or guanidine HCl
    • Guskey L.E., Smith P.C., and Wolff D.A. Patterns of cytopathology and lysosomal enzyme release in poliovirus-infected HEp-2 cells treated with either 2-(alpha-hydroxybenzyl)-benzimidazole or guanidine HCl. J. Gen. Virol. 6 (1970) 151-161
    • (1970) J. Gen. Virol. , vol.6 , pp. 151-161
    • Guskey, L.E.1    Smith, P.C.2    Wolff, D.A.3
  • 24
    • 0021086597 scopus 로고
    • The lysosomal proton pump is electrogenic
    • Harikumar P., and Reeves J.P. The lysosomal proton pump is electrogenic. J. Biol. Chem. 258 (1983) 10403-10410
    • (1983) J. Biol. Chem. , vol.258 , pp. 10403-10410
    • Harikumar, P.1    Reeves, J.P.2
  • 26
    • 0016785479 scopus 로고
    • pH gradient across the lysosomal membrane generated by selective cation permeability and Donnan equilibrium
    • Henning R. pH gradient across the lysosomal membrane generated by selective cation permeability and Donnan equilibrium. Biochim. Biophys. Acta 401 (1975) 307-316
    • (1975) Biochim. Biophys. Acta , vol.401 , pp. 307-316
    • Henning, R.1
  • 28
    • 23844459507 scopus 로고    scopus 로고
    • Shape relaxations in a fluid supported membrane during hydrolysis by phospholipase A2
    • Jensen U.B., and Simonsen A.C. Shape relaxations in a fluid supported membrane during hydrolysis by phospholipase A2. Biochim. Biophys. Acta 1715 (2005) 1-5
    • (2005) Biochim. Biophys. Acta , vol.1715 , pp. 1-5
    • Jensen, U.B.1    Simonsen, A.C.2
  • 31
    • 28544435485 scopus 로고    scopus 로고
    • Lysosomes and autophagy in cell death control
    • Kroemer G., and Jaattela M. Lysosomes and autophagy in cell death control. Nat. Rev. Cancer 5 (2005) 886-897
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 886-897
    • Kroemer, G.1    Jaattela, M.2
  • 34
    • 0021264506 scopus 로고
    • Measurement of delta pH and membrane potential in secretory vesicles isolated from bovine pituitary intermediate lobe
    • Loh Y.P., Tam W.W.H., and Russell J.T. Measurement of delta pH and membrane potential in secretory vesicles isolated from bovine pituitary intermediate lobe. J. Biol. Chem. 259 (1984) 8238-8245
    • (1984) J. Biol. Chem. , vol.259 , pp. 8238-8245
    • Loh, Y.P.1    Tam, W.W.H.2    Russell, J.T.3
  • 40
    • 0000313492 scopus 로고
    • Identification and characterization of a proton pump on lysosomes by fluorescein-isothiocyanate-dextran fluorescence
    • Ohkuma S., Moriyama Y., and Takano T. Identification and characterization of a proton pump on lysosomes by fluorescein-isothiocyanate-dextran fluorescence. Proc. Natl. Acad. Sci. U.S.A. 79 (1982) 2758-2762
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 2758-2762
    • Ohkuma, S.1    Moriyama, Y.2    Takano, T.3
  • 42
    • 0025746712 scopus 로고
    • The transport systems of mammalian lysosomes
    • Pisoni R.L., and Thoene J.G. The transport systems of mammalian lysosomes. Biochim. Biophys. Acta 1071 (1991) 351-373
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 351-373
    • Pisoni, R.L.1    Thoene, J.G.2
  • 43
    • 0000656947 scopus 로고
    • The mechanism of lysosomal acidification
    • Dingle J.T., Dean R.T., and Sly W. (Eds), Elsevier, Amsterdam
    • Reeves J.P. The mechanism of lysosomal acidification. In: Dingle J.T., Dean R.T., and Sly W. (Eds). Lysosomes in Biology and Pathology vol. 7 (1984), Elsevier, Amsterdam 175-199
    • (1984) Lysosomes in Biology and Pathology , vol.7 , pp. 175-199
    • Reeves, J.P.1
  • 44
    • 0017774250 scopus 로고
    • The permeability properties of the lysosomal membrane
    • Reign D.J., and Tager J.M. The permeability properties of the lysosomal membrane. Biochim. Biophys. Acta 472 (1977) 419-449
    • (1977) Biochim. Biophys. Acta , vol.472 , pp. 419-449
    • Reign, D.J.1    Tager, J.M.2
  • 45
    • 0017774250 scopus 로고
    • The permeability properties of the lysosomal membrane
    • Reijngoud D.J., and Tager J.M. The permeability properties of the lysosomal membrane. Biochim. Biophys. Acta 472 (1977) 419-449
    • (1977) Biochim. Biophys. Acta , vol.472 , pp. 419-449
    • Reijngoud, D.J.1    Tager, J.M.2
  • 46
    • 0020107166 scopus 로고
    • Effects of ATP on lysosomes: inhibition of the loss of latency caused by cooling
    • Ruth R.C., and Weglicki W.B. Effects of ATP on lysosomes: inhibition of the loss of latency caused by cooling. Am. J. Physiol. 242 (1982) C192-C199
    • (1982) Am. J. Physiol. , vol.242
    • Ruth, R.C.1    Weglicki, W.B.2
  • 48
    • 51249188620 scopus 로고
    • The movement of molecules across lipid membranes: a molecular theory
    • Trauble H. The movement of molecules across lipid membranes: a molecular theory. J. Membr. Biol. 4 (1971) 193-208
    • (1971) J. Membr. Biol. , vol.4 , pp. 193-208
    • Trauble, H.1
  • 50
    • 0343008014 scopus 로고
    • Lysosomal transport of inorganic ions
    • Thoene J.G. (Ed), CRC Press, Boca Raton
    • Vadgama J., and Jonas A. Lysosomal transport of inorganic ions. In: Thoene J.G. (Ed). Pathophoysiology of Lysosomal Transport (1992), CRC Press, Boca Raton 133-150
    • (1992) Pathophoysiology of Lysosomal Transport , pp. 133-150
    • Vadgama, J.1    Jonas, A.2
  • 51
    • 0024382896 scopus 로고
    • Measurement of pH of intracellular compartments in living cells by fluorescent dyes
    • Van Adelsberg J., Barasch J., and Al-Awqati A. Measurement of pH of intracellular compartments in living cells by fluorescent dyes. Methods Enzymol. 172 (1989) 85-95
    • (1989) Methods Enzymol. , vol.172 , pp. 85-95
    • Van Adelsberg, J.1    Barasch, J.2    Al-Awqati, A.3
  • 52
    • 0021873256 scopus 로고
    • The use of carotenoids and oxonol VI as probes for membrane potential in proteoliposomes
    • Van Walraven H.S., Krab K., Hagendoorn M.J., and Kraayenhof R. The use of carotenoids and oxonol VI as probes for membrane potential in proteoliposomes. FEBS Lett. 184 (1985) 96-99
    • (1985) FEBS Lett. , vol.184 , pp. 96-99
    • Van Walraven, H.S.1    Krab, K.2    Hagendoorn, M.J.3    Kraayenhof, R.4
  • 53
    • 0009945137 scopus 로고    scopus 로고
    • Enhancement of lysosomal osmotic sensitivity induced by the photooxidation of membrane thiol groups
    • Wan F.-Y., Yang L., Zhong Y.-G., Zhu W., Wang Y.-N., and Zhang G.-J. Enhancement of lysosomal osmotic sensitivity induced by the photooxidation of membrane thiol groups. Photochem. Photobiol. 75 (2002) 134-139
    • (2002) Photochem. Photobiol. , vol.75 , pp. 134-139
    • Wan, F.-Y.1    Yang, L.2    Zhong, Y.-G.3    Zhu, W.4    Wang, Y.-N.5    Zhang, G.-J.6
  • 54
    • 0015946885 scopus 로고
    • Changes in lipid composition of triton-filled lysosomes during lysis. Association with activation of acid-active lipases and phospholipases
    • Weglicki W.B., Ruth R.C., Owens K., Griffin H.D., and Waite B.M. Changes in lipid composition of triton-filled lysosomes during lysis. Association with activation of acid-active lipases and phospholipases. Biochim. Biophys. Acta 337 (1974) 145-152
    • (1974) Biochim. Biophys. Acta , vol.337 , pp. 145-152
    • Weglicki, W.B.1    Ruth, R.C.2    Owens, K.3    Griffin, H.D.4    Waite, B.M.5
  • 56
    • 0021346123 scopus 로고
    • A simple procedure for the isolation of highly purified lysosomes from normal rat liver
    • Yamada H., Hayashi H., and Natori Y. A simple procedure for the isolation of highly purified lysosomes from normal rat liver. J. Biochem. 95 (1984) 1155-1160
    • (1984) J. Biochem. , vol.95 , pp. 1155-1160
    • Yamada, H.1    Hayashi, H.2    Natori, Y.3
  • 57
    • 0033767342 scopus 로고    scopus 로고
    • Influence of membrane fluidity modifiers on lysosomal osmotic sensitivity
    • Yang L., Zhang G.-J., Zhong Y.-G., and Zheng Y.-Z. Influence of membrane fluidity modifiers on lysosomal osmotic sensitivity. Cell Biol. Int. 24 (2000) 699-704
    • (2000) Cell Biol. Int. , vol.24 , pp. 699-704
    • Yang, L.1    Zhang, G.-J.2    Zhong, Y.-G.3    Zheng, Y.-Z.4
  • 58
    • 0031012409 scopus 로고    scopus 로고
    • Lysosomal destabilization via increased potassium ion permeability following photodamage
    • Yao J., and Zhang G.-J. Lysosomal destabilization via increased potassium ion permeability following photodamage. Biochim. Biophys. Acta 1323 (1997) 334-342
    • (1997) Biochim. Biophys. Acta , vol.1323 , pp. 334-342
    • Yao, J.1    Zhang, G.-J.2
  • 59
    • 0034194472 scopus 로고    scopus 로고
    • Influence of membrane physical state on the lysosomal proton permeability
    • Zhang G.-J., Liu H.-W., Yang L., Zhong Y.-G., and Zheng Y.-Z. Influence of membrane physical state on the lysosomal proton permeability. J. Membr. Biol. 175 (2000) 53-62
    • (2000) J. Membr. Biol. , vol.175 , pp. 53-62
    • Zhang, G.-J.1    Liu, H.-W.2    Yang, L.3    Zhong, Y.-G.4    Zheng, Y.-Z.5
  • 60
    • 0030922261 scopus 로고    scopus 로고
    • The direct cause of photodamage-induced lysosomal destabilization
    • Zhang G.-J., and Yao J. The direct cause of photodamage-induced lysosomal destabilization. Biochim. Biophys. Acta 1326 (1997) 75-82
    • (1997) Biochim. Biophys. Acta , vol.1326 , pp. 75-82
    • Zhang, G.-J.1    Yao, J.2
  • 62
    • 0034191823 scopus 로고    scopus 로고
    • Effects of photoinduced membrane rigidification on the lysosomal permeability to potassium ions
    • Zhong Y.-G., Zhang G.-J., Yang L., and Zheng Y.-Z. Effects of photoinduced membrane rigidification on the lysosomal permeability to potassium ions. Photochem. Photobiol. 71 (2000) 627-633
    • (2000) Photochem. Photobiol. , vol.71 , pp. 627-633
    • Zhong, Y.-G.1    Zhang, G.-J.2    Yang, L.3    Zheng, Y.-Z.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.