메뉴 건너뛰기




Volumn 77, Issue 3-4, 2007, Pages 209-215

Biological role of hepoxilins: Upregulation of phospholipid hydroperoxide glutathione peroxidase as a cellular response to oxidative stress?

Author keywords

[No Author keywords available]

Indexed keywords

12 HYDROXYICOSATETRAENOIC ACID; ARACHIDONIC ACID; HEPOXILIN A; LEUKOTRIENE; MESSENGER RNA; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; REACTIVE OXYGEN METABOLITE;

EID: 36349031310     PISSN: 09523278     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plefa.2007.08.007     Document Type: Article
Times cited : (11)

References (30)
  • 2
    • 0032499790 scopus 로고    scopus 로고
    • A 12R-lipoxygenase in human skin: mechanistic evidence, molecular cloning, and expression
    • Boeglin W.E., Kim R.B., and Brash A.R. A 12R-lipoxygenase in human skin: mechanistic evidence, molecular cloning, and expression. Proc. Natl. Acad. Sci. USA 95 (1998) 6744-6749
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6744-6749
    • Boeglin, W.E.1    Kim, R.B.2    Brash, A.R.3
  • 5
    • 0032708511 scopus 로고    scopus 로고
    • Insight into prostaglandin, leukotriene, and other eicosanoid functions using mice with targeted gene disruptions
    • Austin S.C., and Funk C.D. Insight into prostaglandin, leukotriene, and other eicosanoid functions using mice with targeted gene disruptions. Prostaglandins other Lipid Mediat. 58 (1999) 231-252
    • (1999) Prostaglandins other Lipid Mediat. , vol.58 , pp. 231-252
    • Austin, S.C.1    Funk, C.D.2
  • 10
    • 34447315030 scopus 로고    scopus 로고
    • The hepoxilin connection in the epidermis
    • Brash A.R., Yu Z., Boeglin W.E., and Schneider C. The hepoxilin connection in the epidermis. FEBS J. 274 (2007) 3494-3502
    • (2007) FEBS J. , vol.274 , pp. 3494-3502
    • Brash, A.R.1    Yu, Z.2    Boeglin, W.E.3    Schneider, C.4
  • 11
    • 0028950166 scopus 로고
    • Hepoxilins: a review on their enzymatic formation, metabolism and chemical synthesis
    • Pace-Asciak C.R., Reynaud D., and Demin P. Hepoxilins: a review on their enzymatic formation, metabolism and chemical synthesis. Lipids 30 (1995) 107-114
    • (1995) Lipids , vol.30 , pp. 107-114
    • Pace-Asciak, C.R.1    Reynaud, D.2    Demin, P.3
  • 12
    • 0030668140 scopus 로고    scopus 로고
    • Characterization and purification of a lipoxygenase inhibitor in human epidermoid carcinoma A431 cells
    • Chen C.-J., Huang H.-S., Lee Y.-T., Yang C.-Y., and Chang W.-C. Characterization and purification of a lipoxygenase inhibitor in human epidermoid carcinoma A431 cells. Biochem. J. 327 (1997) 193-198
    • (1997) Biochem. J. , vol.327 , pp. 193-198
    • Chen, C.-J.1    Huang, H.-S.2    Lee, Y.-T.3    Yang, C.-Y.4    Chang, W.-C.5
  • 13
    • 0032489490 scopus 로고    scopus 로고
    • Identification of a lipoxygenase inhibitor in A431 cells as a phospholipid hydroperoxide glutathione peroxidase
    • Huang H.-S., Chen C.-J., Lu H.S., and Chang W.-C. Identification of a lipoxygenase inhibitor in A431 cells as a phospholipid hydroperoxide glutathione peroxidase. FEBS Lett. 424 (1998) 22-26
    • (1998) FEBS Lett. , vol.424 , pp. 22-26
    • Huang, H.-S.1    Chen, C.-J.2    Lu, H.S.3    Chang, W.-C.4
  • 14
    • 0032723435 scopus 로고    scopus 로고
    • H.S. Huang, C.J. Chen, H. Suzuki, S. Yamamoto, W.C. Chang, Inhibitory effect of phospholipid hydroperoxide glutathione peroxidase on the activity of lipoxygenases and cyclooxygenases. Prostaglandins other Lipid Mediators 58 (1999) 65-75.
  • 15
    • 0029915115 scopus 로고    scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase controls the activity of the 15-lipoxygenase with complex substrates and preserves the specificity of the oxygenation products
    • Schnurr K., Belkner J., Ursini F., Schewe T., and Kühn H. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase controls the activity of the 15-lipoxygenase with complex substrates and preserves the specificity of the oxygenation products. J. Biol. Chem. 271 (1996) 4653-4658
    • (1996) J. Biol. Chem. , vol.271 , pp. 4653-4658
    • Schnurr, K.1    Belkner, J.2    Ursini, F.3    Schewe, T.4    Kühn, H.5
  • 16
    • 0035148235 scopus 로고    scopus 로고
    • Evidence for the presence of phospholipid hydroperoxide glutathione peroxidase in human platelets: implications for its involvement in the regulatory network of the 12-lipoxygenase pathway of AA metabolism
    • Sutherland M., Shankaranarayanan P., Schewe T., and Nigam S. Evidence for the presence of phospholipid hydroperoxide glutathione peroxidase in human platelets: implications for its involvement in the regulatory network of the 12-lipoxygenase pathway of AA metabolism. Biochem. J. 353 (2001) 91-100
    • (2001) Biochem. J. , vol.353 , pp. 91-100
    • Sutherland, M.1    Shankaranarayanan, P.2    Schewe, T.3    Nigam, S.4
  • 17
    • 0037434843 scopus 로고    scopus 로고
    • Biosynthesis of hepoxilins: evidence for the presence of a hepoxilin synthase activity in rat insulinoma cells
    • Shankaranarayanan P., Ciccoli R., and Nigam S. Biosynthesis of hepoxilins: evidence for the presence of a hepoxilin synthase activity in rat insulinoma cells. FEBS Lett. 538 (2003) 107-112
    • (2003) FEBS Lett. , vol.538 , pp. 107-112
    • Shankaranarayanan, P.1    Ciccoli, R.2    Nigam, S.3
  • 20
    • 0031975571 scopus 로고    scopus 로고
    • Membrane translocation of 15-lipoxygenase in hematopoietic cells is calcium-dependent and activates the oxygenase activity of the enzyme
    • Brinckmann R., Schnurr K., Heydeck D., Rosenbach T., Kolde G., and Kühn H. Membrane translocation of 15-lipoxygenase in hematopoietic cells is calcium-dependent and activates the oxygenase activity of the enzyme. Blood 91 (1998) 64-74
    • (1998) Blood , vol.91 , pp. 64-74
    • Brinckmann, R.1    Schnurr, K.2    Heydeck, D.3    Rosenbach, T.4    Kolde, G.5    Kühn, H.6
  • 21
    • 0025886108 scopus 로고
    • Distribution of glutathione peroxidases and glutathione reductase in rat brain mitochondria
    • Panfili E., Sandri G., and Ernster L. Distribution of glutathione peroxidases and glutathione reductase in rat brain mitochondria. FEBS Lett. 290 (1991) 35-37
    • (1991) FEBS Lett. , vol.290 , pp. 35-37
    • Panfili, E.1    Sandri, G.2    Ernster, L.3
  • 22
    • 0028172841 scopus 로고
    • Purification of a cytosolic enzyme from human liver with phospholipid hydroperoxide glutathione peroxidase activity
    • Chambers S.J., Lambert N., and Williamson G. Purification of a cytosolic enzyme from human liver with phospholipid hydroperoxide glutathione peroxidase activity. Int. J. Biochem. 26 (1994) 1279-1286
    • (1994) Int. J. Biochem. , vol.26 , pp. 1279-1286
    • Chambers, S.J.1    Lambert, N.2    Williamson, G.3
  • 23
    • 0027419580 scopus 로고
    • Selenoenzymes regulate the activity of leukocyte 5-lipoxygenase via the peroxide tone
    • Weitzel F., and Wendel A. Selenoenzymes regulate the activity of leukocyte 5-lipoxygenase via the peroxide tone. J. Biol. Chem. 268 (1993) 6288-6292
    • (1993) J. Biol. Chem. , vol.268 , pp. 6288-6292
    • Weitzel, F.1    Wendel, A.2
  • 24
    • 0031939746 scopus 로고    scopus 로고
    • Suppression of leukotriene formation in RBL-2H3 cells that overexpressed phospholipid hydroperoxide glutathione peroxidase
    • Imai H., Narashima K., Arai M., Sakamoto H., Chiba N., and Nakagawa Y. Suppression of leukotriene formation in RBL-2H3 cells that overexpressed phospholipid hydroperoxide glutathione peroxidase. J. Biol. Chem. 273 (1998) 1990-1997
    • (1998) J. Biol. Chem. , vol.273 , pp. 1990-1997
    • Imai, H.1    Narashima, K.2    Arai, M.3    Sakamoto, H.4    Chiba, N.5    Nakagawa, Y.6
  • 25
    • 0030971057 scopus 로고    scopus 로고
    • Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia
    • Ho Y.-S., Magnenat J.-L., Bronson R.T., Cao J., Gargano M., Sugawara M., and Funk C.D. Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia. J. Biol. Chem. 272 (1997) 16644-16651
    • (1997) J. Biol. Chem. , vol.272 , pp. 16644-16651
    • Ho, Y.-S.1    Magnenat, J.-L.2    Bronson, R.T.3    Cao, J.4    Gargano, M.5    Sugawara, M.6    Funk, C.D.7
  • 26
    • 0033739920 scopus 로고    scopus 로고
    • Polysome distribution of phospholipid hydroperoxide glutathione peroxidase mRNA: evidence for a block in elongation at the UGA/selenocysteine codon
    • Fletcher J.E., Copeland P.R., and Driscoll D.M. Polysome distribution of phospholipid hydroperoxide glutathione peroxidase mRNA: evidence for a block in elongation at the UGA/selenocysteine codon. RNA 6 (2000) 1573-1584
    • (2000) RNA , vol.6 , pp. 1573-1584
    • Fletcher, J.E.1    Copeland, P.R.2    Driscoll, D.M.3
  • 27
    • 0021721480 scopus 로고
    • Hepoxilin, a new family of insulin secretagogues formed by intact rat pancreatic islets
    • Pace-Asciak C.R., and Martin J.M. Hepoxilin, a new family of insulin secretagogues formed by intact rat pancreatic islets,. Prostaglandins Leukot. Med. 16 (1984) 173-180
    • (1984) Prostaglandins Leukot. Med. , vol.16 , pp. 173-180
    • Pace-Asciak, C.R.1    Martin, J.M.2
  • 28
    • 0025259294 scopus 로고
    • Lipoxygenase-generated icosanoids inhibit glucose-induced insulin release from rat islets
    • Nathan M.H., and Pek S.B. Lipoxygenase-generated icosanoids inhibit glucose-induced insulin release from rat islets. Prostaglandins Leukot. Essent. Fatty Acids 40 (1990) 21-25
    • (1990) Prostaglandins Leukot. Essent. Fatty Acids , vol.40 , pp. 21-25
    • Nathan, M.H.1    Pek, S.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.