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Molecular Cloning of a Second Human 15S-Lipoxygenase and its Murine Homologue, an 8S-Lipoxygenase

Their Relationship to Other Mammalian Lipoxygenases

  • Chapter
Lipoxygenases and their Metabolites

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 447))

Abstract

The three well recognized lipoxygenases in humans are best known for their occurrence in different types of blood cells (1). And these three enzymes appear to have distinct biological roles. The leukocyte 5S-lipoxygenase clearly functions in the initiation of a metabolic pathway; the leukotriene products have distinct cell receptors and mediate proin-flammatory activities. The platelet 12S lipoxygenase synthesizes 12S-HpETE, and following reduction by cellular peroxidase, the hydroperoxide is converted efficiently and almost exclusively to the hydroxy derivative, 12S-HETE. The 12S-HETE may be a signaling molecule involved in cell-cell communication. Overall, however, there is no strong consensus on the biological role of this highly specific 12S-lipoxygenase product.

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References

  1. Funk, C. D. (1993) Prog. Nuc. Acid Res. Mol. Biol. 45, 67–98.

    Article  CAS  Google Scholar 

  2. Rapoport, S. M. and Schewe, T. (1986) Biochim. Biophys. Acta 864, 471–495.

    PubMed  CAS  Google Scholar 

  3. Kroschwald, P., Kroschwald, A., Wiesner, R., Schewe, T., and Kühn, H. (1986) Biomed. Biochim. Acta 45, 1237–1247.

    PubMed  CAS  Google Scholar 

  4. Kroschwald, P., Kroschwald, A., Kühn, H., Ludwig, P., Thiele, B. J., Höhne, M., Schewe, T., and Rapoport, S. M. (1989) Biochem. Biophys. Res. Commun. 160, 954–960.

    Article  PubMed  CAS  Google Scholar 

  5. Sun, D., and Funk, C. D. (1996) J. Biol. Chem. 271, 24055–24062

    Article  PubMed  CAS  Google Scholar 

  6. Witzum, J. L., and Steinberg, D. (1991) J. Clin. Invest. 88, 1785–1792.

    Article  Google Scholar 

  7. Brash, A. R., Boeglin, W. E., Chang, M. S., and Shieh, B-H. (1996) J. Biol.Chem. 271, 20549–20557.

    Google Scholar 

  8. Woollard, P. M. (1986) Biochem. Biophys. Res. Commun. 136, 169–175.

    Article  PubMed  CAS  Google Scholar 

  9. Baer, A. N., Klaus, M. V., and Green, F. A. (1995) J. Invest. Dermatol. 104, 251–255.

    Article  PubMed  CAS  Google Scholar 

  10. Baer A.N. and Green F. A. 1993 J. Lipid Research 34 1505–1514

    Google Scholar 

  11. Brash, A. R., Boeglin, W. E., and Chang, M. S. (1997) Proc. Natl. Acad. Sci. USA 94, 6148–6152.

    Article  PubMed  CAS  Google Scholar 

  12. Boyington, J. C, Gaffney, B. J, and Amzel, L. M. (1993) Science 260, 1482–1486.

    Article  PubMed  CAS  Google Scholar 

  13. Minor, W., Steczko, J., Stec, B., Otwinowski, Z., Bolin, J. T., Walter, R., and Axelrod, B. (1996) Biochem-istry 35, 10687–10701.

    Article  CAS  Google Scholar 

  14. Nugteren, D. H., and Kivits, G. A. A. (1987) Biochim. Biophys. Acta 921, 135–141.

    PubMed  CAS  Google Scholar 

  15. Liminga, M., Fagerholm, P., and Oliw, E. H. (1994) Exp. Eye Res. 59, 313–321.

    Article  PubMed  CAS  Google Scholar 

  16. Oliw, E. H., Fabiani, R., Johansson, L., and Ronquist, G. (1993) J. Reprod. Fertil. 99, 195–199.

    Article  PubMed  CAS  Google Scholar 

  17. Hunter, J. A., Finkbeiner, W. E., Nadel, J. A., Goetzl, E. J., and Holtzman, M. J. (1985) Proc. Natl. Acad. Sei. USA 82, 4633–4637.

    Article  CAS  Google Scholar 

  18. Kulmin, M., Hamberg, M., Granström, E., Björck, T., Dahlén, B., Matsuda, H., Zetterström, O., and Da-hlén, S-E. (1990) Arch. Biochem. Biophys. 282, 254–262.

    Article  Google Scholar 

  19. Jisaka, M., Kim, R. B., Nanney, L. B., Boeglin, W. E., and Brash, A. R. (1997) J. Biol. Chem. 272, 24410–24416.

    Article  PubMed  CAS  Google Scholar 

  20. Gschwendt, M., Fürstenberger, G., Kittstein, W., Besemfelder, E., Hull, W. E., Hagedorn, H., Opferkuch, H. J., and Marks, F. (1986) Carcinogenesis 7, 449–455.

    Article  PubMed  CAS  Google Scholar 

  21. Hughes, M. A., and Brash, A. R. (1991) Biochim. Biophys. Acta 1081, 347–354.

    PubMed  CAS  Google Scholar 

  22. Fürstenberger, G., Hagedorn, H., Jacobi, T., Besemfelder, E., Stephan, M., Lehmann, W. D., and Marks, F. (1991) J. Biol. Chem. 266, 15738–15745

    PubMed  Google Scholar 

  23. Funk, C. D., Funk, L. B., FitzGerald, G. A., and Samuelsson, B. (1992) Proc. Natl. Acad. Sci. USA 89, 3962–3966.

    Article  PubMed  CAS  Google Scholar 

  24. Bryant, R. W., Bailey, J. M., Schewe, T., and Rapoport, S. M. (1982) J. Biol. Chem. 257, 6050–6055.

    PubMed  CAS  Google Scholar 

  25. Kühn, H., Sprecher, H., and Brash, A. R. (1990) J. Biol. Chem. 265, 16300–16305.

    PubMed  Google Scholar 

  26. Kühn, H., Belkner, J., Wiesner, R., and Brash, A. R. (1990) J. Biol. Chem. 265, 18351–18361.

    PubMed  Google Scholar 

  27. Schnurr, K., Belkner, J., Ursini, F., Schewe, T., and Kühn, H. (1996) J. Biol. Chem. 271, 4653–4658.

    Article  PubMed  CAS  Google Scholar 

  28. Soberman, R. J., Harper, T. W, Betteridge, D., Lewis, R. A., and Austen, K. F. (1985) J. Biol. Chem. 260, 4508–4515.

    PubMed  CAS  Google Scholar 

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Author information

Authors and Affiliations

  1. Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, Tennessee, 37232-6602, USA

    Alan R. Brash, Mitsuo Jisaka & William E. Boeglin

  2. Department of Ophthalmology, Vanderbilt University School of Medicine, Nashville, Tennessee, 37232-6602, USA

    Min S. Chang

Authors
  1. Alan R. Brash
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  2. Mitsuo Jisaka
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  3. William E. Boeglin
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  4. Min S. Chang
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Editor information

Editors and Affiliations

  1. Free University of Berlin, Berlin, Germany

    Santosh Nigam

  2. Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada

    Cecil R. Pace-Asciak

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© 1999 Kluwer Academic/Plenum Publishers, New York

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Brash, A.R., Jisaka, M., Boeglin, W.E., Chang, M.S. (1999). Molecular Cloning of a Second Human 15S-Lipoxygenase and its Murine Homologue, an 8S-Lipoxygenase. In: Nigam, S., Pace-Asciak, C.R. (eds) Lipoxygenases and their Metabolites. Advances in Experimental Medicine and Biology, vol 447. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4861-4_3

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  • DOI: https://doi.org/10.1007/978-1-4615-4861-4_3

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-0-306-46044-9

  • Online ISBN: 978-1-4615-4861-4

  • eBook Packages: Springer Book Archive

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