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LDL Receptor-Related Protein Plays An Essential Role In 12/15-Lipoxygenase-Mediated LDL Oxidation By Macrophages

  • Wanpeng Xu
  • Yoshitaka Takahashi
  • Tadao Iwasaki
  • Hiroaki Hattori
  • Tanihiro Yoshimoto
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 525)

Abstract

Lipoxygenase incorporates a molecular oxygen regiospecifically and stereospecifically into unsaturated fatty acids. There are four classes of enzymes in mammalian tissues; 5-, 8-, 12-, and 15-lipoxygenases, named by the number indicating oxygenation site of arachidonic acid as a substrate [1,2]. Among the enzymes, 12-lipoxygenases are widely distributed in various tissues and species, and there are three isoforms: platelet, leukocyte and epidermis types. Since the leukocyte 12-lipoxygenase and 15- lipoxygenase-1 are highly related in their primary structures and enzymological properties, these enzymes are collectively called as 12/15- lipoxygenase [3].

Keywords

Cholesteryl Ester Cholesteryl Linoleate Diffuse Staining Pattern High Density Lipoprotein Receptor Lipoprotein Deficient Serum 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 2003

Authors and Affiliations

  • Wanpeng Xu
    • 1
  • Yoshitaka Takahashi
    • 1
  • Tadao Iwasaki
    • 2
  • Hiroaki Hattori
    • 2
  • Tanihiro Yoshimoto
    • 1
  1. 1.Department of Molecular PharmacologyKanazawa University Graduate School of Medical ScienceKanazawaJapan
  2. 2.Research DepartmentR&D Center, BML Inc.SaitamaJapan

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