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Structure and Function of Phospholipase A2 Receptor

  • Kohji Hanasaki
  • Hitoshi Arita
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 416)

Abstract

Phospholipase A2 (EC 3.1.1.4: PLA2) is the group name of enzymes that cleave an acyl ester bond at the sn-2 position of glycerophospholipid (1). Mammalian PLA2s are classified into two types, secretory 14 kDa PLA2 and cytosolic higher molecular weight of PLA2 (2). Secretory PLA2 are further classified into two subgroups, group I and group II, on the basis of their characteristics in primary structure (3). Group II PLA2 (PLA2-II) is abundant at inflammatory loci and its expression is modulated by various inflammatory cytokines, and thus this type of PLA2 is thought to play some roles in the pathogenesis of inflammation (4,5). On the other hand, group I PLA2 (PLA2-I) is mainly secreted from the pancreas and the major physiological function of PLA2-I has long been thought to be digestion of phospholipids in nutrients (6). However, recent studies have revealed the presence of this type of PLA2 in several non-digestive organs such as lung and spleen (7). What is the biological role of PLA2-I in non-digestive organs? This question led us to initiate the series of studies on the PLA2 receptor.

Keywords

Mannose Receptor Partial Amino Acid Sequence Secretory PLA2 Venom PLA2 Major Physiological Function 
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 1996

Authors and Affiliations

  • Kohji Hanasaki
    • 1
  • Hitoshi Arita
    • 1
  1. 1.Shionogi Research LaboratoriesShionogi & Co., Ltd.Fukushima-ku, Osaka 553Japan

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