Calcium-dependent generation of N-acylethanolamines and lysophosphatidic acids by glycerophosphodiesterase GDE7

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URI http://shark.lib.kagawa-u.ac.jp/kuir/metadata/28497
Title
Calcium-dependent generation of N-acylethanolamines and lysophosphatidic acids by glycerophosphodiesterase GDE7
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Description

Abstract

N-Acylethanolamines form a class of lipid mediators and include an endocannabinoid arachidonoylethanolamide (anandamide), analgesic and anti-inflammatory palmitoylethanolamide, and appetite-suppressing oleoylethanolamide. In animal tissues, N-acylethanolamines are synthesized from N-acylated ethanolamine phospholipids directly by N-acylphosphatidylethanolamine-hydrolyzing phospholipase D or through multi-step pathways via N-acylethanolamine lysophospholipids. We previously reported that glycerophosphodiesterase (GDE) 4, a member of the GDE family, has lysophospholipase D (lysoPLD) activity hydrolyzing N-acylethanolamine lysophospholipids to N-acylethanolamines. Recently, GDE7 was shown to have lysoPLD activity toward lysophosphatidylcholine to produce lysophosphatidic acid (LPA). Here, we examined the reactivity of GDE7 with N-acylethanolamine lysophospholipids as well as the requirement of divalent cations for its catalytic activity. When overexpressed in HEK293 cells, recombinant GDE7 proteins of human and mouse showed lysoPLD activity toward N-palmitoyl, N-oleoyl, and N-arachidonoyl-lysophosphatidylethanolamines and N-palmitoyl-lysoplasmenylethanolamine to generate their corresponding N-acylethanolamines and LPAs. However, GDE7 hardly hydrolyzed glycerophospho-N-palmitoylethanolamine. Overexpression of GDE7 in HEK293 cells increased endogenous levels of N-acylethanolamines and LPAs. Interestingly, GDE7 was stimulated by micromolar concentrations of Ca2+ but not by millimolar concentrations of Mg2+, while GDE4 was stimulated by Mg2+ but was insensitive to Ca2+. GDE7 was widely distributed in various tissues of humans and mice with the highest levels in their kidney tissues. These results suggested that GDE7 is a novel Ca2+-dependent lysoPLD, which is involved in the generation of both N-acylethanolamines and LPAs.

KEYWORDS:

Glycerophosphodiesterase; Lysophosphatidic acid; Lysophospholipase D; N-acylethanolamine; Phospholipid

Author
著者 Iffat Ara Sonia Rahman
著者(ヨミ) イファット アラ ソニア ラハマン
著者(別表記) Rahman Iffat Ara Sonia
Publication Title
Biochimica et Biophysica Acta
Volume
1861
Issue
12
Start Page
1881
End Page
1892
Publisher
Elsevier
Published Date
2016-09-13
ISSN
0006-3002
PMID
27637550
DOI
10.1016/j.bbalip.2016.09.008
Resource Type
Thesis or Dissertation
Language
eng
Relation
出版社版DOIリンク(URL) : https://doi.org/10.1016/j.bbalip.2016.09.008
Resource URL
https://doi.org/10.1016/j.bbalip.2016.09.008
Relation(isVersionOf)
Publisher's Version
Relation URL(isReplacedBy)
https://doi.org/10.1016/j.bbalip.2016.09.008
Relation(hasVersion)
Publisher's Version
Rights
Elsevier Japanより、機関リポジトリでの公開可能確認済み。エンバーゴ期間満了。 / From Elsevier Japan, publication possibility confirmed in an institutional repository. The embargo period has expired.
Text Version
ETD
Grant ID
博甲第652号
Grant Date
2017-03-24
Degree Name
博士(医学)
Grantor
香川大学
Set
香川大学
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