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Lipoprotein‐associated phospholipase A2 structure and function (774.3)
Author(s) -
Gonzalez Tara,
Bahnson Brian
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.774.3
Subject(s) - lipoprotein associated phospholipase a2 , hydrolase , chemistry , phospholipase a2 , phospholipase , serine , lipoprotein , enzyme , biochemistry , function (biology) , phospholipase c , high density lipoprotein , structure function , microbiology and biotechnology , biology , cholesterol , physics , particle physics
Lipoprotein‐associated phospholipase A 2 (LpPLA 2 ) or plasma platelet‐activating factor acetylhydrolase (pPAFAH) is a serine hydrolase that acts on platelet‐activating factor (PAF) and oxidized phospholipids. The enzyme has a classic α/β hydrolase fold and predicted membrane binding regions. Plasma PAFAH binds readily to both high density lipoproteins (HDL) and low density lipoproteins (LDL) and is believed to play a pro‐atherosclerotic role. The purpose of this study is to further elucidate the structure and function of LpPLA 2 through the use of specific inhibitors. It was necessary to develop and refine an expression method in E. coli to produce high quantities of protein of high purity for a truncated form of LpPLA 2 . Successful expression and purification of this LpPLA 2 construct have been achieved and initial trials of crystallization were positive. The next step in this study is to obtain the crystal structure of LpPLA 2 along with its selective inhibitors. Grant Funding Source : Supported by NIHNHLBI grant #RO1HL084366