At the endoplasmic reticulum (ER) membrane, phosphatidylethanolamine (PE) is hydrolyzed, and has one of its acyl chains cleaved off, by membrane-associated phospholipase A2 gamma 2A, (PLA2G2A) or by calcium-independent phospholipase A2-gamma (PNPLA8), to form 1-acyl lysophosphatidylethanolamine (LPE) (Murakami et al. 2005, Kramer et al. 1989, Singer et al. 2002).
Gelb, MH, Le Calvez, C, Ghomashchi, F, Rouault, M, Singer, AG, Sadilek, M, Bollinger, J, Bezzine, S, Lambeau, G, Lazdunski, M, Nguyen, E
Chow, EP, Hayes, G, Johansen, B, Tizard, R, Kramer, RM, McGray, P, Pepinsky, RB, Hession, C
Takanezawa, Y, Ishikawa, Y, Kuwata, H, Masuda, S, Kudo, I, Ishii, T, Aoki, J, Arai, H, Sumimoto, H, Murakami, M, Ueda-Semmyo, K, Nakatani, Y, Yoda, E
phospholipase A2 activity of PLA2(3) [endoplasmic reticulum membrane]
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