A new hat for an old enzyme: Waste management

被引:9
|
作者
Brueseke, Taylor J. [1 ]
Bell, John D. [1 ]
机构
[1] Brigham Young Univ, Coll Biol & Agr, Dept Physiol & Dev Biol, Provo, UT 84602 USA
关键词
enzyme kinetics; fluorescence; two-photon microscopy; laurdan; binding; apoptosis;
D O I
10.1016/j.bbalip.2006.05.012
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The history of research regarding secretory phospholipase A(2) (sPLA(2)) has often focused in one of two directions. Originally, the enzyme was studied biophysically in terms of its fundamental structure, enzymology, and the relationship between membrane physics and catalytic activity. More recently, a large and growing body of information has accumulated concerning regulatory factors, tissue distribution, and physiological/pathological roles of sPLA2. Evidence is presented that suggests an additional function for the protein in which it helps to clear dead and damaged cells while avoiding digestion of those that are healthy. Apparently, the ability of the enzyme to discriminate between susceptible and resistant cells depends on physical properties of membrane lipids related to order, distribution, and neighbor/neighbor interactions. Investigations into this action of the enzyme offer the rare opportunity to apply biophysical approaches and principles to a physiological setting. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:1270 / 1279
页数:10
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