A new hat for an old enzyme: waste management

TJ Brueseke, JD Bell - Biochimica et Biophysica Acta (BBA)-Molecular and …, 2006 - Elsevier
TJ Brueseke, JD Bell
Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids, 2006Elsevier
The history of research regarding secretory phospholipase A2 (sPLA2) 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 …
The history of research regarding secretory phospholipase A2 (sPLA2) 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.
Elsevier