On The Functional Diversity Of Secreted Phospholipases A_2: Cloning Of Novel Mammalian Enzymes And HIV-1 Antiviral Properties

摘要

Over the past decade, it has become clear that mammalian cells not only express a variety of intracellular phospholipases A_2 (PLA_2), but also a diverse set of secreted phospholipases A_2 (sPLA_2s). While PLA_2s are generally considered as key enzymes which control the production of lipid mediators, the function of the 10 distinct sPLA_2s cloned so far remains ill-defined. Using venom sPLA_2s, two types of specific membrane receptors (N and M) have been identified in various mammalian tissues. Of physiological relevance, the M-type receptor can bind with high affinities to several mammalian sPLA_2s, making it likely that mammalian sPLA_2s are endogenous ligands of the receptors initially identified with venom sPLA_2s, and that the physiological function of the mammalian sPLA_2s is not limited to their catalytic activity.