Several detailed reviews on cellular phospholipase A2 (cPLA2) have been published, however the role of cPLA2 in cell function remains unclear. Continued substantive efforts are required to elucidate a broader understanding of the in vivo functionality for all endogenous phospholipases and an explanation for the need for such diverse phospholipids in various biological membranes, which are not yet at hand.
Recently, we have reported on the preferential deacylation of cardiolipin (CL) of various mammalian myocardia by an endogenous phospholipase (PLA1 and/or PLA2), following in vitro incubation at pH 7.4 and 38°C for 60 minutes of whole tissue homogenate (as source of phospholipids and phospholipases) producing monolysocardiolipin (MLCL) and concurrent reduction of CL. In contrast whole tissue homogenate of rabbit spleen treated similarly selectively deacylated ethanolamine plasmalogen (PE) producing lyso alkenyl PE.
In the present study, whole tissue homogenate of bullfrog cardiac muscle and thigh skeletal muscle, treated similarly revealed the following data: Bullfrog cardiac muscle slightly deacylated CL producing MLCL, Thigh skeletal muscle shows very minute amount of CL and no deacylation products following in vitro incubation, PE plasmalogen is the only alkenyl species of both tissues, Thigh muscle has very minute amount of Sphingomyelin.
These data raised some questions pertaining to the Lipolytic capabilities of diverse tissues from different species of animals and will be discussed in details.
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