Abstract
Phospholipases A2 are believed to play important roles in the production of bioactive mediators by regulating the release of precursors for these compounds from structural membrane phosphoglycerides. It has become clear during the last years that several and distinct cellular phospholipases A2 exist. These can be distinguished in low molecular weight 14 kDa group I (pancreatic-type) and group II (non-pancreatic-type) enzymes and in high molecular weight 85 kDa or cytosolic phospholipase A2. These require Ca2+ for activity, either in their catalytic mechanism as in the case of 14 kDa phospholipases or for translocation from the cytosol to membranes as in the case of cytosolic phospholipase A2. In addition, Ca2+-independent enzymes exist. Each of these phospholipase A2 activities appears to be subject to multiple regulation mechanisms, both at the transcriptional and post-translational level, depending on the cell type and the cell stimulators. This paper summarizes our data on the regulation of phospholipase A2 activities in relation to prostaglandin formation in rat glomerular mesangial cells.
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van den Bosch, H., Vervoordeldonk, M.J.B.M., Sanchéz, R.M., Pfeilschifter, J., Schalkwijk, C.G. (1994). Phospholipases A2 and Prostaglandin Formation in Rat Glomerular Mesangial Cells. In: Mackness, M.I., Clerc, M. (eds) Esterases, Lipases, and Phospholipases. NATO ASI Series, vol 266. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0993-0_24
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DOI: https://doi.org/10.1007/978-1-4899-0993-0_24
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