PLA2R1: expression and function in Cancer.
Lyon, France. In Biochim Biophys Acta, 22 Apr 2014
UNLABELLED: The phospholipase A2 receptor 1 (PLA2R1 or PLA2R) was isolated twenty years ago for its ability to bind several secretory phospholipase A2 proteins (sPLA2).
New insights on membrane mediated effects of 1α,25-dihydroxy vitamin D3 signaling in the musculoskeletal system.
Atlanta, United States. In Steroids, Jan 2014
Long term efforts to investigate the roles of these two receptors demonstrated thatPdia3 is located in caveolae, where it interacts with phospholipase A2 (PLA2) activating protein (PLAA) and caveolin-1 (Cav-1) to initiate rapid signaling via Ca(++)/calmodulin-dependent protein kinase II (CaMKII), PLA2, phospholipase C (PLC), protein kinase C (PKC), and ultimately the ERK1/2 family of mitogen activated protein kinases (MAPK).
sPLA2 and the epidermal barrier.
Seattle, United States. In Biochim Biophys Acta, Dec 2013
The secretory phospholipase 2 (sPLA2) enzymes control important processes in skin and other organs, including inflammation and differentiation.
Secreted Phospholipases A2 - not just Enzymes.
In Acta Chim Slov, 2011
However, since pharmacologically active sPLA2 molecules without enzymatic activity have been discovered, first in snake venom and then also in human, it has become increasingly evident that, on many occasions, the action of these proteins has to be considered as arising from the interplay of their receptor-binding and enzymatic functions.