We cannot fully ascertain the functional consequences of the obse

We cannot fully ascertain the functional consequences of the observed interaction between PLA2 and SSG-2 at this time. Future work will help us clarify this relationship.

Nevertheless, two important processes that have a bearing in cell cycle progression have been identified as subjected to cPLA2 activity in other systems: 1) the production of biologically active molecules and 2) membrane remodeling [53]. There is very little information regarding the effects of the primary metabolites released from the action of PLA2 (arachidonic acid and lysophospholipids) in fungi, Arachidonic acid was see more reported to stimulate adenylate cyclase [54] in S. cerevisiae. If this is also true for S. schenckii, addition of arachidonic acid to the medium would be expected to stimulate the yeast cell cycle and this was what we observed. We had previously reported that dibutyryl derivatives of cAMP inhibit the yeast to mycelium transition in S. schenckii www.selleckchem.com/products/Vorinostat-saha.html [4]. On the other hand, membrane remodeling is also an important function of enzymes such as phospholipases. This process is needed for cell cycle progression and fungal morphogenesis [53]. It has been reported in other systems that in order for the cell cycle to occur there must be a careful balance between membrane phospholipid synthesis and degradation. PLA2 has an important role in the maintenance of this balance [35, 55]. The lipid composition

of the membrane is also essential for the correct receptor-protein interactions and plays an important role in signal transduction. G proteins Olopatadine are usually in molar excess

when compared to the GPRC’s and a large number of inactive GDP-bound heterotrimeric G protein molecules must be available in receptor-rich domains associated to membrane lipids [56]. G proteins can also affect PLA2 activity by a number of different mechanisms such as: increasing the intracellular calcium concentration, transcriptional regulation and stimulation of phosphorylation through different protein kinases such as protein kinase C and MAP kinases (for a review see [57]). The studies presented here constitute the first evidence of the interaction of G protein subunits of fungi with a phospholipase. These results establish for the first time a relationship between G proteins and the pathogenic determinants of fungi. The identification of such an important protein as partners of a G protein alpha subunit in fungi selleck inhibitor suggests a mechanism by which these G proteins can control pathogenicity in fungi. The existence of the interaction reported here may offer an explanation as to why fungi with decreased G protein alpha subunits such as C. parasitica, hypovirus infection [15] and M. grisea with disrupted Gα subunit gene, magB, exhibit reduced levels of virulence [18]. This information is essential if we are to understand the disease producing process of fungi.

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