In comparison with other facility-based studies, the two year mortality of ART patients was 13.2% in Malawi in 2008, 13.7% in South Africa, and 21% in a Ugandan fee-for-service program. The higher mortality in our HC/community-based patients compared to our hospital patients could be explained by their lower educational level, as well geographical barriers to accessing acute care for opportunistic infections or other acute illnesses particularly in the vulnerable early period of ART provision. The differences in mortality could also be attributed to differences in ascertainment, e.g. the inability of the hospital program to properly ascertain mortality in their cohort compared to community volunteers doing home visits. Using these factors, our project results measure up well, as retention of volunteers was high, adequate material, technical and moral support was provided to the volunteers, and the referral of patients was a function of integration with the government health care service. In addition there was a wide-spread acceptance of our program by the communities in the catchment area of the health centre with no resistance to the program reported. The synucleins are small proteins, that have a weak homology to 14.3.3 proteins. The synucleins are considered to be “natively unfolded” although recent work indicates that in cells a-synuclein folds into a dynamic tetramer. There are three members of the synuclein family, a, b and c that are conserved and found throughout vertebrates. The cellular function of synucleins have not yet been discovered. aSynuclein, the most notable family member, is associated with neurodegenerative plaques. Although c-synuclein is found mostly in the peripheral nervous system and in pre-synaptic terminals, its over-expression is associated with cancer progression. c-Synuclein was identified as the breast cancer specific gene protein 1,10 years ago by screening a breast cancer cDNA library. c-Synuclein is highly expressed in infiltrating breast cancer but is undetectable in normal or benign breast lesions, and is partially expressed in ductal carcinomas. While the function of c-synuclein is unknown, it is found in a wide LY2835219 variety of transformed cells and its overexpression leads to a significant increase in proliferation, motility, invasiveness and metastasis. Like c-synuclein, phospholipase C b2 is absent in normal breast tissue, but is highly expressed in transformed tissue where its level of expression is directly related to tumor progression and migration presumably through its regulation by small G proteins. PLCb2 is a member of a larger mammalian PLC family that catalyzes the hydrolysis of phosphatidylinositol 4,5 bisphosphate P2). Cleavage of PIP2 generates the second messengers, diacylglycerol and 1,4,5 inositol trisphosphate P3), which activate protein kinase C and cause the release of Ca2+ from intracellular stores, respectively. All four isoforms of PLCb are strongly activated by Gaq. Additionally, PLCb2 and PLCb3 are activated by Gßc dimers that can potentially be released upon activation of all Ga families. It has also been found that PLCb2 can be activated by members of the Rho family of monomeric G proteins with the strongest activation by Rac1, which is involved in the cytoskeletal rearrangements that accompany cell mobility. PLCb2 is a modular protein composed of an N-terminal pleckstrin homology domain, 4 EF hands, a catalytic domain, a C2 domain and a long C-terminal extension. Crystallographic studies have indicated that Rac1 may promote enzyme activity by binding strongly to the PH domain and promoting membrane binding.