Avid Bioservices Inc (CDMO)

[biopharm]

Unbelievable, F18 driver proteins? ..yes, PS Targeting is bigger than I could ever imagine and now I found => Molecular imaging, specifically positron emission tomography (PET), is a promising modality for early detection and disease staging in Alzheimer’s patients. Recently approved amyloid PET tracers (e.g., F-18 florbetapir, F-18 flutemetamol) can detect cortical fibrillary ß-amyloid (6). Looks like F18 driving proteins will be another reason I will buy more PPHM next week. PS Targeting must be targeted to reduce these amyloid levels and F18 is assisting.

In Alzheimer plaques of beta-amyloid are the cause of the disease. With people that do not develop Alzheimer the beta-amyloid is constantly removed in sufficient amounts so that things stay within acceptable boundaries. However, with Alzheimer - as the article also explains - the removal process cannot keep up and the beta-amyloid plaques grow behind a point where the signs of the disease start to surface and show.

The scientists in the article found that the T-cells and B-cells, part of the immune system BUT NOT present in the brain (because they CANNOT pass the brain blood barrier) play a role in producing antibodies which CAN pass the brain-blood barrier and accumulate in the brain where they associate with microglia to remove the beta-amyloid plaques.

So for the case I want to make, and I know the article says that mainly the B-cells produce these antibodies but I am illustrating a CONCEPT here that applies to lymphocytes in general (T,B,NK), we can ask ourselves the question what would happen to that process if the lymphocytes is bound to something that disables that function.

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Bavituximab just may become the #1 combination treatment for Alzheimers. The story is slowly reaching the right places and I hope Peregrine releases some information soon to show the medical community what possibilities exist for oncology, HIV and hundreds of other auto-immune diseases.

Protein misfolding has been shown to be the direct cause of a number of highly devastating diseases such as Alzheimer's disease, Parkinson's disease, and Creutzfeldt-Jacob syndrome, affecting the aging population globally. The deposition in tissues of amyloid fibrils is a characteristic of all these diseases, and the mechanisms by which these protein aggregates form continue to be intensively investigated. In only a fraction of cases is an underlying mutation responsible, and accordingly, what initiates amyloid formation in vivo is the major question that is addressed. In this study, we show that membranes containing phosphatidylserine (PS), a negatively charged phospholipid, induce a rapid formation of fibers by a variety of proteins, viz., lysozyme, insulin, glyceraldehyde-3-phosphate dehydrogenase, myoglobin, transthyretin, cytochrome c, histone H1, and alpha-lactalbumin. Congo red staining of these fibers yields the characteristic light green birefringence of amyloid, and fluorescent lipid tracers further reveal them to include phospholipids. Our results suggest that PS as well as other acidic phospholipids could provide the physiological low-pH environment on cellular membranes, enhancing protein fibril formation in vivo. Interestingly, all the proteins mentioned above either are cytotoxic or induce apoptosis. PS-protein interaction could be involved in the mechanism of cytotoxicity of the aggregated protein fibrils, perturbing membrane functions. Importantly, our results suggest that this process induced by acidic phospholipids may provide an unprecedented and generic connection between three current major areas of research: (i) mechanism(s) triggering amyloid formation, (ii) cytotoxicity of amyloidal protein aggregates, and (iii) mechanism(s) of action of cytotoxic proteins.

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