1.Default mode network connectivity is linked to cognitive functioning and CSF Aβ1-42 levels in Alzheimer's disease.
Celebi O1, Uzdogan A2, Oguz KK3, Has AC4, Dolgun A5, Cakmakli GY1, Akbiyik F2, Elibol B6, Saka E7. Arch Gerontol Geriatr. 2016 Jan-Feb;62:125-32. doi: 10.1016/j.archger.2015.09.010. Epub 2015 Oct 17.
BACKGROUND: Changes in the default mode network (DMN) activity are early features of Alzheimer's disease (AD) and may be linked to AD-specific Aβ pathology.
2.Early Detection of Autism (ASD) by a Non-invasive Quick Measurement of Markedly Reduced Acetylcholine & DHEA and Increased β-Amyloid (1-42), Asbestos (Chrysotile), Titanium Dioxide, Al, Hg & often Coexisting Virus Infections (CMV, HPV 16 and 18), Bacterial Infections etc. in the Brain and Corresponding Safe Individualized Effective Treatment.
Omura Y, Lu D, Jones MK, Nihrane A, Duvvi H, Shimotsuura Y, Ohki M. Acupunct Electrother Res. 2015;40(3):157-87.
A brief historical background on Autism & some of the important symptoms associated with Autism are summarized. Using strong Electro Magnetic Field Resonance Phenomenon between 2 identical molecules with identical weight (which received U.S. Patent) non-invasively & rapidly we can detect various molecules including neurotransmitters, bacteria, virus, fungus, metals & abnormal molecules. Simple non- invasive measurement of various molecules through pupils & head of diagnosed or suspected Autism patients indicated that in Autism patients following changes were often found: 1) Acetylcholine is markedly reduced; 2) Alzheimer's disease markers (i.e. β-Amyloid (1-42), Tau Protein, Apolipoprotein (Apo E4)) are markedly increased; 3) Chrysotile Asbestos is increased; 4) Titanium Dioxide (TiO2) is moderately increased; 5) Al is moderately increased; 6) Hg is moderately increased; 7) Dopamine, Serotonin & GABA are significantly reduced (up to about 1/10 of normal); 8) Often viral infections (such as CMV, HHV-6, HPV-16, HPV-18, etc.
3.Single molecule experiments emphasize GM1 as a key player of the different cytotoxicity of structurally distinct Aβ1-42 oligomers.
Calamai M1, Evangelisti E2, Cascella R2, Parenti N3, Cecchi C4, Stefani M4, Pavone F3. Biochim Biophys Acta. 2016 Feb;1858(2):386-92. doi: 10.1016/j.bbamem.2015.12.009. Epub 2015 Dec 4.
It is well established that cytotoxic Aβ oligomers are the key factor that triggers the initial tissue and cell modifications eventually culminating in the development of Alzheimer's disease. Aβ1-42 oligomers display a high degree of polymorphism, and several structurally different oligomers have been described. Amongst them, two types, recently classified as A+ and A-, have been shown to possess similar size but distinct toxic properties, as a consequence of their biophysical and structural differences. Here, we have investigated by means of single molecule tracking the oligomer mobility on the plasma membrane of living neuroblastoma cells and the interaction with the ganglioside GM1, a component of membrane rafts. We have found that A+ and A- oligomers display a similar lateral diffusion on the plasma membrane of living cells. However, only the toxic A+ oligomers appear to interact and alter the mobility of GM1. We have also studied the lateral diffusion of each kind of oligomers in cells depleted or enriched in GM1.
