Histochemistry to examine where the proteins were expressed in the hip…

Histochemistry to examine where the proteins were expressed in the hippocampus as well as any changes in cell morphology. In addition, the specificity and reactivity of the available antibodies to the paraffin sections were considered.-Synuclein gene, which encodes a 140-amino-acid protein, is a key player in neurodegenerative diseases. The fibrillar -sheet aggregation of -synuclein is the major constituents of Lewy bodies and Lewy neurites in the pathogenesis of Parkinson disease [21]. However, in comparison to its identified roles in neuropathogenesis, the normal physiological function of -synuclein in neurogenesis is not well understood. As a presynaptic protein, -synuclein, is located in the membrane, interacts with tubulins, is enriched in presynaptic termini, and is involved in microtubule transport and neurotransmitter release [22-24]. Mice lacking -synuclein gene show normal long-term potentiation (LPT) ofLee et al. Proteome Science 2012, 10:72 http://www.proteomesci.com/content/10/1/Page 9 ofAStaining Intensity1800 1600 1400 PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/15501003 1200 1000 800 600 400 200** ** * **Figure 5 Statistical presentation of the immunohistochemical staining of brain sections of rats. Expression levels of AMPA receptor (A) and -synuclein (B) represented by immunoreactivities in the sections were quantitated by a software, iSolution, and statistically compared (*, pDasatinib modulate the redistribution of -synuclein in the hippocampal presynapse for synaptic plasticity and improved cognitive function. This result supports the previous finding that the mRNA level of -synuclein was elevated upon n-3 fatty acid treatment to rats for 3 weeks [9]. Neurofilament medium molecular weight protein (NF-M) is a neuron-specific intermediate filament protein that heteropolymerizes with other immunologically distinct neurofilaments, NF-L and NF-H, and constitutes a major part of the neuronal cytoskeleton [28]. The three different NF proteins form filaments at different stoichiometries under different physiological conditions, and the resulting sidearm structures of the C-termini of the NF proteins along the core fiber can interact with diff.