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10.1186/s40478-017-0477-x http://scihub22266oqcxt.onion/10.1186/s40478-017-0477-x C5641992!5641992!29037261     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29037261&cmd=llinks): Failed to open stream: HTTP request failed! 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Distinct deposition of amyloid-? species in brains with Alzheimer?s disease pathology visualized with MALDI imaging mass spectrometry |pdf=|usr=}}{{29037261}} gab.com Text Distinct deposition of amyloid- species in brains with Alzheimer s disease pathology visualized with MALDI imaging mass spectrometry JO: Acta Neuropathol Commun http://www.kidney.de/pget.php?&tw=1&pmid=29037261 #FOAvip Amyloid ? (A?) deposition in the brain is an early and invariable feature of Alzheimer?s disease (AD). The A? peptides are composed of about 40 amino acids and are generated from amyloid precursor proteins (APP), by ?- and ?-secretases. The distribution of individual A? peptides in the brains of aged people, and those suffering from AD and cerebral amyloid angiopathy (CAA), is not fully characterized. We employed the matrix-assisted laser desorption/ionization-imaging mass spectrometry (MALDI-IMS) to illustrate the spatial distribution of a broad range of A? species in human autopsied brains. With technical advancements such as formic acid pretreatment of frozen autopsied brain samples, we have: i) demonstrated that A?1?42 and A?1?43 were selectively deposited in senile plaques while full-length A? peptides such as A?1?36, 1?37, 1?38, 1?39, 1?40, and A?1?41 were deposited in leptomeningeal blood vessels. ii) Visualized distinct depositions of N-terminal truncated A?40 and A?42, including pyroglutamate modified at Glu-3 (N3pE), only with IMS for the first time. iii) Demonstrated that one single amino acid alteration at the C-terminus between A?1?42 and A?1?41 results in profound changes in their distribution pattern. In vitro, this can be attributed to the difference in the self-aggregation ability amongst A?1?40, A?1?41, and A?1?42. These observations were further confirmed with immunohistochemistry (IHC), using the newly developed anti-A?1?41 antibody. Here, distinct depositions of truncated and/or modified C- and N-terminal fragments of A?s in AD and CAA brains with MALDI-IMS were visualized in a spacio-temporal specific manner. Specifically, A?1?41 was detected both with MALDI-IMS and IHC suggesting that a single amino acid alteration at the C-terminus of A? results in drastic distribution changes. These results suggest that MALDI-IMS could be used as a standard approach in combination with clinical, genetic, and pathological observations in understanding the pathology of AD and CAA.Electronic supplementary material: The online version of this article (10.1186/s40478-017-0477-x) contains supplementary material, which is available to authorized users. Twit Text FOAVip Distinct deposition of amyloid- species in brains with Alzheimer s disease pathology visualized with MALDI imaging mass spectrometry ????Acta Neuropathol Commun http://www.kidney.de/pget.php?&tw=1&pmid=29037261 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29037261 #FOAvip English Wikipedia <ref>{{Cite pmid|29037261}}</ref> Distinct deposition of amyloid-? species in brains with Alzheimer?s disease pathology visualized with MALDI imaging mass spectrometry #MMPMID29037261 Kakuda N; Miyasaka T; Iwasaki N; Nirasawa T; Wada-Kakuda S; Takahashi-Fujigasaki J; Murayama S; Ihara Y; Ikegawa M Acta Neuropathol Commun 2017[]; 5 (�): � PMID29037261show ga Amyloid ? (A?) deposition in the brain is an early and invariable feature of Alzheimer?s disease (AD). The A? peptides are composed of about 40 amino acids and are generated from amyloid precursor proteins (APP), by ?- and ?-secretases. The distribution of individual A? peptides in the brains of aged people, and those suffering from AD and cerebral amyloid angiopathy (CAA), is not fully characterized. We employed the matrix-assisted laser desorption/ionization-imaging mass spectrometry (MALDI-IMS) to illustrate the spatial distribution of a broad range of A? species in human autopsied brains. With technical advancements such as formic acid pretreatment of frozen autopsied brain samples, we have: i) demonstrated that A?1?42 and A?1?43 were selectively deposited in senile plaques while full-length A? peptides such as A?1?36, 1?37, 1?38, 1?39, 1?40, and A?1?41 were deposited in leptomeningeal blood vessels. ii) Visualized distinct depositions of N-terminal truncated A?40 and A?42, including pyroglutamate modified at Glu-3 (N3pE), only with IMS for the first time. iii) Demonstrated that one single amino acid alteration at the C-terminus between A?1?42 and A?1?41 results in profound changes in their distribution pattern. In vitro, this can be attributed to the difference in the self-aggregation ability amongst A?1?40, A?1?41, and A?1?42. These observations were further confirmed with immunohistochemistry (IHC), using the newly developed anti-A?1?41 antibody. Here, distinct depositions of truncated and/or modified C- and N-terminal fragments of A?s in AD and CAA brains with MALDI-IMS were visualized in a spacio-temporal specific manner. Specifically, A?1?41 was detected both with MALDI-IMS and IHC suggesting that a single amino acid alteration at the C-terminus of A? results in drastic distribution changes. These results suggest that MALDI-IMS could be used as a standard approach in combination with clinical, genetic, and pathological observations in understanding the pathology of AD and CAA.Electronic supplementary material: The online version of this article (10.1186/s40478-017-0477-x) contains supplementary material, which is available to authorized users. �Distinct deposition of amyloid-? species in brains with Alzheimer?s di(epmc).pdf DeepDyve Pubget Overpricing