Sulfated glycosaminoglycans in Alzheimer's disease
Using the sulfated alcian blue and alcian blue-MgCl 2 techniques for demonstrating sulfated glycosaminoglycans (GAGs), we have shown sulfated GAGs to be associated with the amyloidotic lesions of Alzheimer's disease, the neuritic plaques, the neurofibrillary tangle, and the congophilic angiopat...
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Veröffentlicht in: | Human pathology 1987-05, Vol.18 (5), p.506-510 |
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creator | Snow, Alan D. Willmer, Jonathan P. Kisilevsky, Robert |
description | Using the sulfated alcian blue and alcian blue-MgCl
2 techniques for demonstrating sulfated glycosaminoglycans (GAGs), we have shown sulfated GAGs to be associated with the amyloidotic lesions of Alzheimer's disease, the neuritic plaques, the neurofibrillary tangle, and the congophilic angiopathy. To determine how specific these findings are to Alzheimer's disease, other neurologic disorders with neurofibrillary tangles and filamentous inclusions were examined. These included progressive supranuclear palsy, Pick's disease, subacute sclerosing panencephalitis, and postencephalitic parkinsonism. Sulfated GAGs were not demonstrated in the neurofibrillary tangles or filamentous structures in any of these disorders. The relationship of GAGs to the pathology of Alzheimer's disease is discussed as is their possible importance in determining the characteristic morphology of the amyloidotic lesion. |
doi_str_mv | 10.1016/S0046-8177(87)80036-9 |
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2 techniques for demonstrating sulfated glycosaminoglycans (GAGs), we have shown sulfated GAGs to be associated with the amyloidotic lesions of Alzheimer's disease, the neuritic plaques, the neurofibrillary tangle, and the congophilic angiopathy. To determine how specific these findings are to Alzheimer's disease, other neurologic disorders with neurofibrillary tangles and filamentous inclusions were examined. These included progressive supranuclear palsy, Pick's disease, subacute sclerosing panencephalitis, and postencephalitic parkinsonism. Sulfated GAGs were not demonstrated in the neurofibrillary tangles or filamentous structures in any of these disorders. The relationship of GAGs to the pathology of Alzheimer's disease is discussed as is their possible importance in determining the characteristic morphology of the amyloidotic lesion.</description><subject>Alzheimer Disease - metabolism</subject><subject>Amyloid - metabolism</subject><subject>Brain - metabolism</subject><subject>Glycosaminoglycans - metabolism</subject><subject>Humans</subject><subject>Neurofibrils - metabolism</subject><issn>0046-8177</issn><issn>1532-8392</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkFtLAzEQhYMotVZ_QmGfvDys5rrJPkkp3qDgQ_U5ZLMTjeylJrtC_fXu2uKrMDAD58wc5kNoTvA1wSS7WWPMs1QRKS-VvFIYsyzND9CUCEZTxXJ6iKZ_lmN0EuMHxoQILiZowoTEVNEpouu-cqaDMnmrtraNpvZNO46miYlvkkX1_Q6-hnARk9JHMBFO0ZEzVYSzfZ-h1_u7l-Vjunp-eFouVqnlhHapKwQlNCsMlxYwK5zILVYCDHDhnHKCEWappEpRDqVjklJBaMlLazJgArMZOt_d3YT2s4fY6dpHC1VlGmj7qKXkSkghB6PYGW1oYwzg9Cb42oStJliPrPQvKz2C0GqokZXOh735PqAvaij_tvZwBv12p8Pw5ZeHoKP10FgofQDb6bL1_yT8ALJQeEk</recordid><startdate>19870501</startdate><enddate>19870501</enddate><creator>Snow, Alan D.</creator><creator>Willmer, Jonathan P.</creator><creator>Kisilevsky, Robert</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19870501</creationdate><title>Sulfated glycosaminoglycans in Alzheimer's disease</title><author>Snow, Alan D. ; Willmer, Jonathan P. ; Kisilevsky, Robert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-fb52126ba47ce03bf59c085eae45ff8f5313c2728824edf3722512d4dca6e3503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Alzheimer Disease - metabolism</topic><topic>Amyloid - metabolism</topic><topic>Brain - metabolism</topic><topic>Glycosaminoglycans - metabolism</topic><topic>Humans</topic><topic>Neurofibrils - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Snow, Alan D.</creatorcontrib><creatorcontrib>Willmer, Jonathan P.</creatorcontrib><creatorcontrib>Kisilevsky, Robert</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Human pathology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Snow, Alan D.</au><au>Willmer, Jonathan P.</au><au>Kisilevsky, Robert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sulfated glycosaminoglycans in Alzheimer's disease</atitle><jtitle>Human pathology</jtitle><addtitle>Hum Pathol</addtitle><date>1987-05-01</date><risdate>1987</risdate><volume>18</volume><issue>5</issue><spage>506</spage><epage>510</epage><pages>506-510</pages><issn>0046-8177</issn><eissn>1532-8392</eissn><abstract>Using the sulfated alcian blue and alcian blue-MgCl
2 techniques for demonstrating sulfated glycosaminoglycans (GAGs), we have shown sulfated GAGs to be associated with the amyloidotic lesions of Alzheimer's disease, the neuritic plaques, the neurofibrillary tangle, and the congophilic angiopathy. To determine how specific these findings are to Alzheimer's disease, other neurologic disorders with neurofibrillary tangles and filamentous inclusions were examined. These included progressive supranuclear palsy, Pick's disease, subacute sclerosing panencephalitis, and postencephalitic parkinsonism. Sulfated GAGs were not demonstrated in the neurofibrillary tangles or filamentous structures in any of these disorders. The relationship of GAGs to the pathology of Alzheimer's disease is discussed as is their possible importance in determining the characteristic morphology of the amyloidotic lesion.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>3570282</pmid><doi>10.1016/S0046-8177(87)80036-9</doi><tpages>5</tpages></addata></record> |
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source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
subjects | Alzheimer Disease - metabolism Amyloid - metabolism Brain - metabolism Glycosaminoglycans - metabolism Humans Neurofibrils - metabolism |
title | Sulfated glycosaminoglycans in Alzheimer's disease |
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