The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy in Alzheimer's disease
Two immunocytochemical probes were used to specifically identify and localize heparan sulphate proteoglycans (HSPGs) in 17 cases of Alzheimer's disease (AD). A monoclonal (HK-102) and an affinity-purified polyclonal antibody, each recognizing specific domains on the protein core of a basement m...
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| Veröffentlicht in: | The American journal of pathology 1988-12, Vol.133 (3), p.456-463 |
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| container_title | The American journal of pathology |
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| creator | Snow, AD Mar, H Nochlin, D Kimata, K Kato, M Suzuki, S Hassell, J Wight, TN |
| description | Two immunocytochemical probes were used to specifically identify and localize heparan sulphate proteoglycans (HSPGs) in 17 cases of Alzheimer's disease (AD). A monoclonal (HK-102) and an affinity-purified polyclonal antibody, each recognizing specific domains on the protein core of a basement membrane-derived HSPG, localized HSPGs to the amyloid fibrils present in neuritic plaques (NPs) and congophilic angiopathy (CA) in the brains of Alzheimer's patients, with weak to no immunostaining in neurofibrillary tangles from the same tissues. HSPGs were also demonstrated in "primitive plaques," suggesting that their accumulation takes place during early stages of plaque development. Immunolocalization of HSPGs to subsets of astrocytes and neuronal cells, particularly those in close proximity to NPs and CA, suggested possible involvement of these two cell types in deposition of HS-PGs into the amyloidotic lesions. The current study not only identifies a new component (HSPGs) present in the amyloid deposits of NPs and CA but also suggests that astrocytes, neurons, or both may be involved in its deposition at these sites. |
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A monoclonal (HK-102) and an affinity-purified polyclonal antibody, each recognizing specific domains on the protein core of a basement membrane-derived HSPG, localized HSPGs to the amyloid fibrils present in neuritic plaques (NPs) and congophilic angiopathy (CA) in the brains of Alzheimer's patients, with weak to no immunostaining in neurofibrillary tangles from the same tissues. HSPGs were also demonstrated in "primitive plaques," suggesting that their accumulation takes place during early stages of plaque development. Immunolocalization of HSPGs to subsets of astrocytes and neuronal cells, particularly those in close proximity to NPs and CA, suggested possible involvement of these two cell types in deposition of HS-PGs into the amyloidotic lesions. The current study not only identifies a new component (HSPGs) present in the amyloid deposits of NPs and CA but also suggests that astrocytes, neurons, or both may be involved in its deposition at these sites.</description><identifier>ISSN: 0002-9440</identifier><identifier>EISSN: 1525-2191</identifier><identifier>PMID: 2974240</identifier><identifier>CODEN: AJPAA4</identifier><language>eng</language><publisher>Bethesda, MD: ASIP</publisher><subject>Alzheimer Disease - metabolism ; Alzheimer Disease - pathology ; Amyloid - analysis ; Antibodies, Monoclonal ; Astrocytes - analysis ; Astrocytes - ultrastructure ; Biological and medical sciences ; Brain - pathology ; Brain - ultrastructure ; Brain Chemistry ; Chondroitin Sulfate Proteoglycans - analysis ; Congo Red ; Glycosaminoglycans - analysis ; Heparan Sulfate Proteoglycans ; Heparitin Sulfate - analysis ; Humans ; Immunoenzyme Techniques ; Immunohistochemistry ; Medical sciences ; Microscopy, Electron ; Neurofibrils - analysis ; Neurofibrils - ultrastructure ; Neurology ; Neurons - analysis ; Neurons - ultrastructure ; Proteoglycans - analysis</subject><ispartof>The American journal of pathology, 1988-12, Vol.133 (3), p.456-463</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1880818/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1880818/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,53769,53771</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19799688$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2974240$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Snow, AD</creatorcontrib><creatorcontrib>Mar, H</creatorcontrib><creatorcontrib>Nochlin, D</creatorcontrib><creatorcontrib>Kimata, K</creatorcontrib><creatorcontrib>Kato, M</creatorcontrib><creatorcontrib>Suzuki, S</creatorcontrib><creatorcontrib>Hassell, J</creatorcontrib><creatorcontrib>Wight, TN</creatorcontrib><title>The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy in Alzheimer's disease</title><title>The American journal of pathology</title><addtitle>Am J Pathol</addtitle><description>Two immunocytochemical probes were used to specifically identify and localize heparan sulphate proteoglycans (HSPGs) in 17 cases of Alzheimer's disease (AD). A monoclonal (HK-102) and an affinity-purified polyclonal antibody, each recognizing specific domains on the protein core of a basement membrane-derived HSPG, localized HSPGs to the amyloid fibrils present in neuritic plaques (NPs) and congophilic angiopathy (CA) in the brains of Alzheimer's patients, with weak to no immunostaining in neurofibrillary tangles from the same tissues. HSPGs were also demonstrated in "primitive plaques," suggesting that their accumulation takes place during early stages of plaque development. Immunolocalization of HSPGs to subsets of astrocytes and neuronal cells, particularly those in close proximity to NPs and CA, suggested possible involvement of these two cell types in deposition of HS-PGs into the amyloidotic lesions. The current study not only identifies a new component (HSPGs) present in the amyloid deposits of NPs and CA but also suggests that astrocytes, neurons, or both may be involved in its deposition at these sites.</description><subject>Alzheimer Disease - metabolism</subject><subject>Alzheimer Disease - pathology</subject><subject>Amyloid - analysis</subject><subject>Antibodies, Monoclonal</subject><subject>Astrocytes - analysis</subject><subject>Astrocytes - ultrastructure</subject><subject>Biological and medical sciences</subject><subject>Brain - pathology</subject><subject>Brain - ultrastructure</subject><subject>Brain Chemistry</subject><subject>Chondroitin Sulfate Proteoglycans - analysis</subject><subject>Congo Red</subject><subject>Glycosaminoglycans - analysis</subject><subject>Heparan Sulfate Proteoglycans</subject><subject>Heparitin Sulfate - analysis</subject><subject>Humans</subject><subject>Immunoenzyme Techniques</subject><subject>Immunohistochemistry</subject><subject>Medical sciences</subject><subject>Microscopy, Electron</subject><subject>Neurofibrils - analysis</subject><subject>Neurofibrils - ultrastructure</subject><subject>Neurology</subject><subject>Neurons - analysis</subject><subject>Neurons - ultrastructure</subject><subject>Proteoglycans - analysis</subject><issn>0002-9440</issn><issn>1525-2191</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUE2LFDEQDaKs4-hPEHJRTw2dr57kIiyLq8KCl_UcapLqTpZ00na6XcZfbw8Oy3oqql699-rVC7JjiquGM8Nekl3btrwxUravyZtaH7a2E7q9IlfcHCSX7Y483gek04wVs0NaehpwghkyrWvqYTljZcEypJODXGnMdNkIGdc5LtHRKcGvFSuF7KkreShTiGmbQx5imWAJpzPlOv0JGEecP1XqY0Wo-Ja86iFVfHepe_Lz9sv9zbfm7sfX7zfXd00QnC-NckZLZZxkR_CCe3VUHl2vOOPOi8544ZjnhgklEfXRdVssUFpi2_YeZS_25PM_3Wk9jugd5mWGZKc5jjCfbIFo_0dyDHYovy3TutVMbwIfLwJzOUdd7Birw5QgY1mrPWh10HK7YE_eP3d6sri8esM_XHCoDlK_PdnF-rTGzMGYTj8zDHEIj3FGW0dIaVNlFh4mJoQVVqpO_AXJ6Jl0</recordid><startdate>19881201</startdate><enddate>19881201</enddate><creator>Snow, AD</creator><creator>Mar, H</creator><creator>Nochlin, D</creator><creator>Kimata, K</creator><creator>Kato, M</creator><creator>Suzuki, S</creator><creator>Hassell, J</creator><creator>Wight, TN</creator><general>ASIP</general><general>American Society for Investigative Pathology</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19881201</creationdate><title>The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy in Alzheimer's disease</title><author>Snow, AD ; Mar, H ; Nochlin, D ; Kimata, K ; Kato, M ; Suzuki, S ; Hassell, J ; Wight, TN</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h322t-5c98459c41bad32d5b5decf5212cd369d3c1d291354ee8bc6742a584e00fde4f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Alzheimer Disease - metabolism</topic><topic>Alzheimer Disease - pathology</topic><topic>Amyloid - analysis</topic><topic>Antibodies, Monoclonal</topic><topic>Astrocytes - analysis</topic><topic>Astrocytes - ultrastructure</topic><topic>Biological and medical sciences</topic><topic>Brain - pathology</topic><topic>Brain - ultrastructure</topic><topic>Brain Chemistry</topic><topic>Chondroitin Sulfate Proteoglycans - analysis</topic><topic>Congo Red</topic><topic>Glycosaminoglycans - analysis</topic><topic>Heparan Sulfate Proteoglycans</topic><topic>Heparitin Sulfate - analysis</topic><topic>Humans</topic><topic>Immunoenzyme Techniques</topic><topic>Immunohistochemistry</topic><topic>Medical sciences</topic><topic>Microscopy, Electron</topic><topic>Neurofibrils - analysis</topic><topic>Neurofibrils - ultrastructure</topic><topic>Neurology</topic><topic>Neurons - analysis</topic><topic>Neurons - ultrastructure</topic><topic>Proteoglycans - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Snow, AD</creatorcontrib><creatorcontrib>Mar, H</creatorcontrib><creatorcontrib>Nochlin, D</creatorcontrib><creatorcontrib>Kimata, K</creatorcontrib><creatorcontrib>Kato, M</creatorcontrib><creatorcontrib>Suzuki, S</creatorcontrib><creatorcontrib>Hassell, J</creatorcontrib><creatorcontrib>Wight, TN</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The American journal of pathology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Snow, AD</au><au>Mar, H</au><au>Nochlin, D</au><au>Kimata, K</au><au>Kato, M</au><au>Suzuki, S</au><au>Hassell, J</au><au>Wight, TN</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy in Alzheimer's disease</atitle><jtitle>The American journal of pathology</jtitle><addtitle>Am J Pathol</addtitle><date>1988-12-01</date><risdate>1988</risdate><volume>133</volume><issue>3</issue><spage>456</spage><epage>463</epage><pages>456-463</pages><issn>0002-9440</issn><eissn>1525-2191</eissn><coden>AJPAA4</coden><abstract>Two immunocytochemical probes were used to specifically identify and localize heparan sulphate proteoglycans (HSPGs) in 17 cases of Alzheimer's disease (AD). A monoclonal (HK-102) and an affinity-purified polyclonal antibody, each recognizing specific domains on the protein core of a basement membrane-derived HSPG, localized HSPGs to the amyloid fibrils present in neuritic plaques (NPs) and congophilic angiopathy (CA) in the brains of Alzheimer's patients, with weak to no immunostaining in neurofibrillary tangles from the same tissues. HSPGs were also demonstrated in "primitive plaques," suggesting that their accumulation takes place during early stages of plaque development. Immunolocalization of HSPGs to subsets of astrocytes and neuronal cells, particularly those in close proximity to NPs and CA, suggested possible involvement of these two cell types in deposition of HS-PGs into the amyloidotic lesions. The current study not only identifies a new component (HSPGs) present in the amyloid deposits of NPs and CA but also suggests that astrocytes, neurons, or both may be involved in its deposition at these sites.</abstract><cop>Bethesda, MD</cop><pub>ASIP</pub><pmid>2974240</pmid><tpages>8</tpages></addata></record> |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Alzheimer Disease - metabolism Alzheimer Disease - pathology Amyloid - analysis Antibodies, Monoclonal Astrocytes - analysis Astrocytes - ultrastructure Biological and medical sciences Brain - pathology Brain - ultrastructure Brain Chemistry Chondroitin Sulfate Proteoglycans - analysis Congo Red Glycosaminoglycans - analysis Heparan Sulfate Proteoglycans Heparitin Sulfate - analysis Humans Immunoenzyme Techniques Immunohistochemistry Medical sciences Microscopy, Electron Neurofibrils - analysis Neurofibrils - ultrastructure Neurology Neurons - analysis Neurons - ultrastructure Proteoglycans - analysis |
| title | The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy in Alzheimer's disease |
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