Detection of d-aspartate in tau proteins associated with Alzheimer paired helical filaments
Paired helical filaments (PHF) characteristic of Alzheimer neurofibrillary lesions are known to contain a modified form of microtubule associated protein tau. These proteins, PHF-tau, differ from normal tau in the extent and the site of phosphorylation. To determine whether PHF-tau, tau proteins fro...
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| Veröffentlicht in: | Brain research 1995-03, Vol.675 (1), p.183-189 |
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| creator | Kenessey, Agnes Yen, Shu-Hui Liu, Wan-Kyng Yang, Xiao-Ran Dunlop, David S. |
| description | Paired helical filaments (PHF) characteristic of Alzheimer neurofibrillary lesions are known to contain a modified form of microtubule associated protein tau. These proteins, PHF-tau, differ from normal tau in the extent and the site of phosphorylation. To determine whether PHF-tau, tau proteins from normal adult brains (N-tau), tau proteins from Alzheimer brains not associated with PHF (A-tau), and tau proteins from fetal brains (F-tau) differ in racemization, these proteins were compared for their
d-aspartate content. The results demonstrated that PHF-tau contain more
d-aspartate than N-tau, A-tau and F-tau. The average percentage
d-aspartate for these proteins, after a correction for background, are 4.9%, 2.8%, 1.6%, and 1% for PHF-tau, N-tau, A-tau and F-tau, respectively. It remains to be determined if the increase in
d-aspartate is a consequence of PHF formation. It is also unknown if the change in
d-aspartate content in PHF-tau is associated with phosphorylation, which alters the susceptibility of tau to proteolysis. |
| doi_str_mv | 10.1016/0006-8993(95)00061-T |
| format | Article |
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d-aspartate content. The results demonstrated that PHF-tau contain more
d-aspartate than N-tau, A-tau and F-tau. The average percentage
d-aspartate for these proteins, after a correction for background, are 4.9%, 2.8%, 1.6%, and 1% for PHF-tau, N-tau, A-tau and F-tau, respectively. It remains to be determined if the increase in
d-aspartate is a consequence of PHF formation. It is also unknown if the change in
d-aspartate content in PHF-tau is associated with phosphorylation, which alters the susceptibility of tau to proteolysis.</description><identifier>ISSN: 0006-8993</identifier><identifier>EISSN: 1872-6240</identifier><identifier>DOI: 10.1016/0006-8993(95)00061-T</identifier><identifier>PMID: 7796127</identifier><identifier>CODEN: BRREAP</identifier><language>eng</language><publisher>London: Elsevier B.V</publisher><subject>Alzheimer Disease - metabolism ; Alzheimer Disease - pathology ; Alzheimer's disease ; Amino Acids - analysis ; Amino Acids - metabolism ; Aspartic Acid - analysis ; Aspartic Acid - metabolism ; Biological and medical sciences ; Brain Chemistry - physiology ; d-Aspartate ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; Electrophoresis, Polyacrylamide Gel ; Female ; Humans ; Hydrolysis ; Immunoblotting ; Medical sciences ; Neurofibrillary Tangles - metabolism ; Neurofibrillary Tangles - pathology ; Neurology ; Normal tau ; PHF-tau ; Pregnancy ; tau Proteins - analysis ; tau Proteins - metabolism</subject><ispartof>Brain research, 1995-03, Vol.675 (1), p.183-189</ispartof><rights>1995</rights><rights>1995 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-74f924cb4ab356606261332d5297d9394f458c8153d6fd906660ce6b5f3dd6fb3</citedby><cites>FETCH-LOGICAL-c417t-74f924cb4ab356606261332d5297d9394f458c8153d6fd906660ce6b5f3dd6fb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-8993(95)00061-T$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3466250$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7796127$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kenessey, Agnes</creatorcontrib><creatorcontrib>Yen, Shu-Hui</creatorcontrib><creatorcontrib>Liu, Wan-Kyng</creatorcontrib><creatorcontrib>Yang, Xiao-Ran</creatorcontrib><creatorcontrib>Dunlop, David S.</creatorcontrib><title>Detection of d-aspartate in tau proteins associated with Alzheimer paired helical filaments</title><title>Brain research</title><addtitle>Brain Res</addtitle><description>Paired helical filaments (PHF) characteristic of Alzheimer neurofibrillary lesions are known to contain a modified form of microtubule associated protein tau. These proteins, PHF-tau, differ from normal tau in the extent and the site of phosphorylation. To determine whether PHF-tau, tau proteins from normal adult brains (N-tau), tau proteins from Alzheimer brains not associated with PHF (A-tau), and tau proteins from fetal brains (F-tau) differ in racemization, these proteins were compared for their
d-aspartate content. The results demonstrated that PHF-tau contain more
d-aspartate than N-tau, A-tau and F-tau. The average percentage
d-aspartate for these proteins, after a correction for background, are 4.9%, 2.8%, 1.6%, and 1% for PHF-tau, N-tau, A-tau and F-tau, respectively. It remains to be determined if the increase in
d-aspartate is a consequence of PHF formation. It is also unknown if the change in
d-aspartate content in PHF-tau is associated with phosphorylation, which alters the susceptibility of tau to proteolysis.</description><subject>Alzheimer Disease - metabolism</subject><subject>Alzheimer Disease - pathology</subject><subject>Alzheimer's disease</subject><subject>Amino Acids - analysis</subject><subject>Amino Acids - metabolism</subject><subject>Aspartic Acid - analysis</subject><subject>Aspartic Acid - metabolism</subject><subject>Biological and medical sciences</subject><subject>Brain Chemistry - physiology</subject><subject>d-Aspartate</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Female</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Immunoblotting</subject><subject>Medical sciences</subject><subject>Neurofibrillary Tangles - metabolism</subject><subject>Neurofibrillary Tangles - pathology</subject><subject>Neurology</subject><subject>Normal tau</subject><subject>PHF-tau</subject><subject>Pregnancy</subject><subject>tau Proteins - analysis</subject><subject>tau Proteins - metabolism</subject><issn>0006-8993</issn><issn>1872-6240</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1rGzEQhkVpSJ2k_6AFHUpJDptKq6_VJRDSJA0EenFOPQitNMIq--FKckr76yPXxsfmNLwzzwzDg9AHSi4pofILIUQ2ndbsXIuLbaDN8g1a0E61jWw5eYsWB-QdOsn5Z42MaXKMjpXSkrZqgX58hQKuxHnCc8C-sXltU7EFcJxwsRu8TnOBOGVsc55drBOPf8eywtfD3xXEERJe25hqdwVDdHbAIQ52hKnkM3QU7JDh_b6eoqe72-XNt-bx-_3DzfVj4zhVpVE86Ja7ntueCSmJbCVlrPWi1cprpnngonMdFczL4DWRlXEgexGYr52enaLPu7v1118byMWMMTsYBjvBvMlGKSY46eSrIJVKEi5UBfkOdGnOOUEw6xRHm_4YSsxWvtmaNVuzRot_gZplXfu4v7_pR_CHpb3tOv-0n9tcTYVkJxfzAWNcylaQil3tMKjSniMkk12EyYGvnl0xfo7__-MFj32f-A</recordid><startdate>19950327</startdate><enddate>19950327</enddate><creator>Kenessey, Agnes</creator><creator>Yen, Shu-Hui</creator><creator>Liu, Wan-Kyng</creator><creator>Yang, Xiao-Ran</creator><creator>Dunlop, David S.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</scope><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>7TK</scope><scope>7X8</scope></search><sort><creationdate>19950327</creationdate><title>Detection of d-aspartate in tau proteins associated with Alzheimer paired helical filaments</title><author>Kenessey, Agnes ; Yen, Shu-Hui ; Liu, Wan-Kyng ; Yang, Xiao-Ran ; Dunlop, David S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-74f924cb4ab356606261332d5297d9394f458c8153d6fd906660ce6b5f3dd6fb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Alzheimer Disease - metabolism</topic><topic>Alzheimer Disease - pathology</topic><topic>Alzheimer's disease</topic><topic>Amino Acids - analysis</topic><topic>Amino Acids - metabolism</topic><topic>Aspartic Acid - analysis</topic><topic>Aspartic Acid - metabolism</topic><topic>Biological and medical sciences</topic><topic>Brain Chemistry - physiology</topic><topic>d-Aspartate</topic><topic>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Female</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>Immunoblotting</topic><topic>Medical sciences</topic><topic>Neurofibrillary Tangles - metabolism</topic><topic>Neurofibrillary Tangles - pathology</topic><topic>Neurology</topic><topic>Normal tau</topic><topic>PHF-tau</topic><topic>Pregnancy</topic><topic>tau Proteins - analysis</topic><topic>tau Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kenessey, Agnes</creatorcontrib><creatorcontrib>Yen, Shu-Hui</creatorcontrib><creatorcontrib>Liu, Wan-Kyng</creatorcontrib><creatorcontrib>Yang, Xiao-Ran</creatorcontrib><creatorcontrib>Dunlop, David S.</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>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Brain research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kenessey, Agnes</au><au>Yen, Shu-Hui</au><au>Liu, Wan-Kyng</au><au>Yang, Xiao-Ran</au><au>Dunlop, David S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Detection of d-aspartate in tau proteins associated with Alzheimer paired helical filaments</atitle><jtitle>Brain research</jtitle><addtitle>Brain Res</addtitle><date>1995-03-27</date><risdate>1995</risdate><volume>675</volume><issue>1</issue><spage>183</spage><epage>189</epage><pages>183-189</pages><issn>0006-8993</issn><eissn>1872-6240</eissn><coden>BRREAP</coden><abstract>Paired helical filaments (PHF) characteristic of Alzheimer neurofibrillary lesions are known to contain a modified form of microtubule associated protein tau. These proteins, PHF-tau, differ from normal tau in the extent and the site of phosphorylation. To determine whether PHF-tau, tau proteins from normal adult brains (N-tau), tau proteins from Alzheimer brains not associated with PHF (A-tau), and tau proteins from fetal brains (F-tau) differ in racemization, these proteins were compared for their
d-aspartate content. The results demonstrated that PHF-tau contain more
d-aspartate than N-tau, A-tau and F-tau. The average percentage
d-aspartate for these proteins, after a correction for background, are 4.9%, 2.8%, 1.6%, and 1% for PHF-tau, N-tau, A-tau and F-tau, respectively. It remains to be determined if the increase in
d-aspartate is a consequence of PHF formation. It is also unknown if the change in
d-aspartate content in PHF-tau is associated with phosphorylation, which alters the susceptibility of tau to proteolysis.</abstract><cop>London</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>7796127</pmid><doi>10.1016/0006-8993(95)00061-T</doi><tpages>7</tpages></addata></record> |
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| ispartof | Brain research, 1995-03, Vol.675 (1), p.183-189 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Alzheimer Disease - metabolism Alzheimer Disease - pathology Alzheimer's disease Amino Acids - analysis Amino Acids - metabolism Aspartic Acid - analysis Aspartic Acid - metabolism Biological and medical sciences Brain Chemistry - physiology d-Aspartate Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Electrophoresis, Polyacrylamide Gel Female Humans Hydrolysis Immunoblotting Medical sciences Neurofibrillary Tangles - metabolism Neurofibrillary Tangles - pathology Neurology Normal tau PHF-tau Pregnancy tau Proteins - analysis tau Proteins - metabolism |
| title | Detection of d-aspartate in tau proteins associated with Alzheimer paired helical filaments |
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