Casein Kinase 1 Is Tightly Associated with Paired‐Helical Filaments Isolated from Alzheimer's Disease Brain
: The protein kinase activity tightly associated with paired helical filaments (PHFs) purified from the brain tissue of individuals with Alzheimer's disease has been characterized in vitro. The activity is shown to phosphorylate casein, an exogenous substrate, with a maximal velocity of ∼2 nmol...
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| Veröffentlicht in: | Journal of neurochemistry 1997-12, Vol.69 (6), p.2506-2515 |
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| container_title | Journal of neurochemistry |
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| creator | Kuret, Jeff Johnson, Ginger S. Cha, Donald Christenson, Erik R. DeMaggio, Anthony J. Hoekstra, Merl F. |
| description | : The protein kinase activity tightly associated with paired helical filaments (PHFs) purified from the brain tissue of individuals with Alzheimer's disease has been characterized in vitro. The activity is shown to phosphorylate casein, an exogenous substrate, with a maximal velocity of ∼2 nmol/min/mg, suggesting it comprises a significant component of the total protein in the PHF preparation. On the basis of substrate selectivity, isoquinoline sulfonamide inhibitor selectivity, in‐gel renaturation assays, and western analysis, the activity consists of closely related members of the α branch of the casein kinase 1 family of protein kinases. Because of its tight association with PHFs and its phosphate‐directed substrate selectivity, casein kinase 1 is positioned to participate in the pathological hyperphosphorylation of tau protein that is observed in neurodegenerative diseases such as Alzheimer's disease. |
| doi_str_mv | 10.1046/j.1471-4159.1997.69062506.x |
| format | Article |
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The activity is shown to phosphorylate casein, an exogenous substrate, with a maximal velocity of ∼2 nmol/min/mg, suggesting it comprises a significant component of the total protein in the PHF preparation. On the basis of substrate selectivity, isoquinoline sulfonamide inhibitor selectivity, in‐gel renaturation assays, and western analysis, the activity consists of closely related members of the α branch of the casein kinase 1 family of protein kinases. Because of its tight association with PHFs and its phosphate‐directed substrate selectivity, casein kinase 1 is positioned to participate in the pathological hyperphosphorylation of tau protein that is observed in neurodegenerative diseases such as Alzheimer's disease.</description><identifier>ISSN: 0022-3042</identifier><identifier>EISSN: 1471-4159</identifier><identifier>DOI: 10.1046/j.1471-4159.1997.69062506.x</identifier><identifier>PMID: 9375684</identifier><identifier>CODEN: JONRA9</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Adult ; Alzheimer Disease - enzymology ; Alzheimer Disease - pathology ; Alzheimer's disease ; Animals ; Biological and medical sciences ; Blotting, Western ; Brain - enzymology ; Brain - pathology ; Casein kinase 1 ; Casein Kinases ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; Humans ; Isoenzymes - metabolism ; Isoquinolines - pharmacology ; Medical sciences ; Mice ; Mice, Inbred BALB C ; Middle Aged ; Neurofibrillary tangles ; Neurofibrils - metabolism ; Neurofibrils - pathology ; Neurology ; Paired‐helical filaments ; Protein Kinases - metabolism ; Protein phosphorylation ; Substrate Specificity ; Tau protein ; tau Proteins - chemistry ; tau Proteins - physiology</subject><ispartof>Journal of neurochemistry, 1997-12, Vol.69 (6), p.2506-2515</ispartof><rights>1998 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4376-f34b14d4bdfe5021e7f0f219cf78475433a1c89e07f6f8101da9b7e9a2090203</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1046%2Fj.1471-4159.1997.69062506.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.1471-4159.1997.69062506.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,781,785,1418,1434,27929,27930,45579,45580,46414,46838</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2089902$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9375684$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kuret, Jeff</creatorcontrib><creatorcontrib>Johnson, Ginger S.</creatorcontrib><creatorcontrib>Cha, Donald</creatorcontrib><creatorcontrib>Christenson, Erik R.</creatorcontrib><creatorcontrib>DeMaggio, Anthony J.</creatorcontrib><creatorcontrib>Hoekstra, Merl F.</creatorcontrib><title>Casein Kinase 1 Is Tightly Associated with Paired‐Helical Filaments Isolated from Alzheimer's Disease Brain</title><title>Journal of neurochemistry</title><addtitle>J Neurochem</addtitle><description>: The protein kinase activity tightly associated with paired helical filaments (PHFs) purified from the brain tissue of individuals with Alzheimer's disease has been characterized in vitro. The activity is shown to phosphorylate casein, an exogenous substrate, with a maximal velocity of ∼2 nmol/min/mg, suggesting it comprises a significant component of the total protein in the PHF preparation. On the basis of substrate selectivity, isoquinoline sulfonamide inhibitor selectivity, in‐gel renaturation assays, and western analysis, the activity consists of closely related members of the α branch of the casein kinase 1 family of protein kinases. Because of its tight association with PHFs and its phosphate‐directed substrate selectivity, casein kinase 1 is positioned to participate in the pathological hyperphosphorylation of tau protein that is observed in neurodegenerative diseases such as Alzheimer's disease.</description><subject>Adult</subject><subject>Alzheimer Disease - enzymology</subject><subject>Alzheimer Disease - pathology</subject><subject>Alzheimer's disease</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Brain - enzymology</subject><subject>Brain - pathology</subject><subject>Casein kinase 1</subject><subject>Casein Kinases</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</subject><subject>Humans</subject><subject>Isoenzymes - metabolism</subject><subject>Isoquinolines - pharmacology</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Middle Aged</subject><subject>Neurofibrillary tangles</subject><subject>Neurofibrils - metabolism</subject><subject>Neurofibrils - pathology</subject><subject>Neurology</subject><subject>Paired‐helical filaments</subject><subject>Protein Kinases - metabolism</subject><subject>Protein phosphorylation</subject><subject>Substrate Specificity</subject><subject>Tau protein</subject><subject>tau Proteins - chemistry</subject><subject>tau Proteins - physiology</subject><issn>0022-3042</issn><issn>1471-4159</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkdFu0zAYhS0EGmXwCEiWQHCV4N9x7FhclW5jgwm46L3lJr-pKycZdqqtXO0ReEaehIR2vUVc2db5zm_7HEJeAcuBCfluk4NQkAkodQ5aq1xqJnnJZH73iMyO2mMyY4zzrGCCPyXPUtowBlJIOCEnulClrMSMtAub0Hf0s-_GDQV6lejSf18PYUfnKfW1twM29NYPa_rN-ojN7_tflxh8bQO98MG22A1pdPXhL-hi39J5-LlG32J8m-iZTzhN_hCt756TJ86GhC8O6ylZXpwvF5fZ9dePV4v5dVaLQsnMFWIFohGrxmHJOKByzHHQtVOVUKUoCgt1pZEpJ10FDBqrVwq15UwzzopT8mY_9ib2P7aYBtP6VGMItsN-m4zSglcA4p8gyDFf4NUIvt-DdexTiujMTfStjTsDzEylmI2ZgjdT8GYqxTyUYu5G98vDNdtVi83Re2hh1F8fdJvGXF20Xe3TEeOs0uO_Ruxsj936gLv_eYH59GXxcCr-AP1rqYg</recordid><startdate>199712</startdate><enddate>199712</enddate><creator>Kuret, Jeff</creator><creator>Johnson, Ginger S.</creator><creator>Cha, Donald</creator><creator>Christenson, Erik R.</creator><creator>DeMaggio, Anthony J.</creator><creator>Hoekstra, Merl F.</creator><general>Blackwell Science Ltd</general><general>Blackwell</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>199712</creationdate><title>Casein Kinase 1 Is Tightly Associated with Paired‐Helical Filaments Isolated from Alzheimer's Disease Brain</title><author>Kuret, Jeff ; Johnson, Ginger S. ; Cha, Donald ; Christenson, Erik R. ; DeMaggio, Anthony J. ; Hoekstra, Merl F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4376-f34b14d4bdfe5021e7f0f219cf78475433a1c89e07f6f8101da9b7e9a2090203</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Adult</topic><topic>Alzheimer Disease - enzymology</topic><topic>Alzheimer Disease - pathology</topic><topic>Alzheimer's disease</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Brain - enzymology</topic><topic>Brain - pathology</topic><topic>Casein kinase 1</topic><topic>Casein Kinases</topic><topic>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</topic><topic>Humans</topic><topic>Isoenzymes - metabolism</topic><topic>Isoquinolines - pharmacology</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Middle Aged</topic><topic>Neurofibrillary tangles</topic><topic>Neurofibrils - metabolism</topic><topic>Neurofibrils - pathology</topic><topic>Neurology</topic><topic>Paired‐helical filaments</topic><topic>Protein Kinases - metabolism</topic><topic>Protein phosphorylation</topic><topic>Substrate Specificity</topic><topic>Tau protein</topic><topic>tau Proteins - chemistry</topic><topic>tau Proteins - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kuret, Jeff</creatorcontrib><creatorcontrib>Johnson, Ginger S.</creatorcontrib><creatorcontrib>Cha, Donald</creatorcontrib><creatorcontrib>Christenson, Erik R.</creatorcontrib><creatorcontrib>DeMaggio, Anthony J.</creatorcontrib><creatorcontrib>Hoekstra, Merl F.</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>Journal of neurochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kuret, Jeff</au><au>Johnson, Ginger S.</au><au>Cha, Donald</au><au>Christenson, Erik R.</au><au>DeMaggio, Anthony J.</au><au>Hoekstra, Merl F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Casein Kinase 1 Is Tightly Associated with Paired‐Helical Filaments Isolated from Alzheimer's Disease Brain</atitle><jtitle>Journal of neurochemistry</jtitle><addtitle>J Neurochem</addtitle><date>1997-12</date><risdate>1997</risdate><volume>69</volume><issue>6</issue><spage>2506</spage><epage>2515</epage><pages>2506-2515</pages><issn>0022-3042</issn><eissn>1471-4159</eissn><coden>JONRA9</coden><abstract>: The protein kinase activity tightly associated with paired helical filaments (PHFs) purified from the brain tissue of individuals with Alzheimer's disease has been characterized in vitro. The activity is shown to phosphorylate casein, an exogenous substrate, with a maximal velocity of ∼2 nmol/min/mg, suggesting it comprises a significant component of the total protein in the PHF preparation. On the basis of substrate selectivity, isoquinoline sulfonamide inhibitor selectivity, in‐gel renaturation assays, and western analysis, the activity consists of closely related members of the α branch of the casein kinase 1 family of protein kinases. Because of its tight association with PHFs and its phosphate‐directed substrate selectivity, casein kinase 1 is positioned to participate in the pathological hyperphosphorylation of tau protein that is observed in neurodegenerative diseases such as Alzheimer's disease.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>9375684</pmid><doi>10.1046/j.1471-4159.1997.69062506.x</doi><tpages>10</tpages></addata></record> |
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| source | Wiley Online Library - AutoHoldings Journals; MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Online Library (Open Access Collection); Free Full-Text Journals in Chemistry |
| subjects | Adult Alzheimer Disease - enzymology Alzheimer Disease - pathology Alzheimer's disease Animals Biological and medical sciences Blotting, Western Brain - enzymology Brain - pathology Casein kinase 1 Casein Kinases Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Humans Isoenzymes - metabolism Isoquinolines - pharmacology Medical sciences Mice Mice, Inbred BALB C Middle Aged Neurofibrillary tangles Neurofibrils - metabolism Neurofibrils - pathology Neurology Paired‐helical filaments Protein Kinases - metabolism Protein phosphorylation Substrate Specificity Tau protein tau Proteins - chemistry tau Proteins - physiology |
| title | Casein Kinase 1 Is Tightly Associated with Paired‐Helical Filaments Isolated from Alzheimer's Disease Brain |
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