Limited proteolytic modification of a neurofilament protein involves a proteinase activated by endogenous levels of calcium
Posttranslational modification of a structural protein by limited proteolysis is demonstrated for the first time in the nervous system. The 145,000 dalton subunit of neurofilaments in mouse retinal ganglion cell (RGC) axons is selectively converted in vitro to the major 143,000 and 140,000 dalton ne...
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| Veröffentlicht in: | Brain research 1983-09, Vol.275 (2), p.384-388 |
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| creator | Nixon, Ralph A. Brown, Beverly A. Marotta, Charles A. |
| description | Posttranslational modification of a structural protein by limited proteolysis is demonstrated for the first time in the nervous system. The 145,000 dalton subunit of neurofilaments in mouse retinal ganglion cell (RGC) axons is selectively converted in vitro to the major 143,000 and 140,000 dalton neurofilament subunits by a neutral proteinase that is activated by endogenous levels of calcium and is distinguishable from other known brain proteinases. The close similarities between this in vitro process and the previously observed modification of the 145,000 dalton neurofilament protein during axoplasmic transport in vivo suggest that the same enzymatic mechanism is involved. These findings imply that limited proteolysis is an active process along central axons in vivo and that this enzyme may play a specific role in the function of the neuronal cytoskeleton. |
| doi_str_mv | 10.1016/0006-8993(83)91003-X |
| format | Article |
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The 145,000 dalton subunit of neurofilaments in mouse retinal ganglion cell (RGC) axons is selectively converted in vitro to the major 143,000 and 140,000 dalton neurofilament subunits by a neutral proteinase that is activated by endogenous levels of calcium and is distinguishable from other known brain proteinases. The close similarities between this in vitro process and the previously observed modification of the 145,000 dalton neurofilament protein during axoplasmic transport in vivo suggest that the same enzymatic mechanism is involved. These findings imply that limited proteolysis is an active process along central axons in vivo and that this enzyme may play a specific role in the function of the neuronal cytoskeleton.</description><identifier>ISSN: 0006-8993</identifier><identifier>EISSN: 1872-6240</identifier><identifier>DOI: 10.1016/0006-8993(83)91003-X</identifier><identifier>PMID: 6414649</identifier><identifier>CODEN: BRREAP</identifier><language>eng</language><publisher>London: Elsevier B.V</publisher><subject>Animals ; Biological and medical sciences ; calcium ; Calcium - metabolism ; Cell structures and functions ; cytoskeletal proteins ; Cytoskeleton, cytoplasm. Intracellular movements ; Electrophoresis, Polyacrylamide Gel ; Enzyme Activation ; Fundamental and applied biological sciences. Psychology ; Intermediate Filament Proteins - genetics ; Intermediate Filament Proteins - isolation & purification ; Kinetics ; Mice ; Mice, Inbred C57BL ; Molecular and cellular biology ; Molecular Weight ; mouse ; Neurofilament Proteins ; neurofilaments ; optic pathway ; Peptide Hydrolases - metabolism ; posttranslational modification ; Protein Processing, Post-Translational ; proteolysis ; retinal ganglion cells</subject><ispartof>Brain research, 1983-09, Vol.275 (2), p.384-388</ispartof><rights>1983 Elsevier Science Publishers B.V., Amsterdam</rights><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c483t-51e586fbdfe743cb68af7902af771e73f3daaf3a54b0d8d5e39cc3e0892fc34f3</citedby><cites>FETCH-LOGICAL-c483t-51e586fbdfe743cb68af7902af771e73f3daaf3a54b0d8d5e39cc3e0892fc34f3</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(83)91003-X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9565667$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6414649$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nixon, Ralph A.</creatorcontrib><creatorcontrib>Brown, Beverly A.</creatorcontrib><creatorcontrib>Marotta, Charles A.</creatorcontrib><title>Limited proteolytic modification of a neurofilament protein involves a proteinase activated by endogenous levels of calcium</title><title>Brain research</title><addtitle>Brain Res</addtitle><description>Posttranslational modification of a structural protein by limited proteolysis is demonstrated for the first time in the nervous system. The 145,000 dalton subunit of neurofilaments in mouse retinal ganglion cell (RGC) axons is selectively converted in vitro to the major 143,000 and 140,000 dalton neurofilament subunits by a neutral proteinase that is activated by endogenous levels of calcium and is distinguishable from other known brain proteinases. The close similarities between this in vitro process and the previously observed modification of the 145,000 dalton neurofilament protein during axoplasmic transport in vivo suggest that the same enzymatic mechanism is involved. These findings imply that limited proteolysis is an active process along central axons in vivo and that this enzyme may play a specific role in the function of the neuronal cytoskeleton.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>calcium</subject><subject>Calcium - metabolism</subject><subject>Cell structures and functions</subject><subject>cytoskeletal proteins</subject><subject>Cytoskeleton, cytoplasm. Intracellular movements</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Activation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Intermediate Filament Proteins - genetics</subject><subject>Intermediate Filament Proteins - isolation & purification</subject><subject>Kinetics</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Molecular and cellular biology</subject><subject>Molecular Weight</subject><subject>mouse</subject><subject>Neurofilament Proteins</subject><subject>neurofilaments</subject><subject>optic pathway</subject><subject>Peptide Hydrolases - metabolism</subject><subject>posttranslational modification</subject><subject>Protein Processing, Post-Translational</subject><subject>proteolysis</subject><subject>retinal ganglion cells</subject><issn>0006-8993</issn><issn>1872-6240</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU-L1TAUxYMo43P0GyhkIaKLatKkabIZkMF_8MCNwuxCmtxIJE3Gpi08_PKmvvKWuklI7u8eDucg9JySt5RQ8Y4QIhqpFHst2RtFCWHN3QN0oLJvG9Fy8hAdLshj9KSUn_XJmCJX6EpwygVXB_T7GMYwg8P3U54hx9McLB6zCz5YM4eccPbY4ATLlH2IZoQ0n9mQcEhrjiuUCuxfpgA2dg6r2TSHE4bk8g9IeSk4wgqxbHrWRBuW8Sl65E0s8Gy_r9H3jx--3X5ujl8_fbl9f2wsl2xuOgqdFH5wHnrO7CCk8b0ibT17Cj3zzBnjmen4QJx0HTBlLQMiVest455do1dn3Wry1wJl1mMoFmI0CaoxLYlQXPHuvyBlfUsk4RXkZ9BOuZQJvL6fwmimk6ZEb-XoLXm9Ja8l03_L0Xd17cWuvwwjuMvS3kadv9znptSM_GSSDeWCqU50QvQVuzljNU5YA0y62ADJggsT2Fm7HP7t4w_9yq62</recordid><startdate>19830926</startdate><enddate>19830926</enddate><creator>Nixon, Ralph A.</creator><creator>Brown, Beverly A.</creator><creator>Marotta, Charles A.</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>19830926</creationdate><title>Limited proteolytic modification of a neurofilament protein involves a proteinase activated by endogenous levels of calcium</title><author>Nixon, Ralph A. ; Brown, Beverly A. ; Marotta, Charles A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c483t-51e586fbdfe743cb68af7902af771e73f3daaf3a54b0d8d5e39cc3e0892fc34f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>calcium</topic><topic>Calcium - metabolism</topic><topic>Cell structures and functions</topic><topic>cytoskeletal proteins</topic><topic>Cytoskeleton, cytoplasm. Intracellular movements</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Activation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Intermediate Filament Proteins - genetics</topic><topic>Intermediate Filament Proteins - isolation & purification</topic><topic>Kinetics</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Molecular and cellular biology</topic><topic>Molecular Weight</topic><topic>mouse</topic><topic>Neurofilament Proteins</topic><topic>neurofilaments</topic><topic>optic pathway</topic><topic>Peptide Hydrolases - metabolism</topic><topic>posttranslational modification</topic><topic>Protein Processing, Post-Translational</topic><topic>proteolysis</topic><topic>retinal ganglion cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nixon, Ralph A.</creatorcontrib><creatorcontrib>Brown, Beverly A.</creatorcontrib><creatorcontrib>Marotta, Charles A.</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>Nixon, Ralph A.</au><au>Brown, Beverly A.</au><au>Marotta, Charles A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Limited proteolytic modification of a neurofilament protein involves a proteinase activated by endogenous levels of calcium</atitle><jtitle>Brain research</jtitle><addtitle>Brain Res</addtitle><date>1983-09-26</date><risdate>1983</risdate><volume>275</volume><issue>2</issue><spage>384</spage><epage>388</epage><pages>384-388</pages><issn>0006-8993</issn><eissn>1872-6240</eissn><coden>BRREAP</coden><abstract>Posttranslational modification of a structural protein by limited proteolysis is demonstrated for the first time in the nervous system. The 145,000 dalton subunit of neurofilaments in mouse retinal ganglion cell (RGC) axons is selectively converted in vitro to the major 143,000 and 140,000 dalton neurofilament subunits by a neutral proteinase that is activated by endogenous levels of calcium and is distinguishable from other known brain proteinases. The close similarities between this in vitro process and the previously observed modification of the 145,000 dalton neurofilament protein during axoplasmic transport in vivo suggest that the same enzymatic mechanism is involved. These findings imply that limited proteolysis is an active process along central axons in vivo and that this enzyme may play a specific role in the function of the neuronal cytoskeleton.</abstract><cop>London</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>6414649</pmid><doi>10.1016/0006-8993(83)91003-X</doi><tpages>5</tpages></addata></record> |
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| ispartof | Brain research, 1983-09, Vol.275 (2), p.384-388 |
| issn | 0006-8993 1872-6240 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Animals Biological and medical sciences calcium Calcium - metabolism Cell structures and functions cytoskeletal proteins Cytoskeleton, cytoplasm. Intracellular movements Electrophoresis, Polyacrylamide Gel Enzyme Activation Fundamental and applied biological sciences. Psychology Intermediate Filament Proteins - genetics Intermediate Filament Proteins - isolation & purification Kinetics Mice Mice, Inbred C57BL Molecular and cellular biology Molecular Weight mouse Neurofilament Proteins neurofilaments optic pathway Peptide Hydrolases - metabolism posttranslational modification Protein Processing, Post-Translational proteolysis retinal ganglion cells |
| title | Limited proteolytic modification of a neurofilament protein involves a proteinase activated by endogenous levels of calcium |
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