Axonal transport of actin and actin-binding proteins in the rat sciatic nerve
Actin is one of the major cytoskeletal proteins carried in slow axonal transport. Since more than 50% of actin in the axon was recovered in the high-speed supernatant, we looked for G-actin-binding proteins in slow axonal transport. Two weeks after injection of l-[ 35S]methionine into the rat spinal...
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| Veröffentlicht in: | Neuroscience research 1994-05, Vol.19 (3), p.295-302 |
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| creator | Tanaka, Kiyoshi Tashiro, Tomoko Sekimoto, Sumito Komiya, Yoshiaki |
| description | Actin is one of the major cytoskeletal proteins carried in slow axonal transport. Since more than 50% of actin in the axon was recovered in the high-speed supernatant, we looked for G-actin-binding proteins in slow axonal transport. Two weeks after injection of
l-[
35S]methionine into the rat spinal cord (L
3–L
5), labeled proteins in the sciatic nerve were extracted and those with potential abilities to interact with G-actin were detected by two independent methods: (A) DNAase I affinity chromatography and (B) blot overlay with biotinylated actin. By method (A), a 68 kDa Ca
2+-dependent binding protein and a 45 kDa Ca
2+-independent binding protein were detected. The 68 kDa protein was also a major protein binding to actin in method (B). The 68 kDa protein was identified with the Ca
2+-dependent phospholipid binding protein annexin VI by two-dimensional electrophoresis and Western blotting. As annexin VI is a component of slow axonal transport, it does not seem to be bound to membranous organelles in the axon. Our results suggest that annexin VI may play a role in the control of actin assembly and membrane-microfilament interaction. |
| doi_str_mv | 10.1016/0168-0102(94)90042-6 |
| format | Article |
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l-[
35S]methionine into the rat spinal cord (L
3–L
5), labeled proteins in the sciatic nerve were extracted and those with potential abilities to interact with G-actin were detected by two independent methods: (A) DNAase I affinity chromatography and (B) blot overlay with biotinylated actin. By method (A), a 68 kDa Ca
2+-dependent binding protein and a 45 kDa Ca
2+-independent binding protein were detected. The 68 kDa protein was also a major protein binding to actin in method (B). The 68 kDa protein was identified with the Ca
2+-dependent phospholipid binding protein annexin VI by two-dimensional electrophoresis and Western blotting. As annexin VI is a component of slow axonal transport, it does not seem to be bound to membranous organelles in the axon. Our results suggest that annexin VI may play a role in the control of actin assembly and membrane-microfilament interaction.</description><identifier>ISSN: 0168-0102</identifier><identifier>EISSN: 1872-8111</identifier><identifier>DOI: 10.1016/0168-0102(94)90042-6</identifier><identifier>PMID: 7520144</identifier><language>eng</language><publisher>Ireland: Elsevier Ireland Ltd</publisher><subject>Actin ; Actin-binding-protein ; Actins - metabolism ; Animals ; Annexin VI ; Axonal Transport ; Calcium - pharmacology ; Calelectrin ; Chromatography, Affinity ; Deoxyribonuclease I ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; Immunoblotting ; Male ; Methionine - metabolism ; Microfilament Proteins - biosynthesis ; Microfilament Proteins - isolation & purification ; Microfilament Proteins - metabolism ; Molecular Weight ; Rats ; Rats, Wistar ; Sciatic nerve ; Sciatic Nerve - physiology ; Spinal Cord - physiology ; Sulfur Radioisotopes</subject><ispartof>Neuroscience research, 1994-05, Vol.19 (3), p.295-302</ispartof><rights>1994</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-d996581a0efe29b9e2ae7185f1523c7063d53fff78026cccaecf5273e13a7d9c3</citedby><cites>FETCH-LOGICAL-c357t-d996581a0efe29b9e2ae7185f1523c7063d53fff78026cccaecf5273e13a7d9c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0168010294900426$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7520144$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tanaka, Kiyoshi</creatorcontrib><creatorcontrib>Tashiro, Tomoko</creatorcontrib><creatorcontrib>Sekimoto, Sumito</creatorcontrib><creatorcontrib>Komiya, Yoshiaki</creatorcontrib><title>Axonal transport of actin and actin-binding proteins in the rat sciatic nerve</title><title>Neuroscience research</title><addtitle>Neurosci Res</addtitle><description>Actin is one of the major cytoskeletal proteins carried in slow axonal transport. Since more than 50% of actin in the axon was recovered in the high-speed supernatant, we looked for G-actin-binding proteins in slow axonal transport. Two weeks after injection of
l-[
35S]methionine into the rat spinal cord (L
3–L
5), labeled proteins in the sciatic nerve were extracted and those with potential abilities to interact with G-actin were detected by two independent methods: (A) DNAase I affinity chromatography and (B) blot overlay with biotinylated actin. By method (A), a 68 kDa Ca
2+-dependent binding protein and a 45 kDa Ca
2+-independent binding protein were detected. The 68 kDa protein was also a major protein binding to actin in method (B). The 68 kDa protein was identified with the Ca
2+-dependent phospholipid binding protein annexin VI by two-dimensional electrophoresis and Western blotting. As annexin VI is a component of slow axonal transport, it does not seem to be bound to membranous organelles in the axon. Our results suggest that annexin VI may play a role in the control of actin assembly and membrane-microfilament interaction.</description><subject>Actin</subject><subject>Actin-binding-protein</subject><subject>Actins - metabolism</subject><subject>Animals</subject><subject>Annexin VI</subject><subject>Axonal Transport</subject><subject>Calcium - pharmacology</subject><subject>Calelectrin</subject><subject>Chromatography, Affinity</subject><subject>Deoxyribonuclease I</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Immunoblotting</subject><subject>Male</subject><subject>Methionine - metabolism</subject><subject>Microfilament Proteins - biosynthesis</subject><subject>Microfilament Proteins - isolation & purification</subject><subject>Microfilament Proteins - metabolism</subject><subject>Molecular Weight</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Sciatic nerve</subject><subject>Sciatic Nerve - physiology</subject><subject>Spinal Cord - physiology</subject><subject>Sulfur Radioisotopes</subject><issn>0168-0102</issn><issn>1872-8111</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtKAzEUhoMotVbfQCEr0cVobjOZbIRSvEHFja5DmjnRyDRTk7To2zt1iksXh3Pg_8_tQ-iUkitKaHXdR10QStiFEpeKEMGKag-NaS1ZUVNK99H4z3KIjlL6IIRwJfgIjWTJCBVijJ6mX10wLc7RhLTqYsadw8ZmH7AJzVAVCx8aH97wKnYZfEi4V_M74GgyTtab7C0OEDdwjA6caROc7PIEvd7dvsweivnz_eNsOi8sL2UuGqWqsqaGgAOmFgqYAUnr0tGScStJxZuSO-dkTVhlrTVgXckkB8qNbJTlE3Q-zO0v-lxDynrpk4W2NQG6ddKyqoSkjPdGMRht7FKK4PQq-qWJ35oSvaWot4j0FpFWQv9S1FXfdrabv14soflr2mHr9ZtBh_7JjYeoewwQLDQ-gs266fz_C34AOsGA9A</recordid><startdate>19940501</startdate><enddate>19940501</enddate><creator>Tanaka, Kiyoshi</creator><creator>Tashiro, Tomoko</creator><creator>Sekimoto, Sumito</creator><creator>Komiya, Yoshiaki</creator><general>Elsevier Ireland Ltd</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>19940501</creationdate><title>Axonal transport of actin and actin-binding proteins in the rat sciatic nerve</title><author>Tanaka, Kiyoshi ; Tashiro, Tomoko ; Sekimoto, Sumito ; Komiya, Yoshiaki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-d996581a0efe29b9e2ae7185f1523c7063d53fff78026cccaecf5273e13a7d9c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Actin</topic><topic>Actin-binding-protein</topic><topic>Actins - metabolism</topic><topic>Animals</topic><topic>Annexin VI</topic><topic>Axonal Transport</topic><topic>Calcium - pharmacology</topic><topic>Calelectrin</topic><topic>Chromatography, Affinity</topic><topic>Deoxyribonuclease I</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Immunoblotting</topic><topic>Male</topic><topic>Methionine - metabolism</topic><topic>Microfilament Proteins - biosynthesis</topic><topic>Microfilament Proteins - isolation & purification</topic><topic>Microfilament Proteins - metabolism</topic><topic>Molecular Weight</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Sciatic nerve</topic><topic>Sciatic Nerve - physiology</topic><topic>Spinal Cord - physiology</topic><topic>Sulfur Radioisotopes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tanaka, Kiyoshi</creatorcontrib><creatorcontrib>Tashiro, Tomoko</creatorcontrib><creatorcontrib>Sekimoto, Sumito</creatorcontrib><creatorcontrib>Komiya, Yoshiaki</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>Neuroscience research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tanaka, Kiyoshi</au><au>Tashiro, Tomoko</au><au>Sekimoto, Sumito</au><au>Komiya, Yoshiaki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Axonal transport of actin and actin-binding proteins in the rat sciatic nerve</atitle><jtitle>Neuroscience research</jtitle><addtitle>Neurosci Res</addtitle><date>1994-05-01</date><risdate>1994</risdate><volume>19</volume><issue>3</issue><spage>295</spage><epage>302</epage><pages>295-302</pages><issn>0168-0102</issn><eissn>1872-8111</eissn><abstract>Actin is one of the major cytoskeletal proteins carried in slow axonal transport. Since more than 50% of actin in the axon was recovered in the high-speed supernatant, we looked for G-actin-binding proteins in slow axonal transport. Two weeks after injection of
l-[
35S]methionine into the rat spinal cord (L
3–L
5), labeled proteins in the sciatic nerve were extracted and those with potential abilities to interact with G-actin were detected by two independent methods: (A) DNAase I affinity chromatography and (B) blot overlay with biotinylated actin. By method (A), a 68 kDa Ca
2+-dependent binding protein and a 45 kDa Ca
2+-independent binding protein were detected. The 68 kDa protein was also a major protein binding to actin in method (B). The 68 kDa protein was identified with the Ca
2+-dependent phospholipid binding protein annexin VI by two-dimensional electrophoresis and Western blotting. As annexin VI is a component of slow axonal transport, it does not seem to be bound to membranous organelles in the axon. Our results suggest that annexin VI may play a role in the control of actin assembly and membrane-microfilament interaction.</abstract><cop>Ireland</cop><pub>Elsevier Ireland Ltd</pub><pmid>7520144</pmid><doi>10.1016/0168-0102(94)90042-6</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0168-0102 |
| ispartof | Neuroscience research, 1994-05, Vol.19 (3), p.295-302 |
| issn | 0168-0102 1872-8111 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76647123 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Actin Actin-binding-protein Actins - metabolism Animals Annexin VI Axonal Transport Calcium - pharmacology Calelectrin Chromatography, Affinity Deoxyribonuclease I Electrophoresis, Gel, Two-Dimensional Electrophoresis, Polyacrylamide Gel Immunoblotting Male Methionine - metabolism Microfilament Proteins - biosynthesis Microfilament Proteins - isolation & purification Microfilament Proteins - metabolism Molecular Weight Rats Rats, Wistar Sciatic nerve Sciatic Nerve - physiology Spinal Cord - physiology Sulfur Radioisotopes |
| title | Axonal transport of actin and actin-binding proteins in the rat sciatic nerve |
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