Evidence that the monoclonal antibodies SMI-31 and SMI-34 recognize different phosphorylation-dependent epitopes of the murine high molecular mass neurofilament subunit
The monoclonal antibodies SMI-31 and SMI-34 react with phosphate-dependent epitopes of the high molecular mass (200 kDa) neurofilament protein (Hphos). Determination of whether or not these monoclonals react with different epitopes would assist in interpretation of post mortem immunocytochemical ana...
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| Veröffentlicht in: | Journal of neuroimmunology 1993-04, Vol.44 (1), p.117-121 |
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| creator | Shea, Thomas B. Beermann, Mary Lou |
| description | The monoclonal antibodies SMI-31 and SMI-34 react with phosphate-dependent epitopes of the high molecular mass (200 kDa) neurofilament protein (Hphos). Determination of whether or not these monoclonals react with different epitopes would assist in interpretation of post mortem immunocytochemical analyses in neurodegenerative disorders and in normal aging. We therefore examined the relative immunoreactivity of these antibodies against Triton-insoluble (cytoskeleton-associated) and Triton-soluble Hphos variants in NB2a/d1 neuroblastoma and post-natal mouse brain in immunoblot analysis. Densitometric analysis yielded a ‘reactivity ratio’ (soluble Hphos/insoluble Hphos) for each antibody. This ratio was approximately 44% and 87% less for SMI-34 than for SMI-31 in neuroblastoma and brain, respectively. These findings confirm that the SMI-34 epitope is distinct from that recognized by SMI-31, and, in these systems, is preferentially associated with the cytoskeleton. |
| doi_str_mv | 10.1016/0165-5728(93)90274-3 |
| format | Article |
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Determination of whether or not these monoclonals react with different epitopes would assist in interpretation of post mortem immunocytochemical analyses in neurodegenerative disorders and in normal aging. We therefore examined the relative immunoreactivity of these antibodies against Triton-insoluble (cytoskeleton-associated) and Triton-soluble Hphos variants in NB2a/d1 neuroblastoma and post-natal mouse brain in immunoblot analysis. Densitometric analysis yielded a ‘reactivity ratio’ (soluble Hphos/insoluble Hphos) for each antibody. This ratio was approximately 44% and 87% less for SMI-34 than for SMI-31 in neuroblastoma and brain, respectively. 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Psychology ; Fundamental immunology ; Mice ; Molecular immunology ; Molecular Weight ; Neurodegeneration ; Neurofibrillary tangle ; Neurofilament phosphorylation ; Neurofilament Proteins - chemistry ; Neurofilament Proteins - immunology ; Neuronal aging ; Phosphorylation ; Polyethylene Glycols ; SMI-31 ; SMI-34 ; Solubility</subject><ispartof>Journal of neuroimmunology, 1993-04, Vol.44 (1), p.117-121</ispartof><rights>1993</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-be3c371389c3d951b8b691ab9e220a3a5d78e6644580bfb31b1c9a6a937a03853</citedby><cites>FETCH-LOGICAL-c386t-be3c371389c3d951b8b691ab9e220a3a5d78e6644580bfb31b1c9a6a937a03853</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0165-5728(93)90274-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4795872$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7684397$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shea, Thomas B.</creatorcontrib><creatorcontrib>Beermann, Mary Lou</creatorcontrib><title>Evidence that the monoclonal antibodies SMI-31 and SMI-34 recognize different phosphorylation-dependent epitopes of the murine high molecular mass neurofilament subunit</title><title>Journal of neuroimmunology</title><addtitle>J Neuroimmunol</addtitle><description>The monoclonal antibodies SMI-31 and SMI-34 react with phosphate-dependent epitopes of the high molecular mass (200 kDa) neurofilament protein (Hphos). Determination of whether or not these monoclonals react with different epitopes would assist in interpretation of post mortem immunocytochemical analyses in neurodegenerative disorders and in normal aging. We therefore examined the relative immunoreactivity of these antibodies against Triton-insoluble (cytoskeleton-associated) and Triton-soluble Hphos variants in NB2a/d1 neuroblastoma and post-natal mouse brain in immunoblot analysis. Densitometric analysis yielded a ‘reactivity ratio’ (soluble Hphos/insoluble Hphos) for each antibody. This ratio was approximately 44% and 87% less for SMI-34 than for SMI-31 in neuroblastoma and brain, respectively. These findings confirm that the SMI-34 epitope is distinct from that recognized by SMI-31, and, in these systems, is preferentially associated with the cytoskeleton.</description><subject>Alzheimer's disease</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antigenic determinants, haptens, artificial antigens</subject><subject>Antigens</subject><subject>Biological and medical sciences</subject><subject>Epitopes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Mice</subject><subject>Molecular immunology</subject><subject>Molecular Weight</subject><subject>Neurodegeneration</subject><subject>Neurofibrillary tangle</subject><subject>Neurofilament phosphorylation</subject><subject>Neurofilament Proteins - chemistry</subject><subject>Neurofilament Proteins - immunology</subject><subject>Neuronal aging</subject><subject>Phosphorylation</subject><subject>Polyethylene Glycols</subject><subject>SMI-31</subject><subject>SMI-34</subject><subject>Solubility</subject><issn>0165-5728</issn><issn>1872-8421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9UU1v1DAUtBCobAv_ACQfEIJDII7tOL4goaqFSkUcgLPlj5eukWMHO6lUfhE_E4dd7ZHDs5_8ZuZZMwi9IO070pL-fS3ecNENbyR9K9tOsIY-QjsyiK4ZWEceo90J8hSdl_KzbQmnTJ6hM9EPjEqxQ3-u7r2DaAEve73UA_CUYrIhRR2wjos3yXko-NuXm4aS-uIOLcMZbLqL_jdg58cRMsQFz_tUauWHoBefYuNghui2Ccx-SXMVSuNhy5p9BLz3d_u6MYBdg8540qXgCGtOow962ohlNWv0yzP0ZNShwPPjfYF-XF99v_zc3H79dHP58baxdOiXxgC1VBA6SEud5MQMppdEGwld12qquRMD9D1jfGjNaCgxxErda0mFbunA6QV6fdCdc_q1QlnU5IuFEHSEtBYluGCEE1GB7AC0OZWSYVRz9pPOD4q0agtIbe6rzX0lqfoXkKKV9vKov5oJ3Il0TKTOXx3nulgdxqyj9eUEY0LyGnCFfTjAoHpx7yGrYv2Wo_M1l0W55P__j7-CI69H</recordid><startdate>19930401</startdate><enddate>19930401</enddate><creator>Shea, Thomas B.</creator><creator>Beermann, Mary Lou</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>7X8</scope></search><sort><creationdate>19930401</creationdate><title>Evidence that the monoclonal antibodies SMI-31 and SMI-34 recognize different phosphorylation-dependent epitopes of the murine high molecular mass neurofilament subunit</title><author>Shea, Thomas B. ; Beermann, Mary Lou</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-be3c371389c3d951b8b691ab9e220a3a5d78e6644580bfb31b1c9a6a937a03853</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Alzheimer's disease</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antigenic determinants, haptens, artificial antigens</topic><topic>Antigens</topic><topic>Biological and medical sciences</topic><topic>Epitopes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Mice</topic><topic>Molecular immunology</topic><topic>Molecular Weight</topic><topic>Neurodegeneration</topic><topic>Neurofibrillary tangle</topic><topic>Neurofilament phosphorylation</topic><topic>Neurofilament Proteins - chemistry</topic><topic>Neurofilament Proteins - immunology</topic><topic>Neuronal aging</topic><topic>Phosphorylation</topic><topic>Polyethylene Glycols</topic><topic>SMI-31</topic><topic>SMI-34</topic><topic>Solubility</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shea, Thomas B.</creatorcontrib><creatorcontrib>Beermann, Mary Lou</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>MEDLINE - Academic</collection><jtitle>Journal of neuroimmunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shea, Thomas B.</au><au>Beermann, Mary Lou</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence that the monoclonal antibodies SMI-31 and SMI-34 recognize different phosphorylation-dependent epitopes of the murine high molecular mass neurofilament subunit</atitle><jtitle>Journal of neuroimmunology</jtitle><addtitle>J Neuroimmunol</addtitle><date>1993-04-01</date><risdate>1993</risdate><volume>44</volume><issue>1</issue><spage>117</spage><epage>121</epage><pages>117-121</pages><issn>0165-5728</issn><eissn>1872-8421</eissn><coden>JNRIDW</coden><abstract>The monoclonal antibodies SMI-31 and SMI-34 react with phosphate-dependent epitopes of the high molecular mass (200 kDa) neurofilament protein (Hphos). Determination of whether or not these monoclonals react with different epitopes would assist in interpretation of post mortem immunocytochemical analyses in neurodegenerative disorders and in normal aging. We therefore examined the relative immunoreactivity of these antibodies against Triton-insoluble (cytoskeleton-associated) and Triton-soluble Hphos variants in NB2a/d1 neuroblastoma and post-natal mouse brain in immunoblot analysis. Densitometric analysis yielded a ‘reactivity ratio’ (soluble Hphos/insoluble Hphos) for each antibody. This ratio was approximately 44% and 87% less for SMI-34 than for SMI-31 in neuroblastoma and brain, respectively. These findings confirm that the SMI-34 epitope is distinct from that recognized by SMI-31, and, in these systems, is preferentially associated with the cytoskeleton.</abstract><cop>London</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>7684397</pmid><doi>10.1016/0165-5728(93)90274-3</doi><tpages>5</tpages></addata></record> |
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| identifier | ISSN: 0165-5728 |
| ispartof | Journal of neuroimmunology, 1993-04, Vol.44 (1), p.117-121 |
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| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Alzheimer's disease Animals Antibodies, Monoclonal - immunology Antigenic determinants, haptens, artificial antigens Antigens Biological and medical sciences Epitopes Fundamental and applied biological sciences. Psychology Fundamental immunology Mice Molecular immunology Molecular Weight Neurodegeneration Neurofibrillary tangle Neurofilament phosphorylation Neurofilament Proteins - chemistry Neurofilament Proteins - immunology Neuronal aging Phosphorylation Polyethylene Glycols SMI-31 SMI-34 Solubility |
| title | Evidence that the monoclonal antibodies SMI-31 and SMI-34 recognize different phosphorylation-dependent epitopes of the murine high molecular mass neurofilament subunit |
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