Axotomy-Induced Changes of the Protein Profile in the Crayfish Ventral Cord Ganglia
We suggest novel experimental model of nerve injury—bilaterally axotomized ganglia of the crayfish ventral nerve cord (VNC). Using proteomic antibody microarrays, we showed upregulation of apoptosis execution proteins (Bcl-10, caspases 3, 6, and 7, SMAC/DIABLO, AIF), proapoptotic signaling proteins...
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| description | We suggest novel experimental model of nerve injury—bilaterally axotomized ganglia of the crayfish ventral nerve cord (VNC). Using proteomic antibody microarrays, we showed upregulation of apoptosis execution proteins (Bcl-10, caspases 3, 6, and 7, SMAC/DIABLO, AIF), proapoptotic signaling proteins and transcription factors (c-Myc, p38, E2F1, p53, GADD153), and multifunctional proteins capable of initiating apoptosis in specific situations (p75, NMDAR2a) in the axotomized VNC ganglia. Simultaneously, anti-apoptotic proteins (p21WAF-1, MDM2, Bcl-x, Mcl-1, MKP1, MAKAPK2, ERK5, APP, calmodulin, estrogen receptor) were overexpressed. Some proteins associated with actin cytoskeleton (α-catenin, catenin p120CTN, cofilin, p35, myosin Vα) were upregulated, whereas other actin-associated proteins (ezrin, distrophin, tropomyosin, spectrin (α + β), phosphorylated Pyk2) were downregulated. Various cytokeratins and β
IV
-tubulin, components of intermediate filament and microtubule cytoskeletons, were also downregulated that could be the result of tissue destruction. Downregulation of proteins involved in clathrin vesicle formation (AP2α and AP2γ, adaptin (β1 + β2), and syntaxin) indicated impairment of vesicular transport and synaptic processes. The levels of L-DOPA decarboxylase, tyrosine, and tryptophan hydroxylases that mediate synthesis of serotonin, dopamine, norepinephrine, and epinephrine decreased. Overexpression of histone deacetylases HDAC1, HDAC2, and HDAC4 contributed to suppression of transcription and protein synthesis. So, the balance of multidirectional processes aimed either at cell death, or to repair and recovery, determines the cell fate. Present data provide integral, albeit incomplete, view on the nervous tissue response to axotomy. Some of these proteins can be probably potential markers of nerve injury and targets for neuroprotective therapy. |
| doi_str_mv | 10.1007/s12031-019-01329-5 |
| format | Article |
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IV
-tubulin, components of intermediate filament and microtubule cytoskeletons, were also downregulated that could be the result of tissue destruction. Downregulation of proteins involved in clathrin vesicle formation (AP2α and AP2γ, adaptin (β1 + β2), and syntaxin) indicated impairment of vesicular transport and synaptic processes. The levels of L-DOPA decarboxylase, tyrosine, and tryptophan hydroxylases that mediate synthesis of serotonin, dopamine, norepinephrine, and epinephrine decreased. Overexpression of histone deacetylases HDAC1, HDAC2, and HDAC4 contributed to suppression of transcription and protein synthesis. So, the balance of multidirectional processes aimed either at cell death, or to repair and recovery, determines the cell fate. Present data provide integral, albeit incomplete, view on the nervous tissue response to axotomy. Some of these proteins can be probably potential markers of nerve injury and targets for neuroprotective therapy.</description><identifier>ISSN: 0895-8696</identifier><identifier>EISSN: 1559-1166</identifier><identifier>DOI: 10.1007/s12031-019-01329-5</identifier><identifier>PMID: 31066008</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Actin ; Adaptin ; Animals ; Antibody microarrays ; Apoptosis ; Apoptosis-inducing factor ; Aromatic-L-amino-acid decarboxylase ; Astacoidea ; Axotomy ; Bcl-10 protein ; Bcl-x protein ; Biomedical and Life Sciences ; Biomedicine ; c-Myc protein ; Calcium-binding protein ; Calmodulin ; Cell Biology ; Cell death ; Cell fate ; CHOP protein ; Clathrin ; Cofilin ; Crayfish ; Cytoskeleton ; Data recovery ; DIABLO protein ; Dihydroxyphenylalanine ; Dopamine ; Epinephrine ; Estrogens ; Extracellular signal-regulated kinase ; Ganglia ; Ganglia, Invertebrate - metabolism ; Ganglia, Invertebrate - pathology ; Levodopa ; Myosin ; Nervous tissues ; Neurochemistry ; Neurology ; Neurosciences ; Norepinephrine ; p38 Protein ; p53 Protein ; Peripheral Nerve Injuries - genetics ; Peripheral Nerve Injuries - metabolism ; Protein biosynthesis ; Protein synthesis ; Proteins ; Proteome - genetics ; Proteome - metabolism ; Proteomics ; Serotonin ; Spectrin ; Transcription factors ; Tryptophan ; Tyrosine ; α-Catenin</subject><ispartof>Journal of molecular neuroscience, 2019-08, Vol.68 (4), p.667-678</ispartof><rights>Springer Science+Business Media, LLC, part of Springer Nature 2019</rights><rights>Journal of Molecular Neuroscience is a copyright of Springer, (2019). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-cd2dc665ac1dfcd6a65db58d054671401e0270edfc5bbc888c3fbe4c2aceafe23</citedby><cites>FETCH-LOGICAL-c375t-cd2dc665ac1dfcd6a65db58d054671401e0270edfc5bbc888c3fbe4c2aceafe23</cites><orcidid>0000-0002-0344-434X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12031-019-01329-5$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12031-019-01329-5$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31066008$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Demyanenko, Svetlana</creatorcontrib><creatorcontrib>Dzreyan, Valentina</creatorcontrib><creatorcontrib>Uzdensky, Anatoly</creatorcontrib><title>Axotomy-Induced Changes of the Protein Profile in the Crayfish Ventral Cord Ganglia</title><title>Journal of molecular neuroscience</title><addtitle>J Mol Neurosci</addtitle><addtitle>J Mol Neurosci</addtitle><description>We suggest novel experimental model of nerve injury—bilaterally axotomized ganglia of the crayfish ventral nerve cord (VNC). Using proteomic antibody microarrays, we showed upregulation of apoptosis execution proteins (Bcl-10, caspases 3, 6, and 7, SMAC/DIABLO, AIF), proapoptotic signaling proteins and transcription factors (c-Myc, p38, E2F1, p53, GADD153), and multifunctional proteins capable of initiating apoptosis in specific situations (p75, NMDAR2a) in the axotomized VNC ganglia. Simultaneously, anti-apoptotic proteins (p21WAF-1, MDM2, Bcl-x, Mcl-1, MKP1, MAKAPK2, ERK5, APP, calmodulin, estrogen receptor) were overexpressed. Some proteins associated with actin cytoskeleton (α-catenin, catenin p120CTN, cofilin, p35, myosin Vα) were upregulated, whereas other actin-associated proteins (ezrin, distrophin, tropomyosin, spectrin (α + β), phosphorylated Pyk2) were downregulated. Various cytokeratins and β
IV
-tubulin, components of intermediate filament and microtubule cytoskeletons, were also downregulated that could be the result of tissue destruction. Downregulation of proteins involved in clathrin vesicle formation (AP2α and AP2γ, adaptin (β1 + β2), and syntaxin) indicated impairment of vesicular transport and synaptic processes. The levels of L-DOPA decarboxylase, tyrosine, and tryptophan hydroxylases that mediate synthesis of serotonin, dopamine, norepinephrine, and epinephrine decreased. Overexpression of histone deacetylases HDAC1, HDAC2, and HDAC4 contributed to suppression of transcription and protein synthesis. So, the balance of multidirectional processes aimed either at cell death, or to repair and recovery, determines the cell fate. Present data provide integral, albeit incomplete, view on the nervous tissue response to axotomy. Some of these proteins can be probably potential markers of nerve injury and targets for neuroprotective therapy.</description><subject>Actin</subject><subject>Adaptin</subject><subject>Animals</subject><subject>Antibody microarrays</subject><subject>Apoptosis</subject><subject>Apoptosis-inducing factor</subject><subject>Aromatic-L-amino-acid decarboxylase</subject><subject>Astacoidea</subject><subject>Axotomy</subject><subject>Bcl-10 protein</subject><subject>Bcl-x protein</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>c-Myc protein</subject><subject>Calcium-binding protein</subject><subject>Calmodulin</subject><subject>Cell Biology</subject><subject>Cell death</subject><subject>Cell fate</subject><subject>CHOP protein</subject><subject>Clathrin</subject><subject>Cofilin</subject><subject>Crayfish</subject><subject>Cytoskeleton</subject><subject>Data recovery</subject><subject>DIABLO protein</subject><subject>Dihydroxyphenylalanine</subject><subject>Dopamine</subject><subject>Epinephrine</subject><subject>Estrogens</subject><subject>Extracellular signal-regulated kinase</subject><subject>Ganglia</subject><subject>Ganglia, Invertebrate - metabolism</subject><subject>Ganglia, Invertebrate - pathology</subject><subject>Levodopa</subject><subject>Myosin</subject><subject>Nervous tissues</subject><subject>Neurochemistry</subject><subject>Neurology</subject><subject>Neurosciences</subject><subject>Norepinephrine</subject><subject>p38 Protein</subject><subject>p53 Protein</subject><subject>Peripheral Nerve Injuries - genetics</subject><subject>Peripheral Nerve Injuries - metabolism</subject><subject>Protein biosynthesis</subject><subject>Protein synthesis</subject><subject>Proteins</subject><subject>Proteome - genetics</subject><subject>Proteome - metabolism</subject><subject>Proteomics</subject><subject>Serotonin</subject><subject>Spectrin</subject><subject>Transcription factors</subject><subject>Tryptophan</subject><subject>Tyrosine</subject><subject>α-Catenin</subject><issn>0895-8696</issn><issn>1559-1166</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kMFq3DAQhkVpaDZpX6CHYuilFycz0kq2j8Ekm4WFBJL0KmRp3HXwWqlkQ_btI3eTBnroQYzQfPOP-Bj7inCGAMV5RA4Cc8AqHcGrXH5gC5SyyhGV-sgWUFYyL1WljtlJjI8AHJdYfmLHAkEpgHLB7i6e_eh3-3w9uMmSy-qtGX5RzHybjVvKboMfqRvm2nY9Zek6P9fB7NsubrOfNIzB9Fntg8tWabTvzGd21Jo-0pfXesoeri7v6-t8c7Na1xeb3IpCjrl13FmlpLHoWuuUUdI1snQgl6rAJSABL4BSTzaNLcvSirahpeXGkmmJi1P245D7FPzvieKod1201PdmID9FzbnACrgUM_r9H_TRT2FIv0sUx6QDCpkofqBs8DEGavVT6HYm7DWCnpXrg3KdlOs_yvU89O01emp25P6OvDlOgDgAMbWS2_C--z-xLxuNi8A</recordid><startdate>20190801</startdate><enddate>20190801</enddate><creator>Demyanenko, Svetlana</creator><creator>Dzreyan, Valentina</creator><creator>Uzdensky, Anatoly</creator><general>Springer US</general><general>Springer Nature B.V</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>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7TK</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88G</scope><scope>8AO</scope><scope>8FD</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M7N</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PSYQQ</scope><scope>Q9U</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-0344-434X</orcidid></search><sort><creationdate>20190801</creationdate><title>Axotomy-Induced Changes of the Protein Profile in the Crayfish Ventral Cord Ganglia</title><author>Demyanenko, Svetlana ; Dzreyan, Valentina ; Uzdensky, Anatoly</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-cd2dc665ac1dfcd6a65db58d054671401e0270edfc5bbc888c3fbe4c2aceafe23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Actin</topic><topic>Adaptin</topic><topic>Animals</topic><topic>Antibody microarrays</topic><topic>Apoptosis</topic><topic>Apoptosis-inducing factor</topic><topic>Aromatic-L-amino-acid decarboxylase</topic><topic>Astacoidea</topic><topic>Axotomy</topic><topic>Bcl-10 protein</topic><topic>Bcl-x protein</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>c-Myc protein</topic><topic>Calcium-binding protein</topic><topic>Calmodulin</topic><topic>Cell Biology</topic><topic>Cell death</topic><topic>Cell fate</topic><topic>CHOP protein</topic><topic>Clathrin</topic><topic>Cofilin</topic><topic>Crayfish</topic><topic>Cytoskeleton</topic><topic>Data recovery</topic><topic>DIABLO protein</topic><topic>Dihydroxyphenylalanine</topic><topic>Dopamine</topic><topic>Epinephrine</topic><topic>Estrogens</topic><topic>Extracellular signal-regulated kinase</topic><topic>Ganglia</topic><topic>Ganglia, Invertebrate - metabolism</topic><topic>Ganglia, Invertebrate - pathology</topic><topic>Levodopa</topic><topic>Myosin</topic><topic>Nervous tissues</topic><topic>Neurochemistry</topic><topic>Neurology</topic><topic>Neurosciences</topic><topic>Norepinephrine</topic><topic>p38 Protein</topic><topic>p53 Protein</topic><topic>Peripheral Nerve Injuries - genetics</topic><topic>Peripheral Nerve Injuries - metabolism</topic><topic>Protein biosynthesis</topic><topic>Protein synthesis</topic><topic>Proteins</topic><topic>Proteome - genetics</topic><topic>Proteome - metabolism</topic><topic>Proteomics</topic><topic>Serotonin</topic><topic>Spectrin</topic><topic>Transcription factors</topic><topic>Tryptophan</topic><topic>Tyrosine</topic><topic>α-Catenin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Demyanenko, Svetlana</creatorcontrib><creatorcontrib>Dzreyan, Valentina</creatorcontrib><creatorcontrib>Uzdensky, Anatoly</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Databases</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest Psychology</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest One Psychology</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular neuroscience</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Demyanenko, Svetlana</au><au>Dzreyan, Valentina</au><au>Uzdensky, Anatoly</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Axotomy-Induced Changes of the Protein Profile in the Crayfish Ventral Cord Ganglia</atitle><jtitle>Journal of molecular neuroscience</jtitle><stitle>J Mol Neurosci</stitle><addtitle>J Mol Neurosci</addtitle><date>2019-08-01</date><risdate>2019</risdate><volume>68</volume><issue>4</issue><spage>667</spage><epage>678</epage><pages>667-678</pages><issn>0895-8696</issn><eissn>1559-1166</eissn><abstract>We suggest novel experimental model of nerve injury—bilaterally axotomized ganglia of the crayfish ventral nerve cord (VNC). Using proteomic antibody microarrays, we showed upregulation of apoptosis execution proteins (Bcl-10, caspases 3, 6, and 7, SMAC/DIABLO, AIF), proapoptotic signaling proteins and transcription factors (c-Myc, p38, E2F1, p53, GADD153), and multifunctional proteins capable of initiating apoptosis in specific situations (p75, NMDAR2a) in the axotomized VNC ganglia. Simultaneously, anti-apoptotic proteins (p21WAF-1, MDM2, Bcl-x, Mcl-1, MKP1, MAKAPK2, ERK5, APP, calmodulin, estrogen receptor) were overexpressed. Some proteins associated with actin cytoskeleton (α-catenin, catenin p120CTN, cofilin, p35, myosin Vα) were upregulated, whereas other actin-associated proteins (ezrin, distrophin, tropomyosin, spectrin (α + β), phosphorylated Pyk2) were downregulated. Various cytokeratins and β
IV
-tubulin, components of intermediate filament and microtubule cytoskeletons, were also downregulated that could be the result of tissue destruction. Downregulation of proteins involved in clathrin vesicle formation (AP2α and AP2γ, adaptin (β1 + β2), and syntaxin) indicated impairment of vesicular transport and synaptic processes. The levels of L-DOPA decarboxylase, tyrosine, and tryptophan hydroxylases that mediate synthesis of serotonin, dopamine, norepinephrine, and epinephrine decreased. Overexpression of histone deacetylases HDAC1, HDAC2, and HDAC4 contributed to suppression of transcription and protein synthesis. So, the balance of multidirectional processes aimed either at cell death, or to repair and recovery, determines the cell fate. Present data provide integral, albeit incomplete, view on the nervous tissue response to axotomy. Some of these proteins can be probably potential markers of nerve injury and targets for neuroprotective therapy.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>31066008</pmid><doi>10.1007/s12031-019-01329-5</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0002-0344-434X</orcidid></addata></record> |
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| subjects | Actin Adaptin Animals Antibody microarrays Apoptosis Apoptosis-inducing factor Aromatic-L-amino-acid decarboxylase Astacoidea Axotomy Bcl-10 protein Bcl-x protein Biomedical and Life Sciences Biomedicine c-Myc protein Calcium-binding protein Calmodulin Cell Biology Cell death Cell fate CHOP protein Clathrin Cofilin Crayfish Cytoskeleton Data recovery DIABLO protein Dihydroxyphenylalanine Dopamine Epinephrine Estrogens Extracellular signal-regulated kinase Ganglia Ganglia, Invertebrate - metabolism Ganglia, Invertebrate - pathology Levodopa Myosin Nervous tissues Neurochemistry Neurology Neurosciences Norepinephrine p38 Protein p53 Protein Peripheral Nerve Injuries - genetics Peripheral Nerve Injuries - metabolism Protein biosynthesis Protein synthesis Proteins Proteome - genetics Proteome - metabolism Proteomics Serotonin Spectrin Transcription factors Tryptophan Tyrosine α-Catenin |
| title | Axotomy-Induced Changes of the Protein Profile in the Crayfish Ventral Cord Ganglia |
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