Transglutaminase 2: Friend or foe? The discordant role in neurons and astrocytes
Members of the transglutaminase family catalyze the formation of isopeptide bonds between a polypeptide‐bound glutamine and a low molecular weight amine (e.g., spermidine) or the ɛ‐amino group of a polypeptide‐bound lysine. Transglutaminase 2 (TG2), a prominent member of this family, is unique becau...
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description | Members of the transglutaminase family catalyze the formation of isopeptide bonds between a polypeptide‐bound glutamine and a low molecular weight amine (e.g., spermidine) or the ɛ‐amino group of a polypeptide‐bound lysine. Transglutaminase 2 (TG2), a prominent member of this family, is unique because in addition to being a transamidating enzyme, it exhibits numerous other activities. As a result, TG2 plays a role in many physiological processes, and its function is highly cell type specific and relies upon a number of factors, including conformation, cellular compartment location, and local concentrations of Ca2+ and guanine nucleotides. TG2 is the most abundant transglutaminase in the central nervous system (CNS) and plays a pivotal role in the CNS injury response. How TG2 affects the cell in response to an insult is strikingly different in astrocytes and neurons. In neurons, TG2 supports survival. Overexpression of TG2 in primary neurons protects against oxygen and glucose deprivation (OGD)‐induced cell death and in vivo results in a reduction in infarct volume subsequent to a stroke. Knockdown of TG2 in primary neurons results in a loss of viability. In contrast, deletion of TG2 from astrocytes results in increased survival following OGD and improved ability to protect neurons from injury. Here, a brief overview of TG2 is provided, followed by a discussion of the role of TG2 in transcriptional regulation, cellular dynamics, and cell death. The differing roles TG2 plays in neurons and astrocytes are highlighted and compared to how TG2 functions in other cell types. |
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The discordant role in neurons and astrocytes</title><source>Wiley-Blackwell Journals</source><source>MEDLINE</source><creator>Quinn, Breandan R. ; Yunes‐Medina, Laura ; Johnson, Gail V. W.</creator><creatorcontrib>Quinn, Breandan R. ; Yunes‐Medina, Laura ; Johnson, Gail V. W.</creatorcontrib><description>Members of the transglutaminase family catalyze the formation of isopeptide bonds between a polypeptide‐bound glutamine and a low molecular weight amine (e.g., spermidine) or the ɛ‐amino group of a polypeptide‐bound lysine. Transglutaminase 2 (TG2), a prominent member of this family, is unique because in addition to being a transamidating enzyme, it exhibits numerous other activities. As a result, TG2 plays a role in many physiological processes, and its function is highly cell type specific and relies upon a number of factors, including conformation, cellular compartment location, and local concentrations of Ca2+ and guanine nucleotides. TG2 is the most abundant transglutaminase in the central nervous system (CNS) and plays a pivotal role in the CNS injury response. How TG2 affects the cell in response to an insult is strikingly different in astrocytes and neurons. In neurons, TG2 supports survival. Overexpression of TG2 in primary neurons protects against oxygen and glucose deprivation (OGD)‐induced cell death and in vivo results in a reduction in infarct volume subsequent to a stroke. Knockdown of TG2 in primary neurons results in a loss of viability. In contrast, deletion of TG2 from astrocytes results in increased survival following OGD and improved ability to protect neurons from injury. Here, a brief overview of TG2 is provided, followed by a discussion of the role of TG2 in transcriptional regulation, cellular dynamics, and cell death. The differing roles TG2 plays in neurons and astrocytes are highlighted and compared to how TG2 functions in other cell types.</description><identifier>ISSN: 0360-4012</identifier><identifier>EISSN: 1097-4547</identifier><identifier>DOI: 10.1002/jnr.24239</identifier><identifier>PMID: 29570839</identifier><language>eng</language><publisher>United States: Wiley Subscription Services, Inc</publisher><subject>Animals ; Apoptosis ; Astrocytes ; Astrocytes - cytology ; Astrocytes - enzymology ; Calcium ; Calcium ions ; Cell death ; Cell Death - physiology ; Central nervous system ; Clonal deletion ; Conformation ; cytoskeleton ; Deprivation ; Gene regulation ; Glutamine ; GTP-Binding Proteins - chemistry ; GTP-Binding Proteins - metabolism ; Guanine ; Humans ; injury ; Low molecular weights ; Lysine ; Models, Molecular ; Molecular chains ; Molecular weight ; neurites ; Neurons ; Neurons - cytology ; Neurons - enzymology ; Nucleotides ; Polypeptides ; Spermidine ; Survival ; Transcription ; transcription regulation ; Transglutaminase 2 ; Transglutaminases - chemistry ; Transglutaminases - metabolism ; Viability</subject><ispartof>Journal of neuroscience research, 2018-07, Vol.96 (7), p.1150-1158</ispartof><rights>2018 Wiley Periodicals, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5359-42e3ec33dcb48a34d91b031fb40197a21187452a1c03783dd245245ee4cedaac3</citedby><cites>FETCH-LOGICAL-c5359-42e3ec33dcb48a34d91b031fb40197a21187452a1c03783dd245245ee4cedaac3</cites><orcidid>0000-0003-3464-0404</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjnr.24239$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjnr.24239$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,780,784,885,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29570839$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Quinn, Breandan R.</creatorcontrib><creatorcontrib>Yunes‐Medina, Laura</creatorcontrib><creatorcontrib>Johnson, Gail V. W.</creatorcontrib><title>Transglutaminase 2: Friend or foe? The discordant role in neurons and astrocytes</title><title>Journal of neuroscience research</title><addtitle>J Neurosci Res</addtitle><description>Members of the transglutaminase family catalyze the formation of isopeptide bonds between a polypeptide‐bound glutamine and a low molecular weight amine (e.g., spermidine) or the ɛ‐amino group of a polypeptide‐bound lysine. Transglutaminase 2 (TG2), a prominent member of this family, is unique because in addition to being a transamidating enzyme, it exhibits numerous other activities. As a result, TG2 plays a role in many physiological processes, and its function is highly cell type specific and relies upon a number of factors, including conformation, cellular compartment location, and local concentrations of Ca2+ and guanine nucleotides. TG2 is the most abundant transglutaminase in the central nervous system (CNS) and plays a pivotal role in the CNS injury response. How TG2 affects the cell in response to an insult is strikingly different in astrocytes and neurons. In neurons, TG2 supports survival. Overexpression of TG2 in primary neurons protects against oxygen and glucose deprivation (OGD)‐induced cell death and in vivo results in a reduction in infarct volume subsequent to a stroke. Knockdown of TG2 in primary neurons results in a loss of viability. In contrast, deletion of TG2 from astrocytes results in increased survival following OGD and improved ability to protect neurons from injury. Here, a brief overview of TG2 is provided, followed by a discussion of the role of TG2 in transcriptional regulation, cellular dynamics, and cell death. The differing roles TG2 plays in neurons and astrocytes are highlighted and compared to how TG2 functions in other cell types.</description><subject>Animals</subject><subject>Apoptosis</subject><subject>Astrocytes</subject><subject>Astrocytes - cytology</subject><subject>Astrocytes - enzymology</subject><subject>Calcium</subject><subject>Calcium ions</subject><subject>Cell death</subject><subject>Cell Death - physiology</subject><subject>Central nervous system</subject><subject>Clonal deletion</subject><subject>Conformation</subject><subject>cytoskeleton</subject><subject>Deprivation</subject><subject>Gene regulation</subject><subject>Glutamine</subject><subject>GTP-Binding Proteins - chemistry</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>Guanine</subject><subject>Humans</subject><subject>injury</subject><subject>Low molecular weights</subject><subject>Lysine</subject><subject>Models, Molecular</subject><subject>Molecular chains</subject><subject>Molecular weight</subject><subject>neurites</subject><subject>Neurons</subject><subject>Neurons - cytology</subject><subject>Neurons - enzymology</subject><subject>Nucleotides</subject><subject>Polypeptides</subject><subject>Spermidine</subject><subject>Survival</subject><subject>Transcription</subject><subject>transcription regulation</subject><subject>Transglutaminase 2</subject><subject>Transglutaminases - chemistry</subject><subject>Transglutaminases - metabolism</subject><subject>Viability</subject><issn>0360-4012</issn><issn>1097-4547</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kU1LJDEQhoMoOn4c9g8sAS_uobXyZXf2sLLIuiqiIuM5ZJIa7aEncZPuXebfGx0VV_BUFPXw8BYvIV8Y7DMAfjALaZ9LLvQKGTHQdSWVrFfJCMQhVBIY3yCbOc8AQGsl1skG16qGRugRuR4nG_JdN_R23gabkfLv9CS1GDyNiU4jHtHxPVLfZheTt6GnKXZI20ADDimGTG1Bbe5TdIse8zZZm9ou487L3CK3J7_Gx6fVxdXvs-OfF5VTQulKchTohPBuIhsrpNdsAoJNJyWuri1nrKml4pY5EHUjvOdlkwpROvTWOrFFfiy9D8Nkjt5h6JPtzENq5zYtTLSt-f8S2ntzF_8apRuoJRTB3osgxT8D5t7My4_YdTZgHLLhwBrgolFP6O4HdBaHFMp7hZK14FLCYaG-LSmXYs4Jp29hGJinnkzpyTz3VNiv79O_ka_FFOBgCfxrO1x8bjLnlzdL5SNKbJxw</recordid><startdate>201807</startdate><enddate>201807</enddate><creator>Quinn, Breandan R.</creator><creator>Yunes‐Medina, Laura</creator><creator>Johnson, Gail V. 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W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5359-42e3ec33dcb48a34d91b031fb40197a21187452a1c03783dd245245ee4cedaac3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Animals</topic><topic>Apoptosis</topic><topic>Astrocytes</topic><topic>Astrocytes - cytology</topic><topic>Astrocytes - enzymology</topic><topic>Calcium</topic><topic>Calcium ions</topic><topic>Cell death</topic><topic>Cell Death - physiology</topic><topic>Central nervous system</topic><topic>Clonal deletion</topic><topic>Conformation</topic><topic>cytoskeleton</topic><topic>Deprivation</topic><topic>Gene regulation</topic><topic>Glutamine</topic><topic>GTP-Binding Proteins - chemistry</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>Guanine</topic><topic>Humans</topic><topic>injury</topic><topic>Low molecular weights</topic><topic>Lysine</topic><topic>Models, Molecular</topic><topic>Molecular chains</topic><topic>Molecular weight</topic><topic>neurites</topic><topic>Neurons</topic><topic>Neurons - cytology</topic><topic>Neurons - enzymology</topic><topic>Nucleotides</topic><topic>Polypeptides</topic><topic>Spermidine</topic><topic>Survival</topic><topic>Transcription</topic><topic>transcription regulation</topic><topic>Transglutaminase 2</topic><topic>Transglutaminases - chemistry</topic><topic>Transglutaminases - metabolism</topic><topic>Viability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Quinn, Breandan R.</creatorcontrib><creatorcontrib>Yunes‐Medina, Laura</creatorcontrib><creatorcontrib>Johnson, Gail V. 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W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transglutaminase 2: Friend or foe? The discordant role in neurons and astrocytes</atitle><jtitle>Journal of neuroscience research</jtitle><addtitle>J Neurosci Res</addtitle><date>2018-07</date><risdate>2018</risdate><volume>96</volume><issue>7</issue><spage>1150</spage><epage>1158</epage><pages>1150-1158</pages><issn>0360-4012</issn><eissn>1097-4547</eissn><abstract>Members of the transglutaminase family catalyze the formation of isopeptide bonds between a polypeptide‐bound glutamine and a low molecular weight amine (e.g., spermidine) or the ɛ‐amino group of a polypeptide‐bound lysine. Transglutaminase 2 (TG2), a prominent member of this family, is unique because in addition to being a transamidating enzyme, it exhibits numerous other activities. As a result, TG2 plays a role in many physiological processes, and its function is highly cell type specific and relies upon a number of factors, including conformation, cellular compartment location, and local concentrations of Ca2+ and guanine nucleotides. TG2 is the most abundant transglutaminase in the central nervous system (CNS) and plays a pivotal role in the CNS injury response. How TG2 affects the cell in response to an insult is strikingly different in astrocytes and neurons. In neurons, TG2 supports survival. Overexpression of TG2 in primary neurons protects against oxygen and glucose deprivation (OGD)‐induced cell death and in vivo results in a reduction in infarct volume subsequent to a stroke. Knockdown of TG2 in primary neurons results in a loss of viability. In contrast, deletion of TG2 from astrocytes results in increased survival following OGD and improved ability to protect neurons from injury. 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subjects | Animals Apoptosis Astrocytes Astrocytes - cytology Astrocytes - enzymology Calcium Calcium ions Cell death Cell Death - physiology Central nervous system Clonal deletion Conformation cytoskeleton Deprivation Gene regulation Glutamine GTP-Binding Proteins - chemistry GTP-Binding Proteins - metabolism Guanine Humans injury Low molecular weights Lysine Models, Molecular Molecular chains Molecular weight neurites Neurons Neurons - cytology Neurons - enzymology Nucleotides Polypeptides Spermidine Survival Transcription transcription regulation Transglutaminase 2 Transglutaminases - chemistry Transglutaminases - metabolism Viability |
title | Transglutaminase 2: Friend or foe? The discordant role in neurons and astrocytes |
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