eIF5A isoforms and cancer: two brothers for two functions?
Eukaryotic translation initiation factor 5A (eIF5A) is the only cellular protein that contains the unusual amino acid hypusine [ N ε -(4-amino-2-hydroxybutyl)lysine]. The role of hypusine formation in the eIF5A protein in the regulation of cell proliferation and apoptosis is addressed in the present...
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Veröffentlicht in: | Amino acids 2013-01, Vol.44 (1), p.103-109 |
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description | Eukaryotic translation initiation factor 5A (eIF5A) is the only cellular protein that contains the unusual amino acid hypusine [
N
ε
-(4-amino-2-hydroxybutyl)lysine]. The role of hypusine formation in the eIF5A protein in the regulation of cell proliferation and apoptosis is addressed in the present review. Moreover, vertebrates carry two genes that encode two eIF5A isoforms, eIF5A-1 and eIF5A-2, which, in humans, are 84% identical. However, the biological functions of these two isoforms may be significantly different. In fact, eIF5A-1 is demonstrable in most cells of different histogenesis, whereas eIF5A-2 protein is detectable only in certain human cancer cells or tissues, suggesting its role as a potential oncogene. In this review we focus our attention on the involvement of eIF5A-1 in the triggering of an apoptotic program and in the regulation of cell proliferation. In addition, the potential oncogenic role and prognostic significance of eIF5A-2 in the prediction of the survival of cancer patients is described. eIF5A-1 and/or the eIF5A-2 isoform may serve as a new molecular diagnostic or prognostic marker or as a molecular target for anti-cancer therapy. |
doi_str_mv | 10.1007/s00726-011-1182-x |
format | Article |
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N
ε
-(4-amino-2-hydroxybutyl)lysine]. The role of hypusine formation in the eIF5A protein in the regulation of cell proliferation and apoptosis is addressed in the present review. Moreover, vertebrates carry two genes that encode two eIF5A isoforms, eIF5A-1 and eIF5A-2, which, in humans, are 84% identical. However, the biological functions of these two isoforms may be significantly different. In fact, eIF5A-1 is demonstrable in most cells of different histogenesis, whereas eIF5A-2 protein is detectable only in certain human cancer cells or tissues, suggesting its role as a potential oncogene. In this review we focus our attention on the involvement of eIF5A-1 in the triggering of an apoptotic program and in the regulation of cell proliferation. In addition, the potential oncogenic role and prognostic significance of eIF5A-2 in the prediction of the survival of cancer patients is described. eIF5A-1 and/or the eIF5A-2 isoform may serve as a new molecular diagnostic or prognostic marker or as a molecular target for anti-cancer therapy.</description><identifier>ISSN: 0939-4451</identifier><identifier>EISSN: 1438-2199</identifier><identifier>DOI: 10.1007/s00726-011-1182-x</identifier><identifier>PMID: 22139412</identifier><language>eng</language><publisher>Vienna: Springer Vienna</publisher><subject>Amino acids ; Analytical Chemistry ; Animals ; Apoptosis ; Biochemical Engineering ; Biochemistry ; Biomedical and Life Sciences ; Cancer ; Cell Transformation, Neoplastic - metabolism ; Control ; Eukaryotic Translation Initiation Factor 5A ; Gene Expression ; Human ; Humans ; Invited Review ; Life Sciences ; Lysine - analogs & derivatives ; Lysine - biosynthesis ; Markers ; Neoplasms - metabolism ; Neoplasms - pathology ; Neurobiology ; Peptide Initiation Factors - genetics ; Peptide Initiation Factors - metabolism ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; Proteins ; Proteomics ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; Survival ; Translations</subject><ispartof>Amino acids, 2013-01, Vol.44 (1), p.103-109</ispartof><rights>Springer-Verlag 2011</rights><rights>Springer-Verlag Wien 2013</rights><rights>Springer-Verlag 2011 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c569t-666977f9be065df8db46a116378962cc5e56188383ff0a1e2d1efa07db9830b53</citedby><cites>FETCH-LOGICAL-c569t-666977f9be065df8db46a116378962cc5e56188383ff0a1e2d1efa07db9830b53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00726-011-1182-x$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00726-011-1182-x$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,313,314,780,784,792,885,27922,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22139412$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Caraglia, M.</creatorcontrib><creatorcontrib>Park, M. H.</creatorcontrib><creatorcontrib>Wolff, E. C.</creatorcontrib><creatorcontrib>Marra, M.</creatorcontrib><creatorcontrib>Abbruzzese, A.</creatorcontrib><title>eIF5A isoforms and cancer: two brothers for two functions?</title><title>Amino acids</title><addtitle>Amino Acids</addtitle><addtitle>Amino Acids</addtitle><description>Eukaryotic translation initiation factor 5A (eIF5A) is the only cellular protein that contains the unusual amino acid hypusine [
N
ε
-(4-amino-2-hydroxybutyl)lysine]. The role of hypusine formation in the eIF5A protein in the regulation of cell proliferation and apoptosis is addressed in the present review. Moreover, vertebrates carry two genes that encode two eIF5A isoforms, eIF5A-1 and eIF5A-2, which, in humans, are 84% identical. However, the biological functions of these two isoforms may be significantly different. In fact, eIF5A-1 is demonstrable in most cells of different histogenesis, whereas eIF5A-2 protein is detectable only in certain human cancer cells or tissues, suggesting its role as a potential oncogene. In this review we focus our attention on the involvement of eIF5A-1 in the triggering of an apoptotic program and in the regulation of cell proliferation. In addition, the potential oncogenic role and prognostic significance of eIF5A-2 in the prediction of the survival of cancer patients is described. eIF5A-1 and/or the eIF5A-2 isoform may serve as a new molecular diagnostic or prognostic marker or as a molecular target for anti-cancer therapy.</description><subject>Amino acids</subject><subject>Analytical Chemistry</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Biochemical Engineering</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cancer</subject><subject>Cell Transformation, Neoplastic - metabolism</subject><subject>Control</subject><subject>Eukaryotic Translation Initiation Factor 5A</subject><subject>Gene Expression</subject><subject>Human</subject><subject>Humans</subject><subject>Invited Review</subject><subject>Life Sciences</subject><subject>Lysine - analogs & derivatives</subject><subject>Lysine - biosynthesis</subject><subject>Markers</subject><subject>Neoplasms - metabolism</subject><subject>Neoplasms - pathology</subject><subject>Neurobiology</subject><subject>Peptide Initiation Factors - genetics</subject><subject>Peptide Initiation Factors - metabolism</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Survival</subject><subject>Translations</subject><issn>0939-4451</issn><issn>1438-2199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</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>eNp1kU1LAzEQhoMotn78AC-y4MXLaibZZBMPSil-geBFzyGbTXSlTWqyq_Xfu7VVquBlAvM-806GF6EDwCeAcXma-kJ4jgFyAEHy-QYaQkFFTkDKTTTEksq8KBgM0E5KLxgDEcC30YAQoLIAMkRn9vaKjbImBRfiNGXa15nR3th4lrXvIatiaJ9tTFkvfzVc503bBJ8u9tCW05Nk91fvLnq8unwY3-R399e349FdbhiXbc45l2XpZGUxZ7UTdVVwDcBpKSQnxjDLOAhBBXUOa7CkBus0LutKCoorRnfR-dJ31lVTWxvr26gnahabqY4fKuhG_VZ886yewpuijHJJSG9wvDKI4bWzqVXTJhk7mWhvQ5cUCGBSUioW6NEf9CV00ffnKSgFlZQQvKBgSZkYUorW_XwGsFoko5bJqD4ZtUhGzfuZw_Urfia-o-gBsgRSL_knG9dW_-v6Cc5fmGc</recordid><startdate>20130101</startdate><enddate>20130101</enddate><creator>Caraglia, M.</creator><creator>Park, M. 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H. ; Wolff, E. C. ; Marra, M. ; Abbruzzese, A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c569t-666977f9be065df8db46a116378962cc5e56188383ff0a1e2d1efa07db9830b53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino acids</topic><topic>Analytical Chemistry</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Biochemical Engineering</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cancer</topic><topic>Cell Transformation, Neoplastic - metabolism</topic><topic>Control</topic><topic>Eukaryotic Translation Initiation Factor 5A</topic><topic>Gene Expression</topic><topic>Human</topic><topic>Humans</topic><topic>Invited Review</topic><topic>Life Sciences</topic><topic>Lysine - analogs & derivatives</topic><topic>Lysine - biosynthesis</topic><topic>Markers</topic><topic>Neoplasms - metabolism</topic><topic>Neoplasms - pathology</topic><topic>Neurobiology</topic><topic>Peptide Initiation Factors - genetics</topic><topic>Peptide Initiation Factors - metabolism</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><topic>Proteins</topic><topic>Proteomics</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>Survival</topic><topic>Translations</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Caraglia, M.</creatorcontrib><creatorcontrib>Park, M. H.</creatorcontrib><creatorcontrib>Wolff, E. 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H.</au><au>Wolff, E. C.</au><au>Marra, M.</au><au>Abbruzzese, A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>eIF5A isoforms and cancer: two brothers for two functions?</atitle><jtitle>Amino acids</jtitle><stitle>Amino Acids</stitle><addtitle>Amino Acids</addtitle><date>2013-01-01</date><risdate>2013</risdate><volume>44</volume><issue>1</issue><spage>103</spage><epage>109</epage><pages>103-109</pages><issn>0939-4451</issn><eissn>1438-2199</eissn><abstract>Eukaryotic translation initiation factor 5A (eIF5A) is the only cellular protein that contains the unusual amino acid hypusine [
N
ε
-(4-amino-2-hydroxybutyl)lysine]. The role of hypusine formation in the eIF5A protein in the regulation of cell proliferation and apoptosis is addressed in the present review. Moreover, vertebrates carry two genes that encode two eIF5A isoforms, eIF5A-1 and eIF5A-2, which, in humans, are 84% identical. However, the biological functions of these two isoforms may be significantly different. In fact, eIF5A-1 is demonstrable in most cells of different histogenesis, whereas eIF5A-2 protein is detectable only in certain human cancer cells or tissues, suggesting its role as a potential oncogene. In this review we focus our attention on the involvement of eIF5A-1 in the triggering of an apoptotic program and in the regulation of cell proliferation. In addition, the potential oncogenic role and prognostic significance of eIF5A-2 in the prediction of the survival of cancer patients is described. eIF5A-1 and/or the eIF5A-2 isoform may serve as a new molecular diagnostic or prognostic marker or as a molecular target for anti-cancer therapy.</abstract><cop>Vienna</cop><pub>Springer Vienna</pub><pmid>22139412</pmid><doi>10.1007/s00726-011-1182-x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino acids Analytical Chemistry Animals Apoptosis Biochemical Engineering Biochemistry Biomedical and Life Sciences Cancer Cell Transformation, Neoplastic - metabolism Control Eukaryotic Translation Initiation Factor 5A Gene Expression Human Humans Invited Review Life Sciences Lysine - analogs & derivatives Lysine - biosynthesis Markers Neoplasms - metabolism Neoplasms - pathology Neurobiology Peptide Initiation Factors - genetics Peptide Initiation Factors - metabolism Protein Isoforms - genetics Protein Isoforms - metabolism Proteins Proteomics RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Survival Translations |
title | eIF5A isoforms and cancer: two brothers for two functions? |
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