L-Methionase: A Therapeutic Enzyme to Treat Malignancies

Cancer is an increasing cause of mortality and morbidity throughout the world. L-methionase has potential application against many types of cancers. L-Methionase is an intracellular enzyme in bacterial species, an extracellular enzyme in fungi, and absent in mammals. L-Methionase producing bacterial...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:BioMed research international 2014-01, Vol.2014 (2014), p.1-13
Hauptverfasser: Sharma, Bhupender, Kanwar, Shamsher Singh, Singh, Sukhdev
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 13
container_issue 2014
container_start_page 1
container_title BioMed research international
container_volume 2014
creator Sharma, Bhupender
Kanwar, Shamsher Singh
Singh, Sukhdev
description Cancer is an increasing cause of mortality and morbidity throughout the world. L-methionase has potential application against many types of cancers. L-Methionase is an intracellular enzyme in bacterial species, an extracellular enzyme in fungi, and absent in mammals. L-Methionase producing bacterial strain(s) can be isolated by 5,5′-dithio-bis-(2-nitrobenzoic acid) as a screening dye. L-Methionine plays an important role in tumour cells. These cells become methionine dependent and eventually follow apoptosis due to methionine limitation in cancer cells. L-Methionine also plays an indispensable role in gene activation and inactivation due to hypermethylation and/or hypomethylation. Membrane transporters such as GLUT1 and ion channels like Na2+, Ca2+, K+, and Cl− become overexpressed. Further, the α-subunit of ATP synthase plays a role in cancer cells growth and development by providing them enhanced nutritional requirements. Currently, selenomethionine is also used as a prodrug in cancer therapy along with enzyme methionase that converts prodrug into active toxic chemical(s) that causes death of cancerous cells/tissue. More recently, fusion protein (FP) consisting of L-methionase linked to annexin-V has been used in cancer therapy. The fusion proteins have advantage that they have specificity only for cancer cells and do not harm the normal cells.
doi_str_mv 10.1155/2014/506287
format Article
fullrecord <record><control><sourceid>gale_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4164312</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A427023348</galeid><sourcerecordid>A427023348</sourcerecordid><originalsourceid>FETCH-LOGICAL-c528t-f38a369707ddda8bd8388c786861e83391b84f0561c918fa4dc7b1905b45c7c3</originalsourceid><addsrcrecordid>eNqNkUtr3DAURk1pSEKaVfbF0E1pcaOrl-UuCkNIHzAhm9kLWb6eUfBIU8luSX59ZCYdpl1VGwl0OLqfvqK4AvIJQIhrSoBfCyKpql8V55QBryRweH04M3ZWXKb0QPJSIEkjT4szKqggjPLzQi2rOxw3LniT8HO5KFcbjGaH0-hseeufHrdYjqFcRTRjeWcGt_bGW4fpTXHSmyHh5ct-Uay-3q5uvlfL-28_bhbLygqqxqpnyjDZ1KTuus6otlNMKVsrqSSgYqyBVvGeCAm2AdUb3tm6hYaIlgtbW3ZRfNlrd1O7xc6iH6MZ9C66rYmPOhin_77xbqPX4ZfmIDkDmgXvXwQx_JwwjXrrksVhMB7DlDRImL-lFjP67h_0IUzR53Qa8oANJ4IdUWszoHa-D_ldO0v1gtOaUMa4ytTHPWVjSClifxgZiJ6b03Nzet9cpt8epzywf3rKwIc9sHG-M7_d_9kwI9ibIxgkyxGeAX2zplA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1561940532</pqid></control><display><type>article</type><title>L-Methionase: A Therapeutic Enzyme to Treat Malignancies</title><source>MEDLINE</source><source>PubMed Central Open Access</source><source>Wiley-Blackwell Open Access Titles</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><creator>Sharma, Bhupender ; Kanwar, Shamsher Singh ; Singh, Sukhdev</creator><contributor>Hmidet, Noomen</contributor><creatorcontrib>Sharma, Bhupender ; Kanwar, Shamsher Singh ; Singh, Sukhdev ; Hmidet, Noomen</creatorcontrib><description>Cancer is an increasing cause of mortality and morbidity throughout the world. L-methionase has potential application against many types of cancers. L-Methionase is an intracellular enzyme in bacterial species, an extracellular enzyme in fungi, and absent in mammals. L-Methionase producing bacterial strain(s) can be isolated by 5,5′-dithio-bis-(2-nitrobenzoic acid) as a screening dye. L-Methionine plays an important role in tumour cells. These cells become methionine dependent and eventually follow apoptosis due to methionine limitation in cancer cells. L-Methionine also plays an indispensable role in gene activation and inactivation due to hypermethylation and/or hypomethylation. Membrane transporters such as GLUT1 and ion channels like Na2+, Ca2+, K+, and Cl− become overexpressed. Further, the α-subunit of ATP synthase plays a role in cancer cells growth and development by providing them enhanced nutritional requirements. Currently, selenomethionine is also used as a prodrug in cancer therapy along with enzyme methionase that converts prodrug into active toxic chemical(s) that causes death of cancerous cells/tissue. More recently, fusion protein (FP) consisting of L-methionase linked to annexin-V has been used in cancer therapy. The fusion proteins have advantage that they have specificity only for cancer cells and do not harm the normal cells.</description><identifier>ISSN: 2314-6133</identifier><identifier>EISSN: 2314-6141</identifier><identifier>DOI: 10.1155/2014/506287</identifier><identifier>PMID: 25250324</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Publishing Corporation</publisher><subject>Amino acids ; Animals ; Bacteriology ; Biopharmaceutics ; Biosynthesis ; Cancer ; Carbon-Sulfur Lyases - therapeutic use ; Cloning ; Enzymes ; Health aspects ; Homocysteine ; Humans ; Medical research ; Medicine, Experimental ; Methionine ; Methionine - metabolism ; Microorganisms ; Models, Biological ; Molecular Targeted Therapy - methods ; Molecular weight ; Neoplasm Proteins - metabolism ; Neoplasms - drug therapy ; Neoplasms - metabolism ; Polyethylene glycol ; Proteins ; Review</subject><ispartof>BioMed research international, 2014-01, Vol.2014 (2014), p.1-13</ispartof><rights>Copyright © 2014 Bhupender Sharma et al.</rights><rights>COPYRIGHT 2014 John Wiley &amp; Sons, Inc.</rights><rights>Copyright © 2014 Bhupender Sharma et al. Bhupender Sharma et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</rights><rights>Copyright © 2014 Bhupender Sharma et al. 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c528t-f38a369707ddda8bd8388c786861e83391b84f0561c918fa4dc7b1905b45c7c3</citedby><cites>FETCH-LOGICAL-c528t-f38a369707ddda8bd8388c786861e83391b84f0561c918fa4dc7b1905b45c7c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4164312/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4164312/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25250324$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Hmidet, Noomen</contributor><creatorcontrib>Sharma, Bhupender</creatorcontrib><creatorcontrib>Kanwar, Shamsher Singh</creatorcontrib><creatorcontrib>Singh, Sukhdev</creatorcontrib><title>L-Methionase: A Therapeutic Enzyme to Treat Malignancies</title><title>BioMed research international</title><addtitle>Biomed Res Int</addtitle><description>Cancer is an increasing cause of mortality and morbidity throughout the world. L-methionase has potential application against many types of cancers. L-Methionase is an intracellular enzyme in bacterial species, an extracellular enzyme in fungi, and absent in mammals. L-Methionase producing bacterial strain(s) can be isolated by 5,5′-dithio-bis-(2-nitrobenzoic acid) as a screening dye. L-Methionine plays an important role in tumour cells. These cells become methionine dependent and eventually follow apoptosis due to methionine limitation in cancer cells. L-Methionine also plays an indispensable role in gene activation and inactivation due to hypermethylation and/or hypomethylation. Membrane transporters such as GLUT1 and ion channels like Na2+, Ca2+, K+, and Cl− become overexpressed. Further, the α-subunit of ATP synthase plays a role in cancer cells growth and development by providing them enhanced nutritional requirements. Currently, selenomethionine is also used as a prodrug in cancer therapy along with enzyme methionase that converts prodrug into active toxic chemical(s) that causes death of cancerous cells/tissue. More recently, fusion protein (FP) consisting of L-methionase linked to annexin-V has been used in cancer therapy. The fusion proteins have advantage that they have specificity only for cancer cells and do not harm the normal cells.</description><subject>Amino acids</subject><subject>Animals</subject><subject>Bacteriology</subject><subject>Biopharmaceutics</subject><subject>Biosynthesis</subject><subject>Cancer</subject><subject>Carbon-Sulfur Lyases - therapeutic use</subject><subject>Cloning</subject><subject>Enzymes</subject><subject>Health aspects</subject><subject>Homocysteine</subject><subject>Humans</subject><subject>Medical research</subject><subject>Medicine, Experimental</subject><subject>Methionine</subject><subject>Methionine - metabolism</subject><subject>Microorganisms</subject><subject>Models, Biological</subject><subject>Molecular Targeted Therapy - methods</subject><subject>Molecular weight</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Neoplasms - drug therapy</subject><subject>Neoplasms - metabolism</subject><subject>Polyethylene glycol</subject><subject>Proteins</subject><subject>Review</subject><issn>2314-6133</issn><issn>2314-6141</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>RHX</sourceid><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>eNqNkUtr3DAURk1pSEKaVfbF0E1pcaOrl-UuCkNIHzAhm9kLWb6eUfBIU8luSX59ZCYdpl1VGwl0OLqfvqK4AvIJQIhrSoBfCyKpql8V55QBryRweH04M3ZWXKb0QPJSIEkjT4szKqggjPLzQi2rOxw3LniT8HO5KFcbjGaH0-hseeufHrdYjqFcRTRjeWcGt_bGW4fpTXHSmyHh5ct-Uay-3q5uvlfL-28_bhbLygqqxqpnyjDZ1KTuus6otlNMKVsrqSSgYqyBVvGeCAm2AdUb3tm6hYaIlgtbW3ZRfNlrd1O7xc6iH6MZ9C66rYmPOhin_77xbqPX4ZfmIDkDmgXvXwQx_JwwjXrrksVhMB7DlDRImL-lFjP67h_0IUzR53Qa8oANJ4IdUWszoHa-D_ldO0v1gtOaUMa4ytTHPWVjSClifxgZiJ6b03Nzet9cpt8epzywf3rKwIc9sHG-M7_d_9kwI9ibIxgkyxGeAX2zplA</recordid><startdate>20140101</startdate><enddate>20140101</enddate><creator>Sharma, Bhupender</creator><creator>Kanwar, Shamsher Singh</creator><creator>Singh, Sukhdev</creator><general>Hindawi Publishing Corporation</general><general>John Wiley &amp; Sons, Inc</general><general>Hindawi Limited</general><scope>ADJCN</scope><scope>AHFXO</scope><scope>RHU</scope><scope>RHW</scope><scope>RHX</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>3V.</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7TK</scope><scope>7U7</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>CWDGH</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>5PM</scope></search><sort><creationdate>20140101</creationdate><title>L-Methionase: A Therapeutic Enzyme to Treat Malignancies</title><author>Sharma, Bhupender ; Kanwar, Shamsher Singh ; Singh, Sukhdev</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c528t-f38a369707ddda8bd8388c786861e83391b84f0561c918fa4dc7b1905b45c7c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino acids</topic><topic>Animals</topic><topic>Bacteriology</topic><topic>Biopharmaceutics</topic><topic>Biosynthesis</topic><topic>Cancer</topic><topic>Carbon-Sulfur Lyases - therapeutic use</topic><topic>Cloning</topic><topic>Enzymes</topic><topic>Health aspects</topic><topic>Homocysteine</topic><topic>Humans</topic><topic>Medical research</topic><topic>Medicine, Experimental</topic><topic>Methionine</topic><topic>Methionine - metabolism</topic><topic>Microorganisms</topic><topic>Models, Biological</topic><topic>Molecular Targeted Therapy - methods</topic><topic>Molecular weight</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Neoplasms - drug therapy</topic><topic>Neoplasms - metabolism</topic><topic>Polyethylene glycol</topic><topic>Proteins</topic><topic>Review</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sharma, Bhupender</creatorcontrib><creatorcontrib>Kanwar, Shamsher Singh</creatorcontrib><creatorcontrib>Singh, Sukhdev</creatorcontrib><collection>الدوريات العلمية والإحصائية - e-Marefa Academic and Statistical Periodicals</collection><collection>معرفة - المحتوى العربي الأكاديمي المتكامل - e-Marefa Academic Complete</collection><collection>Hindawi Publishing Complete</collection><collection>Hindawi Publishing Subscription Journals</collection><collection>Hindawi Publishing Open Access</collection><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>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</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 Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies &amp; Aerospace Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>Middle East &amp; Africa Database</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>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Advanced Technologies &amp; Aerospace Database</collection><collection>ProQuest Advanced Technologies &amp; Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Publicly Available Content Database</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>PubMed Central (Full Participant titles)</collection><jtitle>BioMed research international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sharma, Bhupender</au><au>Kanwar, Shamsher Singh</au><au>Singh, Sukhdev</au><au>Hmidet, Noomen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>L-Methionase: A Therapeutic Enzyme to Treat Malignancies</atitle><jtitle>BioMed research international</jtitle><addtitle>Biomed Res Int</addtitle><date>2014-01-01</date><risdate>2014</risdate><volume>2014</volume><issue>2014</issue><spage>1</spage><epage>13</epage><pages>1-13</pages><issn>2314-6133</issn><eissn>2314-6141</eissn><abstract>Cancer is an increasing cause of mortality and morbidity throughout the world. L-methionase has potential application against many types of cancers. L-Methionase is an intracellular enzyme in bacterial species, an extracellular enzyme in fungi, and absent in mammals. L-Methionase producing bacterial strain(s) can be isolated by 5,5′-dithio-bis-(2-nitrobenzoic acid) as a screening dye. L-Methionine plays an important role in tumour cells. These cells become methionine dependent and eventually follow apoptosis due to methionine limitation in cancer cells. L-Methionine also plays an indispensable role in gene activation and inactivation due to hypermethylation and/or hypomethylation. Membrane transporters such as GLUT1 and ion channels like Na2+, Ca2+, K+, and Cl− become overexpressed. Further, the α-subunit of ATP synthase plays a role in cancer cells growth and development by providing them enhanced nutritional requirements. Currently, selenomethionine is also used as a prodrug in cancer therapy along with enzyme methionase that converts prodrug into active toxic chemical(s) that causes death of cancerous cells/tissue. More recently, fusion protein (FP) consisting of L-methionase linked to annexin-V has been used in cancer therapy. The fusion proteins have advantage that they have specificity only for cancer cells and do not harm the normal cells.</abstract><cop>Cairo, Egypt</cop><pub>Hindawi Publishing Corporation</pub><pmid>25250324</pmid><doi>10.1155/2014/506287</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 2314-6133
ispartof BioMed research international, 2014-01, Vol.2014 (2014), p.1-13
issn 2314-6133
2314-6141
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4164312
source MEDLINE; PubMed Central Open Access; Wiley-Blackwell Open Access Titles; PubMed Central; Alma/SFX Local Collection
subjects Amino acids
Animals
Bacteriology
Biopharmaceutics
Biosynthesis
Cancer
Carbon-Sulfur Lyases - therapeutic use
Cloning
Enzymes
Health aspects
Homocysteine
Humans
Medical research
Medicine, Experimental
Methionine
Methionine - metabolism
Microorganisms
Models, Biological
Molecular Targeted Therapy - methods
Molecular weight
Neoplasm Proteins - metabolism
Neoplasms - drug therapy
Neoplasms - metabolism
Polyethylene glycol
Proteins
Review
title L-Methionase: A Therapeutic Enzyme to Treat Malignancies
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-12T16%3A40%3A13IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=L-Methionase:%20A%20Therapeutic%20Enzyme%20to%20Treat%20Malignancies&rft.jtitle=BioMed%20research%20international&rft.au=Sharma,%20Bhupender&rft.date=2014-01-01&rft.volume=2014&rft.issue=2014&rft.spage=1&rft.epage=13&rft.pages=1-13&rft.issn=2314-6133&rft.eissn=2314-6141&rft_id=info:doi/10.1155/2014/506287&rft_dat=%3Cgale_pubme%3EA427023348%3C/gale_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1561940532&rft_id=info:pmid/25250324&rft_galeid=A427023348&rfr_iscdi=true