Methylthioadenosine nucleoside phosphorylase deficiency in methylthio-dependent cancer cells
The cleavage of the methylthio group from methylthioadenosine is shown to involve two enzymes, a nucleosidase which catalyses the phosphorolytic cleavage of methylthioadenosine to yield adenine and 5-methylthioribose-1-phosphate and an enzyme which uses the latter compound as substrate and catalyses...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1978-07, Vol.83 (1), p.27-35 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Toohey, John I. |
| description | The cleavage of the methylthio group from methylthioadenosine is shown to involve two enzymes, a nucleosidase which catalyses the phosphorolytic cleavage of methylthioadenosine to yield adenine and 5-methylthioribose-1-phosphate and an enzyme which uses the latter compound as substrate and catalyses the release of the methylthio group as an ether-extractable product. Three malignant murine hematopoietic cell lines which require methylthio group supplementation for proliferation
in vitro are shown to lack methylthioadenosine nucleosidase activity while retaining activity of the second enzyme. Four cell lines which are methylthio-independent
in vitro contain activity of both enzymes. The data suggest that the requirement for exogenous methylthio groups in certain cells is caused by the block in their biosynthetic pathway imposed by methylthioadenosine nucleoside phosphorylase deficiency. Secondarily, the data suggest that all cells require methylthio or related groups for division. |
| doi_str_mv | 10.1016/0006-291X(78)90393-5 |
| format | Article |
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in vitro are shown to lack methylthioadenosine nucleosidase activity while retaining activity of the second enzyme. Four cell lines which are methylthio-independent
in vitro contain activity of both enzymes. The data suggest that the requirement for exogenous methylthio groups in certain cells is caused by the block in their biosynthetic pathway imposed by methylthioadenosine nucleoside phosphorylase deficiency. Secondarily, the data suggest that all cells require methylthio or related groups for division.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(78)90393-5</identifier><identifier>PMID: 100109</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine - analogs & derivatives ; Adenosine Deaminase - metabolism ; Arsenates - pharmacology ; Cell Line ; Hydrolases ; Kinetics ; Pentosyltransferases - deficiency ; Phosphates - pharmacology ; Purine-Nucleoside Phosphorylase - deficiency ; Purine-Nucleoside Phosphorylase - metabolism ; Ribosemonophosphates ; Thionucleosides ; Thionucleotides</subject><ispartof>Biochemical and biophysical research communications, 1978-07, Vol.83 (1), p.27-35</ispartof><rights>1978</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-72112641d6ec3de90c8a212feda7405d2c8e545c4d3482c3d46cabf6b72313cd3</citedby><cites>FETCH-LOGICAL-c356t-72112641d6ec3de90c8a212feda7405d2c8e545c4d3482c3d46cabf6b72313cd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(78)90393-5$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/100109$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Toohey, John I.</creatorcontrib><title>Methylthioadenosine nucleoside phosphorylase deficiency in methylthio-dependent cancer cells</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The cleavage of the methylthio group from methylthioadenosine is shown to involve two enzymes, a nucleosidase which catalyses the phosphorolytic cleavage of methylthioadenosine to yield adenine and 5-methylthioribose-1-phosphate and an enzyme which uses the latter compound as substrate and catalyses the release of the methylthio group as an ether-extractable product. Three malignant murine hematopoietic cell lines which require methylthio group supplementation for proliferation
in vitro are shown to lack methylthioadenosine nucleosidase activity while retaining activity of the second enzyme. Four cell lines which are methylthio-independent
in vitro contain activity of both enzymes. The data suggest that the requirement for exogenous methylthio groups in certain cells is caused by the block in their biosynthetic pathway imposed by methylthioadenosine nucleoside phosphorylase deficiency. Secondarily, the data suggest that all cells require methylthio or related groups for division.</description><subject>Adenosine - analogs & derivatives</subject><subject>Adenosine Deaminase - metabolism</subject><subject>Arsenates - pharmacology</subject><subject>Cell Line</subject><subject>Hydrolases</subject><subject>Kinetics</subject><subject>Pentosyltransferases - deficiency</subject><subject>Phosphates - pharmacology</subject><subject>Purine-Nucleoside Phosphorylase - deficiency</subject><subject>Purine-Nucleoside Phosphorylase - metabolism</subject><subject>Ribosemonophosphates</subject><subject>Thionucleosides</subject><subject>Thionucleotides</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtLAzEQxoP4qtX_oIc9iR5WM0n2dRGk-IKKFwUPQkiTWRrZR012hf3vzbZSPHkYZmC-72PmR8gM6BVQSK8ppWnMCni_yPLLgvKCx8kemQAtaMyAin0y2UmOyYn3n5QCiLQ4IocQRlpMyMczdquh6la2VQab1tsGo6bXFYbRYLRetT6UGyrlMTJYWm2x0UNkm6jeWWODa2yCv4u0ajS6SGNV-VNyUKrK49lvn5K3-7vX-WO8eHl4mt8uYs2TtIszBsBSASZFzQ0WVOeKASvRqEzQxDCdYyISLQwXOQsSkWq1LNNlxjhwbfiUnG9z16796tF3srZ-vEA12PZeZgIy4JQFodgKtWu9d1jKtbO1coMEKkemcgQmR2Ayy-WGqUyCbfab3y9rNH9MI8SwvtmuMfz4bdFJv4GExjrUnTSt_T__B0IwiDY</recordid><startdate>19780714</startdate><enddate>19780714</enddate><creator>Toohey, John I.</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>19780714</creationdate><title>Methylthioadenosine nucleoside phosphorylase deficiency in methylthio-dependent cancer cells</title><author>Toohey, John I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-72112641d6ec3de90c8a212feda7405d2c8e545c4d3482c3d46cabf6b72313cd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Adenosine - analogs & derivatives</topic><topic>Adenosine Deaminase - metabolism</topic><topic>Arsenates - pharmacology</topic><topic>Cell Line</topic><topic>Hydrolases</topic><topic>Kinetics</topic><topic>Pentosyltransferases - deficiency</topic><topic>Phosphates - pharmacology</topic><topic>Purine-Nucleoside Phosphorylase - deficiency</topic><topic>Purine-Nucleoside Phosphorylase - metabolism</topic><topic>Ribosemonophosphates</topic><topic>Thionucleosides</topic><topic>Thionucleotides</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Toohey, John I.</creatorcontrib><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Toohey, John I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Methylthioadenosine nucleoside phosphorylase deficiency in methylthio-dependent cancer cells</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1978-07-14</date><risdate>1978</risdate><volume>83</volume><issue>1</issue><spage>27</spage><epage>35</epage><pages>27-35</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The cleavage of the methylthio group from methylthioadenosine is shown to involve two enzymes, a nucleosidase which catalyses the phosphorolytic cleavage of methylthioadenosine to yield adenine and 5-methylthioribose-1-phosphate and an enzyme which uses the latter compound as substrate and catalyses the release of the methylthio group as an ether-extractable product. Three malignant murine hematopoietic cell lines which require methylthio group supplementation for proliferation
in vitro are shown to lack methylthioadenosine nucleosidase activity while retaining activity of the second enzyme. Four cell lines which are methylthio-independent
in vitro contain activity of both enzymes. The data suggest that the requirement for exogenous methylthio groups in certain cells is caused by the block in their biosynthetic pathway imposed by methylthioadenosine nucleoside phosphorylase deficiency. Secondarily, the data suggest that all cells require methylthio or related groups for division.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>100109</pmid><doi>10.1016/0006-291X(78)90393-5</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1978-07, Vol.83 (1), p.27-35 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Adenosine - analogs & derivatives Adenosine Deaminase - metabolism Arsenates - pharmacology Cell Line Hydrolases Kinetics Pentosyltransferases - deficiency Phosphates - pharmacology Purine-Nucleoside Phosphorylase - deficiency Purine-Nucleoside Phosphorylase - metabolism Ribosemonophosphates Thionucleosides Thionucleotides |
| title | Methylthioadenosine nucleoside phosphorylase deficiency in methylthio-dependent cancer cells |
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