Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase
A cDNA clone encoding for the bovine pancreatic cholesterol esterase has been sequenced. Pancreatic cholesterol esterases hydrolyze dietary cholesterol esters to cholesterol and free fatty acids, which are then absorbed from the gut. Northern blots reveal that the positive signal at 1.9 kilobases is...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1989-11, Vol.164 (3), p.1302-1309 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Kyger, Erich M. Wiegand, Roger C. Lange, Louis G. |
| description | A cDNA clone encoding for the bovine pancreatic cholesterol esterase has been sequenced. Pancreatic cholesterol esterases hydrolyze dietary cholesterol esters to cholesterol and free fatty acids, which are then absorbed from the gut. Northern blots reveal that the positive signal at 1.9 kilobases is much more intense in the cow than in calf pancreas, indicating that the induction of the enzyme is due to increased transcription or stability of mRNA. The primary structure of this enzyme is similar to that of the rat pancreatic lysophospholipase. We found that homogeneous human and bovine pancreatic cholesterol esterases have high levels of lysophospholipase activity, indicating that these two activities reside within the same protein. Therefore, the metabolism of dietary neutral lipids and polar lipids may be linked through a single enzyme. |
| doi_str_mv | 10.1016/0006-291X(89)91811-1 |
| format | Article |
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Pancreatic cholesterol esterases hydrolyze dietary cholesterol esters to cholesterol and free fatty acids, which are then absorbed from the gut. Northern blots reveal that the positive signal at 1.9 kilobases is much more intense in the cow than in calf pancreas, indicating that the induction of the enzyme is due to increased transcription or stability of mRNA. The primary structure of this enzyme is similar to that of the rat pancreatic lysophospholipase. We found that homogeneous human and bovine pancreatic cholesterol esterases have high levels of lysophospholipase activity, indicating that these two activities reside within the same protein. 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Pancreatic cholesterol esterases hydrolyze dietary cholesterol esters to cholesterol and free fatty acids, which are then absorbed from the gut. Northern blots reveal that the positive signal at 1.9 kilobases is much more intense in the cow than in calf pancreas, indicating that the induction of the enzyme is due to increased transcription or stability of mRNA. The primary structure of this enzyme is similar to that of the rat pancreatic lysophospholipase. We found that homogeneous human and bovine pancreatic cholesterol esterases have high levels of lysophospholipase activity, indicating that these two activities reside within the same protein. Therefore, the metabolism of dietary neutral lipids and polar lipids may be linked through a single enzyme.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Blotting, Northern</subject><subject>Carboxylic Ester Hydrolases - genetics</subject><subject>Cattle</subject><subject>Cloning, Molecular</subject><subject>DNA - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Library</subject><subject>genes</subject><subject>Genes. Genome</subject><subject>Humans</subject><subject>Lysophospholipase - genetics</subject><subject>Lysophospholipase - metabolism</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>pancreas</subject><subject>Pancreas - enzymology</subject><subject>Phospholipases - genetics</subject><subject>Sterol Esterase - genetics</subject><subject>Sterol Esterase - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1r3DAQhkVJSTZp_0ELPoSQHJxobFkfl0JZkrQQyKWF3oQsjbsqWsuRvIH8-2izyx7TwzAw7zPD8BDyBeg1UOA3lFJeNwr-XEp1pUAC1PCBLIAqWjdA2RFZHJATcprzP0oBGFfH5LjpFG1ouyD3yxBHP_6t4lDNK6z6-OxHrCYz2oRm9rayqxgwz5hiqN66yXgTXnKcVjGXCn4qk0_k42BCxs_7fkZ-393-Wv6oHx7vfy6_P9SWyXause-N65E62YreQSuxwQ7ACSs5sm7gVDUCmekNsxStA95LOaBDQxUTTdOekYvd3SnFp035R699thiCGTFushaq7Tre8f-C0DEuhBQFZDvQpphzwkFPya9NetFA9Va03lrUW4taKv0mWkNZ-7q_v-nX6A5Le7MlP9_nJlsThlSM-nzAOBcgFSvYtx2GRdqzx6Sz9ThadD6hnbWL_v0_XgGnU5sq</recordid><startdate>19891115</startdate><enddate>19891115</enddate><creator>Kyger, Erich M.</creator><creator>Wiegand, Roger C.</creator><creator>Lange, Louis G.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</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>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19891115</creationdate><title>Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase</title><author>Kyger, Erich M. ; Wiegand, Roger C. ; Lange, Louis G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c483t-ebbadbe0d837bd138e2e511d7c86e45f60927e4aba4c0ecd16b88fedea0947223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Blotting, Northern</topic><topic>Carboxylic Ester Hydrolases - genetics</topic><topic>Cattle</topic><topic>Cloning, Molecular</topic><topic>DNA - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Library</topic><topic>genes</topic><topic>Genes. Genome</topic><topic>Humans</topic><topic>Lysophospholipase - genetics</topic><topic>Lysophospholipase - metabolism</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>pancreas</topic><topic>Pancreas - enzymology</topic><topic>Phospholipases - genetics</topic><topic>Sterol Esterase - genetics</topic><topic>Sterol Esterase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kyger, Erich M.</creatorcontrib><creatorcontrib>Wiegand, Roger C.</creatorcontrib><creatorcontrib>Lange, Louis G.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</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>Kyger, Erich M.</au><au>Wiegand, Roger C.</au><au>Lange, Louis G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1989-11-15</date><risdate>1989</risdate><volume>164</volume><issue>3</issue><spage>1302</spage><epage>1309</epage><pages>1302-1309</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>A cDNA clone encoding for the bovine pancreatic cholesterol esterase has been sequenced. Pancreatic cholesterol esterases hydrolyze dietary cholesterol esters to cholesterol and free fatty acids, which are then absorbed from the gut. Northern blots reveal that the positive signal at 1.9 kilobases is much more intense in the cow than in calf pancreas, indicating that the induction of the enzyme is due to increased transcription or stability of mRNA. The primary structure of this enzyme is similar to that of the rat pancreatic lysophospholipase. We found that homogeneous human and bovine pancreatic cholesterol esterases have high levels of lysophospholipase activity, indicating that these two activities reside within the same protein. Therefore, the metabolism of dietary neutral lipids and polar lipids may be linked through a single enzyme.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2590203</pmid><doi>10.1016/0006-291X(89)91811-1</doi><tpages>8</tpages></addata></record> |
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| subjects | Amino Acid Sequence Animals Base Sequence Biological and medical sciences Blotting, Northern Carboxylic Ester Hydrolases - genetics Cattle Cloning, Molecular DNA - genetics Fundamental and applied biological sciences. Psychology Gene Library genes Genes. Genome Humans Lysophospholipase - genetics Lysophospholipase - metabolism Molecular and cellular biology Molecular genetics Molecular Sequence Data pancreas Pancreas - enzymology Phospholipases - genetics Sterol Esterase - genetics Sterol Esterase - metabolism |
| title | Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase |
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