Phospholipid removal during degradation of rat plasma very low density lipoprotein in vitro1

The hydrolysis of glycerophospholipids in very low density lipoprotein by enzyme(s) released into circulation after the injection of heparin to rats was studied. [32P]Lysolecithin was formed rapidly from [32P]lecithin when very low density lipoprotein, labeled biosynthetically with 32P, was incubate...

Full description

Saved in:
Bibliographic Details
Published in:Journal of lipid research 1976-11, Vol.17 (6), p.578-587
Main Authors: Eisenberg, S, Schurr, D
Format: Article
Language:English
Subjects:
[32P]lecithin
[32P]sphingomyelin
heparin releasable hospholipase activity
lipoprotein-phospholipids
lysolecithin
supradiaphragmatic rats
“hepatic” and “extrahepatic” lipoprotein lipase
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page 587
container_issue 6
container_start_page 578
container_title Journal of lipid research
container_volume 17
creator Eisenberg, S
Schurr, D
description The hydrolysis of glycerophospholipids in very low density lipoprotein by enzyme(s) released into circulation after the injection of heparin to rats was studied. [32P]Lysolecithin was formed rapidly from [32P]lecithin when very low density lipoprotein, labeled biosynthetically with 32P, was incubated with postheparin plasma. The [32P]lysolecithin was associated with the plasma protein fraction of density greater than 1.21 g/ml, whereas [32P]lecithin exchanged between very low and high density lipoproteins. Inhibition of the plasma lecithin: cholesterol acyl transferase activity did not change the excess [32P]lysolecithin formation in postheparin plasma, and only a negligible amount of radioactivity was associated with blood cells when the incubation was repeated in whole blood. Analysis of the results has demonstrated that phospholipids are removed from VLDL by two pathways: hydrolysis of glycerophospholipids by the heparin-releasable phospholipase activity (>50%) and transfer to high density lipoproteins (
doi_str_mv 10.1016/S0022-2275(20)41729-8
format article
fullrecord <record><control><sourceid>elsevier_doaj_</sourceid><recordid>TN_cdi_doaj_primary_oai_doaj_org_article_542b9ba7769a425baa4c97ba81010f82</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0022227520417298</els_id><doaj_id>oai_doaj_org_article_542b9ba7769a425baa4c97ba81010f82</doaj_id><sourcerecordid>S0022227520417298</sourcerecordid><originalsourceid>FETCH-LOGICAL-d1228-e6d78fb8427c8f5c35bbd49a725137f8bb28145ee2bd044c2805669328a0b47d3</originalsourceid><addsrcrecordid>eNo9kF1LwzAUhoMoOKc_QcilXlST06RJr0SGH4OBgnonhJMm3TK6pqR1sn9vN0U4cA4vLw-Hh5BLzm4448XtG2MAGYCSV8CuBVdQZvqITLjMy0xBAcdk8l85JWd9v2aMC1HwCfl8XcW-W8UmdMHR5Ddxiw11Xym0S-r8MqHDIcSWxpomHGjXYL9BuvVpR5v4PVbaPgzjHbrYpTj40NJxtmFIkZ-Tkxqb3l_87Sn5eHx4nz1ni5en-ex-kTkOoDNfOKVrqwWoSteyyqW1TpSoQPJc1dpa0FxI78E6JkQFmsmiKHPQyKxQLp-S-S_XRVybLoUNpp2JGMwhiGlpMA2haryRAmxpUamiRAHSIoqqVBb1aJLVGkbW3S_Ljw9vg0-mr4JvK-9C8tUwEoPhzOzFm4N4s7dqgJmDeKPzHyR-d2s</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Phospholipid removal during degradation of rat plasma very low density lipoprotein in vitro1</title><source>ScienceDirect Journals</source><creator>Eisenberg, S ; Schurr, D</creator><creatorcontrib>Eisenberg, S ; Schurr, D</creatorcontrib><description>The hydrolysis of glycerophospholipids in very low density lipoprotein by enzyme(s) released into circulation after the injection of heparin to rats was studied. [32P]Lysolecithin was formed rapidly from [32P]lecithin when very low density lipoprotein, labeled biosynthetically with 32P, was incubated with postheparin plasma. The [32P]lysolecithin was associated with the plasma protein fraction of density greater than 1.21 g/ml, whereas [32P]lecithin exchanged between very low and high density lipoproteins. Inhibition of the plasma lecithin: cholesterol acyl transferase activity did not change the excess [32P]lysolecithin formation in postheparin plasma, and only a negligible amount of radioactivity was associated with blood cells when the incubation was repeated in whole blood. Analysis of the results has demonstrated that phospholipids are removed from VLDL by two pathways: hydrolysis of glycerophospholipids by the heparin-releasable phospholipase activity (&gt;50%) and transfer to high density lipoproteins (&lt;50%). The tissue origin of the postheparin phospholipase was studied in plasma obtained from intact rats and supradiaphragmatic rats using specific inhibitors of the extrahepatic lipase system (protamine sulfate and 0.5 M NaCl). The phospholipase activity could be ascribed to both the hepatic and extrahepatic lipase systems. It is concluded that hydrolysis of glycerophospholipids is the major mechanism responsible for the removal of phospholipids from very low density lipoprotein during the degradation of the lipoprotein. It is suggested that phospholipid hydrolysis occurs concomitantly with triglyceride hydrolysis, predominantly in extrahepatic tissues.</description><identifier>ISSN: 0022-2275</identifier><identifier>EISSN: 1539-7262</identifier><identifier>DOI: 10.1016/S0022-2275(20)41729-8</identifier><language>eng</language><publisher>Elsevier Inc</publisher><subject>[32P]lecithin ; [32P]sphingomyelin ; heparin releasable hospholipase activity ; lipoprotein-phospholipids ; lysolecithin ; supradiaphragmatic rats ; “hepatic” and “extrahepatic” lipoprotein lipase</subject><ispartof>Journal of lipid research, 1976-11, Vol.17 (6), p.578-587</ispartof><rights>1976 © 1976 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0022227520417298$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3549,27924,27925,45780</link.rule.ids></links><search><creatorcontrib>Eisenberg, S</creatorcontrib><creatorcontrib>Schurr, D</creatorcontrib><title>Phospholipid removal during degradation of rat plasma very low density lipoprotein in vitro1</title><title>Journal of lipid research</title><description>The hydrolysis of glycerophospholipids in very low density lipoprotein by enzyme(s) released into circulation after the injection of heparin to rats was studied. [32P]Lysolecithin was formed rapidly from [32P]lecithin when very low density lipoprotein, labeled biosynthetically with 32P, was incubated with postheparin plasma. The [32P]lysolecithin was associated with the plasma protein fraction of density greater than 1.21 g/ml, whereas [32P]lecithin exchanged between very low and high density lipoproteins. Inhibition of the plasma lecithin: cholesterol acyl transferase activity did not change the excess [32P]lysolecithin formation in postheparin plasma, and only a negligible amount of radioactivity was associated with blood cells when the incubation was repeated in whole blood. Analysis of the results has demonstrated that phospholipids are removed from VLDL by two pathways: hydrolysis of glycerophospholipids by the heparin-releasable phospholipase activity (&gt;50%) and transfer to high density lipoproteins (&lt;50%). The tissue origin of the postheparin phospholipase was studied in plasma obtained from intact rats and supradiaphragmatic rats using specific inhibitors of the extrahepatic lipase system (protamine sulfate and 0.5 M NaCl). The phospholipase activity could be ascribed to both the hepatic and extrahepatic lipase systems. It is concluded that hydrolysis of glycerophospholipids is the major mechanism responsible for the removal of phospholipids from very low density lipoprotein during the degradation of the lipoprotein. It is suggested that phospholipid hydrolysis occurs concomitantly with triglyceride hydrolysis, predominantly in extrahepatic tissues.</description><subject>[32P]lecithin</subject><subject>[32P]sphingomyelin</subject><subject>heparin releasable hospholipase activity</subject><subject>lipoprotein-phospholipids</subject><subject>lysolecithin</subject><subject>supradiaphragmatic rats</subject><subject>“hepatic” and “extrahepatic” lipoprotein lipase</subject><issn>0022-2275</issn><issn>1539-7262</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>DOA</sourceid><recordid>eNo9kF1LwzAUhoMoOKc_QcilXlST06RJr0SGH4OBgnonhJMm3TK6pqR1sn9vN0U4cA4vLw-Hh5BLzm4448XtG2MAGYCSV8CuBVdQZvqITLjMy0xBAcdk8l85JWd9v2aMC1HwCfl8XcW-W8UmdMHR5Ddxiw11Xym0S-r8MqHDIcSWxpomHGjXYL9BuvVpR5v4PVbaPgzjHbrYpTj40NJxtmFIkZ-Tkxqb3l_87Sn5eHx4nz1ni5en-ex-kTkOoDNfOKVrqwWoSteyyqW1TpSoQPJc1dpa0FxI78E6JkQFmsmiKHPQyKxQLp-S-S_XRVybLoUNpp2JGMwhiGlpMA2haryRAmxpUamiRAHSIoqqVBb1aJLVGkbW3S_Ljw9vg0-mr4JvK-9C8tUwEoPhzOzFm4N4s7dqgJmDeKPzHyR-d2s</recordid><startdate>197611</startdate><enddate>197611</enddate><creator>Eisenberg, S</creator><creator>Schurr, D</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>DOA</scope></search><sort><creationdate>197611</creationdate><title>Phospholipid removal during degradation of rat plasma very low density lipoprotein in vitro1</title><author>Eisenberg, S ; Schurr, D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-d1228-e6d78fb8427c8f5c35bbd49a725137f8bb28145ee2bd044c2805669328a0b47d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>[32P]lecithin</topic><topic>[32P]sphingomyelin</topic><topic>heparin releasable hospholipase activity</topic><topic>lipoprotein-phospholipids</topic><topic>lysolecithin</topic><topic>supradiaphragmatic rats</topic><topic>“hepatic” and “extrahepatic” lipoprotein lipase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Eisenberg, S</creatorcontrib><creatorcontrib>Schurr, D</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Journal of lipid research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Eisenberg, S</au><au>Schurr, D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phospholipid removal during degradation of rat plasma very low density lipoprotein in vitro1</atitle><jtitle>Journal of lipid research</jtitle><date>1976-11</date><risdate>1976</risdate><volume>17</volume><issue>6</issue><spage>578</spage><epage>587</epage><pages>578-587</pages><issn>0022-2275</issn><eissn>1539-7262</eissn><abstract>The hydrolysis of glycerophospholipids in very low density lipoprotein by enzyme(s) released into circulation after the injection of heparin to rats was studied. [32P]Lysolecithin was formed rapidly from [32P]lecithin when very low density lipoprotein, labeled biosynthetically with 32P, was incubated with postheparin plasma. The [32P]lysolecithin was associated with the plasma protein fraction of density greater than 1.21 g/ml, whereas [32P]lecithin exchanged between very low and high density lipoproteins. Inhibition of the plasma lecithin: cholesterol acyl transferase activity did not change the excess [32P]lysolecithin formation in postheparin plasma, and only a negligible amount of radioactivity was associated with blood cells when the incubation was repeated in whole blood. Analysis of the results has demonstrated that phospholipids are removed from VLDL by two pathways: hydrolysis of glycerophospholipids by the heparin-releasable phospholipase activity (&gt;50%) and transfer to high density lipoproteins (&lt;50%). The tissue origin of the postheparin phospholipase was studied in plasma obtained from intact rats and supradiaphragmatic rats using specific inhibitors of the extrahepatic lipase system (protamine sulfate and 0.5 M NaCl). The phospholipase activity could be ascribed to both the hepatic and extrahepatic lipase systems. It is concluded that hydrolysis of glycerophospholipids is the major mechanism responsible for the removal of phospholipids from very low density lipoprotein during the degradation of the lipoprotein. It is suggested that phospholipid hydrolysis occurs concomitantly with triglyceride hydrolysis, predominantly in extrahepatic tissues.</abstract><pub>Elsevier Inc</pub><doi>10.1016/S0022-2275(20)41729-8</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0022-2275
ispartof Journal of lipid research, 1976-11, Vol.17 (6), p.578-587
issn 0022-2275
1539-7262
language eng
recordid cdi_doaj_primary_oai_doaj_org_article_542b9ba7769a425baa4c97ba81010f82
source ScienceDirect Journals
subjects [32P]lecithin
[32P]sphingomyelin
heparin releasable hospholipase activity
lipoprotein-phospholipids
lysolecithin
supradiaphragmatic rats
“hepatic” and “extrahepatic” lipoprotein lipase
title Phospholipid removal during degradation of rat plasma very low density lipoprotein in vitro1
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-27T20%3A07%3A20IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-elsevier_doaj_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Phospholipid%20removal%20during%20degradation%20of%20rat%20plasma%20very%20low%20density%20lipoprotein%20in%20vitro1&rft.jtitle=Journal%20of%20lipid%20research&rft.au=Eisenberg,%20S&rft.date=1976-11&rft.volume=17&rft.issue=6&rft.spage=578&rft.epage=587&rft.pages=578-587&rft.issn=0022-2275&rft.eissn=1539-7262&rft_id=info:doi/10.1016/S0022-2275(20)41729-8&rft_dat=%3Celsevier_doaj_%3ES0022227520417298%3C/elsevier_doaj_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-d1228-e6d78fb8427c8f5c35bbd49a725137f8bb28145ee2bd044c2805669328a0b47d3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true