Triacylglycerol hydrolysis in isolated hepatic endosomes

Three endosomal compartments including the compartment for uncoupling receptor and ligand (CURL), multivesicular bodies (MVB), and a putative recycling fraction (retrosomes) were isolated from rat liver homogenates fifteen minutes after a bolus injection of very low density lipoprotein (VLDL) was de...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:The Journal of biological chemistry 1992-02, Vol.267 (5), p.3396-3401
Hauptverfasser: Hornick, C A, Thouron, C, DeLamatre, J G, Huang, J
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 3401
container_issue 5
container_start_page 3396
container_title The Journal of biological chemistry
container_volume 267
creator Hornick, C A
Thouron, C
DeLamatre, J G
Huang, J
description Three endosomal compartments including the compartment for uncoupling receptor and ligand (CURL), multivesicular bodies (MVB), and a putative recycling fraction (retrosomes) were isolated from rat liver homogenates fifteen minutes after a bolus injection of very low density lipoprotein (VLDL) was delivered into a femoral vein. Assays for enzyme markers indicate a minimal contamination with either lysosomes or Golgi. The increase in specific activity of the radiolabeled ligand (VLDL) during the isolation procedure from homogenate to MVB, demonstrates a 200-250-fold purification of this organelle. All three fractions have the ability to catabolize triacylglycerol substrate both as triolein and as VLDL triacylglycerol. Furthermore, incubation of isolated endosomes following injection of endogenously labeled VLDL demonstrate their ability to hydrolyze VLDL triacylglycerol in situ. Three distinct lipolytic pH optima were found at pH 5.5, 7.1, and 8.6. The effects of serum, MgCl2, CaCl2, NaCl, sodium dodecyl sulfate, bile acids, and antibody to hepatic triacylglycerol lipase on the individual endosome fractions demonstrated distinct lipolytic activities in the different compartments. Results indicate that both an endosomal neutral lipase as well as hepatic triacylglycerol lipase make a significant contribution to lipolytic processing of endocytosed lipoproteins prior to their resecretion of further processing in hepatic lysosomes.
doi_str_mv 10.1016/S0021-9258(19)50744-X
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_72802622</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>16177949</sourcerecordid><originalsourceid>FETCH-LOGICAL-c409t-26b5ea686667d01762ee67ae6c29bd180bf2b68f2fb8f00652773ec99fc4bd223</originalsourceid><addsrcrecordid>eNqNkEtLw0AUhQdRaq3-hEJwIbqIziOZx1KKLyi4sEJ3w8zkphlJOjXTIvn3po3o1rs5i3POvdwPoSnBtwQTfveGMSWporm8JuomxyLL0uURGhMsWcpysjxG49_IKTqL8QP3kykyQiMimBCKjZFctN64rl7VnYM21EnVFb100cfErxMfQ222UCQVbMzWuwTWRYihgXiOTkpTR7j40Ql6f3xYzJ7T-evTy-x-nroMq21Kuc3BcMk5FwUmglMALgxwR5UtiMS2pJbLkpZWlhjznArBwClVuswWlLIJuhr2btrwuYO41Y2PDurarCHsohZUYsr_ESSc9C9nqg_mQ9C1IcYWSr1pfWPaThOs92j1Aa3ec9NE6QNavex7058DO9tA8dcaWPb-5eBXflV9-Ra09cFV0GjKhc41Y4qzb434gAE</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16177949</pqid></control><display><type>article</type><title>Triacylglycerol hydrolysis in isolated hepatic endosomes</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Hornick, C A ; Thouron, C ; DeLamatre, J G ; Huang, J</creator><creatorcontrib>Hornick, C A ; Thouron, C ; DeLamatre, J G ; Huang, J</creatorcontrib><description>Three endosomal compartments including the compartment for uncoupling receptor and ligand (CURL), multivesicular bodies (MVB), and a putative recycling fraction (retrosomes) were isolated from rat liver homogenates fifteen minutes after a bolus injection of very low density lipoprotein (VLDL) was delivered into a femoral vein. Assays for enzyme markers indicate a minimal contamination with either lysosomes or Golgi. The increase in specific activity of the radiolabeled ligand (VLDL) during the isolation procedure from homogenate to MVB, demonstrates a 200-250-fold purification of this organelle. All three fractions have the ability to catabolize triacylglycerol substrate both as triolein and as VLDL triacylglycerol. Furthermore, incubation of isolated endosomes following injection of endogenously labeled VLDL demonstrate their ability to hydrolyze VLDL triacylglycerol in situ. Three distinct lipolytic pH optima were found at pH 5.5, 7.1, and 8.6. The effects of serum, MgCl2, CaCl2, NaCl, sodium dodecyl sulfate, bile acids, and antibody to hepatic triacylglycerol lipase on the individual endosome fractions demonstrated distinct lipolytic activities in the different compartments. Results indicate that both an endosomal neutral lipase as well as hepatic triacylglycerol lipase make a significant contribution to lipolytic processing of endocytosed lipoproteins prior to their resecretion of further processing in hepatic lysosomes.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)50744-X</identifier><identifier>PMID: 1737793</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Cell Fractionation ; Centrifugation, Density Gradient ; Cholesterol Esters - metabolism ; Cholic Acid ; Cholic Acids - pharmacology ; Deoxycholic Acid - pharmacology ; Diglycerides - metabolism ; endosomes ; Fatty Acids, Nonesterified - metabolism ; Kinetics ; Lipase - isolation &amp; purification ; Lipase - metabolism ; Lipoproteins, VLDL - metabolism ; Liver - metabolism ; Liver - ultrastructure ; Male ; Microscopy, Electron ; Oleic Acid ; Oleic Acids - metabolism ; Organelles - drug effects ; Organelles - metabolism ; Organelles - ultrastructure ; Phospholipids - metabolism ; Rats ; Rats, Inbred Strains ; triacylglycerol ; Triglycerides - metabolism</subject><ispartof>The Journal of biological chemistry, 1992-02, Vol.267 (5), p.3396-3401</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-26b5ea686667d01762ee67ae6c29bd180bf2b68f2fb8f00652773ec99fc4bd223</citedby><cites>FETCH-LOGICAL-c409t-26b5ea686667d01762ee67ae6c29bd180bf2b68f2fb8f00652773ec99fc4bd223</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1737793$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hornick, C A</creatorcontrib><creatorcontrib>Thouron, C</creatorcontrib><creatorcontrib>DeLamatre, J G</creatorcontrib><creatorcontrib>Huang, J</creatorcontrib><title>Triacylglycerol hydrolysis in isolated hepatic endosomes</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Three endosomal compartments including the compartment for uncoupling receptor and ligand (CURL), multivesicular bodies (MVB), and a putative recycling fraction (retrosomes) were isolated from rat liver homogenates fifteen minutes after a bolus injection of very low density lipoprotein (VLDL) was delivered into a femoral vein. Assays for enzyme markers indicate a minimal contamination with either lysosomes or Golgi. The increase in specific activity of the radiolabeled ligand (VLDL) during the isolation procedure from homogenate to MVB, demonstrates a 200-250-fold purification of this organelle. All three fractions have the ability to catabolize triacylglycerol substrate both as triolein and as VLDL triacylglycerol. Furthermore, incubation of isolated endosomes following injection of endogenously labeled VLDL demonstrate their ability to hydrolyze VLDL triacylglycerol in situ. Three distinct lipolytic pH optima were found at pH 5.5, 7.1, and 8.6. The effects of serum, MgCl2, CaCl2, NaCl, sodium dodecyl sulfate, bile acids, and antibody to hepatic triacylglycerol lipase on the individual endosome fractions demonstrated distinct lipolytic activities in the different compartments. Results indicate that both an endosomal neutral lipase as well as hepatic triacylglycerol lipase make a significant contribution to lipolytic processing of endocytosed lipoproteins prior to their resecretion of further processing in hepatic lysosomes.</description><subject>Animals</subject><subject>Cell Fractionation</subject><subject>Centrifugation, Density Gradient</subject><subject>Cholesterol Esters - metabolism</subject><subject>Cholic Acid</subject><subject>Cholic Acids - pharmacology</subject><subject>Deoxycholic Acid - pharmacology</subject><subject>Diglycerides - metabolism</subject><subject>endosomes</subject><subject>Fatty Acids, Nonesterified - metabolism</subject><subject>Kinetics</subject><subject>Lipase - isolation &amp; purification</subject><subject>Lipase - metabolism</subject><subject>Lipoproteins, VLDL - metabolism</subject><subject>Liver - metabolism</subject><subject>Liver - ultrastructure</subject><subject>Male</subject><subject>Microscopy, Electron</subject><subject>Oleic Acid</subject><subject>Oleic Acids - metabolism</subject><subject>Organelles - drug effects</subject><subject>Organelles - metabolism</subject><subject>Organelles - ultrastructure</subject><subject>Phospholipids - metabolism</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>triacylglycerol</subject><subject>Triglycerides - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEtLw0AUhQdRaq3-hEJwIbqIziOZx1KKLyi4sEJ3w8zkphlJOjXTIvn3po3o1rs5i3POvdwPoSnBtwQTfveGMSWporm8JuomxyLL0uURGhMsWcpysjxG49_IKTqL8QP3kykyQiMimBCKjZFctN64rl7VnYM21EnVFb100cfErxMfQ222UCQVbMzWuwTWRYihgXiOTkpTR7j40Ql6f3xYzJ7T-evTy-x-nroMq21Kuc3BcMk5FwUmglMALgxwR5UtiMS2pJbLkpZWlhjznArBwClVuswWlLIJuhr2btrwuYO41Y2PDurarCHsohZUYsr_ESSc9C9nqg_mQ9C1IcYWSr1pfWPaThOs92j1Aa3ec9NE6QNavex7058DO9tA8dcaWPb-5eBXflV9-Ra09cFV0GjKhc41Y4qzb434gAE</recordid><startdate>19920215</startdate><enddate>19920215</enddate><creator>Hornick, C A</creator><creator>Thouron, C</creator><creator>DeLamatre, J G</creator><creator>Huang, J</creator><general>American Society for Biochemistry and Molecular Biology</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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19920215</creationdate><title>Triacylglycerol hydrolysis in isolated hepatic endosomes</title><author>Hornick, C A ; Thouron, C ; DeLamatre, J G ; Huang, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-26b5ea686667d01762ee67ae6c29bd180bf2b68f2fb8f00652773ec99fc4bd223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Animals</topic><topic>Cell Fractionation</topic><topic>Centrifugation, Density Gradient</topic><topic>Cholesterol Esters - metabolism</topic><topic>Cholic Acid</topic><topic>Cholic Acids - pharmacology</topic><topic>Deoxycholic Acid - pharmacology</topic><topic>Diglycerides - metabolism</topic><topic>endosomes</topic><topic>Fatty Acids, Nonesterified - metabolism</topic><topic>Kinetics</topic><topic>Lipase - isolation &amp; purification</topic><topic>Lipase - metabolism</topic><topic>Lipoproteins, VLDL - metabolism</topic><topic>Liver - metabolism</topic><topic>Liver - ultrastructure</topic><topic>Male</topic><topic>Microscopy, Electron</topic><topic>Oleic Acid</topic><topic>Oleic Acids - metabolism</topic><topic>Organelles - drug effects</topic><topic>Organelles - metabolism</topic><topic>Organelles - ultrastructure</topic><topic>Phospholipids - metabolism</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>triacylglycerol</topic><topic>Triglycerides - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hornick, C A</creatorcontrib><creatorcontrib>Thouron, C</creatorcontrib><creatorcontrib>DeLamatre, J G</creatorcontrib><creatorcontrib>Huang, J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hornick, C A</au><au>Thouron, C</au><au>DeLamatre, J G</au><au>Huang, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Triacylglycerol hydrolysis in isolated hepatic endosomes</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-02-15</date><risdate>1992</risdate><volume>267</volume><issue>5</issue><spage>3396</spage><epage>3401</epage><pages>3396-3401</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Three endosomal compartments including the compartment for uncoupling receptor and ligand (CURL), multivesicular bodies (MVB), and a putative recycling fraction (retrosomes) were isolated from rat liver homogenates fifteen minutes after a bolus injection of very low density lipoprotein (VLDL) was delivered into a femoral vein. Assays for enzyme markers indicate a minimal contamination with either lysosomes or Golgi. The increase in specific activity of the radiolabeled ligand (VLDL) during the isolation procedure from homogenate to MVB, demonstrates a 200-250-fold purification of this organelle. All three fractions have the ability to catabolize triacylglycerol substrate both as triolein and as VLDL triacylglycerol. Furthermore, incubation of isolated endosomes following injection of endogenously labeled VLDL demonstrate their ability to hydrolyze VLDL triacylglycerol in situ. Three distinct lipolytic pH optima were found at pH 5.5, 7.1, and 8.6. The effects of serum, MgCl2, CaCl2, NaCl, sodium dodecyl sulfate, bile acids, and antibody to hepatic triacylglycerol lipase on the individual endosome fractions demonstrated distinct lipolytic activities in the different compartments. Results indicate that both an endosomal neutral lipase as well as hepatic triacylglycerol lipase make a significant contribution to lipolytic processing of endocytosed lipoproteins prior to their resecretion of further processing in hepatic lysosomes.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1737793</pmid><doi>10.1016/S0021-9258(19)50744-X</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0021-9258
ispartof The Journal of biological chemistry, 1992-02, Vol.267 (5), p.3396-3401
issn 0021-9258
1083-351X
language eng
recordid cdi_proquest_miscellaneous_72802622
source MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection
subjects Animals
Cell Fractionation
Centrifugation, Density Gradient
Cholesterol Esters - metabolism
Cholic Acid
Cholic Acids - pharmacology
Deoxycholic Acid - pharmacology
Diglycerides - metabolism
endosomes
Fatty Acids, Nonesterified - metabolism
Kinetics
Lipase - isolation & purification
Lipase - metabolism
Lipoproteins, VLDL - metabolism
Liver - metabolism
Liver - ultrastructure
Male
Microscopy, Electron
Oleic Acid
Oleic Acids - metabolism
Organelles - drug effects
Organelles - metabolism
Organelles - ultrastructure
Phospholipids - metabolism
Rats
Rats, Inbred Strains
triacylglycerol
Triglycerides - metabolism
title Triacylglycerol hydrolysis in isolated hepatic endosomes
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-18T03%3A57%3A11IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Triacylglycerol%20hydrolysis%20in%20isolated%20hepatic%20endosomes&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Hornick,%20C%20A&rft.date=1992-02-15&rft.volume=267&rft.issue=5&rft.spage=3396&rft.epage=3401&rft.pages=3396-3401&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1016/S0021-9258(19)50744-X&rft_dat=%3Cproquest_cross%3E16177949%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16177949&rft_id=info:pmid/1737793&rfr_iscdi=true