Insulin-like growth factor-II (IGF-II) inhibits both the cellular uptake of β-galactosidase and the binding of β-galactosidase to purified IGF-II/mannose 6-phosphate receptor
The insulin-like growth factor-II/mannose 6-phosphate receptor which targets acid hydrolases to lysosomes, has two different binding sites, one for the mannose 6-phosphate (Man-6-P) recognition marker on lysosomal enzymes and the other for insulin-like growth factor-II (IGF-II). We have asked whethe...
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| Veröffentlicht in: | The Journal of biological chemistry 1989-03, Vol.264 (8), p.4710-4714 |
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| creator | Kiess, W Thomas, C L Greenstein, L A Lee, L Sklar, M M Rechler, M M Sahagian, G G Nissley, S P |
| description | The insulin-like growth factor-II/mannose 6-phosphate receptor which targets acid hydrolases to lysosomes, has two different binding sites, one for the mannose 6-phosphate (Man-6-P) recognition marker on lysosomal enzymes and the other for insulin-like growth factor-II (IGF-II). We have asked whether IGF-II can regulate the cellular uptake of the lysosomal enzyme 125I-β-galactosidase by modulating the binding of 125I-β-galactosidase to the IGF-II/Man-6-P receptor. We first isolated high affinity 125I-β-galactosidase by affinity chromatography on an IGF-II/Man-6-P receptor-Sepharose column. Specific uptake (mannose 6-phosphate-inhibitable) of 125I-β-galactosidase in BRL 3A2 rat liver cells and in rat C6 glial cells was 3.7–4.8 and 4.0–8.0% of added tracer, respectively. The cell-associated 125I-β-galactosidase in the uptake experiments largely represented internalized radioligand as measured by acid or mannose 6-phosphate washing. The uptake of 125I-β-galactosidase was inhibited by an antiserum (No. 3637) specific for the IGF-II/Man-6-P receptor. Low concentrations of IGF-II also inhibited the uptake of 125I-β-galactosidase. Maximal concentrations of IGF-II inhibited uptake by 73 ± 8% (mean ± S.D.) in C6 cells and by 77 ± 6% in BRL 3A2 cells compared to the level of inhibition by mannose 6-phosphate. The relative potency of IGF-II, IGF-I, and insulin (IGF-II ≫ IGF-I; insulin, inactive) were characteristic of the relative affinities of the ligands for the IGF-II/Man-6-P receptor. IGF-II also partially inhibited the binding of 125I-β-galactosidase to C6 and BRL 3A2 cells at 4 ° C and inhibited the binding to highly purified IGF-II/Man-6-P receptor by 58 ± 14%. We conclude that IGF-II inhibits the cellular uptake of 125I-β-galactosidase and that this inhibition is partly explained by the ability of IGF-II to inhibit binding of 125I-β-galactosidase to the IGF-II/Man-6-P receptor. |
| doi_str_mv | 10.1016/S0021-9258(18)83801-7 |
| format | Article |
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We have asked whether IGF-II can regulate the cellular uptake of the lysosomal enzyme 125I-β-galactosidase by modulating the binding of 125I-β-galactosidase to the IGF-II/Man-6-P receptor. We first isolated high affinity 125I-β-galactosidase by affinity chromatography on an IGF-II/Man-6-P receptor-Sepharose column. Specific uptake (mannose 6-phosphate-inhibitable) of 125I-β-galactosidase in BRL 3A2 rat liver cells and in rat C6 glial cells was 3.7–4.8 and 4.0–8.0% of added tracer, respectively. The cell-associated 125I-β-galactosidase in the uptake experiments largely represented internalized radioligand as measured by acid or mannose 6-phosphate washing. The uptake of 125I-β-galactosidase was inhibited by an antiserum (No. 3637) specific for the IGF-II/Man-6-P receptor. Low concentrations of IGF-II also inhibited the uptake of 125I-β-galactosidase. Maximal concentrations of IGF-II inhibited uptake by 73 ± 8% (mean ± S.D.) in C6 cells and by 77 ± 6% in BRL 3A2 cells compared to the level of inhibition by mannose 6-phosphate. The relative potency of IGF-II, IGF-I, and insulin (IGF-II ≫ IGF-I; insulin, inactive) were characteristic of the relative affinities of the ligands for the IGF-II/Man-6-P receptor. IGF-II also partially inhibited the binding of 125I-β-galactosidase to C6 and BRL 3A2 cells at 4 ° C and inhibited the binding to highly purified IGF-II/Man-6-P receptor by 58 ± 14%. We conclude that IGF-II inhibits the cellular uptake of 125I-β-galactosidase and that this inhibition is partly explained by the ability of IGF-II to inhibit binding of 125I-β-galactosidase to the IGF-II/Man-6-P receptor.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)83801-7</identifier><identifier>PMID: 2538455</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Animals ; beta -galactosidase ; beta-Galactosidase - isolation & purification ; beta-Galactosidase - metabolism ; Biological and medical sciences ; Biological Transport ; Cell Line ; Cell receptors ; Cell structures and functions ; Chromatography, Affinity ; Female ; Fundamental and applied biological sciences. Psychology ; Galactosidases - metabolism ; Immunosorbent Techniques ; insulin-like growth factor II ; Insulin-Like Growth Factor II - pharmacology ; Liver - metabolism ; lysosomes ; Molecular and cellular biology ; Neuroglia - metabolism ; Placenta - analysis ; Pregnancy ; Rats ; Receptor, IGF Type 2 ; Receptors, Cell Surface - metabolism ; Receptors, Somatomedin ; Somatomedins - pharmacology</subject><ispartof>The Journal of biological chemistry, 1989-03, Vol.264 (8), p.4710-4714</ispartof><rights>1989 © 1989 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c494t-df234d4a9794ab864d90139e94e77cfa2b5a44494e5abf8f0ad58617465e631c3</citedby><cites>FETCH-LOGICAL-c494t-df234d4a9794ab864d90139e94e77cfa2b5a44494e5abf8f0ad58617465e631c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7307998$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2538455$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kiess, W</creatorcontrib><creatorcontrib>Thomas, C L</creatorcontrib><creatorcontrib>Greenstein, L A</creatorcontrib><creatorcontrib>Lee, L</creatorcontrib><creatorcontrib>Sklar, M M</creatorcontrib><creatorcontrib>Rechler, M M</creatorcontrib><creatorcontrib>Sahagian, G G</creatorcontrib><creatorcontrib>Nissley, S P</creatorcontrib><title>Insulin-like growth factor-II (IGF-II) inhibits both the cellular uptake of β-galactosidase and the binding of β-galactosidase to purified IGF-II/mannose 6-phosphate receptor</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The insulin-like growth factor-II/mannose 6-phosphate receptor which targets acid hydrolases to lysosomes, has two different binding sites, one for the mannose 6-phosphate (Man-6-P) recognition marker on lysosomal enzymes and the other for insulin-like growth factor-II (IGF-II). We have asked whether IGF-II can regulate the cellular uptake of the lysosomal enzyme 125I-β-galactosidase by modulating the binding of 125I-β-galactosidase to the IGF-II/Man-6-P receptor. We first isolated high affinity 125I-β-galactosidase by affinity chromatography on an IGF-II/Man-6-P receptor-Sepharose column. Specific uptake (mannose 6-phosphate-inhibitable) of 125I-β-galactosidase in BRL 3A2 rat liver cells and in rat C6 glial cells was 3.7–4.8 and 4.0–8.0% of added tracer, respectively. The cell-associated 125I-β-galactosidase in the uptake experiments largely represented internalized radioligand as measured by acid or mannose 6-phosphate washing. The uptake of 125I-β-galactosidase was inhibited by an antiserum (No. 3637) specific for the IGF-II/Man-6-P receptor. Low concentrations of IGF-II also inhibited the uptake of 125I-β-galactosidase. Maximal concentrations of IGF-II inhibited uptake by 73 ± 8% (mean ± S.D.) in C6 cells and by 77 ± 6% in BRL 3A2 cells compared to the level of inhibition by mannose 6-phosphate. The relative potency of IGF-II, IGF-I, and insulin (IGF-II ≫ IGF-I; insulin, inactive) were characteristic of the relative affinities of the ligands for the IGF-II/Man-6-P receptor. IGF-II also partially inhibited the binding of 125I-β-galactosidase to C6 and BRL 3A2 cells at 4 ° C and inhibited the binding to highly purified IGF-II/Man-6-P receptor by 58 ± 14%. We conclude that IGF-II inhibits the cellular uptake of 125I-β-galactosidase and that this inhibition is partly explained by the ability of IGF-II to inhibit binding of 125I-β-galactosidase to the IGF-II/Man-6-P receptor.</description><subject>Animals</subject><subject>beta -galactosidase</subject><subject>beta-Galactosidase - isolation & purification</subject><subject>beta-Galactosidase - metabolism</subject><subject>Biological and medical sciences</subject><subject>Biological Transport</subject><subject>Cell Line</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Chromatography, Affinity</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Galactosidases - metabolism</subject><subject>Immunosorbent Techniques</subject><subject>insulin-like growth factor II</subject><subject>Insulin-Like Growth Factor II - pharmacology</subject><subject>Liver - metabolism</subject><subject>lysosomes</subject><subject>Molecular and cellular biology</subject><subject>Neuroglia - metabolism</subject><subject>Placenta - analysis</subject><subject>Pregnancy</subject><subject>Rats</subject><subject>Receptor, IGF Type 2</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Somatomedin</subject><subject>Somatomedins - pharmacology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFu1DAQhiMEKkvhESpZCKH2EGondmyfEKpou1IlDoDEzXLsycaQtYOdUPFWiAfhmersrvaE1LnM4f_-mbH_ojgj-B3BpLn8jHFFSlkxcU7EhagFJiV_UqwIFnVZM_LtabE6Is-LFyl9x7moJCfFScVqQRlbFX_WPs2D8-XgfgDaxHA_9ajTZgqxXK_R-frmOvcL5HzvWjcl1IYMTD0gA8MwDzqieZx09oYO_ftbbvSwmJOzOgHS3u7Y1nnr_Oa_zBTQOEfXObBov-1yq70PWWrKsQ9p7PUEKIKBMV_1snjW6SHBq0M_Lb5ef_xydVvefbpZX324Kw2VdCptV9XUUi25pLoVDbUSk1qCpMC56XTVMk1pRoHpthMd1paJhnDaMGhqYurT4u1-7hjDzxnSpLYuLW_WHsKcFBcSi6amj4KEES4azjPI9qCJIaUInRqj2-r4WxGslkjVLlK15KWIULtI1eI7OyyY2y3Yo-uQYdbfHHSdjB66qL1x6YjxGnMpRcZe77Hebfp7F0G1LpgetqpqqBKKcoIz9H4PQf7aXw6iSsaBN2CzwUzKBvfItQ8okMs8</recordid><startdate>19890315</startdate><enddate>19890315</enddate><creator>Kiess, W</creator><creator>Thomas, C L</creator><creator>Greenstein, L A</creator><creator>Lee, L</creator><creator>Sklar, M M</creator><creator>Rechler, M M</creator><creator>Sahagian, G G</creator><creator>Nissley, S P</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19890315</creationdate><title>Insulin-like growth factor-II (IGF-II) inhibits both the cellular uptake of β-galactosidase and the binding of β-galactosidase to purified IGF-II/mannose 6-phosphate receptor</title><author>Kiess, W ; Thomas, C L ; Greenstein, L A ; Lee, L ; Sklar, M M ; Rechler, M M ; Sahagian, G G ; Nissley, S P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c494t-df234d4a9794ab864d90139e94e77cfa2b5a44494e5abf8f0ad58617465e631c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Animals</topic><topic>beta -galactosidase</topic><topic>beta-Galactosidase - isolation & purification</topic><topic>beta-Galactosidase - metabolism</topic><topic>Biological and medical sciences</topic><topic>Biological Transport</topic><topic>Cell Line</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Chromatography, Affinity</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Galactosidases - metabolism</topic><topic>Immunosorbent Techniques</topic><topic>insulin-like growth factor II</topic><topic>Insulin-Like Growth Factor II - pharmacology</topic><topic>Liver - metabolism</topic><topic>lysosomes</topic><topic>Molecular and cellular biology</topic><topic>Neuroglia - metabolism</topic><topic>Placenta - analysis</topic><topic>Pregnancy</topic><topic>Rats</topic><topic>Receptor, IGF Type 2</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Somatomedin</topic><topic>Somatomedins - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kiess, W</creatorcontrib><creatorcontrib>Thomas, C L</creatorcontrib><creatorcontrib>Greenstein, L A</creatorcontrib><creatorcontrib>Lee, L</creatorcontrib><creatorcontrib>Sklar, M M</creatorcontrib><creatorcontrib>Rechler, M M</creatorcontrib><creatorcontrib>Sahagian, G G</creatorcontrib><creatorcontrib>Nissley, S P</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>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>Kiess, W</au><au>Thomas, C L</au><au>Greenstein, L A</au><au>Lee, L</au><au>Sklar, M M</au><au>Rechler, M M</au><au>Sahagian, G G</au><au>Nissley, S P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Insulin-like growth factor-II (IGF-II) inhibits both the cellular uptake of β-galactosidase and the binding of β-galactosidase to purified IGF-II/mannose 6-phosphate receptor</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1989-03-15</date><risdate>1989</risdate><volume>264</volume><issue>8</issue><spage>4710</spage><epage>4714</epage><pages>4710-4714</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The insulin-like growth factor-II/mannose 6-phosphate receptor which targets acid hydrolases to lysosomes, has two different binding sites, one for the mannose 6-phosphate (Man-6-P) recognition marker on lysosomal enzymes and the other for insulin-like growth factor-II (IGF-II). We have asked whether IGF-II can regulate the cellular uptake of the lysosomal enzyme 125I-β-galactosidase by modulating the binding of 125I-β-galactosidase to the IGF-II/Man-6-P receptor. We first isolated high affinity 125I-β-galactosidase by affinity chromatography on an IGF-II/Man-6-P receptor-Sepharose column. Specific uptake (mannose 6-phosphate-inhibitable) of 125I-β-galactosidase in BRL 3A2 rat liver cells and in rat C6 glial cells was 3.7–4.8 and 4.0–8.0% of added tracer, respectively. The cell-associated 125I-β-galactosidase in the uptake experiments largely represented internalized radioligand as measured by acid or mannose 6-phosphate washing. The uptake of 125I-β-galactosidase was inhibited by an antiserum (No. 3637) specific for the IGF-II/Man-6-P receptor. Low concentrations of IGF-II also inhibited the uptake of 125I-β-galactosidase. Maximal concentrations of IGF-II inhibited uptake by 73 ± 8% (mean ± S.D.) in C6 cells and by 77 ± 6% in BRL 3A2 cells compared to the level of inhibition by mannose 6-phosphate. The relative potency of IGF-II, IGF-I, and insulin (IGF-II ≫ IGF-I; insulin, inactive) were characteristic of the relative affinities of the ligands for the IGF-II/Man-6-P receptor. IGF-II also partially inhibited the binding of 125I-β-galactosidase to C6 and BRL 3A2 cells at 4 ° C and inhibited the binding to highly purified IGF-II/Man-6-P receptor by 58 ± 14%. We conclude that IGF-II inhibits the cellular uptake of 125I-β-galactosidase and that this inhibition is partly explained by the ability of IGF-II to inhibit binding of 125I-β-galactosidase to the IGF-II/Man-6-P receptor.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2538455</pmid><doi>10.1016/S0021-9258(18)83801-7</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1989-03, Vol.264 (8), p.4710-4714 |
| issn | 0021-9258 1083-351X |
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| subjects | Animals beta -galactosidase beta-Galactosidase - isolation & purification beta-Galactosidase - metabolism Biological and medical sciences Biological Transport Cell Line Cell receptors Cell structures and functions Chromatography, Affinity Female Fundamental and applied biological sciences. Psychology Galactosidases - metabolism Immunosorbent Techniques insulin-like growth factor II Insulin-Like Growth Factor II - pharmacology Liver - metabolism lysosomes Molecular and cellular biology Neuroglia - metabolism Placenta - analysis Pregnancy Rats Receptor, IGF Type 2 Receptors, Cell Surface - metabolism Receptors, Somatomedin Somatomedins - pharmacology |
| title | Insulin-like growth factor-II (IGF-II) inhibits both the cellular uptake of β-galactosidase and the binding of β-galactosidase to purified IGF-II/mannose 6-phosphate receptor |
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