Regulation of endogenously catalyzed ADP-ribosylation in adipocyte plasma membranes by Ca2+ and calmodulin
The effects of Ca2+ and calmodulin on endogenously catalyzed ADP-ribosylation were investigated in adipocyte plasma membranes. Four specific proteins of 70, 65, 61 and 52 kDa were labeled with [32P]ADP-ribose and ADP-ribosylation of the proteins was highly dependent upon the conditions employed. ADP...
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| Veröffentlicht in: | Cell calcium (Edinburgh) 1985-12, Vol.6 (6), p.491-501 |
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| creator | GRAVES, C. B MCDONALD, J. M |
| description | The effects of Ca2+ and calmodulin on endogenously catalyzed ADP-ribosylation were investigated in adipocyte plasma membranes. Four specific proteins of 70, 65, 61 and 52 kDa were labeled with [32P]ADP-ribose and ADP-ribosylation of the proteins was highly dependent upon the conditions employed. ADP-ribosylation of the 70 kDa protein was observed only in membranes supplemented with Ca2+. Maximal incorporation of [32P] into the protein was achieved with free Ca2+ concentrations of 90 microM. Calcium-stimulated ADP-ribosylation of the 70 kDa protein was inhibited by calmodulin. Half-maximal inhibition was observed in membranes incubated with 1.2 microM calmodulin. The effect of calmodulin was characterized by an inhibition of the incorporation of [32P]ADP-ribose as opposed to a stimulation of its removal. ADP-ribosylation of the 61 kDa protein was not altered by added Ca2+ and/or calmodulin whereas ADP-ribosylation of the 65 kDa protein was partially (50%) inhibited by free Ca2+ concentrations between 10(-6) - 10(-5) M. These results provide evidence that the adipocyte plasma membrane contains ADP-ribosyltransferase activities and demonstrate that ADP-ribosylation of a 70 kDa protein is regulated by Ca2+ and calmodulin. |
| doi_str_mv | 10.1016/0143-4160(85)90024-7 |
| format | Article |
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B ; MCDONALD, J. M</creator><creatorcontrib>GRAVES, C. B ; MCDONALD, J. M</creatorcontrib><description>The effects of Ca2+ and calmodulin on endogenously catalyzed ADP-ribosylation were investigated in adipocyte plasma membranes. Four specific proteins of 70, 65, 61 and 52 kDa were labeled with [32P]ADP-ribose and ADP-ribosylation of the proteins was highly dependent upon the conditions employed. ADP-ribosylation of the 70 kDa protein was observed only in membranes supplemented with Ca2+. Maximal incorporation of [32P] into the protein was achieved with free Ca2+ concentrations of 90 microM. Calcium-stimulated ADP-ribosylation of the 70 kDa protein was inhibited by calmodulin. Half-maximal inhibition was observed in membranes incubated with 1.2 microM calmodulin. The effect of calmodulin was characterized by an inhibition of the incorporation of [32P]ADP-ribose as opposed to a stimulation of its removal. ADP-ribosylation of the 61 kDa protein was not altered by added Ca2+ and/or calmodulin whereas ADP-ribosylation of the 65 kDa protein was partially (50%) inhibited by free Ca2+ concentrations between 10(-6) - 10(-5) M. These results provide evidence that the adipocyte plasma membrane contains ADP-ribosyltransferase activities and demonstrate that ADP-ribosylation of a 70 kDa protein is regulated by Ca2+ and calmodulin.</description><identifier>ISSN: 0143-4160</identifier><identifier>EISSN: 1532-1991</identifier><identifier>DOI: 10.1016/0143-4160(85)90024-7</identifier><identifier>PMID: 3937599</identifier><identifier>CODEN: CECADV</identifier><language>eng</language><publisher>Oxford: Elsevier</publisher><subject>Adenosine Diphosphate Ribose - metabolism ; Adipose Tissue - drug effects ; Adipose Tissue - metabolism ; Animals ; Biological and medical sciences ; Calcium - pharmacology ; Calmodulin - pharmacology ; Cell Membrane - drug effects ; Cell Membrane - metabolism ; Cell membranes. Ionic channels. Membrane pores ; Cell structures and functions ; Edetic Acid - pharmacology ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Membrane Proteins - isolation & purification ; Membrane Proteins - metabolism ; Molecular and cellular biology ; Molecular Weight ; Nucleoside Diphosphate Sugars - metabolism ; Rats</subject><ispartof>Cell calcium (Edinburgh), 1985-12, Vol.6 (6), p.491-501</ispartof><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c1789-278ad0831d02e11caefe7604d1877067b86b9c21e11c947b41de092c518136f73</citedby><cites>FETCH-LOGICAL-c1789-278ad0831d02e11caefe7604d1877067b86b9c21e11c947b41de092c518136f73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8789963$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3937599$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>GRAVES, C. B</creatorcontrib><creatorcontrib>MCDONALD, J. M</creatorcontrib><title>Regulation of endogenously catalyzed ADP-ribosylation in adipocyte plasma membranes by Ca2+ and calmodulin</title><title>Cell calcium (Edinburgh)</title><addtitle>Cell Calcium</addtitle><description>The effects of Ca2+ and calmodulin on endogenously catalyzed ADP-ribosylation were investigated in adipocyte plasma membranes. Four specific proteins of 70, 65, 61 and 52 kDa were labeled with [32P]ADP-ribose and ADP-ribosylation of the proteins was highly dependent upon the conditions employed. ADP-ribosylation of the 70 kDa protein was observed only in membranes supplemented with Ca2+. Maximal incorporation of [32P] into the protein was achieved with free Ca2+ concentrations of 90 microM. Calcium-stimulated ADP-ribosylation of the 70 kDa protein was inhibited by calmodulin. Half-maximal inhibition was observed in membranes incubated with 1.2 microM calmodulin. The effect of calmodulin was characterized by an inhibition of the incorporation of [32P]ADP-ribose as opposed to a stimulation of its removal. ADP-ribosylation of the 61 kDa protein was not altered by added Ca2+ and/or calmodulin whereas ADP-ribosylation of the 65 kDa protein was partially (50%) inhibited by free Ca2+ concentrations between 10(-6) - 10(-5) M. These results provide evidence that the adipocyte plasma membrane contains ADP-ribosyltransferase activities and demonstrate that ADP-ribosylation of a 70 kDa protein is regulated by Ca2+ and calmodulin.</description><subject>Adenosine Diphosphate Ribose - metabolism</subject><subject>Adipose Tissue - drug effects</subject><subject>Adipose Tissue - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calcium - pharmacology</subject><subject>Calmodulin - pharmacology</subject><subject>Cell Membrane - drug effects</subject><subject>Cell Membrane - metabolism</subject><subject>Cell membranes. Ionic channels. Membrane pores</subject><subject>Cell structures and functions</subject><subject>Edetic Acid - pharmacology</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kinetics</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular and cellular biology</subject><subject>Molecular Weight</subject><subject>Nucleoside Diphosphate Sugars - metabolism</subject><subject>Rats</subject><issn>0143-4160</issn><issn>1532-1991</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE1P3DAURS1URAfKPwDJiwpRobTvxYk_lmhoCxJSq6qsLcd2UJATT-PJIv31OBDN6i3u8ZXvIeQC4SsC8m-AFSsq5HAt6y8KoKwKcUQ2WLOyQKXwA9kckI_kNKUXAFBM4Ak5YfnWSm3Iyx__PAWz7-JAY0v94OKzH-KUwkyt2Zsw__eO3t79LsauiWle0W6gxnW7aOe9p7tgUm9o7_tmNINPtJnp1pQ31Awul4Q-uil0wydy3JqQ_Pl6z8jTj-9_t_fF46-fD9vbx8KikKoohTQOJEMHpUe0xrdecKgcSiGAi0byRtkSl0xVoqnQeVClrVEi461gZ-TqvXc3xn-TT3vdd8n6EPLf8jAtOMdSAGSwegftGFMafat3Y9ebcdYIelGsF3968adlrd8U66X_cu2fmt67w6PVac4_r7lJeX2bndguHTCZRyrO2CuUe4Nw</recordid><startdate>198512</startdate><enddate>198512</enddate><creator>GRAVES, C. B</creator><creator>MCDONALD, J. M</creator><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>7X8</scope></search><sort><creationdate>198512</creationdate><title>Regulation of endogenously catalyzed ADP-ribosylation in adipocyte plasma membranes by Ca2+ and calmodulin</title><author>GRAVES, C. B ; MCDONALD, J. M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1789-278ad0831d02e11caefe7604d1877067b86b9c21e11c947b41de092c518136f73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Adenosine Diphosphate Ribose - metabolism</topic><topic>Adipose Tissue - drug effects</topic><topic>Adipose Tissue - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calcium - pharmacology</topic><topic>Calmodulin - pharmacology</topic><topic>Cell Membrane - drug effects</topic><topic>Cell Membrane - metabolism</topic><topic>Cell membranes. Ionic channels. Membrane pores</topic><topic>Cell structures and functions</topic><topic>Edetic Acid - pharmacology</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kinetics</topic><topic>Membrane Proteins - isolation & purification</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular and cellular biology</topic><topic>Molecular Weight</topic><topic>Nucleoside Diphosphate Sugars - metabolism</topic><topic>Rats</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>GRAVES, C. B</creatorcontrib><creatorcontrib>MCDONALD, J. M</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>MEDLINE - Academic</collection><jtitle>Cell calcium (Edinburgh)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>GRAVES, C. B</au><au>MCDONALD, J. M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of endogenously catalyzed ADP-ribosylation in adipocyte plasma membranes by Ca2+ and calmodulin</atitle><jtitle>Cell calcium (Edinburgh)</jtitle><addtitle>Cell Calcium</addtitle><date>1985-12</date><risdate>1985</risdate><volume>6</volume><issue>6</issue><spage>491</spage><epage>501</epage><pages>491-501</pages><issn>0143-4160</issn><eissn>1532-1991</eissn><coden>CECADV</coden><abstract>The effects of Ca2+ and calmodulin on endogenously catalyzed ADP-ribosylation were investigated in adipocyte plasma membranes. Four specific proteins of 70, 65, 61 and 52 kDa were labeled with [32P]ADP-ribose and ADP-ribosylation of the proteins was highly dependent upon the conditions employed. ADP-ribosylation of the 70 kDa protein was observed only in membranes supplemented with Ca2+. Maximal incorporation of [32P] into the protein was achieved with free Ca2+ concentrations of 90 microM. Calcium-stimulated ADP-ribosylation of the 70 kDa protein was inhibited by calmodulin. Half-maximal inhibition was observed in membranes incubated with 1.2 microM calmodulin. The effect of calmodulin was characterized by an inhibition of the incorporation of [32P]ADP-ribose as opposed to a stimulation of its removal. ADP-ribosylation of the 61 kDa protein was not altered by added Ca2+ and/or calmodulin whereas ADP-ribosylation of the 65 kDa protein was partially (50%) inhibited by free Ca2+ concentrations between 10(-6) - 10(-5) M. These results provide evidence that the adipocyte plasma membrane contains ADP-ribosyltransferase activities and demonstrate that ADP-ribosylation of a 70 kDa protein is regulated by Ca2+ and calmodulin.</abstract><cop>Oxford</cop><pub>Elsevier</pub><pmid>3937599</pmid><doi>10.1016/0143-4160(85)90024-7</doi><tpages>11</tpages></addata></record> |
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| identifier | ISSN: 0143-4160 |
| ispartof | Cell calcium (Edinburgh), 1985-12, Vol.6 (6), p.491-501 |
| issn | 0143-4160 1532-1991 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Adenosine Diphosphate Ribose - metabolism Adipose Tissue - drug effects Adipose Tissue - metabolism Animals Biological and medical sciences Calcium - pharmacology Calmodulin - pharmacology Cell Membrane - drug effects Cell Membrane - metabolism Cell membranes. Ionic channels. Membrane pores Cell structures and functions Edetic Acid - pharmacology Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Kinetics Membrane Proteins - isolation & purification Membrane Proteins - metabolism Molecular and cellular biology Molecular Weight Nucleoside Diphosphate Sugars - metabolism Rats |
| title | Regulation of endogenously catalyzed ADP-ribosylation in adipocyte plasma membranes by Ca2+ and calmodulin |
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