Insulin induces tyrosine dephosphorylation of a 92 kDa protein in suspended monocytes
Monocytes bear insulin receptors similar to those expressed in other tissues, but insulin action in these cells remains unclear. There is evidence that adhesion, by generating a complex array of irreversible transformations, may modify the response of cells to other stimuli, such as hormones. The pr...
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| Veröffentlicht in: | Journal of endocrinological investigation 1998-02, Vol.21 (2), p.93-97 |
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| container_end_page | 97 |
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| container_title | Journal of endocrinological investigation |
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| creator | ZOPPINI, G GALANTE, P ZARDINI, M MUGGEO, M |
| description | Monocytes bear insulin receptors similar to those expressed in other tissues, but insulin action in these cells remains unclear. There is evidence that adhesion, by generating a complex array of irreversible transformations, may modify the response of cells to other stimuli, such as hormones. The present study aimed to characterise the pattern of insulin induced tyrosine phosphorylation of monocytes in suspension. Monocytes in suspension were obtained by sequential gradient centrifugation and the tyrosine phosphoproteins were analyzed by immunoblot with antiphosphotyrosine antibodies. The major result of the study is that in suspended monocytes insulin induced a dose and time dependent dephosphorylation of a protein with a molecular mass of about 92 kDa without stimulating the tyrosine phosphorylation of the Insulin Receptor Substrat-1 (IRS-1). In conclusion, we showed that in monocytes in suspension insulin seems to activate a tyrosine phosphatase, which, in turn, dephosphorylates a protein with an apparent molecular weight of 92 kDa. |
| doi_str_mv | 10.1007/BF03350321 |
| format | Article |
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There is evidence that adhesion, by generating a complex array of irreversible transformations, may modify the response of cells to other stimuli, such as hormones. The present study aimed to characterise the pattern of insulin induced tyrosine phosphorylation of monocytes in suspension. Monocytes in suspension were obtained by sequential gradient centrifugation and the tyrosine phosphoproteins were analyzed by immunoblot with antiphosphotyrosine antibodies. The major result of the study is that in suspended monocytes insulin induced a dose and time dependent dephosphorylation of a protein with a molecular mass of about 92 kDa without stimulating the tyrosine phosphorylation of the Insulin Receptor Substrat-1 (IRS-1). In conclusion, we showed that in monocytes in suspension insulin seems to activate a tyrosine phosphatase, which, in turn, dephosphorylates a protein with an apparent molecular weight of 92 kDa.</description><identifier>ISSN: 0391-4097</identifier><identifier>EISSN: 1720-8386</identifier><identifier>DOI: 10.1007/BF03350321</identifier><identifier>PMID: 9585382</identifier><identifier>CODEN: JEIND7</identifier><language>eng</language><publisher>Milano: Kurtis</publisher><subject>Biological and medical sciences ; Cell receptors ; Cell structures and functions ; Fundamental and applied biological sciences. Psychology ; Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors ; Humans ; Immunoblotting ; Insulin - pharmacology ; Kinetics ; Molecular and cellular biology ; Molecular Weight ; Monocytes - drug effects ; Monocytes - metabolism ; Phosphoproteins - metabolism ; Phosphorylation ; Phosphotyrosine - metabolism ; Receptor, Insulin - isolation & purification ; Receptor, Insulin - metabolism</subject><ispartof>Journal of endocrinological investigation, 1998-02, Vol.21 (2), p.93-97</ispartof><rights>1998 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c311t-2a176608baef2d6352a1d19a4bbd07edfe34b6389c305fe8e20601f9909404113</citedby><cites>FETCH-LOGICAL-c311t-2a176608baef2d6352a1d19a4bbd07edfe34b6389c305fe8e20601f9909404113</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2214934$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9585382$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>ZOPPINI, G</creatorcontrib><creatorcontrib>GALANTE, P</creatorcontrib><creatorcontrib>ZARDINI, M</creatorcontrib><creatorcontrib>MUGGEO, M</creatorcontrib><title>Insulin induces tyrosine dephosphorylation of a 92 kDa protein in suspended monocytes</title><title>Journal of endocrinological investigation</title><addtitle>J Endocrinol Invest</addtitle><description>Monocytes bear insulin receptors similar to those expressed in other tissues, but insulin action in these cells remains unclear. There is evidence that adhesion, by generating a complex array of irreversible transformations, may modify the response of cells to other stimuli, such as hormones. The present study aimed to characterise the pattern of insulin induced tyrosine phosphorylation of monocytes in suspension. Monocytes in suspension were obtained by sequential gradient centrifugation and the tyrosine phosphoproteins were analyzed by immunoblot with antiphosphotyrosine antibodies. The major result of the study is that in suspended monocytes insulin induced a dose and time dependent dephosphorylation of a protein with a molecular mass of about 92 kDa without stimulating the tyrosine phosphorylation of the Insulin Receptor Substrat-1 (IRS-1). In conclusion, we showed that in monocytes in suspension insulin seems to activate a tyrosine phosphatase, which, in turn, dephosphorylates a protein with an apparent molecular weight of 92 kDa.</description><subject>Biological and medical sciences</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Insulin - pharmacology</subject><subject>Kinetics</subject><subject>Molecular and cellular biology</subject><subject>Molecular Weight</subject><subject>Monocytes - drug effects</subject><subject>Monocytes - metabolism</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Phosphotyrosine - metabolism</subject><subject>Receptor, Insulin - isolation & purification</subject><subject>Receptor, Insulin - metabolism</subject><issn>0391-4097</issn><issn>1720-8386</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkDFPwzAQhS0EKqWwsCN5QAxIgbOdxPYIhUKlSix0jpz4LAKJU-JkyL8n0KgMp5Puffd09wi5ZHDHAOT94wqESEBwdkTmTHKIlFDpMZmD0CyKQctTchbCJ4CQQskZmelEJULxOdmufeir0tPS277AQLuhbULpkVrcfTRhrHaoTFc2njaOGqo5_XoydNc2Hf6t0dCHHXqLltaNb4qhw3BOTpypAl5MfUG2q-f35Wu0eXtZLx82USEY6yJumExTULlBx20qknFgmTZxnluQaB2KOE-F0oWAxKFCDikwpzXoGGLGxILc7H3Hc757DF1Wl6HAqjIemz5kUqtUQqpH8HYPFuN3oUWX7dqyNu2QMch-M8z-Mxzhq8m1z2u0B3QKbdSvJ92EwlSuNb4owwHjnMVaxOIHiwh4IQ</recordid><startdate>19980201</startdate><enddate>19980201</enddate><creator>ZOPPINI, G</creator><creator>GALANTE, P</creator><creator>ZARDINI, M</creator><creator>MUGGEO, M</creator><general>Kurtis</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>19980201</creationdate><title>Insulin induces tyrosine dephosphorylation of a 92 kDa protein in suspended monocytes</title><author>ZOPPINI, G ; GALANTE, P ; ZARDINI, M ; MUGGEO, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c311t-2a176608baef2d6352a1d19a4bbd07edfe34b6389c305fe8e20601f9909404113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Biological and medical sciences</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>Insulin - pharmacology</topic><topic>Kinetics</topic><topic>Molecular and cellular biology</topic><topic>Molecular Weight</topic><topic>Monocytes - drug effects</topic><topic>Monocytes - metabolism</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Phosphotyrosine - metabolism</topic><topic>Receptor, Insulin - isolation & purification</topic><topic>Receptor, Insulin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>ZOPPINI, G</creatorcontrib><creatorcontrib>GALANTE, P</creatorcontrib><creatorcontrib>ZARDINI, M</creatorcontrib><creatorcontrib>MUGGEO, 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>Journal of endocrinological investigation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>ZOPPINI, G</au><au>GALANTE, P</au><au>ZARDINI, M</au><au>MUGGEO, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Insulin induces tyrosine dephosphorylation of a 92 kDa protein in suspended monocytes</atitle><jtitle>Journal of endocrinological investigation</jtitle><addtitle>J Endocrinol Invest</addtitle><date>1998-02-01</date><risdate>1998</risdate><volume>21</volume><issue>2</issue><spage>93</spage><epage>97</epage><pages>93-97</pages><issn>0391-4097</issn><eissn>1720-8386</eissn><coden>JEIND7</coden><abstract>Monocytes bear insulin receptors similar to those expressed in other tissues, but insulin action in these cells remains unclear. There is evidence that adhesion, by generating a complex array of irreversible transformations, may modify the response of cells to other stimuli, such as hormones. The present study aimed to characterise the pattern of insulin induced tyrosine phosphorylation of monocytes in suspension. Monocytes in suspension were obtained by sequential gradient centrifugation and the tyrosine phosphoproteins were analyzed by immunoblot with antiphosphotyrosine antibodies. The major result of the study is that in suspended monocytes insulin induced a dose and time dependent dephosphorylation of a protein with a molecular mass of about 92 kDa without stimulating the tyrosine phosphorylation of the Insulin Receptor Substrat-1 (IRS-1). In conclusion, we showed that in monocytes in suspension insulin seems to activate a tyrosine phosphatase, which, in turn, dephosphorylates a protein with an apparent molecular weight of 92 kDa.</abstract><cop>Milano</cop><pub>Kurtis</pub><pmid>9585382</pmid><doi>10.1007/BF03350321</doi><tpages>5</tpages></addata></record> |
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| ispartof | Journal of endocrinological investigation, 1998-02, Vol.21 (2), p.93-97 |
| issn | 0391-4097 1720-8386 |
| language | eng |
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| subjects | Biological and medical sciences Cell receptors Cell structures and functions Fundamental and applied biological sciences. Psychology Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors Humans Immunoblotting Insulin - pharmacology Kinetics Molecular and cellular biology Molecular Weight Monocytes - drug effects Monocytes - metabolism Phosphoproteins - metabolism Phosphorylation Phosphotyrosine - metabolism Receptor, Insulin - isolation & purification Receptor, Insulin - metabolism |
| title | Insulin induces tyrosine dephosphorylation of a 92 kDa protein in suspended monocytes |
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