Phosphorylation control by insulin in adipocytes is interfered with at a post-receptor step by phosphoinositol and glucosamine
Inositol-phosphates, glucosamine and glucose-6-phosphate blocked the effects of insulin on target protein phosphorylation in adipocytes, but the unsubstituted or sulphated derivatives of inositol or of glucose, or N-acetyl-glucosamine were without effect. The insulin stimulated tyrosine phosphorylat...
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| Veröffentlicht in: | FEBS letters 1990-07, Vol.268 (1), p.169-172 |
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| creator | Strålfors, Peter Alemany, Susana |
| description | Inositol-phosphates, glucosamine and glucose-6-phosphate blocked the effects of insulin on target protein phosphorylation in adipocytes, but the unsubstituted or sulphated derivatives of inositol or of glucose, or
N-acetyl-glucosamine were without effect. The insulin stimulated tyrosine phosphorylation of the insulin receptor was not affected. The sugar-phospates inositol-phosphate and glucose-6-phosphate did not enter into the cells. They also blocked the insulin-like effects of a potential second messenger of insulin, a phosphooligosaccharide (POS), which has previously been shown to mimick the effects of insulin on protein phosphorylation in intact cells. |
| doi_str_mv | 10.1016/0014-5793(90)81000-E |
| format | Article |
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N-acetyl-glucosamine were without effect. The insulin stimulated tyrosine phosphorylation of the insulin receptor was not affected. The sugar-phospates inositol-phosphate and glucose-6-phosphate did not enter into the cells. They also blocked the insulin-like effects of a potential second messenger of insulin, a phosphooligosaccharide (POS), which has previously been shown to mimick the effects of insulin on protein phosphorylation in intact cells.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(90)81000-E</identifier><identifier>PMID: 1696549</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Adipocyte ; adipocytes ; Adipose Tissue - metabolism ; Animals ; Biological and medical sciences ; Cell physiology ; Fundamental and applied biological sciences. Psychology ; Glucosamine ; Glucosamine - pharmacology ; Hormonal regulation ; In Vitro Techniques ; Inositol Phosphates - pharmacology ; Insulin ; Insulin - physiology ; Insulin receptor ; Male ; Molecular and cellular biology ; Oligosaccharides - pharmacology ; Phosphoinositol ; Phosphorylation ; Phosphotyrosine ; Protein phosphorylation ; Rats ; Receptor, Insulin - metabolism ; Sugar Phosphates - pharmacology ; Tyrosine - analogs & derivatives ; Tyrosine - metabolism</subject><ispartof>FEBS letters, 1990-07, Vol.268 (1), p.169-172</ispartof><rights>1990</rights><rights>FEBS Letters 268 (1990) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c396E-784558a832be5a40fcdcb962d673dfdbe6e40628fe4657a01a42b38aa4a3e41c3</citedby><cites>FETCH-LOGICAL-c396E-784558a832be5a40fcdcb962d673dfdbe6e40628fe4657a01a42b38aa4a3e41c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/001457939081000E$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19794019$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1696549$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Strålfors, Peter</creatorcontrib><creatorcontrib>Alemany, Susana</creatorcontrib><title>Phosphorylation control by insulin in adipocytes is interfered with at a post-receptor step by phosphoinositol and glucosamine</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Inositol-phosphates, glucosamine and glucose-6-phosphate blocked the effects of insulin on target protein phosphorylation in adipocytes, but the unsubstituted or sulphated derivatives of inositol or of glucose, or
N-acetyl-glucosamine were without effect. The insulin stimulated tyrosine phosphorylation of the insulin receptor was not affected. The sugar-phospates inositol-phosphate and glucose-6-phosphate did not enter into the cells. They also blocked the insulin-like effects of a potential second messenger of insulin, a phosphooligosaccharide (POS), which has previously been shown to mimick the effects of insulin on protein phosphorylation in intact cells.</description><subject>Adipocyte</subject><subject>adipocytes</subject><subject>Adipose Tissue - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell physiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glucosamine</subject><subject>Glucosamine - pharmacology</subject><subject>Hormonal regulation</subject><subject>In Vitro Techniques</subject><subject>Inositol Phosphates - pharmacology</subject><subject>Insulin</subject><subject>Insulin - physiology</subject><subject>Insulin receptor</subject><subject>Male</subject><subject>Molecular and cellular biology</subject><subject>Oligosaccharides - pharmacology</subject><subject>Phosphoinositol</subject><subject>Phosphorylation</subject><subject>Phosphotyrosine</subject><subject>Protein phosphorylation</subject><subject>Rats</subject><subject>Receptor, Insulin - metabolism</subject><subject>Sugar Phosphates - pharmacology</subject><subject>Tyrosine - analogs & derivatives</subject><subject>Tyrosine - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUGL1TAUhYso43P0Hyhko4yLatKkabIZ0KFPhQFd6Dqkya0v0pfUJHXoxt8-7fTh7FQIXLj3uyfJOUXxnOA3BBP-FmPCyrqR9ELi14JgjMv2QbEjoqElZVw8LHZ_kMfFk5R-LAgRRJ4VZ4RLXjO5K35_OYQ0HkKcB51d8MgEn2MYUDcj59M0OL9UpK0bg5kzJOSW4zPEHiJYdOPyAemMNBpDymUEA2MOEaUM46oxbvLOh-TyIqu9Rd-HyYSkj87D0-JRr4cEz071vPi2b79efSyvP3_4dPXuujRU8rZsBKtroQWtOqg1w72xppO8sryhtrcdcGCYV6IHxutGY6JZ1VGhNdMUGDH0vHi16Y4x_JwgZXV0ycAwaA9hSqqRkhIs6D9BUjeLwWwF2QaaGFKK0KsxuqOOsyJYrfmo1Xy1mq8kVnf5qHZZe3HSn7oj2PulLZBl_vI018nooY_aG5fuMdlIhsnK7Tfuxg0w_9fdat--r9bB2pf4rrs-6HITgsX-Xw6iSsaBN2DdEmZWNri__-gWKK3CWg</recordid><startdate>19900730</startdate><enddate>19900730</enddate><creator>Strålfors, Peter</creator><creator>Alemany, Susana</creator><general>Elsevier B.V</general><general>Elsevier</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>19900730</creationdate><title>Phosphorylation control by insulin in adipocytes is interfered with at a post-receptor step by phosphoinositol and glucosamine</title><author>Strålfors, Peter ; Alemany, Susana</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c396E-784558a832be5a40fcdcb962d673dfdbe6e40628fe4657a01a42b38aa4a3e41c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Adipocyte</topic><topic>adipocytes</topic><topic>Adipose Tissue - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell physiology</topic><topic>Fundamental and applied biological sciences. 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N-acetyl-glucosamine were without effect. The insulin stimulated tyrosine phosphorylation of the insulin receptor was not affected. The sugar-phospates inositol-phosphate and glucose-6-phosphate did not enter into the cells. They also blocked the insulin-like effects of a potential second messenger of insulin, a phosphooligosaccharide (POS), which has previously been shown to mimick the effects of insulin on protein phosphorylation in intact cells.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>1696549</pmid><doi>10.1016/0014-5793(90)81000-E</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Adipocyte adipocytes Adipose Tissue - metabolism Animals Biological and medical sciences Cell physiology Fundamental and applied biological sciences. Psychology Glucosamine Glucosamine - pharmacology Hormonal regulation In Vitro Techniques Inositol Phosphates - pharmacology Insulin Insulin - physiology Insulin receptor Male Molecular and cellular biology Oligosaccharides - pharmacology Phosphoinositol Phosphorylation Phosphotyrosine Protein phosphorylation Rats Receptor, Insulin - metabolism Sugar Phosphates - pharmacology Tyrosine - analogs & derivatives Tyrosine - metabolism |
| title | Phosphorylation control by insulin in adipocytes is interfered with at a post-receptor step by phosphoinositol and glucosamine |
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