Activation of SH2-Containing Proteins by Insulin in Proliferating Mouse Parotid Gland Acinar Cells
Abstract Chronic treatment of mice with insulin results in hypertrophy and hyperplasia of the parotid and submandibular glands (Wang et al.: 1994, Proc Soc Exp Biol Med 205:353–361). Hyperplasia of the parotid gland is mediated by the elevation of tyrosine phosphorylation of phospholipase Cγ, p21ras...
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Veröffentlicht in: | Experimental biology and medicine (Maywood, N.J.) N.J.), 1994-12, Vol.207 (3), p.317-323 |
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creator | Wang, Pao-Li Purushotham, Karnam R. Humphreys-Beher, Michael G. |
description | Abstract
Chronic treatment of mice with insulin results in hypertrophy and hyperplasia of the parotid and submandibular glands (Wang et al.: 1994, Proc Soc Exp Biol Med 205:353–361). Hyperplasia of the parotid gland is mediated by the elevation of tyrosine phosphorylation of phospholipase Cγ, p21ras-GTPase activating protein (p21ras-GAP) and phosphatidylinositol 3-kinase. These proteins were found to be associated with the insulin receptor substrate-1 most likely through src homology (SH2) domains of these proteins. There was also a transient increase in intracellular cAMP and protein kinase A during the first day of treatment which declined by Day 3 to near control values. Protein kinase C activity, on the other hand, remained elevated for the 3-day injection regimen. Thus, acinar cell proliferation induced by insulin requires activation of many of the same signaling components as other tyrosine kinase possessing growth factor receptors. |
doi_str_mv | 10.3181/00379727-207-43822 |
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Chronic treatment of mice with insulin results in hypertrophy and hyperplasia of the parotid and submandibular glands (Wang et al.: 1994, Proc Soc Exp Biol Med 205:353–361). Hyperplasia of the parotid gland is mediated by the elevation of tyrosine phosphorylation of phospholipase Cγ, p21ras-GTPase activating protein (p21ras-GAP) and phosphatidylinositol 3-kinase. These proteins were found to be associated with the insulin receptor substrate-1 most likely through src homology (SH2) domains of these proteins. There was also a transient increase in intracellular cAMP and protein kinase A during the first day of treatment which declined by Day 3 to near control values. Protein kinase C activity, on the other hand, remained elevated for the 3-day injection regimen. Thus, acinar cell proliferation induced by insulin requires activation of many of the same signaling components as other tyrosine kinase possessing growth factor receptors.</description><identifier>ISSN: 0037-9727</identifier><identifier>ISSN: 1535-3702</identifier><identifier>EISSN: 1535-3699</identifier><identifier>DOI: 10.3181/00379727-207-43822</identifier><identifier>PMID: 7800688</identifier><language>eng</language><publisher>London, England: SAGE Publications</publisher><subject>Animals ; Cell Division ; Cyclic AMP - biosynthesis ; Cyclic AMP-Dependent Protein Kinases - biosynthesis ; GTPase-Activating Proteins ; Insulin - pharmacology ; Male ; Mice ; Mice, Inbred BALB C ; Parotid Gland - cytology ; Parotid Gland - drug effects ; Parotid Gland - metabolism ; Phosphatidylinositol 3-Kinases ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor) - metabolism ; Proteins - metabolism ; Type C Phospholipases - metabolism ; Tyrosine - metabolism</subject><ispartof>Experimental biology and medicine (Maywood, N.J.), 1994-12, Vol.207 (3), p.317-323</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c338t-79ff59bc2bd068e25ac7959fbeff364932f9d0598be157ab8b48543c0f3103ee3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7800688$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Pao-Li</creatorcontrib><creatorcontrib>Purushotham, Karnam R.</creatorcontrib><creatorcontrib>Humphreys-Beher, Michael G.</creatorcontrib><title>Activation of SH2-Containing Proteins by Insulin in Proliferating Mouse Parotid Gland Acinar Cells</title><title>Experimental biology and medicine (Maywood, N.J.)</title><addtitle>Proc Soc Exp Biol Med</addtitle><description>Abstract
Chronic treatment of mice with insulin results in hypertrophy and hyperplasia of the parotid and submandibular glands (Wang et al.: 1994, Proc Soc Exp Biol Med 205:353–361). Hyperplasia of the parotid gland is mediated by the elevation of tyrosine phosphorylation of phospholipase Cγ, p21ras-GTPase activating protein (p21ras-GAP) and phosphatidylinositol 3-kinase. These proteins were found to be associated with the insulin receptor substrate-1 most likely through src homology (SH2) domains of these proteins. There was also a transient increase in intracellular cAMP and protein kinase A during the first day of treatment which declined by Day 3 to near control values. Protein kinase C activity, on the other hand, remained elevated for the 3-day injection regimen. Thus, acinar cell proliferation induced by insulin requires activation of many of the same signaling components as other tyrosine kinase possessing growth factor receptors.</description><subject>Animals</subject><subject>Cell Division</subject><subject>Cyclic AMP - biosynthesis</subject><subject>Cyclic AMP-Dependent Protein Kinases - biosynthesis</subject><subject>GTPase-Activating Proteins</subject><subject>Insulin - pharmacology</subject><subject>Male</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Parotid Gland - cytology</subject><subject>Parotid Gland - drug effects</subject><subject>Parotid Gland - metabolism</subject><subject>Phosphatidylinositol 3-Kinases</subject><subject>Phosphorylation</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - metabolism</subject><subject>Proteins - metabolism</subject><subject>Type C Phospholipases - metabolism</subject><subject>Tyrosine - metabolism</subject><issn>0037-9727</issn><issn>1535-3702</issn><issn>1535-3699</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kFFLwzAUhYMoc07_gCDkybe4NGmb5HEU3QaKA_U5JG0yMrp0Jq2wf2_mpo9C4ELuOYdzPwBuM_xAM55NMaZMMMIQwQzllBNyBsZZQQtESyHOwfggQAfFJbiKcYNxVjBSjsCIcYxLzsdAz-refanedR52Fr4tCKo63yvnnV_DVeh643yEeg-XPg6t8zC99N06a0KyJdFLN0QDVyppXQPnrfINnNXOqwAr07bxGlxY1UZzc5oT8PH0-F4t0PPrfFnNnlFNKe8RE9YWQtdEN6maIYWqmSiE1cZaWuaCEisaXAiuTbpCaa5zXuS0xpZmmBpDJ-D-mLsL3edgYi-3LtapgfImVZSsFDihIElIjsI6dDEGY-UuuK0Ke5lheQArf8HKBFb-gE2mu1P6oLem-bOcSKb99LiPam3kphuCT8f-l_gNwMyBLg</recordid><startdate>19941201</startdate><enddate>19941201</enddate><creator>Wang, Pao-Li</creator><creator>Purushotham, Karnam R.</creator><creator>Humphreys-Beher, Michael G.</creator><general>SAGE Publications</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>7X8</scope></search><sort><creationdate>19941201</creationdate><title>Activation of SH2-Containing Proteins by Insulin in Proliferating Mouse Parotid Gland Acinar Cells</title><author>Wang, Pao-Li ; Purushotham, Karnam R. ; Humphreys-Beher, Michael G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c338t-79ff59bc2bd068e25ac7959fbeff364932f9d0598be157ab8b48543c0f3103ee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Cell Division</topic><topic>Cyclic AMP - biosynthesis</topic><topic>Cyclic AMP-Dependent Protein Kinases - biosynthesis</topic><topic>GTPase-Activating Proteins</topic><topic>Insulin - pharmacology</topic><topic>Male</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Parotid Gland - cytology</topic><topic>Parotid Gland - drug effects</topic><topic>Parotid Gland - metabolism</topic><topic>Phosphatidylinositol 3-Kinases</topic><topic>Phosphorylation</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - metabolism</topic><topic>Proteins - metabolism</topic><topic>Type C Phospholipases - metabolism</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Pao-Li</creatorcontrib><creatorcontrib>Purushotham, Karnam R.</creatorcontrib><creatorcontrib>Humphreys-Beher, Michael G.</creatorcontrib><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>Experimental biology and medicine (Maywood, N.J.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Pao-Li</au><au>Purushotham, Karnam R.</au><au>Humphreys-Beher, Michael G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of SH2-Containing Proteins by Insulin in Proliferating Mouse Parotid Gland Acinar Cells</atitle><jtitle>Experimental biology and medicine (Maywood, N.J.)</jtitle><addtitle>Proc Soc Exp Biol Med</addtitle><date>1994-12-01</date><risdate>1994</risdate><volume>207</volume><issue>3</issue><spage>317</spage><epage>323</epage><pages>317-323</pages><issn>0037-9727</issn><issn>1535-3702</issn><eissn>1535-3699</eissn><abstract>Abstract
Chronic treatment of mice with insulin results in hypertrophy and hyperplasia of the parotid and submandibular glands (Wang et al.: 1994, Proc Soc Exp Biol Med 205:353–361). Hyperplasia of the parotid gland is mediated by the elevation of tyrosine phosphorylation of phospholipase Cγ, p21ras-GTPase activating protein (p21ras-GAP) and phosphatidylinositol 3-kinase. These proteins were found to be associated with the insulin receptor substrate-1 most likely through src homology (SH2) domains of these proteins. There was also a transient increase in intracellular cAMP and protein kinase A during the first day of treatment which declined by Day 3 to near control values. Protein kinase C activity, on the other hand, remained elevated for the 3-day injection regimen. Thus, acinar cell proliferation induced by insulin requires activation of many of the same signaling components as other tyrosine kinase possessing growth factor receptors.</abstract><cop>London, England</cop><pub>SAGE Publications</pub><pmid>7800688</pmid><doi>10.3181/00379727-207-43822</doi><tpages>7</tpages></addata></record> |
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subjects | Animals Cell Division Cyclic AMP - biosynthesis Cyclic AMP-Dependent Protein Kinases - biosynthesis GTPase-Activating Proteins Insulin - pharmacology Male Mice Mice, Inbred BALB C Parotid Gland - cytology Parotid Gland - drug effects Parotid Gland - metabolism Phosphatidylinositol 3-Kinases Phosphorylation Phosphotransferases (Alcohol Group Acceptor) - metabolism Proteins - metabolism Type C Phospholipases - metabolism Tyrosine - metabolism |
title | Activation of SH2-Containing Proteins by Insulin in Proliferating Mouse Parotid Gland Acinar Cells |
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