Interaction of Btk and Akt in B cell signaling

Reactive oxygen species (ROS) or reactive oxygen intermediates (ROIs) mediate complex signaling involving multiple pathways. In this report, we demonstrate for the first time that endogenous Bruton's tyrosine kinase (Btk) and Akt can interact with each other in DT40 chicken B cells and human Na...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biochemical and biophysical research communications 2002-05, Vol.293 (5), p.1319-1326
Hauptverfasser: Lindvall, Jessica, Islam, Tahmina C
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 1326
container_issue 5
container_start_page 1319
container_title Biochemical and biophysical research communications
container_volume 293
creator Lindvall, Jessica
Islam, Tahmina C
description Reactive oxygen species (ROS) or reactive oxygen intermediates (ROIs) mediate complex signaling involving multiple pathways. In this report, we demonstrate for the first time that endogenous Bruton's tyrosine kinase (Btk) and Akt can interact with each other in DT40 chicken B cells and human Nalm6 B cells and that this interaction is inducible following H 2O 2 stimulation. This interaction is supported by visualizing the co-localization of Btk and Akt in the perinuclear region and membrane ruffles in COS-7 cells. We have also shown the involvement of phosphatidylinositol 3-kinase (PI 3-K) and Btk in the phosphorylation of Akt following stimulation by hydrogen peroxide (H 2O 2). Interestingly, Akt phosphorylation was found in the presence of Btk even in the absence of oxidative stress. In addition, we have investigated the involvement of PI 3-K in the MAPKs and ERK and JNK phosphorylation, in the presence or absence of Btk. Phosphorylation of both ERK and JNK increased when the PI 3-K pathway was inhibited and both pathways were modulated positively by Btk. Taken together, based on the study of endogenous conditions, we show the novel interaction of Btk and Akt in H 2O 2 signaling in B cells.
doi_str_mv 10.1016/S0006-291X(02)00382-0
format Article
fullrecord <record><control><sourceid>proquest_swepu</sourceid><recordid>TN_cdi_swepub_primary_oai_swepub_ki_se_593788</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X02003820</els_id><sourcerecordid>19724824</sourcerecordid><originalsourceid>FETCH-LOGICAL-c545t-44ae307922486a7b3eee1f7c1255d73cf08210f0fa062d568085a5276bb1933d3</originalsourceid><addsrcrecordid>eNqFkU9P20AQxVcVqATaj1DkEyoHw8z-96kCRAtSJA60Um-r9XqMliR26nWo-PbdkDScEKcdrX5v3sw8xr4gnCGgPr8HAF3yCn9_BX4KICwv4QObIFRQcgS5xyY75IAdpvQIgCh19ZEdIAcltTITdnbbjTT4MMa-K_q2uBxnhe-a4mI2FrErLotA83mR4kPn57F7-MT2Wz9P9Hn7HrFf369_Xt2U07sft1cX0zIoqcZSSk8CTMW5tNqbWhARtiYgV6oxIrRg84gttB40b5S2YJVX3Oi6xkqIRhyxctM3_aXlqnbLIS788Ox6H932a5YrcqoSxtrM2zf55dA3r6L_QrSi4qh5lp5spJn7s6I0ukVM6619R_0qOYMWpJTwLoiVyetymUG1AcPQpzRQuxsHwa3Dcy_huXUyDrh7Cc-tDY63Bqt6Qc2raptWBr5tAMqnf4o0uBQidYGaOFAYXdPHdyz-AW4pp3g</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19724824</pqid></control><display><type>article</type><title>Interaction of Btk and Akt in B cell signaling</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Lindvall, Jessica ; Islam, Tahmina C</creator><creatorcontrib>Lindvall, Jessica ; Islam, Tahmina C</creatorcontrib><description>Reactive oxygen species (ROS) or reactive oxygen intermediates (ROIs) mediate complex signaling involving multiple pathways. In this report, we demonstrate for the first time that endogenous Bruton's tyrosine kinase (Btk) and Akt can interact with each other in DT40 chicken B cells and human Nalm6 B cells and that this interaction is inducible following H 2O 2 stimulation. This interaction is supported by visualizing the co-localization of Btk and Akt in the perinuclear region and membrane ruffles in COS-7 cells. We have also shown the involvement of phosphatidylinositol 3-kinase (PI 3-K) and Btk in the phosphorylation of Akt following stimulation by hydrogen peroxide (H 2O 2). Interestingly, Akt phosphorylation was found in the presence of Btk even in the absence of oxidative stress. In addition, we have investigated the involvement of PI 3-K in the MAPKs and ERK and JNK phosphorylation, in the presence or absence of Btk. Phosphorylation of both ERK and JNK increased when the PI 3-K pathway was inhibited and both pathways were modulated positively by Btk. Taken together, based on the study of endogenous conditions, we show the novel interaction of Btk and Akt in H 2O 2 signaling in B cells.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(02)00382-0</identifier><identifier>PMID: 12054657</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Akt ; Animals ; B cells ; B-Lymphocytes - metabolism ; Btk ; Cell Line ; Chickens ; COS Cells ; Dose-Response Relationship, Drug ; Enzyme Inhibitors - pharmacology ; Hydrogen peroxide ; Hydrogen Peroxide - pharmacology ; Immunoblotting ; Medicin och hälsovetenskap ; Microscopy, Fluorescence ; Oxidative Stress ; Oxygen - metabolism ; Phosphatidylinositol 3-Kinases - metabolism ; Phosphorylation ; PI 3-K ; Precipitin Tests ; Protein Binding ; Protein-Serine-Threonine Kinases ; Protein-Tyrosine Kinases - metabolism ; Proto-Oncogene Proteins - metabolism ; Proto-Oncogene Proteins c-akt ; Signal Transduction ; Time Factors ; Transfection</subject><ispartof>Biochemical and biophysical research communications, 2002-05, Vol.293 (5), p.1319-1326</ispartof><rights>2002 Elsevier Science (USA)</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c545t-44ae307922486a7b3eee1f7c1255d73cf08210f0fa062d568085a5276bb1933d3</citedby><cites>FETCH-LOGICAL-c545t-44ae307922486a7b3eee1f7c1255d73cf08210f0fa062d568085a5276bb1933d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-291X(02)00382-0$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12054657$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:18392162$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Lindvall, Jessica</creatorcontrib><creatorcontrib>Islam, Tahmina C</creatorcontrib><title>Interaction of Btk and Akt in B cell signaling</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Reactive oxygen species (ROS) or reactive oxygen intermediates (ROIs) mediate complex signaling involving multiple pathways. In this report, we demonstrate for the first time that endogenous Bruton's tyrosine kinase (Btk) and Akt can interact with each other in DT40 chicken B cells and human Nalm6 B cells and that this interaction is inducible following H 2O 2 stimulation. This interaction is supported by visualizing the co-localization of Btk and Akt in the perinuclear region and membrane ruffles in COS-7 cells. We have also shown the involvement of phosphatidylinositol 3-kinase (PI 3-K) and Btk in the phosphorylation of Akt following stimulation by hydrogen peroxide (H 2O 2). Interestingly, Akt phosphorylation was found in the presence of Btk even in the absence of oxidative stress. In addition, we have investigated the involvement of PI 3-K in the MAPKs and ERK and JNK phosphorylation, in the presence or absence of Btk. Phosphorylation of both ERK and JNK increased when the PI 3-K pathway was inhibited and both pathways were modulated positively by Btk. Taken together, based on the study of endogenous conditions, we show the novel interaction of Btk and Akt in H 2O 2 signaling in B cells.</description><subject>Akt</subject><subject>Animals</subject><subject>B cells</subject><subject>B-Lymphocytes - metabolism</subject><subject>Btk</subject><subject>Cell Line</subject><subject>Chickens</subject><subject>COS Cells</subject><subject>Dose-Response Relationship, Drug</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Hydrogen peroxide</subject><subject>Hydrogen Peroxide - pharmacology</subject><subject>Immunoblotting</subject><subject>Medicin och hälsovetenskap</subject><subject>Microscopy, Fluorescence</subject><subject>Oxidative Stress</subject><subject>Oxygen - metabolism</subject><subject>Phosphatidylinositol 3-Kinases - metabolism</subject><subject>Phosphorylation</subject><subject>PI 3-K</subject><subject>Precipitin Tests</subject><subject>Protein Binding</subject><subject>Protein-Serine-Threonine Kinases</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Proto-Oncogene Proteins - metabolism</subject><subject>Proto-Oncogene Proteins c-akt</subject><subject>Signal Transduction</subject><subject>Time Factors</subject><subject>Transfection</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9P20AQxVcVqATaj1DkEyoHw8z-96kCRAtSJA60Um-r9XqMliR26nWo-PbdkDScEKcdrX5v3sw8xr4gnCGgPr8HAF3yCn9_BX4KICwv4QObIFRQcgS5xyY75IAdpvQIgCh19ZEdIAcltTITdnbbjTT4MMa-K_q2uBxnhe-a4mI2FrErLotA83mR4kPn57F7-MT2Wz9P9Hn7HrFf369_Xt2U07sft1cX0zIoqcZSSk8CTMW5tNqbWhARtiYgV6oxIrRg84gttB40b5S2YJVX3Oi6xkqIRhyxctM3_aXlqnbLIS788Ox6H932a5YrcqoSxtrM2zf55dA3r6L_QrSi4qh5lp5spJn7s6I0ukVM6619R_0qOYMWpJTwLoiVyetymUG1AcPQpzRQuxsHwa3Dcy_huXUyDrh7Cc-tDY63Bqt6Qc2raptWBr5tAMqnf4o0uBQidYGaOFAYXdPHdyz-AW4pp3g</recordid><startdate>20020524</startdate><enddate>20020524</enddate><creator>Lindvall, Jessica</creator><creator>Islam, Tahmina C</creator><general>Elsevier Inc</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>7T5</scope><scope>H94</scope><scope>7X8</scope><scope>ADTPV</scope><scope>AOWAS</scope></search><sort><creationdate>20020524</creationdate><title>Interaction of Btk and Akt in B cell signaling</title><author>Lindvall, Jessica ; Islam, Tahmina C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c545t-44ae307922486a7b3eee1f7c1255d73cf08210f0fa062d568085a5276bb1933d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Akt</topic><topic>Animals</topic><topic>B cells</topic><topic>B-Lymphocytes - metabolism</topic><topic>Btk</topic><topic>Cell Line</topic><topic>Chickens</topic><topic>COS Cells</topic><topic>Dose-Response Relationship, Drug</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Hydrogen peroxide</topic><topic>Hydrogen Peroxide - pharmacology</topic><topic>Immunoblotting</topic><topic>Medicin och hälsovetenskap</topic><topic>Microscopy, Fluorescence</topic><topic>Oxidative Stress</topic><topic>Oxygen - metabolism</topic><topic>Phosphatidylinositol 3-Kinases - metabolism</topic><topic>Phosphorylation</topic><topic>PI 3-K</topic><topic>Precipitin Tests</topic><topic>Protein Binding</topic><topic>Protein-Serine-Threonine Kinases</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Proto-Oncogene Proteins - metabolism</topic><topic>Proto-Oncogene Proteins c-akt</topic><topic>Signal Transduction</topic><topic>Time Factors</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lindvall, Jessica</creatorcontrib><creatorcontrib>Islam, Tahmina C</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>SwePub</collection><collection>SwePub Articles</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lindvall, Jessica</au><au>Islam, Tahmina C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of Btk and Akt in B cell signaling</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2002-05-24</date><risdate>2002</risdate><volume>293</volume><issue>5</issue><spage>1319</spage><epage>1326</epage><pages>1319-1326</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Reactive oxygen species (ROS) or reactive oxygen intermediates (ROIs) mediate complex signaling involving multiple pathways. In this report, we demonstrate for the first time that endogenous Bruton's tyrosine kinase (Btk) and Akt can interact with each other in DT40 chicken B cells and human Nalm6 B cells and that this interaction is inducible following H 2O 2 stimulation. This interaction is supported by visualizing the co-localization of Btk and Akt in the perinuclear region and membrane ruffles in COS-7 cells. We have also shown the involvement of phosphatidylinositol 3-kinase (PI 3-K) and Btk in the phosphorylation of Akt following stimulation by hydrogen peroxide (H 2O 2). Interestingly, Akt phosphorylation was found in the presence of Btk even in the absence of oxidative stress. In addition, we have investigated the involvement of PI 3-K in the MAPKs and ERK and JNK phosphorylation, in the presence or absence of Btk. Phosphorylation of both ERK and JNK increased when the PI 3-K pathway was inhibited and both pathways were modulated positively by Btk. Taken together, based on the study of endogenous conditions, we show the novel interaction of Btk and Akt in H 2O 2 signaling in B cells.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12054657</pmid><doi>10.1016/S0006-291X(02)00382-0</doi><tpages>8</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-291X
ispartof Biochemical and biophysical research communications, 2002-05, Vol.293 (5), p.1319-1326
issn 0006-291X
1090-2104
language eng
recordid cdi_swepub_primary_oai_swepub_ki_se_593788
source MEDLINE; Elsevier ScienceDirect Journals Complete
subjects Akt
Animals
B cells
B-Lymphocytes - metabolism
Btk
Cell Line
Chickens
COS Cells
Dose-Response Relationship, Drug
Enzyme Inhibitors - pharmacology
Hydrogen peroxide
Hydrogen Peroxide - pharmacology
Immunoblotting
Medicin och hälsovetenskap
Microscopy, Fluorescence
Oxidative Stress
Oxygen - metabolism
Phosphatidylinositol 3-Kinases - metabolism
Phosphorylation
PI 3-K
Precipitin Tests
Protein Binding
Protein-Serine-Threonine Kinases
Protein-Tyrosine Kinases - metabolism
Proto-Oncogene Proteins - metabolism
Proto-Oncogene Proteins c-akt
Signal Transduction
Time Factors
Transfection
title Interaction of Btk and Akt in B cell signaling
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T07%3A22%3A55IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_swepu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Interaction%20of%20Btk%20and%20Akt%20in%20B%20cell%20signaling&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Lindvall,%20Jessica&rft.date=2002-05-24&rft.volume=293&rft.issue=5&rft.spage=1319&rft.epage=1326&rft.pages=1319-1326&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/S0006-291X(02)00382-0&rft_dat=%3Cproquest_swepu%3E19724824%3C/proquest_swepu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=19724824&rft_id=info:pmid/12054657&rft_els_id=S0006291X02003820&rfr_iscdi=true