Loading…

AMP-Activated protein kinase is activated by the stimulations of G(q)-coupled receptors

The AMP-activated protein kinase (AMPK) functions as a metabolic sensor that monitors cellular AMP and ATP levels. Platelet-activating factor (PAF) activates endogeneous AMPKalpha1 in Chinese hamster ovary cells expressing the PAF receptor coupled with both G(i) and G(q), but its activity was not in...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical and biophysical research communications 2000-09, Vol.276 (1), p.16-22
Main Authors: Kishi, K, Yuasa, T, Minami, A, Yamada, M, Hagi, A, Hayashi, H, Kemp, B E, Witters, L A, Ebina, Y
Format: Article
Language:English
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page 22
container_issue 1
container_start_page 16
container_title Biochemical and biophysical research communications
container_volume 276
creator Kishi, K
Yuasa, T
Minami, A
Yamada, M
Hagi, A
Hayashi, H
Kemp, B E
Witters, L A
Ebina, Y
description The AMP-activated protein kinase (AMPK) functions as a metabolic sensor that monitors cellular AMP and ATP levels. Platelet-activating factor (PAF) activates endogeneous AMPKalpha1 in Chinese hamster ovary cells expressing the PAF receptor coupled with both G(i) and G(q), but its activity was not inhibited after treatment with islet-activating protein. Norepinephrine and bradykinin also activated AMPKalpha1 in cells expressing the G(q)-coupled alpha(1b)-adrenergic receptor and bradykinin receptor, respectively. Stimulations of the G(i)-coupled alpha(2A)-adrenergic receptor, fMet-Leu-Phe receptor, prostaglandin EP3alpha receptor, and G(s)-coupled beta(2)-adrenergic receptor did not activate AMPKalpha1. AMPKalpha1 thus is activated specifically by stimulation of G(q)-coupled receptors. G(q)-coupled receptors transmit the signal for GLUT4 translocation and glucose uptake through an insulin-independent pathway. However, direct activation of AMPKalpha1 with treatment of 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside did not trigger GLUT4 translocation nor stimulate glucose uptake in our cells. Thus, activation of AMPKalpha1 via G(q) is not sufficient to trigger GLUT4 translocation or stimulate glucose uptake.
doi_str_mv 10.1006/bbrc.2000.3417
format article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_72293576</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>72293576</sourcerecordid><originalsourceid>FETCH-LOGICAL-p207t-e2180dc02f081b5cf7ef6deb4314d01591c471fae62b5fcabaaec2b3b1cc6a983</originalsourceid><addsrcrecordid>eNo9kM1LAzEUxHNQbK1ePUpOooet72U_0j2WolWo6EHR25JkXzC6X91khf73rlg9zcD8GIZh7AxhjgDZtda9mQsAmMcJygM2HW0WiRzfJuzY-w8AxCTLj9gEf3iQ6ZS9Lh-eoqUJ7ksFKnnXt4Fcwz9dozxx57n6z_SOh3fiPrh6qFRwbeN5a_n6cnsVmXboqpHpyVAX2t6fsEOrKk-ne52xl9ub59VdtHlc36-Wm6gTIENEAhdQGhAWFqhTYyXZrCSdxJiUgGmOJpFoFWVCp9YorRQZoWONxmQqX8QzdvHbOy7fDuRDUTtvqKpUQ-3gCylEHqcyG8HzPTjomsqi612t-l3xd0X8DQVRX-o</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>72293576</pqid></control><display><type>article</type><title>AMP-Activated protein kinase is activated by the stimulations of G(q)-coupled receptors</title><source>ScienceDirect Freedom Collection 2022-2024</source><creator>Kishi, K ; Yuasa, T ; Minami, A ; Yamada, M ; Hagi, A ; Hayashi, H ; Kemp, B E ; Witters, L A ; Ebina, Y</creator><creatorcontrib>Kishi, K ; Yuasa, T ; Minami, A ; Yamada, M ; Hagi, A ; Hayashi, H ; Kemp, B E ; Witters, L A ; Ebina, Y</creatorcontrib><description>The AMP-activated protein kinase (AMPK) functions as a metabolic sensor that monitors cellular AMP and ATP levels. Platelet-activating factor (PAF) activates endogeneous AMPKalpha1 in Chinese hamster ovary cells expressing the PAF receptor coupled with both G(i) and G(q), but its activity was not inhibited after treatment with islet-activating protein. Norepinephrine and bradykinin also activated AMPKalpha1 in cells expressing the G(q)-coupled alpha(1b)-adrenergic receptor and bradykinin receptor, respectively. Stimulations of the G(i)-coupled alpha(2A)-adrenergic receptor, fMet-Leu-Phe receptor, prostaglandin EP3alpha receptor, and G(s)-coupled beta(2)-adrenergic receptor did not activate AMPKalpha1. AMPKalpha1 thus is activated specifically by stimulation of G(q)-coupled receptors. G(q)-coupled receptors transmit the signal for GLUT4 translocation and glucose uptake through an insulin-independent pathway. However, direct activation of AMPKalpha1 with treatment of 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside did not trigger GLUT4 translocation nor stimulate glucose uptake in our cells. Thus, activation of AMPKalpha1 via G(q) is not sufficient to trigger GLUT4 translocation or stimulate glucose uptake.</description><identifier>ISSN: 0006-291X</identifier><identifier>DOI: 10.1006/bbrc.2000.3417</identifier><identifier>PMID: 11006075</identifier><language>eng</language><publisher>United States</publisher><subject>AMP-Activated Protein Kinases ; Animals ; Biological Transport ; CHO Cells ; Cricetinae ; Enzyme Activation ; Glucose - metabolism ; Glucose Transporter Type 4 ; GTP-Binding Protein alpha Subunits, Gq-G11 ; Heterotrimeric GTP-Binding Proteins - metabolism ; Monosaccharide Transport Proteins - metabolism ; Multienzyme Complexes - metabolism ; Muscle Proteins ; Protein-Serine-Threonine Kinases - metabolism ; Receptors, Adrenergic, alpha-1 - metabolism ; Receptors, Bradykinin - metabolism ; Signal Transduction</subject><ispartof>Biochemical and biophysical research communications, 2000-09, Vol.276 (1), p.16-22</ispartof><rights>Copyright 2000 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11006075$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kishi, K</creatorcontrib><creatorcontrib>Yuasa, T</creatorcontrib><creatorcontrib>Minami, A</creatorcontrib><creatorcontrib>Yamada, M</creatorcontrib><creatorcontrib>Hagi, A</creatorcontrib><creatorcontrib>Hayashi, H</creatorcontrib><creatorcontrib>Kemp, B E</creatorcontrib><creatorcontrib>Witters, L A</creatorcontrib><creatorcontrib>Ebina, Y</creatorcontrib><title>AMP-Activated protein kinase is activated by the stimulations of G(q)-coupled receptors</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The AMP-activated protein kinase (AMPK) functions as a metabolic sensor that monitors cellular AMP and ATP levels. Platelet-activating factor (PAF) activates endogeneous AMPKalpha1 in Chinese hamster ovary cells expressing the PAF receptor coupled with both G(i) and G(q), but its activity was not inhibited after treatment with islet-activating protein. Norepinephrine and bradykinin also activated AMPKalpha1 in cells expressing the G(q)-coupled alpha(1b)-adrenergic receptor and bradykinin receptor, respectively. Stimulations of the G(i)-coupled alpha(2A)-adrenergic receptor, fMet-Leu-Phe receptor, prostaglandin EP3alpha receptor, and G(s)-coupled beta(2)-adrenergic receptor did not activate AMPKalpha1. AMPKalpha1 thus is activated specifically by stimulation of G(q)-coupled receptors. G(q)-coupled receptors transmit the signal for GLUT4 translocation and glucose uptake through an insulin-independent pathway. However, direct activation of AMPKalpha1 with treatment of 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside did not trigger GLUT4 translocation nor stimulate glucose uptake in our cells. Thus, activation of AMPKalpha1 via G(q) is not sufficient to trigger GLUT4 translocation or stimulate glucose uptake.</description><subject>AMP-Activated Protein Kinases</subject><subject>Animals</subject><subject>Biological Transport</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Enzyme Activation</subject><subject>Glucose - metabolism</subject><subject>Glucose Transporter Type 4</subject><subject>GTP-Binding Protein alpha Subunits, Gq-G11</subject><subject>Heterotrimeric GTP-Binding Proteins - metabolism</subject><subject>Monosaccharide Transport Proteins - metabolism</subject><subject>Multienzyme Complexes - metabolism</subject><subject>Muscle Proteins</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Receptors, Adrenergic, alpha-1 - metabolism</subject><subject>Receptors, Bradykinin - metabolism</subject><subject>Signal Transduction</subject><issn>0006-291X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNo9kM1LAzEUxHNQbK1ePUpOooet72U_0j2WolWo6EHR25JkXzC6X91khf73rlg9zcD8GIZh7AxhjgDZtda9mQsAmMcJygM2HW0WiRzfJuzY-w8AxCTLj9gEf3iQ6ZS9Lh-eoqUJ7ksFKnnXt4Fcwz9dozxx57n6z_SOh3fiPrh6qFRwbeN5a_n6cnsVmXboqpHpyVAX2t6fsEOrKk-ne52xl9ub59VdtHlc36-Wm6gTIENEAhdQGhAWFqhTYyXZrCSdxJiUgGmOJpFoFWVCp9YorRQZoWONxmQqX8QzdvHbOy7fDuRDUTtvqKpUQ-3gCylEHqcyG8HzPTjomsqi612t-l3xd0X8DQVRX-o</recordid><startdate>20000916</startdate><enddate>20000916</enddate><creator>Kishi, K</creator><creator>Yuasa, T</creator><creator>Minami, A</creator><creator>Yamada, M</creator><creator>Hagi, A</creator><creator>Hayashi, H</creator><creator>Kemp, B E</creator><creator>Witters, L A</creator><creator>Ebina, Y</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20000916</creationdate><title>AMP-Activated protein kinase is activated by the stimulations of G(q)-coupled receptors</title><author>Kishi, K ; Yuasa, T ; Minami, A ; Yamada, M ; Hagi, A ; Hayashi, H ; Kemp, B E ; Witters, L A ; Ebina, Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p207t-e2180dc02f081b5cf7ef6deb4314d01591c471fae62b5fcabaaec2b3b1cc6a983</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>AMP-Activated Protein Kinases</topic><topic>Animals</topic><topic>Biological Transport</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Enzyme Activation</topic><topic>Glucose - metabolism</topic><topic>Glucose Transporter Type 4</topic><topic>GTP-Binding Protein alpha Subunits, Gq-G11</topic><topic>Heterotrimeric GTP-Binding Proteins - metabolism</topic><topic>Monosaccharide Transport Proteins - metabolism</topic><topic>Multienzyme Complexes - metabolism</topic><topic>Muscle Proteins</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Receptors, Adrenergic, alpha-1 - metabolism</topic><topic>Receptors, Bradykinin - metabolism</topic><topic>Signal Transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kishi, K</creatorcontrib><creatorcontrib>Yuasa, T</creatorcontrib><creatorcontrib>Minami, A</creatorcontrib><creatorcontrib>Yamada, M</creatorcontrib><creatorcontrib>Hagi, A</creatorcontrib><creatorcontrib>Hayashi, H</creatorcontrib><creatorcontrib>Kemp, B E</creatorcontrib><creatorcontrib>Witters, L A</creatorcontrib><creatorcontrib>Ebina, Y</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kishi, K</au><au>Yuasa, T</au><au>Minami, A</au><au>Yamada, M</au><au>Hagi, A</au><au>Hayashi, H</au><au>Kemp, B E</au><au>Witters, L A</au><au>Ebina, Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>AMP-Activated protein kinase is activated by the stimulations of G(q)-coupled receptors</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2000-09-16</date><risdate>2000</risdate><volume>276</volume><issue>1</issue><spage>16</spage><epage>22</epage><pages>16-22</pages><issn>0006-291X</issn><abstract>The AMP-activated protein kinase (AMPK) functions as a metabolic sensor that monitors cellular AMP and ATP levels. Platelet-activating factor (PAF) activates endogeneous AMPKalpha1 in Chinese hamster ovary cells expressing the PAF receptor coupled with both G(i) and G(q), but its activity was not inhibited after treatment with islet-activating protein. Norepinephrine and bradykinin also activated AMPKalpha1 in cells expressing the G(q)-coupled alpha(1b)-adrenergic receptor and bradykinin receptor, respectively. Stimulations of the G(i)-coupled alpha(2A)-adrenergic receptor, fMet-Leu-Phe receptor, prostaglandin EP3alpha receptor, and G(s)-coupled beta(2)-adrenergic receptor did not activate AMPKalpha1. AMPKalpha1 thus is activated specifically by stimulation of G(q)-coupled receptors. G(q)-coupled receptors transmit the signal for GLUT4 translocation and glucose uptake through an insulin-independent pathway. However, direct activation of AMPKalpha1 with treatment of 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside did not trigger GLUT4 translocation nor stimulate glucose uptake in our cells. Thus, activation of AMPKalpha1 via G(q) is not sufficient to trigger GLUT4 translocation or stimulate glucose uptake.</abstract><cop>United States</cop><pmid>11006075</pmid><doi>10.1006/bbrc.2000.3417</doi><tpages>7</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-291X
ispartof Biochemical and biophysical research communications, 2000-09, Vol.276 (1), p.16-22
issn 0006-291X
language eng
recordid cdi_proquest_miscellaneous_72293576
source ScienceDirect Freedom Collection 2022-2024
subjects AMP-Activated Protein Kinases
Animals
Biological Transport
CHO Cells
Cricetinae
Enzyme Activation
Glucose - metabolism
Glucose Transporter Type 4
GTP-Binding Protein alpha Subunits, Gq-G11
Heterotrimeric GTP-Binding Proteins - metabolism
Monosaccharide Transport Proteins - metabolism
Multienzyme Complexes - metabolism
Muscle Proteins
Protein-Serine-Threonine Kinases - metabolism
Receptors, Adrenergic, alpha-1 - metabolism
Receptors, Bradykinin - metabolism
Signal Transduction
title AMP-Activated protein kinase is activated by the stimulations of G(q)-coupled receptors
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T23%3A28%3A08IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=AMP-Activated%20protein%20kinase%20is%20activated%20by%20the%20stimulations%20of%20G(q)-coupled%20receptors&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Kishi,%20K&rft.date=2000-09-16&rft.volume=276&rft.issue=1&rft.spage=16&rft.epage=22&rft.pages=16-22&rft.issn=0006-291X&rft_id=info:doi/10.1006/bbrc.2000.3417&rft_dat=%3Cproquest_pubme%3E72293576%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-p207t-e2180dc02f081b5cf7ef6deb4314d01591c471fae62b5fcabaaec2b3b1cc6a983%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=72293576&rft_id=info:pmid/11006075&rfr_iscdi=true