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...
Saved in:
Published in: | Biochemical and biophysical research communications 2000-09, Vol.276 (1), p.16-22 |
---|---|
Main Authors: | , , , , , , , , |
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 |