Endocrine control of TAG lipase in the fat body of the migratory locust, Locusta migratoria
Aspects of the role and activation of the enzyme triacylglycerol lipase (TAG lipase) in the fat body of the migratory locust Locusta migratoria were investigated. TAG lipase is under the hormonal control of the three endogenous adipokinetic peptides of the migratory locust, Locmi-AKH-I, Locmi-AKH-II...
Gespeichert in:
Veröffentlicht in: | Insect biochemistry and molecular biology 2006-10, Vol.36 (10), p.759-768 |
---|---|
Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 768 |
---|---|
container_issue | 10 |
container_start_page | 759 |
container_title | Insect biochemistry and molecular biology |
container_volume | 36 |
creator | Auerswald, Lutz Gäde, Gerd |
description | Aspects of the role and activation of the enzyme triacylglycerol lipase (TAG lipase) in the fat body of the migratory locust
Locusta migratoria were investigated. TAG lipase is under the hormonal control of the three endogenous adipokinetic peptides of the migratory locust, Locmi-AKH-I, Locmi-AKH-II and Locmi-AKH-III. Injection of low doses (5–10
pmol) of each peptide causes an increase in lipase activity. The activation of lipase is time dependent: an elevated activity was recorded 15
min after injection of 10
pmol Locmi-AKH-I and maximum activation was reached after 45–60
min. The activation of TAG lipase is also dose-dependent. Doses of 2
pmol of each Locmi-AKH had no effect, whereas 5
pmol caused a significant activation. Maximum activation is reached with a dose of 10
pmol. Analogues of the second messengers cAMP (cpt-cAMP) and IP
3 (F-IP
3) both activate the enzyme glycogen phosphorylase whereas only cpt-cAMP, but not F-IP
3, activates TAG lipase; cpt-cAMP elevates the lipid levels in the haemolymph. Activation of lipase is specific to the three endogenous AKH peptides: 5
pmol of the endogenous peptide Locmi-HrTH and 10
pmol of corazonin failed to activate lipase. High doses of octopamine did not activate lipase nor did they elevate the lipid concentration in the haemolymph. TAG lipase is stimulated by flight activity but activation is slower than that of glycogen phosphorylase: after 30
min of flight or after 5
min of flight plus 1
h of subsequent rest, activity of TAG lipase is increased, but not immediately after 5
min of flight. In contrast, glycogen phosphorylase is activated significantly after 5
min of flight. These activation patterns of the two enzymes mirror-image the concentration of their substrates in the haemolymph: there is a significant decrease in the concentration of carbohydrates after 5
min of flight, whereas no change of the concentration of lipids can be measured after such short time of flight activity; however, a subsequent rest period of 1
h is sufficient to increase the lipid concentration. |
doi_str_mv | 10.1016/j.ibmb.2006.07.004 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_68932763</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0965174806001469</els_id><sourcerecordid>68932763</sourcerecordid><originalsourceid>FETCH-LOGICAL-c475t-445c6a2f0f0cdd6b2c1bfe697a418626d20b10fc1a9847d42f86f13895af42403</originalsourceid><addsrcrecordid>eNqFkE1v1DAQhq0K1C6lf6AH6hMnEsaOYzsSl6oqBWklDrSnHizHH8WrJN7a2Ur773HYVbnB6dVonhnNPAhdEqgJEP55U4d-7GsKwGsQNQA7QSsiRVcBZfAGraDjbUUEk2foXc4bKARrxSk6IwKokIyu0OPtZKNJYXLYxGlOccDR4_vrOzyErc4OhwnPvxz2esZ9tPulu9RjeEp6jmmPh2h2ef6E139Sv3aCfo_eej1kd3HMc_Tw9fb-5lu1_nH3_eZ6XRkm2rkqNxmuqQcPxlreU0N673gnNCOSU24p9AS8IbqTTFhGveSeNLJrtWfl0eYcfTzs3ab4vHN5VmPIxg2DnlzcZcVl11DBm_-CpGskJW1XQHoATYo5J-fVNoVRp70ioBb3aqMW92pxr0CoYrYMfThu3_Wjs39HjrILcHUAvI5KP6WQ1cNPCqQBQihwLgrx5UC4ousluKSyCW4yzobkzKxsDP-64DcNjZ2g</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19382159</pqid></control><display><type>article</type><title>Endocrine control of TAG lipase in the fat body of the migratory locust, Locusta migratoria</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Auerswald, Lutz ; Gäde, Gerd</creator><creatorcontrib>Auerswald, Lutz ; Gäde, Gerd</creatorcontrib><description>Aspects of the role and activation of the enzyme triacylglycerol lipase (TAG lipase) in the fat body of the migratory locust
Locusta migratoria were investigated. TAG lipase is under the hormonal control of the three endogenous adipokinetic peptides of the migratory locust, Locmi-AKH-I, Locmi-AKH-II and Locmi-AKH-III. Injection of low doses (5–10
pmol) of each peptide causes an increase in lipase activity. The activation of lipase is time dependent: an elevated activity was recorded 15
min after injection of 10
pmol Locmi-AKH-I and maximum activation was reached after 45–60
min. The activation of TAG lipase is also dose-dependent. Doses of 2
pmol of each Locmi-AKH had no effect, whereas 5
pmol caused a significant activation. Maximum activation is reached with a dose of 10
pmol. Analogues of the second messengers cAMP (cpt-cAMP) and IP
3 (F-IP
3) both activate the enzyme glycogen phosphorylase whereas only cpt-cAMP, but not F-IP
3, activates TAG lipase; cpt-cAMP elevates the lipid levels in the haemolymph. Activation of lipase is specific to the three endogenous AKH peptides: 5
pmol of the endogenous peptide Locmi-HrTH and 10
pmol of corazonin failed to activate lipase. High doses of octopamine did not activate lipase nor did they elevate the lipid concentration in the haemolymph. TAG lipase is stimulated by flight activity but activation is slower than that of glycogen phosphorylase: after 30
min of flight or after 5
min of flight plus 1
h of subsequent rest, activity of TAG lipase is increased, but not immediately after 5
min of flight. In contrast, glycogen phosphorylase is activated significantly after 5
min of flight. These activation patterns of the two enzymes mirror-image the concentration of their substrates in the haemolymph: there is a significant decrease in the concentration of carbohydrates after 5
min of flight, whereas no change of the concentration of lipids can be measured after such short time of flight activity; however, a subsequent rest period of 1
h is sufficient to increase the lipid concentration.</description><identifier>ISSN: 0965-1748</identifier><identifier>EISSN: 1879-0240</identifier><identifier>DOI: 10.1016/j.ibmb.2006.07.004</identifier><identifier>PMID: 17027842</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>adipokinetic hormone ; Adrenergic alpha-Agonists - pharmacology ; AKH ; Animals ; cyclic AMP ; dose response ; enzyme activation ; Enzyme Activation - drug effects ; enzyme activity ; fat body ; Fat Body - enzymology ; Flight, Animal ; glycogen ; Glycogen phosphorylase ; Hemolymph - enzymology ; hormonal regulation ; Insect ; insect flight ; Insect Hormones - pharmacology ; Insect Hormones - physiology ; Insect Proteins - metabolism ; Insect Proteins - physiology ; Lipase ; Lipase - blood ; Lipase - metabolism ; Lipase - physiology ; lipid content ; Lipids - blood ; Locust ; Locusta migratoria ; Locusta migratoria - enzymology ; locusts ; Octopamine ; Octopamine - pharmacology ; Oligopeptides - pharmacology ; Oligopeptides - physiology ; phosphorylase ; Pyrrolidonecarboxylic Acid - analogs & derivatives ; Pyrrolidonecarboxylic Acid - pharmacology ; Second messengers ; Triacylglycerol ; triacylglycerol lipase</subject><ispartof>Insect biochemistry and molecular biology, 2006-10, Vol.36 (10), p.759-768</ispartof><rights>2006 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c475t-445c6a2f0f0cdd6b2c1bfe697a418626d20b10fc1a9847d42f86f13895af42403</citedby><cites>FETCH-LOGICAL-c475t-445c6a2f0f0cdd6b2c1bfe697a418626d20b10fc1a9847d42f86f13895af42403</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ibmb.2006.07.004$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17027842$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Auerswald, Lutz</creatorcontrib><creatorcontrib>Gäde, Gerd</creatorcontrib><title>Endocrine control of TAG lipase in the fat body of the migratory locust, Locusta migratoria</title><title>Insect biochemistry and molecular biology</title><addtitle>Insect Biochem Mol Biol</addtitle><description>Aspects of the role and activation of the enzyme triacylglycerol lipase (TAG lipase) in the fat body of the migratory locust
Locusta migratoria were investigated. TAG lipase is under the hormonal control of the three endogenous adipokinetic peptides of the migratory locust, Locmi-AKH-I, Locmi-AKH-II and Locmi-AKH-III. Injection of low doses (5–10
pmol) of each peptide causes an increase in lipase activity. The activation of lipase is time dependent: an elevated activity was recorded 15
min after injection of 10
pmol Locmi-AKH-I and maximum activation was reached after 45–60
min. The activation of TAG lipase is also dose-dependent. Doses of 2
pmol of each Locmi-AKH had no effect, whereas 5
pmol caused a significant activation. Maximum activation is reached with a dose of 10
pmol. Analogues of the second messengers cAMP (cpt-cAMP) and IP
3 (F-IP
3) both activate the enzyme glycogen phosphorylase whereas only cpt-cAMP, but not F-IP
3, activates TAG lipase; cpt-cAMP elevates the lipid levels in the haemolymph. Activation of lipase is specific to the three endogenous AKH peptides: 5
pmol of the endogenous peptide Locmi-HrTH and 10
pmol of corazonin failed to activate lipase. High doses of octopamine did not activate lipase nor did they elevate the lipid concentration in the haemolymph. TAG lipase is stimulated by flight activity but activation is slower than that of glycogen phosphorylase: after 30
min of flight or after 5
min of flight plus 1
h of subsequent rest, activity of TAG lipase is increased, but not immediately after 5
min of flight. In contrast, glycogen phosphorylase is activated significantly after 5
min of flight. These activation patterns of the two enzymes mirror-image the concentration of their substrates in the haemolymph: there is a significant decrease in the concentration of carbohydrates after 5
min of flight, whereas no change of the concentration of lipids can be measured after such short time of flight activity; however, a subsequent rest period of 1
h is sufficient to increase the lipid concentration.</description><subject>adipokinetic hormone</subject><subject>Adrenergic alpha-Agonists - pharmacology</subject><subject>AKH</subject><subject>Animals</subject><subject>cyclic AMP</subject><subject>dose response</subject><subject>enzyme activation</subject><subject>Enzyme Activation - drug effects</subject><subject>enzyme activity</subject><subject>fat body</subject><subject>Fat Body - enzymology</subject><subject>Flight, Animal</subject><subject>glycogen</subject><subject>Glycogen phosphorylase</subject><subject>Hemolymph - enzymology</subject><subject>hormonal regulation</subject><subject>Insect</subject><subject>insect flight</subject><subject>Insect Hormones - pharmacology</subject><subject>Insect Hormones - physiology</subject><subject>Insect Proteins - metabolism</subject><subject>Insect Proteins - physiology</subject><subject>Lipase</subject><subject>Lipase - blood</subject><subject>Lipase - metabolism</subject><subject>Lipase - physiology</subject><subject>lipid content</subject><subject>Lipids - blood</subject><subject>Locust</subject><subject>Locusta migratoria</subject><subject>Locusta migratoria - enzymology</subject><subject>locusts</subject><subject>Octopamine</subject><subject>Octopamine - pharmacology</subject><subject>Oligopeptides - pharmacology</subject><subject>Oligopeptides - physiology</subject><subject>phosphorylase</subject><subject>Pyrrolidonecarboxylic Acid - analogs & derivatives</subject><subject>Pyrrolidonecarboxylic Acid - pharmacology</subject><subject>Second messengers</subject><subject>Triacylglycerol</subject><subject>triacylglycerol lipase</subject><issn>0965-1748</issn><issn>1879-0240</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1v1DAQhq0K1C6lf6AH6hMnEsaOYzsSl6oqBWklDrSnHizHH8WrJN7a2Ur773HYVbnB6dVonhnNPAhdEqgJEP55U4d-7GsKwGsQNQA7QSsiRVcBZfAGraDjbUUEk2foXc4bKARrxSk6IwKokIyu0OPtZKNJYXLYxGlOccDR4_vrOzyErc4OhwnPvxz2esZ9tPulu9RjeEp6jmmPh2h2ef6E139Sv3aCfo_eej1kd3HMc_Tw9fb-5lu1_nH3_eZ6XRkm2rkqNxmuqQcPxlreU0N673gnNCOSU24p9AS8IbqTTFhGveSeNLJrtWfl0eYcfTzs3ab4vHN5VmPIxg2DnlzcZcVl11DBm_-CpGskJW1XQHoATYo5J-fVNoVRp70ioBb3aqMW92pxr0CoYrYMfThu3_Wjs39HjrILcHUAvI5KP6WQ1cNPCqQBQihwLgrx5UC4ousluKSyCW4yzobkzKxsDP-64DcNjZ2g</recordid><startdate>20061001</startdate><enddate>20061001</enddate><creator>Auerswald, Lutz</creator><creator>Gäde, Gerd</creator><general>Elsevier Ltd</general><scope>FBQ</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>7SS</scope><scope>7X8</scope></search><sort><creationdate>20061001</creationdate><title>Endocrine control of TAG lipase in the fat body of the migratory locust, Locusta migratoria</title><author>Auerswald, Lutz ; Gäde, Gerd</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c475t-445c6a2f0f0cdd6b2c1bfe697a418626d20b10fc1a9847d42f86f13895af42403</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>adipokinetic hormone</topic><topic>Adrenergic alpha-Agonists - pharmacology</topic><topic>AKH</topic><topic>Animals</topic><topic>cyclic AMP</topic><topic>dose response</topic><topic>enzyme activation</topic><topic>Enzyme Activation - drug effects</topic><topic>enzyme activity</topic><topic>fat body</topic><topic>Fat Body - enzymology</topic><topic>Flight, Animal</topic><topic>glycogen</topic><topic>Glycogen phosphorylase</topic><topic>Hemolymph - enzymology</topic><topic>hormonal regulation</topic><topic>Insect</topic><topic>insect flight</topic><topic>Insect Hormones - pharmacology</topic><topic>Insect Hormones - physiology</topic><topic>Insect Proteins - metabolism</topic><topic>Insect Proteins - physiology</topic><topic>Lipase</topic><topic>Lipase - blood</topic><topic>Lipase - metabolism</topic><topic>Lipase - physiology</topic><topic>lipid content</topic><topic>Lipids - blood</topic><topic>Locust</topic><topic>Locusta migratoria</topic><topic>Locusta migratoria - enzymology</topic><topic>locusts</topic><topic>Octopamine</topic><topic>Octopamine - pharmacology</topic><topic>Oligopeptides - pharmacology</topic><topic>Oligopeptides - physiology</topic><topic>phosphorylase</topic><topic>Pyrrolidonecarboxylic Acid - analogs & derivatives</topic><topic>Pyrrolidonecarboxylic Acid - pharmacology</topic><topic>Second messengers</topic><topic>Triacylglycerol</topic><topic>triacylglycerol lipase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Auerswald, Lutz</creatorcontrib><creatorcontrib>Gäde, Gerd</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>MEDLINE - Academic</collection><jtitle>Insect biochemistry and molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Auerswald, Lutz</au><au>Gäde, Gerd</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Endocrine control of TAG lipase in the fat body of the migratory locust, Locusta migratoria</atitle><jtitle>Insect biochemistry and molecular biology</jtitle><addtitle>Insect Biochem Mol Biol</addtitle><date>2006-10-01</date><risdate>2006</risdate><volume>36</volume><issue>10</issue><spage>759</spage><epage>768</epage><pages>759-768</pages><issn>0965-1748</issn><eissn>1879-0240</eissn><abstract>Aspects of the role and activation of the enzyme triacylglycerol lipase (TAG lipase) in the fat body of the migratory locust
Locusta migratoria were investigated. TAG lipase is under the hormonal control of the three endogenous adipokinetic peptides of the migratory locust, Locmi-AKH-I, Locmi-AKH-II and Locmi-AKH-III. Injection of low doses (5–10
pmol) of each peptide causes an increase in lipase activity. The activation of lipase is time dependent: an elevated activity was recorded 15
min after injection of 10
pmol Locmi-AKH-I and maximum activation was reached after 45–60
min. The activation of TAG lipase is also dose-dependent. Doses of 2
pmol of each Locmi-AKH had no effect, whereas 5
pmol caused a significant activation. Maximum activation is reached with a dose of 10
pmol. Analogues of the second messengers cAMP (cpt-cAMP) and IP
3 (F-IP
3) both activate the enzyme glycogen phosphorylase whereas only cpt-cAMP, but not F-IP
3, activates TAG lipase; cpt-cAMP elevates the lipid levels in the haemolymph. Activation of lipase is specific to the three endogenous AKH peptides: 5
pmol of the endogenous peptide Locmi-HrTH and 10
pmol of corazonin failed to activate lipase. High doses of octopamine did not activate lipase nor did they elevate the lipid concentration in the haemolymph. TAG lipase is stimulated by flight activity but activation is slower than that of glycogen phosphorylase: after 30
min of flight or after 5
min of flight plus 1
h of subsequent rest, activity of TAG lipase is increased, but not immediately after 5
min of flight. In contrast, glycogen phosphorylase is activated significantly after 5
min of flight. These activation patterns of the two enzymes mirror-image the concentration of their substrates in the haemolymph: there is a significant decrease in the concentration of carbohydrates after 5
min of flight, whereas no change of the concentration of lipids can be measured after such short time of flight activity; however, a subsequent rest period of 1
h is sufficient to increase the lipid concentration.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>17027842</pmid><doi>10.1016/j.ibmb.2006.07.004</doi><tpages>10</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0965-1748 |
ispartof | Insect biochemistry and molecular biology, 2006-10, Vol.36 (10), p.759-768 |
issn | 0965-1748 1879-0240 |
language | eng |
recordid | cdi_proquest_miscellaneous_68932763 |
source | MEDLINE; Elsevier ScienceDirect Journals Complete |
subjects | adipokinetic hormone Adrenergic alpha-Agonists - pharmacology AKH Animals cyclic AMP dose response enzyme activation Enzyme Activation - drug effects enzyme activity fat body Fat Body - enzymology Flight, Animal glycogen Glycogen phosphorylase Hemolymph - enzymology hormonal regulation Insect insect flight Insect Hormones - pharmacology Insect Hormones - physiology Insect Proteins - metabolism Insect Proteins - physiology Lipase Lipase - blood Lipase - metabolism Lipase - physiology lipid content Lipids - blood Locust Locusta migratoria Locusta migratoria - enzymology locusts Octopamine Octopamine - pharmacology Oligopeptides - pharmacology Oligopeptides - physiology phosphorylase Pyrrolidonecarboxylic Acid - analogs & derivatives Pyrrolidonecarboxylic Acid - pharmacology Second messengers Triacylglycerol triacylglycerol lipase |
title | Endocrine control of TAG lipase in the fat body of the migratory locust, Locusta migratoria |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-05T15%3A24%3A25IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Endocrine%20control%20of%20TAG%20lipase%20in%20the%20fat%20body%20of%20the%20migratory%20locust,%20Locusta%20migratoria&rft.jtitle=Insect%20biochemistry%20and%20molecular%20biology&rft.au=Auerswald,%20Lutz&rft.date=2006-10-01&rft.volume=36&rft.issue=10&rft.spage=759&rft.epage=768&rft.pages=759-768&rft.issn=0965-1748&rft.eissn=1879-0240&rft_id=info:doi/10.1016/j.ibmb.2006.07.004&rft_dat=%3Cproquest_cross%3E68932763%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=19382159&rft_id=info:pmid/17027842&rft_els_id=S0965174806001469&rfr_iscdi=true |