Cellular localization and associations of the major lipolytic proteins in human skeletal muscle at rest and during exercise
Lipolysis involves the sequential breakdown of fatty acids from triacylglycerol and is increased during energy stress such as exercise. Adipose triglyceride lipase (ATGL) is a key regulator of skeletal muscle lipolysis and perilipin (PLIN) 5 is postulated to be an important regulator of ATGL action...
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| description | Lipolysis involves the sequential breakdown of fatty acids from triacylglycerol and is increased during energy stress such as exercise. Adipose triglyceride lipase (ATGL) is a key regulator of skeletal muscle lipolysis and perilipin (PLIN) 5 is postulated to be an important regulator of ATGL action of muscle lipolysis. Hence, we hypothesized that non-genomic regulation such as cellular localization and the interaction of these key proteins modulate muscle lipolysis during exercise. PLIN5, ATGL and CGI-58 were highly (>60%) colocated with Oil Red O (ORO) stained lipid droplets. PLIN5 was significantly colocated with ATGL, mitochondria and CGI-58, indicating a close association between the key lipolytic effectors in resting skeletal muscle. The colocation of the lipolytic proteins, their independent association with ORO and the PLIN5/ORO colocation were not altered after 60 min of moderate intensity exercise. Further experiments in cultured human myocytes showed that PLIN5 colocation with ORO or mitochondria is unaffected by pharmacological activation of lipolytic pathways. Together, these data suggest that the major lipolytic proteins are highly expressed at the lipid droplet and colocate in resting skeletal muscle, that their localization and interactions appear to remain unchanged during prolonged exercise, and, accordingly, that other post-translational mechanisms are likely regulators of skeletal muscle lipolysis. |
| doi_str_mv | 10.1371/journal.pone.0103062 |
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Adipose triglyceride lipase (ATGL) is a key regulator of skeletal muscle lipolysis and perilipin (PLIN) 5 is postulated to be an important regulator of ATGL action of muscle lipolysis. Hence, we hypothesized that non-genomic regulation such as cellular localization and the interaction of these key proteins modulate muscle lipolysis during exercise. PLIN5, ATGL and CGI-58 were highly (>60%) colocated with Oil Red O (ORO) stained lipid droplets. PLIN5 was significantly colocated with ATGL, mitochondria and CGI-58, indicating a close association between the key lipolytic effectors in resting skeletal muscle. The colocation of the lipolytic proteins, their independent association with ORO and the PLIN5/ORO colocation were not altered after 60 min of moderate intensity exercise. Further experiments in cultured human myocytes showed that PLIN5 colocation with ORO or mitochondria is unaffected by pharmacological activation of lipolytic pathways. Together, these data suggest that the major lipolytic proteins are highly expressed at the lipid droplet and colocate in resting skeletal muscle, that their localization and interactions appear to remain unchanged during prolonged exercise, and, accordingly, that other post-translational mechanisms are likely regulators of skeletal muscle lipolysis.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0103062</identifier><identifier>PMID: 25054327</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>1-Acylglycerol-3-Phosphate O-Acyltransferase - analysis ; 1-Acylglycerol-3-Phosphate O-Acyltransferase - metabolism ; Adipocytes ; Adult ; Biology ; Biology and Life Sciences ; Cells, Cultured ; Endocrinology ; Exercise ; Exercise - physiology ; Fatty acids ; Gene expression ; Humans ; Identification ; Intracellular Signaling Peptides and Proteins - analysis ; Intracellular Signaling Peptides and Proteins - metabolism ; Kinases ; Laboratories ; Lipase ; Lipase - analysis ; Lipase - metabolism ; Lipids ; Lipolysis ; Localization ; Medicine and Health Sciences ; Metabolism ; Mitochondria ; Mitochondrial DNA ; Muscle Fibers, Skeletal - chemistry ; Muscle Fibers, Skeletal - physiology ; Muscle Fibers, Skeletal - ultrastructure ; Muscle Proteins - analysis ; Muscle Proteins - metabolism ; Muscle, Skeletal - physiology ; Muscle, Skeletal - ultrastructure ; Muscles ; Musculoskeletal system ; Myocytes ; Nutrition ; Perilipin-5 ; Pharmacology ; Phosphorylation ; Physical fitness ; Physiology ; Post-translation ; Proteins ; Regulators ; Research and Analysis Methods ; Rest - physiology ; Skeletal muscle ; Studies ; Triglycerides ; Workloads ; Young Adult</subject><ispartof>PloS one, 2014-07, Vol.9 (7), p.e103062-e103062</ispartof><rights>COPYRIGHT 2014 Public Library of Science</rights><rights>2014 Mason et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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Adipose triglyceride lipase (ATGL) is a key regulator of skeletal muscle lipolysis and perilipin (PLIN) 5 is postulated to be an important regulator of ATGL action of muscle lipolysis. Hence, we hypothesized that non-genomic regulation such as cellular localization and the interaction of these key proteins modulate muscle lipolysis during exercise. PLIN5, ATGL and CGI-58 were highly (>60%) colocated with Oil Red O (ORO) stained lipid droplets. PLIN5 was significantly colocated with ATGL, mitochondria and CGI-58, indicating a close association between the key lipolytic effectors in resting skeletal muscle. The colocation of the lipolytic proteins, their independent association with ORO and the PLIN5/ORO colocation were not altered after 60 min of moderate intensity exercise. Further experiments in cultured human myocytes showed that PLIN5 colocation with ORO or mitochondria is unaffected by pharmacological activation of lipolytic pathways. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mason, Rachael R</au><au>Meex, Ruth C R</au><au>Russell, Aaron P</au><au>Canny, Benedict J</au><au>Watt, Matthew J</au><au>Moro, Cedric</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cellular localization and associations of the major lipolytic proteins in human skeletal muscle at rest and during exercise</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2014-07-23</date><risdate>2014</risdate><volume>9</volume><issue>7</issue><spage>e103062</spage><epage>e103062</epage><pages>e103062-e103062</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Lipolysis involves the sequential breakdown of fatty acids from triacylglycerol and is increased during energy stress such as exercise. Adipose triglyceride lipase (ATGL) is a key regulator of skeletal muscle lipolysis and perilipin (PLIN) 5 is postulated to be an important regulator of ATGL action of muscle lipolysis. Hence, we hypothesized that non-genomic regulation such as cellular localization and the interaction of these key proteins modulate muscle lipolysis during exercise. PLIN5, ATGL and CGI-58 were highly (>60%) colocated with Oil Red O (ORO) stained lipid droplets. PLIN5 was significantly colocated with ATGL, mitochondria and CGI-58, indicating a close association between the key lipolytic effectors in resting skeletal muscle. The colocation of the lipolytic proteins, their independent association with ORO and the PLIN5/ORO colocation were not altered after 60 min of moderate intensity exercise. Further experiments in cultured human myocytes showed that PLIN5 colocation with ORO or mitochondria is unaffected by pharmacological activation of lipolytic pathways. Together, these data suggest that the major lipolytic proteins are highly expressed at the lipid droplet and colocate in resting skeletal muscle, that their localization and interactions appear to remain unchanged during prolonged exercise, and, accordingly, that other post-translational mechanisms are likely regulators of skeletal muscle lipolysis.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>25054327</pmid><doi>10.1371/journal.pone.0103062</doi><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS); EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | 1-Acylglycerol-3-Phosphate O-Acyltransferase - analysis 1-Acylglycerol-3-Phosphate O-Acyltransferase - metabolism Adipocytes Adult Biology Biology and Life Sciences Cells, Cultured Endocrinology Exercise Exercise - physiology Fatty acids Gene expression Humans Identification Intracellular Signaling Peptides and Proteins - analysis Intracellular Signaling Peptides and Proteins - metabolism Kinases Laboratories Lipase Lipase - analysis Lipase - metabolism Lipids Lipolysis Localization Medicine and Health Sciences Metabolism Mitochondria Mitochondrial DNA Muscle Fibers, Skeletal - chemistry Muscle Fibers, Skeletal - physiology Muscle Fibers, Skeletal - ultrastructure Muscle Proteins - analysis Muscle Proteins - metabolism Muscle, Skeletal - physiology Muscle, Skeletal - ultrastructure Muscles Musculoskeletal system Myocytes Nutrition Perilipin-5 Pharmacology Phosphorylation Physical fitness Physiology Post-translation Proteins Regulators Research and Analysis Methods Rest - physiology Skeletal muscle Studies Triglycerides Workloads Young Adult |
| title | Cellular localization and associations of the major lipolytic proteins in human skeletal muscle at rest and during exercise |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T15%3A10%3A16IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cellular%20localization%20and%20associations%20of%20the%20major%20lipolytic%20proteins%20in%20human%20skeletal%20muscle%20at%20rest%20and%20during%20exercise&rft.jtitle=PloS%20one&rft.au=Mason,%20Rachael%20R&rft.date=2014-07-23&rft.volume=9&rft.issue=7&rft.spage=e103062&rft.epage=e103062&rft.pages=e103062-e103062&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0103062&rft_dat=%3Cgale_plos_%3EA418127726%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1547892698&rft_id=info:pmid/25054327&rft_galeid=A418127726&rft_doaj_id=oai_doaj_org_article_286f42fe2a434126ab0ec28c2a2f371c&rfr_iscdi=true |