Isolation and quantitation of adiponectin higher order complexes.
Identifieur interne : 001A67 ( PubMed/Curation ); précédent : 001A66; suivant : 001A68Isolation and quantitation of adiponectin higher order complexes.
Auteurs : Joseph M. Rutkowski [États-Unis] ; Philipp E. Scherer [États-Unis]Source :
- Methods in enzymology [ 1557-7988 ] ; 2014.
Descripteurs français
- KwdFr :
- MESH :
- anatomopathologie : Adipocytes, Tissu adipeux.
- isolement et purification : Adiponectine.
- métabolisme : Adipocytes, Glucose, Tissu adipeux.
- sang : Adipokines, Adiponectine.
- Humains, Masse moléculaire.
English descriptors
- KwdEn :
- MESH :
- chemical , blood : Adipokines, Adiponectin.
- chemical , isolation & purification : Adiponectin.
- metabolism : Adipocytes, Adipose Tissue, Glucose.
- pathology : Adipocytes, Adipose Tissue.
- Humans, Molecular Weight.
Abstract
Adiponectin is a circulating bioactive hormone secreted by adipocytes as oligomers ranging in size from 90 kDa trimers and 180 kDa hexamers to larger high molecular weight oligomers that may reach 18- or 36-mers in size. While total circulating adiponectin levels correlate well with metabolic health, it is the relative distribution of adiponectin complexes that is most clinically relevant to glucose sensitivity and inflammation. High molecular weight adiponectin best mirrors insulin sensitivity, while trimeric adiponectin dominates with insulin resistance and adipose tissue inflammation. Experimental animal and in vitro models have also linked the relative fraction of high molecular weight adiponectin to its positive effects. Quantitating adiponectin size distribution thus provides a window into metabolic health and can serve as a surrogate marker for adipose tissue fitness. Here, we present a detailed protocol for isolating and quantitating adiponectin complexes in serum or plasma that has been extensively utilized for both human clinical samples and numerous animal models under various experimental conditions. Examples are presented of different adiponectin distributions and tips are provided for optimization using available equipment. Comparison of this rigorous approach to other available methods is also discussed. In total, this summary is a blueprint for the expanded quantitation and study of adiponectin complexes.
DOI: 10.1016/B978-0-12-411619-1.00013-6
PubMed: 24480350
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Scherer</name><affiliation wicri:level="1"><nlm:affiliation>Touchstone Diabetes Center, Department of Internal Medicine, UT Southwestern Medical Center, Dallas, Texas, USA; Department of Cell Biology, UT Southwestern Medical Center, Dallas, Texas, USA. 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While total circulating adiponectin levels correlate well with metabolic health, it is the relative distribution of adiponectin complexes that is most clinically relevant to glucose sensitivity and inflammation. High molecular weight adiponectin best mirrors insulin sensitivity, while trimeric adiponectin dominates with insulin resistance and adipose tissue inflammation. Experimental animal and in vitro models have also linked the relative fraction of high molecular weight adiponectin to its positive effects. Quantitating adiponectin size distribution thus provides a window into metabolic health and can serve as a surrogate marker for adipose tissue fitness. Here, we present a detailed protocol for isolating and quantitating adiponectin complexes in serum or plasma that has been extensively utilized for both human clinical samples and numerous animal models under various experimental conditions. Examples are presented of different adiponectin distributions and tips are provided for optimization using available equipment. Comparison of this rigorous approach to other available methods is also discussed. In total, this summary is a blueprint for the expanded quantitation and study of adiponectin complexes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24480350</PMID><DateCompleted><Year>2014</Year><Month>09</Month><Day>19</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1557-7988</ISSN><JournalIssue CitedMedium="Internet"><Volume>537</Volume><PubDate><Year>2014</Year></PubDate></JournalIssue><Title>Methods in enzymology</Title><ISOAbbreviation>Meth. Enzymol.</ISOAbbreviation></Journal><ArticleTitle>Isolation and quantitation of adiponectin higher order complexes.</ArticleTitle><Pagination><MedlinePgn>243-59</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/B978-0-12-411619-1.00013-6</ELocationID><ELocationID EIdType="pii" ValidYN="Y">B978-0-12-411619-1.00013-6</ELocationID><Abstract><AbstractText>Adiponectin is a circulating bioactive hormone secreted by adipocytes as oligomers ranging in size from 90 kDa trimers and 180 kDa hexamers to larger high molecular weight oligomers that may reach 18- or 36-mers in size. While total circulating adiponectin levels correlate well with metabolic health, it is the relative distribution of adiponectin complexes that is most clinically relevant to glucose sensitivity and inflammation. High molecular weight adiponectin best mirrors insulin sensitivity, while trimeric adiponectin dominates with insulin resistance and adipose tissue inflammation. Experimental animal and in vitro models have also linked the relative fraction of high molecular weight adiponectin to its positive effects. Quantitating adiponectin size distribution thus provides a window into metabolic health and can serve as a surrogate marker for adipose tissue fitness. Here, we present a detailed protocol for isolating and quantitating adiponectin complexes in serum or plasma that has been extensively utilized for both human clinical samples and numerous animal models under various experimental conditions. Examples are presented of different adiponectin distributions and tips are provided for optimization using available equipment. Comparison of this rigorous approach to other available methods is also discussed. In total, this summary is a blueprint for the expanded quantitation and study of adiponectin complexes.</AbstractText><CopyrightInformation>© 2014 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rutkowski</LastName><ForeName>Joseph M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Touchstone Diabetes Center, Department of Internal Medicine, UT Southwestern Medical Center, Dallas, Texas, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Scherer</LastName><ForeName>Philipp E</ForeName><Initials>PE</Initials><AffiliationInfo><Affiliation>Touchstone Diabetes Center, Department of Internal Medicine, UT Southwestern Medical Center, Dallas, Texas, USA; Department of Cell Biology, UT Southwestern Medical Center, Dallas, Texas, USA. Electronic address: philipp.scherer@utsouthwestern.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>P01 DK088761</GrantID><Acronym>DK</Acronym><Agency>NIDDK NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01-DK55758</GrantID><Acronym>DK</Acronym><Agency>NIDDK NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P01-DK088761</GrantID><Acronym>DK</Acronym><Agency>NIDDK NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01-DK099110</GrantID><Acronym>DK</Acronym><Agency>NIDDK NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 DK099110</GrantID><Acronym>DK</Acronym><Agency>NIDDK NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 DK055758</GrantID><Acronym>DK</Acronym><Agency>NIDDK NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType 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