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dc.contributor.authorBriggs, David
dc.contributor.authorGiron, Rebecca
dc.contributor.authorMalinowski, Pamela
dc.contributor.authorNunez, Martha
dc.contributor.authorTsao, Tsu-Shuen
dc.date.accessioned2016-05-20T08:58:49Z
dc.date.available2016-05-20T08:58:49Z
dc.date.issued2011en
dc.identifier.citationBriggs et al. BMC Biochemistry 2011, 12:24 http://www.biomedcentral.com/1471-2091/12/24en
dc.identifier.doi10.1186/1471-2091-12-24en
dc.identifier.urihttp://hdl.handle.net/10150/610110
dc.description.abstractBACKGROUND:Adiponectin is an adipocyte-secreted hormone with insulin-sensitizing and anti-inflammatory actions. The assembly of trimeric, hexameric, and higher molecular weight (HMW) species of adiponectin is a topic of significant interest because physiological actions of adiponectin are oligomer-specific. In addition, adiponectin assembly is an example of oxidative oligomerization of multi-subunit protein complexes in endoplasmic reticulum (ER).RESULTS:We previously reported that trimers assemble into HMW adiponectin via intermediates stabilized by disulfide bonds, and complete oxidation of available cysteines locks adiponectin in hexameric conformation. In this study, we examined the effects of redox environment on the rate of oligomer formation and the distribution of oligomers. Reassembly of adiponectin under oxidizing conditions accelerated disulfide bonding but favored formation of hexamers over the HMW species. Increased ratios of HMW to hexameric adiponectin could be achieved rapidly under oxidizing conditions by promoting disulfide rearrangement.CONCLUSIONS:Based upon these observations, we propose oxidative assembly of multi-subunit adiponectin complexes in a defined and stable redox environment is favored under oxidizing conditions coupled with high rates of disulfide rearrangement.
dc.language.isoenen
dc.publisherBioMed Centralen
dc.relation.urlhttp://www.biomedcentral.com/1471-2091/12/24en
dc.rights© 2011 Briggs et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0)en
dc.titleRole of redox environment on the oligomerization of higher molecular weight adiponectinen
dc.typeArticleen
dc.identifier.eissn1471-2091en
dc.contributor.departmentDepartment of Chemistry and Biochemistry, University of Arizona, 1656 E Mabel St MRB 430J, Tucson, AZ, 85724, USAen
dc.identifier.journalBMC Biochemistryen
dc.description.collectioninformationThis item is part of the UA Faculty Publications collection. For more information this item or other items in the UA Campus Repository, contact the University of Arizona Libraries at repository@u.library.arizona.edu.en
dc.eprint.versionFinal published versionen
refterms.dateFOA2018-06-25T05:18:52Z
html.description.abstractBACKGROUND:Adiponectin is an adipocyte-secreted hormone with insulin-sensitizing and anti-inflammatory actions. The assembly of trimeric, hexameric, and higher molecular weight (HMW) species of adiponectin is a topic of significant interest because physiological actions of adiponectin are oligomer-specific. In addition, adiponectin assembly is an example of oxidative oligomerization of multi-subunit protein complexes in endoplasmic reticulum (ER).RESULTS:We previously reported that trimers assemble into HMW adiponectin via intermediates stabilized by disulfide bonds, and complete oxidation of available cysteines locks adiponectin in hexameric conformation. In this study, we examined the effects of redox environment on the rate of oligomer formation and the distribution of oligomers. Reassembly of adiponectin under oxidizing conditions accelerated disulfide bonding but favored formation of hexamers over the HMW species. Increased ratios of HMW to hexameric adiponectin could be achieved rapidly under oxidizing conditions by promoting disulfide rearrangement.CONCLUSIONS:Based upon these observations, we propose oxidative assembly of multi-subunit adiponectin complexes in a defined and stable redox environment is favored under oxidizing conditions coupled with high rates of disulfide rearrangement.


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