Document Detail

Synthesis and assembly of functional high molecular weight adiponectin multimers in an engineered strain of Escherichia coli.
MedLine Citation:
PMID:  22376164     Owner:  NLM     Status:  Publisher    
Adiponectin has many beneficial effects on cardiovascular and obesity-related disorders. It is part of a class of proteins that contains short collagenous domains along with surfactant proteins A & D, and complement C1q. This class of biomacromolecules requires post-translational modifications to form biologically active assemblies. By introducing a set of post-translational modifying enzymes into Escherichia coli, we have created a prokaryotic expression system that functionally assembles adiponectin, as assessed by the ability of produced adiponectin multimers to suppress human endothelial cell apoptosis. This study represents the first example of the assembly of functional high order multimers of any member of this class of proteins outside of eukaryotic cells. Furthermore, the results give fundamental insight into the process of assembly such as the necessity and sufficiency of various post-translational steps for functional assembly. We expect that fine-tuning of the expression system will allow for efficient production and functional assembly of biomolecules that assemble via short collagenous domains.
Sheng Ding; Daniel M Pinkas; Annelise E Barron
Related Documents :
8662724 - Purification, cloning, and sequence analysis of a mr = 30,000 protein from sea urchin a...
17047254 - Zp2 and zp3 traffic independently within oocytes prior to assembly into the extracellul...
22533924 - Enzml: multi-label prediction of enzyme classes using interpro signatures.
22894154 - Identification of an extracellular antifungal protein from the endophytic fungus collet...
1653704 - Recombinant expression and properties of the human calcium-binding extracellular matrix...
23334514 - Secretory production of single-chain antibody (scfv) in brevibacillus choshinensis usin...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-2-29
Journal Detail:
Title:  Biomacromolecules     Volume:  -     ISSN:  1526-4602     ISO Abbreviation:  -     Publication Date:  2012 Feb 
Date Detail:
Created Date:  2012-3-1     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100892849     Medline TA:  Biomacromolecules     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  The use and safety of combined resistance and aerobic training in a patient with complications relat...
Next Document:  Cardiovascular, ocular and bone adverse reactions associated with thiazolidinediones: a disproportio...