Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2005-6-30
pubmed:abstractText
Serum Amyloid A (SAA) is an acute phase reactant protein that is predominantly found bound to high-density lipoprotein in plasma. Upon inflammation, the plasma concentration of SAA can increase dramatically, occasionally leading to the development of amyloid A (AA) amyloidosis, which involves the deposition of SAA amyloid fibrils in major organs. We previously found that the murine isoform SAA2.2 exists in aqueous solution as a hexamer containing a central channel. Here we show using various biophysical and biochemical techniques that the SAA2.2 hexamer can be totally dissociated into monomer by approximately 2 M urea, with the concerted loss of its alpha-helical structure. However, limited trypsin proteolysis experiments in urea showed a conserved digestion profile, suggesting the preservation of major backbone topological features in the urea-denatured state of SAA2.2. The marginal stability of hexameric SAA2.2 and the presence of residual structure in the denatured monomeric protein suggest that both forms may interconvert in vivo to exert different functions to meet the various needs during normal physiological conditions and in response to inflammatory stimuli.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-10066777, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-10211410, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-10504381, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-10507051, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-10550212, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-10608507, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-11454373, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-11782689, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-11849673, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-11877368, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-11910019, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-12456883, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-15047161, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-15520805, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-198813, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-2835617, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-3561251, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-3922050, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-7746330, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-8033906, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-8054364, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-8161701, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-8188253, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-8836154, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-8906588, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-9767146, http://linkedlifedata.com/resource/pubmed/commentcorrection/15937280-978136
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0961-8368
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1811-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Urea-induced denaturation of apolipoprotein serum amyloid A reveals marginal stability of hexamer.
pubmed:affiliation
Rensselaer Polytechnic Institute, Department of Chemistry and Chemical Biology, Troy, NY 12180, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural