Linked Life Data

12091459

Source:http://linkedlifedata.com/resource/pubmed/id/12091459

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-7-1
pubmed:abstractText
As many GPI anchored proteins, PrP(C) and its abnormal conformer PrP(Sc), are inserted into membrane microdomains known as rafts. Upon raft disruption, PrP(C) becomes soluble, while PrP(Sc) aggregates into insoluble structures. It was recently published that, as opposed to PrP(C), PrP(Sc), as well as its protease resistant core PrP27-30, can bind specifically to plasminogen and other serum components. These findings were suggested to have important physiological implications in transmissible spongiform encephalopathies (TSE) diagnosis and pathogenesis. In this work, we show that the binding of PrP(Sc) or PrP 27-30 to serum proteins occurs only at specific detergent combinations, in which disease associated PrPs are present in aggregated structures. At detergent conditions in which rafts are intact, it is actually PrP(C.) that binds to blood proteins, albeit not directly, but through neighboring rafts components. Our results therefore indicate that the binding of PrP(Sc) to blood components has no physiological relevance.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
82
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-5
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
The binding of prion proteins to serum components is affected by detergent extraction conditions.
pubmed:affiliation
Department of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital, Jerusalem, Israel 91120.
pubmed:publicationType
Journal Article