Linked Life Data

12440480

Source:http://linkedlifedata.com/resource/pubmed/id/12440480

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2002-11-20
pubmed:abstractText
Familial amyloidosis of the Finnish type (FAF) is caused by two proteolytic cleavages of mutant gelsolin leading to the accumulation of FAF amyloid in the patients' tissues. Here, we demonstrate that, in mouse pituitary corticotropic AtT20 cells, the enzyme responsible for the first cleavage of mutant secretory FAF gelsolin to FAF amyloid precursor is present in reasonable amounts. Furthermore, in At T20 cells stably expressing alpha1-PDX a potent inhibitor of most proprotein convertases, this cleavage was inhibited The present data provide strong evidence that proprotein convertases, possibly furin or PC5, are involved in the initialpathological cleavage of mutant secretory FAF gelsolin leading ultimately to the amyloid disease.
pubmed:language
eng
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:author
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
83-7
pubmed:dateRevised
2006-11-15
pubmed:articleTitle
Role of proprotein convertases in the pathogenic processing of the amyloidosis-associated form of secretory gelsolin.
pubmed:affiliation
Biomedicum Helsinki, Department of Molecular Medicine, National Public Health Institute, Finland. Hannele.Kangas@ktl.fi