Linked Life Data

12884739

Source:http://linkedlifedata.com/resource/pubmed/id/12884739

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2003-7-29
pubmed:abstractText
Amyloidosis is a disorder of protein metabolism in which normally soluble autologous proteins are deposited in tissues as abnormal insoluble fibrils, causing structural and functional disruptions. We have recently identified the novel localized amyloidosis accompanied by trichiasis. The precursor protein of amyloid deposits was mutated lactoferrin and all the patients had lactoferrin Glu561Asp. The disease was classified hereditary amyloidosis whose risk factor is trichiasis. We examined the therapeutic possibilities for mutated transthyretin(ATTR) related familial amyloidotic polyneurpathy(FAP), one of the systemic amyloidoses. Cr3+ suppressed amyloid formation by stabilizing ATTR structure in vitro. BSB is a useful new diagnostic tool to detect amyloid deposits both in in vitro and in vivo and may have therapeutic potential for preventing amyloid deposition. Gene therapy using single-stranded oligonuclotides(SSOs) may become a promising tool for therapy instead of liver transplantation. SSOs with athrocollagen effectively replaced the TTR gene both in vitro and in vivo.
pubmed:language
jpn
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0047-1860
pubmed:author
pubmed:issnType
Print
pubmed:volume
51
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
530-5
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
[Analyses of pathogenesis and therapeutic approaches for hereditary amyloidosis].
pubmed:affiliation
Department of Laboratory Medicine, Kumamoto University School of Medicine, Kumamoto 860-8556.
pubmed:publicationType
Journal Article, English Abstract, Review