Linked Life Data

2464557

Source:http://linkedlifedata.com/resource/pubmed/id/2464557

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1989-3-23
pubmed:abstractText
Electron-microscopic, histochemical and immunological studies have shown that the deposits of primary and secondary localized cutaneous amyloid (amyloid K) consist mainly of keratin filament material. The amyloid P component is the second most significant constituent. Pathogenetically, defective keratinocyte apoptosis is the most likely mechanism of generation for amyloid K. Apoptosis is a distinct mode of cell death according to which individual basal keratinocytes disintegrate in physiological and pathological conditions to form membrane-bound "apoptotic" bodies consisting mainly of keratin filament aggregates. These lose their protective membrane and drop into the upper dermis, where they present as keratin (Civatte, cytoid) bodies, which are regularly coated with immunoglobulins. Overproduction of keratin bodies and/or a defect in their degradation by enzymatic digestion or phagocytosis by macrophages and fibroblasts, followed by conversion into amyloid fibrils, may be responsible for the generation of deposits of amyloid K.
pubmed:language
ger
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0017-8470
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
419-25
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
[Amyloid K].
pubmed:affiliation
Universitätsklinik für Dermatologie und Venerologie Innsbruck.
pubmed:publicationType
Journal Article, English Abstract, Review