liu.seSearch for publications in DiVA
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Senile aortic amyloid: Evidence for two distinct forms of localized deposits
Linköping University, Department of Neuroscience and Locomotion, Pathology. Linköping University, Faculty of Health Sciences.
Department of Medicine, Dartmouth Medical School, Hanover, New Hampshire.
Department of Pathology, Hospital of Jönköping, Jönköping, Sweden.
1992 (English)In: American Journal of Pathology, ISSN 0002-9440, E-ISSN 1525-2191, Vol. 140, no 4, 871-877 p.Article in journal (Refereed) Published
Abstract [en]

Aortic tissues obtained at autopsy were examined from 84 patients (age, 18-96 years). Amyloid deposits were present in the media in 61 of 63 (97%) of the patients above the age of 50. In addition, intimal amyloid deposits were present in 35% of this group. Intimal amyloid differed from medial amyloid both in its morphologic characteristics and its association with atherosclerosis. An antiserum raised to a low molecular weight protein extracted from amyloid fibrils of the aortic media reacted specifically with medial amyloid but did not react with intimal deposits. Neither type of amyloid reacted with anti-ATTR (Senile systemic amyloid), anti-AANF (isolated atrial amyloid), or antisera to other known forms of amyloid. These findings are consistent with the presence of two separate forms of localized amyloid in the aging aorta.

Place, publisher, year, edition, pages
1992. Vol. 140, no 4, 871-877 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-79732PubMedID: 1562050OAI: oai:DiVA.org:liu-79732DiVA: diva2:544065
Available from: 2012-08-13 Created: 2012-08-13 Last updated: 2017-12-07Bibliographically approved
In thesis
1. Apolipoprotein A-1 derived amyloid in the atherosclerotic intima of the human aorta
Open this publication in new window or tab >>Apolipoprotein A-1 derived amyloid in the atherosclerotic intima of the human aorta
2000 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Amyloid is insoluble fibrillar protein deposited in the extracellular space. The resulting heterogeneous group of disorders, amyloidosis, can be sporadic or hereditary, and the amyloid is systemically distributed or localized in single organs. Systemic hereditary amyloidoses are disorders caused by mutant forms of plasma proteins such as transthyretin (TTR) or less frequently, apolipoprotein A-1 (apo A-1), the major protein in high-density lipoprotein (HDL). Local deposition of amyloid associated with aging may be pathogenically important in Alzheimer's disease and type II diabetes. Localized amyloid in the medial and intimal layer of the aorta, commonly found in elderly humans, is of unknown sigoificance. The aim of this work was to investigate the nature of amyloid in the atherosclerotic intima of the human aorta, its fibrillogenesis and potential pathogenic importance. Two biochemically different forms of localized amyloid deposits in the aorta were identified; one affecting the atherosclerotic plaques of the intima and the other the media. Amyloid fibrils from the media has subse quently been found to consist of a protein fragment derived from lactadherin. Purified amyloid protein from atherosclerotic plaques of aortas in utopsy cases was shown by amino acid sequence analysis to be derived from apo A-1. Apo A-1 derived amyloid was immunohistochemically confirmed in 14% of 72 autopsy cases. A mutation was found in the apo A-1 gene (Δ Lys 1 07) in one of the 9 cases with intimal amyloid. Thus wild type, as well as mutant apo A-1, is amyloidogenic in humans. There was a tendency towards higher plasma levels of apo A-1 in patients with apo A-1 derived amyloid who underwent arterial reconstruction, compared to those without amyloid (p= 0.055). Levels of LDL- and total cholesterol were higher in the group with amyloid. Atherosclerosis induces high concentration of the acute phase reactant SAA in atherosclerotic lesions. SAA may displace apo A-1 from HDL, which, in addition to high levels of plasma apo A-1, could lead to an increased concentration oflipid free apo A-1 in the intima. Conformational changes in apo A-1 are then induced, making it more prone to fibril formation. Since some forms of amyloid fibrils are known to be cytotoxic, apo A-1 derived amyloid may contribute to the injury caused by other factors in atherosclerotic lesions.

Place, publisher, year, edition, pages
Linköping: Linköping University Electronic Press, 2000. 74 p.
Series
Linköping University Medical Dissertations, ISSN 0345-0082 ; 636
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-28611 (URN)13766 (Local ID)91-7219-737-4 (ISBN)13766 (Archive number)13766 (OAI)
Public defence
2000-09-15, Berzeliussalen, Hälsouniversitetet, Linköping, 09:00 (Swedish)
Available from: 2009-10-09 Created: 2009-10-09 Last updated: 2012-08-13Bibliographically approved

Open Access in DiVA

No full text

Other links

PubMedFull-text
By organisation
PathologyFaculty of Health Sciences
In the same journal
American Journal of Pathology
Medical and Health Sciences

Search outside of DiVA

GoogleGoogle Scholar

pubmed
urn-nbn

Altmetric score

pubmed
urn-nbn
Total: 35 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf