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Medin amyloid - a matter close to the heart : Studies on medin amyloid formation and involvement in aortic pathologyLarsson, Annika January 2008 (has links)
Amyloidoses are a group of protein misfolding diseases characterized by deposits of insoluble fibrillar protein aggregates. Medin amyloid, which is the focus of this thesis, appears in the media of the thoracic aorta in nearly all individuals over 50 years. The fibrils are derived from a 50 amino acid residue fragment of the precursor protein lactadherin. How medin amyloid arises is unknown, but in paper I we demonstrated, with immunohistochemical and in vitro binding experiments, that both lactadherin and medin interact with elastin, implying that the elastic fibre is central in amyloid formation. In paper II, we further showed that the last 18-19 amino acid residues constitute the amyloid-promoting region. In paper III, the consequence of medin deposition was investigated. Aortic specimens from patients with thoracic aorta aneurysm and dissection were examined for medin content. The tissue findings indicated that the two disease groups contained more medin oligomers than normal aortas. Interestingly, recent reports demonstrate that the toxicity of amyloid proteins is attributed to prefibrillar oligomeric aggregates rather than to mature fibrils. In support of this finding, we observed that prefibrillar medin, in contrast to medin fibrils, was toxic in cell culture. Amyloid formation is a nucleation-dependent process. Addition of preformed fibrils to an amyloid protein solution dramatically accelerates fibrillation, a phenomenon called seeding. In paper IV, serum amyloid A-derived (AA) amyloid was found co-localized with medin deposits in the aorta. In vitro, medin fibrils enhanced the formation of AA fibrils, indicative of a seeding mechanism. The data are of great importance as they suggest that one type of amyloid is capable of inducing fibrillation and deposition of another amyloid type. In conclusion, the results of this thesis shed light on how medin is formed, the function of lactadherin and the consequences of medin deposition for aortic pathology.
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Vliv některých faktorů na postižení ledvin u AA amyloidózy / The influence of some factors on renal impairment in AA amyloidosisPotyšová, Zuzana January 2011 (has links)
Introduction: Available data suggest an association between presence of secondary (AA) amyloidosis and MCP-1 (monocyte chemoatracttant protein-1) and MIP-1alpha (macrophage inflammatory protein-1 alpha) genes polymorphisms. Some studies have also shown an impact of polymorphisms in exon 3 of SAA 1 (serum amyloid A 1) gene on the incidence of AA amyloidosis in different populations. Methods: The incidence of single genotypes MCP-1, MIP-1alpha and SAA 1 genes was investigated. Serum levels of SAA, MCP-1 and MIP-1alpha were measured and potential relation between serum levels and genotypes were analyzed. All examinations were performed in patients with AA amyloidosis (43), rheumatoid arthritis (RA) without amyloidosis and healthy control group (100). Results: Significantly more frequent occurrence of 1.1/1.1 genotype in SAA 1 was recorded in AA amyloidosis group compared to RA group as well as in control group (p<0,001). No statistically significant differences in distribution of another genotypes were found. Distribution of neither 1.1/1.1 genotype nor another ones did not vary among RA group and control group. No significant difference in distribution of another examined genotypes was recorded among all three groups. Serum concentrations of SAA were statistically significantly higher in AA amyloidosis group...
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Vliv některých faktorů na postižení ledvin u AA amyloidózy / The influence of some factors on renal impairment in AA amyloidosisPotyšová, Zuzana January 2011 (has links)
Introduction: Available data suggest an association between presence of secondary (AA) amyloidosis and MCP-1 (monocyte chemoatracttant protein-1) and MIP-1alpha (macrophage inflammatory protein-1 alpha) genes polymorphisms. Some studies have also shown an impact of polymorphisms in exon 3 of SAA 1 (serum amyloid A 1) gene on the incidence of AA amyloidosis in different populations. Methods: The incidence of single genotypes MCP-1, MIP-1alpha and SAA 1 genes was investigated. Serum levels of SAA, MCP-1 and MIP-1alpha were measured and potential relation between serum levels and genotypes were analyzed. All examinations were performed in patients with AA amyloidosis (43), rheumatoid arthritis (RA) without amyloidosis and healthy control group (100). Results: Significantly more frequent occurrence of 1.1/1.1 genotype in SAA 1 was recorded in AA amyloidosis group compared to RA group as well as in control group (p<0,001). No statistically significant differences in distribution of another genotypes were found. Distribution of neither 1.1/1.1 genotype nor another ones did not vary among RA group and control group. No significant difference in distribution of another examined genotypes was recorded among all three groups. Serum concentrations of SAA were statistically significantly higher in AA amyloidosis group...
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Can Feeding Amyloid Fibrils Trigger Amyloid Formation in C. Elegans?Norrby, Katarina January 2023 (has links)
Amyloidosis are diseases caused by misfolded proteins that have transformed into extracellular insoluble amyloid fibrils. One type of amyloidosis is AA amyloidosis caused by AA amyloid and diseases connected are Rheumatoid arthritis and Tuberculosis. C. Elegans is a nematode used as a model organism and in this experiment. They are transgenic and express GFP (green fluorescent protein), a probe that mark the body-wall muscle cells in order to be visible in fluorescence microscopes. Worms expressing AA45 and AA76 as well as a GFP control were fed with E. Coli OP50 and amyloid AA896 or Lin100. One control group was only fed with OP50. Three different aspects were researched: the size of the worms, their movements and a confocal microscope was used to detect amyloid. Neither the size of the worms nor the movements seemed to be linked to AA amyloid formation. However, amyloid were detected in worms expressing AA45 and AA76 but not in the GFP control when studied through a confocal microscope. In this research it is shown that worms fed with amyloid fibrils and expressing AA45 or AA76 start forming amyloid in the body-wall muscle. This can be of much help in future research in order to make simpler diagnostical methods which can reduce the time for patients to start treatment and improve chances of survival or living with the disease with less complications.
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