Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis
-
Amyloidosis is a disease group caused by pathological aggregation and deposition of peptides in diverse tissue sites. Apart from the fibril protein, amyloid deposits frequently enclose non-fibrillar constituents. In routine diagnostics, we noticed the presence of complement 9 (C9) in amyloid. ⋯ No data were found regarding caspase 3. Our findings demonstrate the ubiquitous, spatial and specific enrichment of C9 in amyloid deposits irrespective of amyloid-, organ- or tissue type. Our findings lend support to the hypothesis that amyloidosis might activate the complement cascade, which could lead to the formation of the membrane attack complex and cell death.
-
More than 30 proteins and peptides have been found to form amyloid fibrils in human diseases. Fibrils formed by transthyretin (TTR) are associated with ATTR amyloidosis, affecting many vital organs, including the heart and peripheral nervous system. Congo red staining is the gold standard method for detection of amyloid deposits in tissue. ⋯ Using this method, we achieved sensitive detection of monomeric TTR in a microplate immunoassay and immunofluorescence labelling of ex vivo tissue from two patients containing ATTR aggregates. The system's utility was confirmed on sections from a patient with AA amyloidosis and liver sections from inflamed mouse. These results suggest that the detection system constitutes important new technology for highly sensitive detection of microscopic amounts of ATTR amyloid deposited in tissue.
-
Amyloidosis comprises a range of protein-folding disorders characterised by a buildup of amyloid deposits in one or multiple organs. The pathogenesis and pathologic findings of amyloidosis can vary widely due to the nature of the precursor protein. In veterinary medicine, there are 10 proteins known to form amyloid deposits in various organs. ⋯ This review addresses the transmission of AA amyloidosis pertinent to institutions, such as zoos, housing multiple individuals and species in relatively close proximity. In addition, this review includes summarisation for definitive diagnosis of single or multiple cases of amyloidosis affecting free-living wild and zoo animals. Insights into the diversity, transmission, and pathogenesis of known amyloidogenic proteins and species prevalently affected may help to establish a preventive intervention and stimulate the discovery of new diagnostic and therapeutic strategies.
-
Finnish gelsolin amyloidosis (AGel amyloidosis) is an inherited systemic amyloidosis with well-known ophthalmological, neurological and cutaneous symptoms. Additionally, cardiomyopathies, conduction disorders and need of cardiac pacemakers occur in some patients. This study focuses on electrocardiographic (ECG) findings in AGel amyloidosis and their relation to cardiac magnetic resonance (CMR) changes. We also assessed whether ECG abnormalities were associated with pacemaker implantation and mortality. ⋯ Conduction disorders and septal LGE are common in AGel amyloidosis, whereas other ECG and CMR findings typically observed in most common cardiac amyloidosis types were rare. Septal pathology seen in CMR may interfere with the cardiac conduction system in AGel amyloidosis, explaining conduction disorders, although pacemaker therapy is rarely required.