Background and objectives. Interactions between hydrophobic compounds like cholesterol and lithocholic acid and alpha-1-antitrypsin (α-1-AT) have previously been described. We studied the putative interaction between a-1-AT and the insoluble, hydrophobic, β-pleated sheet, light-chain-derived fibrils that predominate the tissue deposits in primary immunocytic (AL) related amyloidosis. Subjects and methods. Amyloid fibrils were isolated from two cases with lambda and two cases with kappa AL amyloidosis. Results. The lambda fibrils could be completely disaggregated (as shown by light and electron microscopy and Congo red uptake) by a-1-AT added in the molar ratio 1:5, whereas fibrirs with predominantly kappa chains remained unaffected. The lambda-chain interaction was accompanied by characteristic changes of the physicochemical and biological properties of α-1-AT apparent in an increased thermal stability and loss of elastase-inhibitory activity. These findings are compatible with a transition of a-I-AT from a native, stressed conformation to a relaxed form. Conclusions. Disaggregation of lambda AL amyloid fibrils can be achieved by addition of α-1-AT. The findings may have therapeutic implications in primary amyloidosis.
|Number of pages||7|
|Journal||Journal of Internal Medicine|
|Publication status||Published - 1995|
- Amyloid fibrils
ASJC Scopus subject areas
- Internal Medicine