ABSTRACT
Therapeutic options for patients with primary systemic (AL) amyloidosis are limited to reducing light chain synthesis using anti-plasma cell chemotherapy given in conventional amounts or high doses combined with autologous stem cell transplantation. This approach, particularly dose-intensive therapy, has extended survival and, in some cases, resulted in improved organ function over time. Importantly, amyloid deposition is not necessarily irreversible, as evidenced experimentally and clinically in cases of both primary secondary amyloidosis. Compelling evidence of in situ resolution of AL deposits has come from chemical analyses of fibrillar extracts where it has been determined that, most often, the protein constituents are not composed of intact light chains, but rather, consist of fragments that seemingly result from proteolytic degradation. Elimination of amyloid tumors also was expedited when the extracts were first incubated overnight with mouse immune serum. Further, the resolving amyloidomas were extensively infiltrated by activated neutrophils.
