Many cancer types are intrinsically associated with specific types of amyloidosis, in which amyloid is accumulated locally inside tumors or systemically. Usually, this condition relates to the hyperproduction of specific amylogenic proteins. Recently, we found that the accumulation of amyloid beta (Aβ) peptide immunofluorescence is linked to glioma cells in mouse tumors. Here we report that amyloid-specific histochemical dyes reveal amyloid accumulation in all human glioma samples. Application of two different antibodies against Aβ peptide (a polyclonal antibody against human Aβ1-42 and a monoclonal pan-specific mAb-2 antibody against Aβ) showed that the amyloid in glioma samples contains Aβ. Amyloid was linked to glioma cells expressing glial-specific fibrillary acidic protein (GFAP) and to glioma blood vessels. Astrocytes close to the glioma site and to affected vessels also accumulated Aβ. We discuss whether amyloid is produced by glioma cells or is the result of systemic production of Aβ in response to glioma development due to an innate immunity reaction. We conclude that amyloid build-up in glioma tumors is a part of the tumor environment, and may be used as a target for developing a novel class of anti-tumor drugs and as an antigen for glioma visualization.
Keywords: brain; cancer; human; microscopy; tumor immunology.
© 2020 The Authors. Clinical & Experimental Immunology published by John Wiley & Sons Ltd on behalf of British Society for Immunology.