Wasteosomes (or corpora amylacea) appear in the human brain with advancing age and in some neurodegenerative diseases. They have been proposed to accumulate waste substances and to contribute to a brain-cleaning mechanism. In this context, wasteosomes may have the potential to entrap some of the proteins that misfold, aggregate and accumulate in neurodegenerative diseases. In this work, we aim to characterize wasteosomes in the three primary frontotemporal lobar degeneration (FTLD) proteinopathies: FTLD with tau (FTLD-tau), FTLD with TAR DNA-binding protein 43 (FTLD-TDP) and FTLD with Fused in Sarcoma (FTLD-FUS). Cryopreserved human hippocampal sections were obtained from 4 cases of FTLD-tau, 3 cases of FTLD-TDP, and 3 cases of FTLD-FUS. Immunofluorescence methods with prior antigen retrieval were applied to detect tau, phosphorylated-TDP-43 (pTDP-43) and FUS in wasteosomes. Our results revealed the presence of tau, pTDP-43 and FUS in wasteosomes from FTLD-tau, FTLD-TDP, and FTLD-FUS, respectively. The staining of tau and pTDP-43 was placed in the peripheral part of the wasteosomes, while that of FUS was located in their central part. These results corroborate that wasteosomes may entrap misfolded proteins and indicate that the composition of wasteosomes differs depending on the proteinopathy. We conclude that wasteosomes in FTLD can contain tau, TDP-43 or FUS in concordance with the affected protein. Moreover, since there is currently no established biomarker for the diagnosis of FTLD, we propose to study the presence of these proteins in wasteosomes obtained from the cerebrospinal fluid as a potential tool diagnostic for FTLD.