The secretory vesicles (DCSV type) isolated from model neuronal-like chromaffin cells were demonstrated in this study to contain pGlu-Aβ(3-40/42) and QC, combined with Aβ(1-40/42). Prior studies indicate the presence of β-secretases, γ-secretase complex, and α-secretase in DCSV [, , ]. The DCSV contain cathepsin B that has been identified as a new alternative β-secretase [–], and the well-known β-secretase BACE1 [, ], an aspartyl protease [–]. The γ-secretase complex components are present in these DCSV [], composed of presenilins 1 and 2, nicastrin, Aph-1, and PEN-2 that together function as γ-secretase [, ]. The α-secretase ADAM10 protease is also present in DCSV []. These findings illustrate the presence of the APP processing machinery for production of pGlu-Aβ and Aβ peptides in neurotransmitter secretory vesicles containing neuropeptides and catecholamines.