Proteolytic cleavage of the amyloid peptides from the amyloid protein precursor (APP) by APP secretases is a key event in Alzheimer`s disease (AD) pathogenesis. Both overexpression of the APP and abnormal APP processing play key roles, resulting in the production ofβ-amyloid peptide (Aβ) fragments, that are neurotoxic and proinflammatory. APP is cleaved by three types of proteases, α-,β-, and γ-secretases. Enzymatic processing byβ- and γ-secretases cleaves on the N- and C-terminal ends of theβ-amyloid, respectively. In the previous studies, it has been demonstrated that APP was expressed in adipose cells and its expression levels were correlated to the plasma levels ofβ-amyloid. The purpose of this study was to figure out if adipose cells express secretases which can cleave APP intoβ-amyloid peptides. To see gene expression of representativeβ-and γ-secretase, BACE1 (beta-site APP-cleaving enzyme 1) and PSEN1(presenilin 1), gene expression data from two previous microarray studies were reanalyzed and real-time PCR was performed with adipose cells from human subcutaneous and visceral adipose tissue samples. Microarray data demonstrated that both BACE1 and PSEN1 were expressed in isolated subcutaneous adipocytes and preadipocytes. BACE1 expression in adipocytes was upregulated in obese subjects. Gene expression of both BACE1 and PSEN1 was confirmed in adipocytes and preadipocytes isolated from subcutaneous and visceral adipose tissues. PSEN1 expression in all types of adipose cells was higher than a brain autopsy sample from a person who died of Alzheimer`s disease. In summary, BACE1 and PSEN1 are highly expressed in adipose cells in visceral and subcutaneous adipose tissue depots and upregulated in obesity, suggesting a possible role for enzymatic machinery for APP processing toβ-amyloid peptides.