Parathyroid hormone (PTH) is released from the parathyroid glands and regulates bone and mineral metabolism. It is a single-chain 84-amino acid polypeptide with a molecular weight of 9,425 Daltons. It is synthesized and secreted by the parathyroid glands, and rapidly cleared from plasma (half-life <5 min). PTH is metabolized to C-terminal fragments by the liver and kidneys, and cleared by the kidney, either as intact PTH or as C-terminal fragments [1]. Background : The objective of this study was to evaluate the role of proteases on the degradation of parathyroid hormone (PTH) in blood samples.Methods : Protease inhibitors with specificity against serine proteases (aprotinin), cysteine proteases (E-64), serine and cysteine proteases (leupeptin), metalloproteases (EDTA), or a protease inhibitor cocktail with a broad spectrum of inhibitory activity were added to blood samples. After storage at room temperature (0-48 hr), PTH levels were measured.Results : PTH levels in samples with the protease inhibitor cocktail did not change significantly after 48 hr of storage at room temperature, but the average PTH levels decreased by 40.7% and 20.1%, in samples stored at room temperature and stored at 4°C without protease inhibitors, respectively. PTH levels in samples with leupeptin were stable for up to 24 hr. After 48 hr, the mean PTH levels decreased by 17.1%, 16.0%, 26.2%, and 32.1%, with 500 KIU/mL aprotinin, 100 μ mol/L leupeptin, 10 μ mol/L E-64, and 10 μ mol/L EDTA, respectively, in the samples stored at room temperature.Conclusions : The decrease in PTH levels in blood samples seemed to be due to the degradation of PTH by proteases. Various proteases, including especially serine proteases, would act together to degrade PTH in blood specimen. The PTH degradation may be inhibited in blood specimen with protease inhibitor cocktail. (Korean J Lab Med 2009;29:104-9)