The aim of the work is to study the efficiency of rhythmic cold exposures (RCEs; 5 ± 1°C, frequency 0.1 Hz, 65 min) on the activities of proteinases, nontrypsin-like proteinases (NTLP), tripsininhibitory activity (TIA) α-1-proteinase inhibitor (α-1-PI) and α-2-macroglobulin (α-2-MG) in blood serum, tissues of the brain and internal organs in male rats with alcohol-dependent hypertension (ADH) by highly sensitive (10-9 – 10-10 g) enzymatic methods. ADH was modelled by chronic (for 10 months) alcoholization of rats by the «two-bottle» method. It was noted that ADH decreases the proteinases activity in tissues, maximally in the lungs, kidneys and heart (by 6, 7 and 10 times, respectively). RCEs promotes the proteinases activation, it is most pronounced in blood serum, kidneys and liver (20, 8 and 5 times, respectively), in intact rats – in the lungs (5 times). ADH decrease the NTLP activity in the liver by 10 times and less in the kidneys, which may be due to a violation of protein biosynthesis, and in the blood serum and brain tissues it increases, in the cerebral cortex by 10 times. RCEs promotes the NTLP activation, at ADH by 2-4 times, in the intact rats by 10 or more times. The ADH decreased the α-2-MG activity, it is most pronounced in the hypothalamus, lungs, kidneys by 100 times and less in the heart. RCEs promotes the α-2-MG activation: at ADH below the control level, in the intact rats – in the brain tissues and kidneys, which may be due to the participation of syn- and catatoxical adaptive mechanisms. The α-1-PI activity decreases at ADH and the background of RCEs, which is associated with a shift in the balance in the proteinase-proteinase inhibitor system. Thus, RCEs lead to reverse changes caused by ADH in rats, promote activation of proteinases, NTLP, α-2-MG, which is associated with the functioning of regulatory systems of the body, the development of hormesis, the formation of high resistance to external and internal stressors, expanding adaptive capabilities. At the same time, low TIA α-1-IP promotes activation of proteinases, NTLP.