Key result
Cryoactivation of human plasma at -5°C for 4 days increased renin activity, which strongly correlated with trypsin-induced activation (r=0.88, P<0.001), suggesting mediation by a trypsin-like enzyme.
Effect estimate: r = 0.88
p-value: p=<0.001
Cryoactivation of plasma renin appears to be mediated by a trypsin-like serine enzyme that destroys an inhibitor of the renin-renin substrate reaction.
May artifactually elevate renin activity in stored plasma samples; leaves open the enzyme's physiological role in vivo.
The mechanism of increased renin activity after human plasma had been kept at -5 degrees C for 4 days (cryoactivation) was investigated. 2. The increase in renin activity of human plasma by cryoactivation was closely correlated to the increase obtained by incubation with trypsin (r = 0.88, P less than 0.001, n = 10). 3. An inhibitor of thiol enzyme, N-ethylmaleimide did not inhibit cryoactivation. 4. Soyabean trypsin inhibitor and di-isopropylflurophosphate (DFP) inhibited cryoactivation, suggesting that the cryoactivation may be due to the action of a trypsin-like serine enzyme. 5. In an experiment in the rat haemorrhagic shock caused parallel and cryoactivated plasma, the renin activity being about two times higher in the latter. No significant differences were found in the concentrations of renin and renin substrate between the non-cryoactivated and cryoactivated plasma samples. 6. The results may indicate that a destruction of an inhibitor of the renin-renin substrate reaction is responsible for the increase of renin activity after exposure of rat plasma to low temperature. A trypsin-like enzyme in plasma might have destroyed the inhibitor during this procedure.
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Hara et al. (1978) studied this question. Cryoactivation vs. Non-cryoactivated plasma was evaluated on Increase in renin activity (r = 0.88, p=<0.001). Cryoactivation of human plasma at -5°C for 4 days increased renin activity, which strongly correlated with trypsin-induced activation (r=0.88, P<0.001), suggesting mediation by a trypsin-like enzyme.
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