The study demonstrates that key enzymes in the rat striatum remain stable postmortem, suggesting that their kinetic parameters can be reliably investigated in human brain tissue obtained postmortem.
Answers are grounded in this paper and cite their sources.
Supports postmortem human striatal enzyme assays; leaves open validation in clinical autopsy cohorts.
The stability of dopamine-sensitive adenylate cyclase, guanylate cyclase, ATPase, and GTPase was measured in homogenates of rat striatal tissue frozen from 0 to 24 h postmortem. ATPase, GTPase, and Mg2+-dependent guanylate cyclase activities showed no significant change over this period. Mn2+-dependent guanylate cyclase activity was stable for 10 h postmortem. Basal and dopamine-stimulated adenylate cyclase activity decreased markedly during the first 5 h. However, when measured in washed membrane preparations, these adenylate cyclase activities remained stable for at least 10 h. Therefore, the postmortem loss of a soluble activator, such as GTP, may decrease the adenylate cyclase activity in homogenates. These results are not consistent with an earlier suggestion that there is a postmortem degradation of the enzyme itself. Other kinetic parameters of dopamine-sensitive adenylate cyclase can also be measured independently of postmortem changes. Thus, it is possible to investigate kinetic parameters of dopamine-sensitive adenylate cyclase, guanylate cyclase, ATPase, and GTPase in human brain obtained postmortem.
No takes yet. Share an insight, caveat, or question.
Nicol et al. (1981) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: