Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Postmortem Changes”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 127 records · Page 7Linked to original sources
PubMedDate not supplied

Postmortem changes in the phosphorylation state of tau-protein in the rat brain.

The phosphorylation state of tau-protein is crucial for the regulation of neuronal microtubule organization. Functional conclusions on tau-protein require an accurate assessment of phosphorylated sites. Therefore, the in vivo distribution and postmortem preservation of some phospho-epitopes on tau-protein were examined in the rat brain under different fixation and preparation conditions. Detection of tau-protein with a phosphorylation-independent antiserum revealed both axonal and somatodendritic localizations, which were not influenced by a postmortem interval of 30 min. The phospho-epitopes recognized by 12E8, AT8, and PHF-1 were mainly localized in the somatodendritic compartment. The binding sites of AT8 and PHF-1 were rapidly dephosphorylated postmortem, whereas the Tau-1 epitope was unmasked in the somatodendritic region. The axonally located phospho-epitope of AT270 and the nuclear epitope of AT100 were still detectable after a postmortem interval of 30 min. Postmortem dephosphorylation and inhibition of this process by PP1 and/or PP2A was further demonstrated on Western blot. In conclusion, rapid processing of tau-protein is essential for the correct assessment of investigations on phospho-isoforms.

Animals↗
PubMed1984

Quantitative analysis of postmortem changes in myocardial norepinephrine using HPLC with electrochemical detection.

Myocardial adrenergic function may be important in the pathophysiology of many cardiac abnormalities, and quantitative analysis of catecholamines in cardiac tissue can provide insight in the role of adrenergic neurons in specific disorders. Our purpose was to determine the stability of myocardial catecholamines postmortem to assess the validity of using postmortem samples to represent premorbid conditions and to provide information applicable to proper handling of biopsy specimens. Serial myocardial samples were obtained postmortem in rats and dogs for which norepinephrine and dopamine levels were analyzed using high-pressure liquid chromatography with electrochemical detection. No significant differences in catecholamine content were found between samples taken immediately after death and those taken 15 minutes later. Thereafter, a progressive decline in catecholamines was observed. We conclude that biopsy or postmortem samples frozen within 15 minutes of death will accurately reflect premortem catecholamine values.

Animals↗
PubMed1994

Postmortem changes in the levels and localization of microtubule-associated proteins (tau, MAP2 and MAP1B) in the rat and human hippocampus.

The neuronal cytoskeleton is disrupted in neurodegenerative disorders such as Alzheimer's disease. Due to the lack of suitable animal models, studies examining the events involved in the neurodegeneration have relied on postmortem human brain tissue obtained from individuals with the disease and from normal controls. However, it is uncertain if the neuronal cytoskeleton is stable during the postmortem interval. Immunohistochemistry and immunoblots were used to examine the microtubule-associated proteins tau, MAP2, and MAP1B in the rat hippocampus at various times after death. Shortly after death, tau immunoreactivity was lost from axons and accumulated in somatodendritic compartments. MAP2 and MAP1B also accumulated in neuronal cell bodies prior to a loss of immunostaining in some regions, notably subiculum. Immunoblots confirmed a loss of MAP2 and MAP1B within a few hours after death. Tau levels remained constant during the 8-hour postmortem interval examined, although the electrophoretic mobility of some tau bands was altered. Human brain tissue obtained at autopsy and at surgery demonstrated similar cytoskeletal alterations in postmortem tissue. These results demonstrate that microtubules and associated proteins are not stable postmortem.

Adolescent↗
PubMedDate not supplied

[Maggot-induced postmortem changes simulating gunshot wounds].

In the warm season, human cadavers often are the breeding ground of fly larvae. In special conditions, the damage by maggots can take on the appearance of bullet holes. Preexisting injuries allow the maggots to penetrate the skin also in parts other than the body apertures commonly infested. Round tissue damage similar to gunshot-wounds are favored by the fact that the larvae of some types of flies bundle together to form feeding communities. The enzymes from the salivary glands of the fly larvae may in some rare instances even lead to perforation of bone lamellae (e.g. in the region of the orbital roofs). The case reports deal with 2 cases in which changes due to damage by maggots primarily gave the impression of gunshot-wounds.

Adult↗
PubMedDate not supplied

Fluorophotometric studies on postmortem changes in porcine corneal endothelial barrier functions.

Using an in vitro fluorophotometric technique, we studied the effect of postmortem storage duration on the endothelial barrier function of porcine corneas. A marked decay in endothelial barrier function was demonstrated that correlated with duration of storage. This decay appears to be nearly complete after 2 weeks of storage. This loss of barrier function correlated grossly with ultrastructural changes demonstrated on scanning electron microscopy.

Animals↗