PubMed · 4769323
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F M Foote. 1973. Death from a caustic detergent.. https://pubmed.ncbi.nlm.nih.gov/4769323/
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The purpose of this article is to describe a protocol that provides suggestions and guides the clinical practice of writing cause-of-death statements for death certificates, autopsy reports, and other medical documents. The 16 members of the Autopsy Committee of the College of American Pathologists (CAP), Northfield, Ill, were appointed by the CAP officers based on demonstrated interest and expertise in autopsy performance and reporting. The committee perceived a need for specific instructions aimed at promoting consistency, accuracy, and completeness when writing cause-of-death statements. Development of a protocol was supported by CAP after approval by the CAP board of governors. The framework for the protocol was based on recommendations of the National Center for Health Statistics, Hyattsville, Md, with additional concepts added by the autopsy committee. The protocol for writing cause-of-death statements for natural causes is expected to foster consistency, accuracy, and completeness in the writing of cause-of-death statements. The quality of individual death certificates, autopsy reports, and national mortality data may improve through protocol usage. Application of the protocol principles should impose no ongoing costs at any user level because no new products or personnel are required for its application.
The multifunctional mammalian apurinic/apyrimidinic endonuclease (APE) is responsible for the repair of apurinic/apyrimidinic sites in DNA. In addition, this enzyme has been shown to function as a redox factor facilitating the DNA-binding capability of JUN and FOS, as well as numerous other transcription factors through the alteration of the transcription factor redox state. Biochemical studies of organ homogenates have shown that APE is present in the different tissues studied at similar concentrations. The present study examines the immunohistochemical distribution of APE in several organs and demonstrates new and unexpected patterns of cellular and subcellular localization of this enzyme. In the hippocampus, the APE protein was highly expressed in neurons of the dentate gyrus and regions CA3 and CA4, and unexpectedly, the staining was primarily cytoplasmic. AP endonuclease immunoreactivity in the cerebellum was found in the granule and Purkinje cells, both cytoplasmic and nuclear. APE staining of the hypoglossal nucleus of the brainstem, where motor neurons that control tongue movement reside, showed reactivity in the cytoplasmic Nissl substance. Skin, liver, and duodenum demonstrated nuclear staining; however, in the duodenum, only the enterocyte nuclei of the proximal villus and the crypts of Lieberkuhn were stained, with no staining of the distal villus. These results suggest that APE has different regulatory and functional roles in different cells and organs of the body. This study shows the importance of correlating in vitro findings in tissue culture cells with the organism as a whole. The cytoplasmic staining seen in parts of the brain and in liver suggests that there may be additional functions for the APE yet to be described.