GET THE APP

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Indexed in: ESCI (Thomson Reuters)

Abstract

Author(s):Filiz Eren, Nursel Turkmen Inan?r, Recep Fedakar, Bulent Eren, Murat Serdar Gurses, Mustafa Numan Ural, Sumeyya Akyol, Busra Aynekin and Kadir Demircan

Alzheimer’s disease (AD) is encountered as an important health problem. It was exposed that in the pathophysiology of AD, formation, and aggregation of amyloid β from amyloid precursor protein ( APP), was restrained by α-secretase group, ADAM (a disintegrin and metalloproteinase) enzymes. From this perspective, ADAM group of enzymes can be presumably used in the future both as a diagnostic marker, and potential treatment modality. In our study, 9 cases with or without AD in different age groups with various causes of death who were autopsied in the Bursa Morgue Department of the Council of Forensic Medicine of Turkey were included in the study. Tissue samples harvested from temporal regions of the brains of the cases were immunohistochemically stained with β-amyloid precursor protein (APP), ADAM9, ADAM10, and ADAM17. The specimens were evaluated as for distribution, and intensity of staining. The lowest mean distribution score of immunohistochemical staining (2.44) was detected for β-APP, and ADAM 9, while it was 3 for ADAM10. The highest distribution score (3.11) belonged to ADAM17. Our aim was to analyze histochemically cerebral β-APP and ADAM9, ADAM10, ADAM17 expressions in cases with and without a clinical diagnosis of Alzheimer’s disease. Based on their staining patterns, we revealed their characteristic features, compared our study results with those of the scarce number of studies in the literature, and despite our limited number of cases, we intended to contribute to the future studies.


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