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    A case of adult-onset metachromatic leukodystrophy beginning with behavioral symptoms
    (Klinik Psikiyatri Dergisi, 2023) Tunali, Cemile Hazan; Unal, Sueheyla; Acar, Ceren; Ozer, Emel Saglar
    Metachromatic leukodystrophy is a rare inherited disor-der of the nervous system with great clinical variability characterized by loss of both cognitive and motor func-tions upon extensive white matter damage by the accu-mulation of sulfatides. Although metachromatic leukodystrophy usually affects children, many cases of adult leukodystrophy have been reported in the litera-ture in the last few years. Adult-onset leukodystrophy typically presents with a progressive syndrome that includes various combinations of cognitive impairment, spasticity, apraxia, ataxia, and upper motor neuron ma-nifestations. In this article, we decided to present this case to draw attention to the fact that the adult form of metachromatic leukodystrophy, which presents with psychotic symptoms and behavioural problems, should be considered in the differential diagnosis of psychotic pictures. In a 48-year-old male patient who did not have any psychiatric or neurological problems before, symp-toms such as meaningless shouting, running away from home, restlessness, and audio-visual hallucinations were added to the clinical picture that started with confusion and disorganized behaviour in a short time. MRI, plasma aryl sulfatase A level (ARSA) and gene analysis were per-formed for differential diagnosis in the patient. It is known that the patient has a sibling who died before the age of one, and two nephews diagnosed with an autism spectrum disorder. Heterozygous c.1283C>A (p P428Q) mutation was detected in the patient, which was not previously reported in the literature or mutation databases. The chromosomal region -22q13.33-in which the ARSA gene with this mutation is located is also a can-didate region for autism. In this respect, it was thought that this mutation might be related to disorganized behavioural problems.
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    Investigation of Fibrillar Aggregates Formed by Pathogenic Pre-pro-vasopressin Mutants that Cause ADNDI
    (Endocrine Soc, 2025) Vaizoglu, Refika Dilara; Erdem, Beril; Gul, Mehmet; Acar, Ceren; Ozdemirel, Huseyin Ozgur; Ozer, Emel Saglar; Mergen, Hatice
    Context: Aggregations of unfolded or misfolded proteins, both inside and outside cells, are implicated in numerous diseases, collectively known as amyloidosis. Particularly, autosomal dominant neurohypophyseal diabetes insipidus (ADNDI) is a rare disease caused by mutations in the AVPNPII gene, leading to the inability to secrete arginine vasopressin. These misfolded proteins accumulate within the endoplasmic reticulum (ER), causing cellular dysfunction. Objective: This study aimed to investigate the formation of amyloid-like aggregates within the cell resulting from misfolded mutant precursor proteins, which induce disulfide-linked oligomers due to the G45C, 207_209delGGC, G88V, C98X, C104F, E108D-1, E108D-2 and R122H mutations identified by our group in the AVP-NPII gene of ADNDI patients. Methods: Deglycosylation studies were performed to analyze the glycosylation patterns of mutant protein precursors. The involvement of these precursors in the ER-related degradation pathway was studied by conducting protease inhibition experiments. Disulfide-linked oligomer analysis determined the oligomerization status of the mutant precursors. Immunofluorescence and electron microscopy studies provided evidence of aggregate structures in the ER lumen. In vitro studies involved bacterial expression and fibril formation in Escherichia coli (E. coli). Results: Our findings demonstrated that the N-glycan structure of mutant precursors remains intact within the ER. Protease inhibition experiments indicated the involvement of these precursors in the ER-related degradation pathway. Disulfide-linked oligomer analysis revealed homo-oligomer structures in mutations. Immunofluorescence and electron microscopy studies confirmed the presence of aggregate structures in the ER lumen. In vitro studies showed that mutant precursors could form fibril structures in E. coli. Conclusion: Our study may support the idea that ADNDI belongs to the group of neurodegenerative diseases due to the formation of fibrillar amyloid aggregates in the cell.