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Leukocyte Lysosomal Enzymes in Alzheimer's Disease and Down's Syndrome

^a Departments of Chemistry and Biochemistry, School of Medicine, University of Zagreb, Croatia
^b Departments of Forensic Medicine and Criminology, School of Medicine, University of Zagreb, Croatia
^c University Department for Neurology, University Hospital "Sestre milosrdnice," Zagreb, Croatia
^d Neurological Institute, New York Presbyterian Hospital at Columbia University, New York

Svjetlana Kalanj-Bognar, Department of Chemistry and Biochemistry, School of Medicine, University of Zagreb, ©alata 3, 10000 Zagreb, Croatia E-mail: Svjetla{at}mamef.mef.hr.

Decision Editor: John Faulkner, PhD

Previous studies suggested the possibility of accelerated lysosomal degradation of brain gangliosides in Alzheimer's disease (AD). As AD pathology affects both neural and nonneural tissues, the aim of this study was to determine possible changes of glycosphingolipid metabolism in available peripheral cells in AD and Down's syndrome (DS). The activities of several lysosomal enzymes involved in catabolism of gangliosides and sulfatides were measured in leukocytes from subjects with dementia of the Alzheimer type, DS, and age-matched controls, by fluorimetry and spectrophotometry using specific substrates. The results showed a statistically significant increase of ß-galactosidase activity in both dementia of the Alzheimer type and DS leukocytes when compared with age-matched controls (p < .01 and p < .05, respectively; Student's t test). Not significantly increased activities of ß-galactosidase, ß-hexosaminidase, ß-hexosaminidase A, and slightly decreased activity of arylsulfatase A were observed in control leukocytes with aging. Our results indicate that a metabolic dysfunction and the acceleration of at least some lysosomal catabolic pathways are present in AD and DS nonneural cells.