We attempted to determine whether changes in protein kinase C (PKC) activity in Alzheimer's disease (AD) brains are also present in cultured skin fibroblasts from living patients. Biopsies collected from shoulder skin were transferred to culture plates with an appropriate growth medium, and histone-directed PKC activity as well as phorbol ester binding were individually determined in soluble and particulate fractions prepared from AD and non-AD fibroblast cell lines. Binding experiments indicated that PKC was unevenly distributed between cytosol (78%) and particulate (22%). The Bmax values for phorbol ester binding in soluble and particulate fractions were similar in AD and non-AD patients. Kd values in the cytosol were 94% higher in AD patients, indicating lower affinity of the enzyme for the ligand. Accordingly, the soluble PKC activity was 30% lower in AD patients. The data suggest that the changes in PKC phosphorylating activity represent a diffuse cellular defect in AD and are not confined to the brain. The alterations of the enzyme may participate in the disregulation in processing of beta-amyloid precursor protein in AD.

Govoni, S., Bergamaschi, S., Racchi, M., Battaini, F.m., Binetti, G., Bianchetti, A., et al. (1993). Cytosol protein kinase C downregulation in fibroblasts from Alzheimer's disease patients. NEUROLOGY, 43(12), 2581-2586.

Cytosol protein kinase C downregulation in fibroblasts from Alzheimer's disease patients

BATTAINI, FIORENZO MARIA;TRABUCCHI, MARCO MARIO
1993-12-01

Abstract

We attempted to determine whether changes in protein kinase C (PKC) activity in Alzheimer's disease (AD) brains are also present in cultured skin fibroblasts from living patients. Biopsies collected from shoulder skin were transferred to culture plates with an appropriate growth medium, and histone-directed PKC activity as well as phorbol ester binding were individually determined in soluble and particulate fractions prepared from AD and non-AD fibroblast cell lines. Binding experiments indicated that PKC was unevenly distributed between cytosol (78%) and particulate (22%). The Bmax values for phorbol ester binding in soluble and particulate fractions were similar in AD and non-AD patients. Kd values in the cytosol were 94% higher in AD patients, indicating lower affinity of the enzyme for the ligand. Accordingly, the soluble PKC activity was 30% lower in AD patients. The data suggest that the changes in PKC phosphorylating activity represent a diffuse cellular defect in AD and are not confined to the brain. The alterations of the enzyme may participate in the disregulation in processing of beta-amyloid precursor protein in AD.
dic-1993
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/14
English
Con Impact Factor ISI
Male; Aged, 80 and over; Protein Kinase C; Female; Cytosol; Aged; Skin; Alzheimer Disease; Phorbol 12,13-Dibutyrate; Fibroblasts; Humans
Govoni, S., Bergamaschi, S., Racchi, M., Battaini, F.m., Binetti, G., Bianchetti, A., et al. (1993). Cytosol protein kinase C downregulation in fibroblasts from Alzheimer's disease patients. NEUROLOGY, 43(12), 2581-2586.
Govoni, S; Bergamaschi, S; Racchi, M; Battaini, Fm; Binetti, G; Bianchetti, A; Trabucchi, Mm
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/51562
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