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

S. Govoni, S. Bergamaschi, M. Racchi, F. Battaini, G. Binetti, A. Bianchetti, M. Trabucchi

Research output: Contribution to journalArticlepeer-review

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 β-amyloid precursor protein in AD.

Original languageEnglish
Pages (from-to)2581-2586
Number of pages6
JournalNeurology
Volume43
Issue number12
Publication statusPublished - Dec 1993

ASJC Scopus subject areas

  • Neuroscience(all)
  • Arts and Humanities (miscellaneous)
  • Clinical Neurology

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