This Article  • References  • Full text PDF  • Reply to article  • Send to a friend  • Save in My Folder  • Save to citation manager  • Permissions  Citing Articles  • Citation map  • Citing articles on HighWire  • Contact me when this article is cited  Related Content  • Similar articles in this journal  Social Bookmarking   What's this?

Tuan Van Huynh; Gregory Cole, PhD; Robert Katzman, MD; Kuo-Ping Huang, PhD; Tsunao Saitoh, PhD

Arch Neurol. 1989;46(11):1195-1199.

Abstract
• Abnormal protein kinase C levels and protein kinase C-dependent phosphorylation are biochemical alterations in brain tissue obtained from patients with Alzheimer's disease. Because many biochemical and biophysical abnormalities are found in peripheral tissues of patients with Alzheimer's disease, we studied protein kinase C levels and the in vitro phosphorylation of proteins under protein kinase C-activating conditions in fibroblasts derived from patients with Alzheimer's disease. The concentration of protein kinase C-like immunoreactivity was reduced in Alzheimer's disease samples, although the protein kinase C activity determined by the phosphorylation of exogenous histone was not. The degree of in vitro phosphorylation of an Mr 79000 protein in the presence of protein kinase C activators was less in Alzheimer's disease than in control fibroblast cytosol, and a reduction was more prominent in cases of familial Alzheimer's disease than in sporadic Alzheimer's disease. Therefore, the aberrant phosphorylation mediated by protein kinase C is found not only in the brain but also in fibroblasts.

Author Affiliations
From the Department of Neurosciences, School of Medicine (M-024), and Center for Molecular Genetics, University of California San Diego, La Jolla (Drs Huynh, Cole, Katzman, and Saitoh); and the Section of Metabolic Regulation, Endocrinology and Reproduction Research Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Md (Dr Huang).

Footnotes
Accepted for publication March 13, 1989.

Reprint requests to Department of Neurosciences, School of Medicine (M-024), University of California San Diego, La Jolla, CA 92093 (Dr Saitoh).

CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter     What's this?

THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES

An internally controlled peripheral biomarker for Alzheimer's disease: Erk1 and Erk2 responses to the inflammatory signal bradykinin
Khan and Alkon
Proc. Natl. Acad. Sci. USA 2006;103:13203-13207.
ABSTRACT | FULL TEXT  

Proteolytic imbalance in Alzheimer fibroblasts as potential pathological trait of disease
Paoletti and Tombaccini
FASEB J. 1998;12:925-927.
FULL TEXT  

Alzheimer's-specific effects of soluble beta -amyloid on protein kinase C-alpha and -gamma degradation in human fibroblasts
Favit et al.
Proc. Natl. Acad. Sci. USA 1998;95:5562-5567.
ABSTRACT | FULL TEXT  

Peripheral markers in testing pathophysiological hypotheses and diagnosing Alzheimer's disease
Gasparini et al.
FASEB J. 1998;12:17-34.
ABSTRACT | FULL TEXT  

Expression of 'Alzheimer Antigens' in Cultured Skin Fibroblasts
Blass et al.
Arch Neurol 1991;48:709-717.
ABSTRACT  

Induction of Alzheimer Antigens by an Uncoupler of Oxidative Phosphorylation
Blass et al.
Arch Neurol 1990;47:864-869.
ABSTRACT