Premium
Differential distribution of laminins in Alzheimer disease and normal human brain tissue
Author(s) -
Palu Edouard,
Liesi Päivi
Publication year - 2002
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.10292
Subject(s) - laminin , senile plaques , pathology , neurite , white matter , grey matter , biology , alzheimer's disease , human brain , immunocytochemistry , astrocyte , neuroscience , microbiology and biotechnology , medicine , disease , central nervous system , extracellular matrix , biochemistry , in vitro , magnetic resonance imaging , radiology
Immunocytochemistry, Western blotting, and RT‐PCR were used to identify the isoforms of laminin expressed in the Alzheimer disease, but not in normal human brain tissue. We found that α1 laminin was heavily over‐expressed in Alzheimer disease frontal cortex, and localized in reactive astrocytes of the grey and white matter, and as punctate deposits in the senile placques of the Alzheimer brain tissue. Antibodies against the C‐terminal neurite outgrowth domain of the γ1 laminin demonstrated expression of the γ1 laminin in GFAP‐immunoreactive reactive astrocytes of the Alzheimer disease frontal cortex. The γ1 laminin was also heavily over‐expressed in reactive astrocytes of both grey and white matter. Although antibodies against the C‐terminal neurite outgrowth domain failed to localize γ1 laminin in senile plaques, antibodies against the N‐terminal domains of the γ1 laminin demonstrated γ1 laminin as punctate deposits in the senile plaques. The present results indicate that enhanced and specialized expression patterns of α1 and γ1 laminins distinctly associate these two laminins with the Alzheimer disease. The fact that domain specific antibodies localize both α1 and γ1 laminins in the senile plaques as punctate deposits and in astrocytes of both the gray and white matter indicate that these laminins and their specific domains may have distinct functions in the pathophysiology of the Alzheimer disease. © 2002 Wiley‐Liss, Inc.