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Alzheimer's disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact.
Author(s) -
Shivers B. D.,
Hilbich C.,
Multhaup G.,
Salbaum M.,
Beyreuther K.,
Seeburg P. H.
Publication year - 1988
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1988.tb02952.x
Subject(s) - biology , glycoprotein , disease , membrane glycoproteins , cell , microbiology and biotechnology , brain cell , neuroscience , alzheimer's disease , expression (computer science) , brain disease , biochemistry , medicine , computer science , programming language
The cloned cDNA encoding the rat cognate of the human A4 amyloid precursor protein was isolated from a rat brain library. The predicted primary structure of the 695‐amino acid‐long protein displays 97% identity to its human homologue shown previously to resemble an integral membrane protein. The protein was detected in rodent brain and muscle by Western blot analysis. Using in situ hybridization and immunocytochemistry on rat brain sections, we discovered that rat amyloidogenic glycoprotein (rAG) and its mRNA are ubiquitously and abundantly expressed in neurons indicating a neuronal original for the amyloid deposits observed in humans with Alzheimer's disease (AD). The protein appears in patches on or near the plasma membranes of neurons suggesting a role for this protein in cell contact. Highest expression was seen in rat brain regions where amyloid is deposited in AD but also in areas which do not contain deposits in AD. Since amyloid deposits are rarely observed in rat brain, we conclude that high expression of AG is not the sole cause of amyloidosis.