S100 proteins in Corpora Amylacea from normal human brain

Citation
D. Hoyaux et al., S100 proteins in Corpora Amylacea from normal human brain, BRAIN RES, 867(1-2), 2000, pp. 280-288
Citations number
45
Categorie Soggetti
Neurosciences & Behavoir
Journal title
BRAIN RESEARCH
ISSN journal
00068993 → ACNP
Volume
867
Issue
1-2
Year of publication
2000
Pages
280 - 288
Database
ISI
SICI code
0006-8993(20000609)867:1-2<280:SPICAF>2.0.ZU;2-C
Abstract
Corpora amylacea (C.A.) also named polyglucosan bodies (P.B.) are one of th e hallmarks of normal brain aging. Although their functions are not yet cle ar. C.A. increase in number in patients suffering from neurodegenerative di seases. C.A. contain 88% of hexoses and 4% of proteins. Most of the protein s in C.A. are aging or stress proteins such as heat shock proteins, ubiquit inated proteins and advanced glycation end products which are also proinfla mmatory products. Stimulated by the potential rule played by some S100 prot eins in the inflammatory process which may be triggered in C.A., we investi gated, by immunohistochemistry, the presence of different S100 proteins (S1 00A1. S100A2, S100A3, S100A4, S100A5, S100A6, S100A8; S100A9, S100A12 and S 100B) in C.A; from normal human brain. Among the ten S100 proteins analyzed , nine (S100A) were detected in C.A. Three S100 proteins (S100A8, S100A9, S 100A12) which are highly expressed in activated macrophages and used as inf lammatory markers were detected in C.A. S100A8 was, in addition, found in t hick neuronal processes from the pens. One (S100B) could not be found in C. A. although it was highly expressed in astrocytes. In C.A.. the staining in tensity was estimated by computer-assisted microscopy and gave th; followin g order: S100A1 congruent to S100A8 congruent to S100A9>S1005 greater than or equal to S100A4>S100A12>S100A6>S100A2=S100A3. The potential inflammatory role-played by S100 proteins in C.A. is discussed. (C) 2000 Elsevier Scien ce B.V. All rights reserved.