Literature DB >> 10837826

S100 proteins in Corpora amylacea from normal human brain.

D Hoyaux1, C Decaestecker, C W Heizmann, T Vogl, B W Schäfer, I Salmon, R Kiss, R Pochet.   

Abstract

Corpora amylacea (C.A.) also named polyglucosan bodies (P.B.) are one of the hallmarks of normal brain aging. Although their functions are not yet clear, C.A. increase in number in patients suffering from neurodegenerative diseases. C.A. contain 88% of hexoses and 4% of proteins. Most of the proteins in C.A. are aging or stress proteins such as heat shock proteins, ubiquitinated proteins and advanced glycation end products which are also proinflammatory products. Stimulated by the potential role played by some S100 proteins in the inflammatory process which may be triggered in C.A., we investigated, by immunohistochemistry, the presence of different S100 proteins (S100A1, S100A2, S100A3, S100A4, S100A5, S100A6, S100A8, S100A9, S100A12 and S100B) 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, S100A12) which are highly expressed in activated macrophages and used as inflammatory markers were detected in C.A. S100A8 was, in addition, found in thick neuronal processes from the pons. One (S100B) could not be found in C.A. although it was highly expressed in astrocytes. In C.A., the staining intensity was estimated by computer-assisted microscopy and gave the following order: S100A1 congruent withS100A8 congruent with S100A9>S100A5> or =S100A4>S100A12>S100A6> S100A2=S100A3. The potential inflammatory role played by S100 proteins in C.A. is discussed.

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Year:  2000        PMID: 10837826     DOI: 10.1016/s0006-8993(00)02393-3

Source DB:  PubMed          Journal:  Brain Res        ISSN: 0006-8993            Impact factor:   3.252


  24 in total

1.  Localization of blood proteins thrombospondin1 and ADAMTS13 to cerebral corpora amylacea.

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2.  Characterization of corpora amylacea glycoconjugates in normal and hyperplastic glands of human prostate.

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3.  S100A6 amyloid fibril formation is calcium-modulated and enhances superoxide dismutase-1 (SOD1) aggregation.

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4.  Acute inflammatory proteins constitute the organic matrix of prostatic corpora amylacea and calculi in men with prostate cancer.

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5.  S100 protein family and its application in clinical practice.

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Review 8.  Epigenetic approaches to psychiatric disorders.

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Review 9.  Eosinophils in glioblastoma biology.

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10.  Aggregation of human S100A8 and S100A9 amyloidogenic proteins perturbs proteostasis in a yeast model.

Authors:  Ekaterina Eremenko; Anat Ben-Zvi; Ludmilla A Morozova-Roche; Dina Raveh
Journal:  PLoS One       Date:  2013-03-06       Impact factor: 3.240

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