TY - JOUR
T1 - Exploring the elusive composition of corpora amylacea of human brain
AU - Augé, Elisabet
AU - Duran, Jordi
AU - Guinovart, Joan J.
AU - Pelegrí, Carme
AU - Vilaplana, Jordi
N1 - Funding Information:
This study was funded by grants BFU2013-47382-P, BFU2016-78398-P and BFU2017-84345-P awarded by the Spanish Ministerio de Economía y Competitividad (MINECO), by Agencia Estatal de Investigación (AEI) and by European Regional Development Funds and by the Centros de Investigación Biomédica en Red (CIBER) at the Instituto de Salud Carlos III. We thank the Generalitat de Catalunya for funding our research group (2017/ SGR625). E. Augé received the pre-doctoral Ajuts de Personal Investigador en Formació fellowship from the Universitat de Barcelona (APIF-UB). We are indebted to the IDIBAPS Biobank for sample and data procurement, especially to Laura Molina and Teresa Ximelis for their advice. We are sincerely grateful to Lídia Bardia, from the Advanced Digital Microscopy of the Institute for Research in Biomedicine - IRB Barcelona, for her help in the confocal studies, and to Michael Maudsley and Tanya Yates for correcting the English version of the manuscript.
Publisher Copyright:
© 2018, The Author(s).
PY - 2018/12/1
Y1 - 2018/12/1
N2 - Corpora amylacea (CA) are polyglucosan bodies that accumulate in the human brain during ageing and are also present in large numbers in neurodegenerative conditions. Theories regarding the function of CA are regularly updated as new components are described. In previous work, we revealed the presence of some neo-epitopes in CA and the existence of some natural IgM antibodies directed against these neo-epitopes. We also noted that these neo-epitopes and IgMs were the cause of false staining in CA immunohistochemical studies, and disproved the proposed presence of β-amyloid peptides and tau protein in them. Here we extend the list of components erroneously attributed to CA. We show that, contrary to previous descriptions, CA do not contain GFAP, S100, AQP4, NeuN or class III β-tubulin, and we question the presence of other components. Nonetheless, we observe that CA contains ubiquitin and p62, both of them associated with processes of elimination of waste substances, and also glycogen synthase, an indispensable enzyme for polyglucosan formation. In summary, this study shows that it is imperative to continue reviewing previous studies about CA but, more importantly, it shows that the vision of CA as structures involved in protective or cleaning mechanisms remains the most consistent theory.
AB - Corpora amylacea (CA) are polyglucosan bodies that accumulate in the human brain during ageing and are also present in large numbers in neurodegenerative conditions. Theories regarding the function of CA are regularly updated as new components are described. In previous work, we revealed the presence of some neo-epitopes in CA and the existence of some natural IgM antibodies directed against these neo-epitopes. We also noted that these neo-epitopes and IgMs were the cause of false staining in CA immunohistochemical studies, and disproved the proposed presence of β-amyloid peptides and tau protein in them. Here we extend the list of components erroneously attributed to CA. We show that, contrary to previous descriptions, CA do not contain GFAP, S100, AQP4, NeuN or class III β-tubulin, and we question the presence of other components. Nonetheless, we observe that CA contains ubiquitin and p62, both of them associated with processes of elimination of waste substances, and also glycogen synthase, an indispensable enzyme for polyglucosan formation. In summary, this study shows that it is imperative to continue reviewing previous studies about CA but, more importantly, it shows that the vision of CA as structures involved in protective or cleaning mechanisms remains the most consistent theory.
UR - http://www.scopus.com/inward/record.url?scp=85053205029&partnerID=8YFLogxK
U2 - 10.1038/s41598-018-31766-y
DO - 10.1038/s41598-018-31766-y
M3 - Article
C2 - 30202002
AN - SCOPUS:85053205029
SN - 2045-2322
VL - 8
JO - Scientific Reports
JF - Scientific Reports
IS - 1
M1 - 13525
ER -