TY - JOUR
T1 - Novel role of transglutaminase 1 in corpora amylacea formation?
AU - Wilhelmus, Micha M.M.
AU - Verhaar, Robin
AU - Bol, John G.J.M.
AU - van Dam, Anne Marie
AU - Hoozemans, Jeroen J.M.
AU - Rozemuller, Annemieke J.M.
AU - Drukarch, Benjamin
PY - 2011/5/1
Y1 - 2011/5/1
N2 - Corpora amylacea (CA) are both age and neurodegeneration-related spherical bodies, consisting of polymerized proteins, often thought to be involved in sequestration of hazardous products of cellular metabolism in brain. Although CA formation is associated with cellular stress, the process underlying their formation remains obscure. Transglutaminases (TGs) are stress associated enzymes that induce molecular cross-links, leading to polymerization of substrate proteins. TG expression and activity are elevated in Alzheimer's disease (AD) and Parkinson's disease (PD), and TG-catalyzed cross-links are present in their lesions. Considering the nature of CA, the aim of this study was to investigate the presence of TGs and TG cross-links in CA of healthy aging brain, AD and PD brain, using immunohistochemistry. We observed TG1 and TG cross-links in CA, together with typical cytoskeletal proteins. Furthermore, the presence of proteins associated with AD or PD pathogenesis was not altered in CA of disease brain compared to controls. We propose that TG1-catalyzed cross-linking and consequent polymerization of cytoskeletal and cytoskeleton-associated proteins may underlie CA formation.
AB - Corpora amylacea (CA) are both age and neurodegeneration-related spherical bodies, consisting of polymerized proteins, often thought to be involved in sequestration of hazardous products of cellular metabolism in brain. Although CA formation is associated with cellular stress, the process underlying their formation remains obscure. Transglutaminases (TGs) are stress associated enzymes that induce molecular cross-links, leading to polymerization of substrate proteins. TG expression and activity are elevated in Alzheimer's disease (AD) and Parkinson's disease (PD), and TG-catalyzed cross-links are present in their lesions. Considering the nature of CA, the aim of this study was to investigate the presence of TGs and TG cross-links in CA of healthy aging brain, AD and PD brain, using immunohistochemistry. We observed TG1 and TG cross-links in CA, together with typical cytoskeletal proteins. Furthermore, the presence of proteins associated with AD or PD pathogenesis was not altered in CA of disease brain compared to controls. We propose that TG1-catalyzed cross-linking and consequent polymerization of cytoskeletal and cytoskeleton-associated proteins may underlie CA formation.
KW - Aging
KW - Alzheimer's disease
KW - Corpora amylacea
KW - Parkinson's disease
KW - Protein cross-linking
KW - Transglutaminases
UR - http://www.scopus.com/inward/record.url?scp=79954608346&partnerID=8YFLogxK
U2 - 10.1016/j.neurobiolaging.2009.04.019
DO - 10.1016/j.neurobiolaging.2009.04.019
M3 - Article
C2 - 19464759
AN - SCOPUS:79954608346
SN - 0197-4580
VL - 32
SP - 845
EP - 856
JO - Neurobiology of Aging
JF - Neurobiology of Aging
IS - 5
ER -