TY - JOUR
T1 - Calcyclin binding protein and Siah-1 interacting protein in Alzheimer's disease pathology
T2 - neuronal localization and possible function
AU - Wasik, Urzula
AU - Schneider, Gabriela
AU - Mietelska-Porowska, Ann
AU - Mazurkiewicz, Marcin
AU - Fabczak, Hanna
AU - Weis, Serge
AU - Zabke, Claudia
AU - Harrington, Charles Robert
AU - Filipek, Anna
AU - Niewiadomska, Grazyna
PY - 2013/5
Y1 - 2013/5
N2 - The calcyclin binding protein and Siah-1 interacting protein (CacyBP/SIP) protein was shown to play a role in the organization of microtubules. In this work we have examined the neuronal distribution and possible function of CacyBP/SIP in cytoskeletal pathophysiology. We have used brain tissue from Alzheimer’s disease (AD) patients and from transgenic mice modeling 2 different pathologies characteristic for AD: amyloid and tau. In the brain from AD patients, CacyBP/SIP was found to be almost exclusively present in neuronal somata, and in control patients it was seen in the somata and neuronal processes. In mice doubly transgenic for amyloid precursor protein and presenilin 1 there was no difference in CacyBP/SIP neuronal localization in comparison with the nontransgenic animals. By contrast in tau transgenic mice, localization of CacyBP/SIP was similar to that observed for AD patients. To find the relation between CacyBP/SIP and tau we examined dephosphorylation of tau by CacyBP/SIP. We found that indeed it exhibited phosphatase activity toward tau. Altogether, our results suggest that CacyBP/SIP might play a role in AD pathology.
AB - The calcyclin binding protein and Siah-1 interacting protein (CacyBP/SIP) protein was shown to play a role in the organization of microtubules. In this work we have examined the neuronal distribution and possible function of CacyBP/SIP in cytoskeletal pathophysiology. We have used brain tissue from Alzheimer’s disease (AD) patients and from transgenic mice modeling 2 different pathologies characteristic for AD: amyloid and tau. In the brain from AD patients, CacyBP/SIP was found to be almost exclusively present in neuronal somata, and in control patients it was seen in the somata and neuronal processes. In mice doubly transgenic for amyloid precursor protein and presenilin 1 there was no difference in CacyBP/SIP neuronal localization in comparison with the nontransgenic animals. By contrast in tau transgenic mice, localization of CacyBP/SIP was similar to that observed for AD patients. To find the relation between CacyBP/SIP and tau we examined dephosphorylation of tau by CacyBP/SIP. We found that indeed it exhibited phosphatase activity toward tau. Altogether, our results suggest that CacyBP/SIP might play a role in AD pathology.
KW - Alzheimer's disease (AD) CacyBP/SIP S100A6 Amyloidosis Tau mice Phosphatase activity
U2 - 10.1016/j.neurobiolaging.2012.11.007
DO - 10.1016/j.neurobiolaging.2012.11.007
M3 - Article
SN - 0197-4580
VL - 34
SP - 1380
EP - 1388
JO - Neurobiology of Aging
JF - Neurobiology of Aging
IS - 5
ER -