Application of CLARITY to Investigate the 3D Architecture of 14-3-3 Zeta Protein in AD
International Journal of Biomedical Science and Engineering
Volume 5, Issue 6, December 2017, Pages: 68-71
Received: Dec. 5, 2017;
Published: Dec. 6, 2017
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Honghong Song, College of Life Science and Technology, University of Electronic Science and Technology of China, Chengdu, China
Juan Feng, College of Life Science and Technology, University of Electronic Science and Technology of China, Chengdu, China
Jian Li, College of Life Science, Beijing University of Chinese Medicine, Beijing, China
Yang Xia, College of Life Science and Technology, University of Electronic Science and Technology of China, Chengdu, China
Dezhong Yao, College of Life Science and Technology, University of Electronic Science and Technology of China, Chengdu, China
CLARITY (Clear Lipid–exchanged Acrylamide–hybridized Rigid Imaging/ Immunostaining/ in situ–hybridization–compatible Tissue hydrogel) is a powerful, innovative, whole brain-clearing technology, and it has been successfully combined with the immunofluorescence staining to achieve the 3D visualization of some proteins or cells in mm-thick brain tissue or even the intact brains. These 3D information help to gain deeper understanding on the pathologic mechanism of some neuronal diseases (for example Parkinson and Alzheimer). 14-3-3 zeta is a highly-expressed protein in Alzheimer’s disease (AD) brain, which was closely related with the formation of Tau aggregation and neurofibrillary tangles. However, little useful information has been available concerning the 3D architecture of 14-3-3 zeta in AD disease. In this paper, the transgenic AD mice were used and the 1mm-thick brain slices were passively clarified. Immunofluorescence staining results showed that different from the control group, 14-3-3 zeta was mainly present around the hippocampus in AD mice. Additionally, the morphology of 14-3-3 zeta protein was filamentous with different lengths. This result will be helpful for exploring the in vivo role of 14-3-3 zeta protein during the progression of AD.
Application of CLARITY to Investigate the 3D Architecture of 14-3-3 Zeta Protein in AD, International Journal of Biomedical Science and Engineering.
Vol. 5, No. 6,
2017, pp. 68-71.
Chung K, Wallace J, Kim SY, et al. Structural and molecular interrogation of intact biological systems. Nature, 2013, 497(7449): 332-337.
Dodt HU, Leischner U, Schierloh A, et al. Ultramicroscopy: three-dimensional visualization of neuronal networks in the whole mouse brain. Nat Methods., 2007, 4(4): 331-336.
Ertürk A, Becker K, Jährling N, et al. Three-dimensional imaging of solvent-cleared organs using 3DISCO. Nat Protoc., 2012, 7(11):1983-1995.
Hama H, Kurokawa H, Kawano H, et al. Sca/e: a chemical approach for fluorescence imaging and reconstruction of transparent mouse Brain. Nat Neurosci., 2011, 14(11): 1481-1488.
Ke MT, Fujimoto S, Imai T. See DB: a simple and morphology-preserving optical clearing agent for neuronal circuit reconstruction. Nat Neurosci. 2013., 16(8): 1154-1161.
Susaki EA, Tainaka K, Perrin D, Whole-brain imaging with single-cell resolution using chemical cocktails and computational analysis. Cell, 2014, 157(3): 726-739.
Chung K, Deisseroth K. CLARITY for mapping the nervous system. Nat Methods., 2013, 10: 508–513.
Chung K, Wallace J, Kim SY, et al. Structural and molecular interrogation of intact biological systems. Nature, 2013, 497: 332-337.
Bastrup J, Larson PH. Optimized CLARITY technique detects reduced parvalbumin density in a genetic model of schizophrenia. Journal of neuroscience methods, 2017, 283: 23-32.
Deisseroth K. Optical and chemical discoveries recognized for impact on biology and psychiatry. EMBO Reports, 2017, 18(6): 859-860.
Milgroom A, Ralston E. Clearing skeletal muscle with CLARITY for light microscopy imaging. Cell Biology International, 2016, 40(4): 478-483.
Muzumdar MD, Dorans KJ, Chung KM, et al. Clonal dynamics following p53 loss of heterozygosity in Kras-driven cancers. Nature Communications, 2016, 7: 12685.
Ding Y, Lee J, Ma J, et al. Light-sheet fluorescence imaging to localize cardiac lineage and protein distribution. Scientific Reports, 2017, 7: 42209. doi: 10.1038/srep42209.
Leuze C, Aswendt M, Ferenczi E, et al. The separate effects of lipids and proteins on brain MRI contrast revealed through tissue clearing. Neuro Image, 2017, 156: 412-422.
Syed AM, Wilhelm S, Glancy DR. Three-dimensional optical mapping of nanoparticle distribution in intact tissues. ACS Nano, 2016, 10(5): 5468-5478.
Ando K, Laborde Q, Lazar A, et al. Inside Alzheimer brain with CLARITY: senile plaques, neurofibrillary tangles and axons in 3-D. Acta Neuropathol., 2014, 28(3): 457-459.
Liu AK, Hurry ME, Ng OT et al. Bringing CLARITY to the human brain: visualization of Lewy pathology in three dimensions. Neuropathology and applied neurobiology, 2016, 42: 573-587.
Matta A, Siu KW, Ralhan R. 14-3-3 zeta as novel molecular target for cancer therapy. Expert Opin ther Targets., 2012, 16(5): 515-523.
Toyo-oka K, Wachi T, Hunt RF, et al. 14-3-3 ε and ζ regulate neurogenesis and differentiation of neuronal progenitor cells in the developing brain. J Neurosci., 2014, 34(36): 12168-12181.
Ding H, Underwood R, Lavalley N, et al. 14-3-3 inhibition promotes dopaminergic neuron loss and 14-3-3 theta overexpression promotes recovery in the MPTP mouse model of Parkinson's disease. Neuroscience, 2015, 307: 73-82.
Omi K, Hachiya NS, Tanaka M, et al. 14-3-3 zeta is indispensable for aggregate formation of polyglutamine-expanded huntingtin protein. Neurosci Lett., 2008, 24(431): 45-50.
Qureshi HY, Li T, MacDonald R et al. Interaction of 14-3-3 zeta with microtubule-associated protein tau within Alzheimer's disease neurofibrillary tangles, Biochemistry, 2013, 52: 6445-6455.
Boston PF, Jackson P, Kynoch PA, Thompson RJ. Purification, properties, and immunohistochemical localisation of human brain 14-3-3 protein. J Neurochem., 1982, 38(5): 1466-1474.