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Bu, Guojun

0000-0003-3491-1016

Mayo Clinic

Division of Life Science and State Key Laboratory of Nervous System Disorders, The Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China.

Citations 57

Modeling Neurodegenerative Microenvironment Using Cortical Organoids Derived from Human Stem Cells

Tissue Engineering Part A | January 24, 2018 | Volume: 24 | Issue: 13-14 | Pages: 1125-1137

10.1089/ten.tea.2017.0423 | PMID 29361890

Distinct spatiotemporal accumulation of N-truncated and full-length amyloid-β42 in Alzheimer’s disease

Brain | October 18, 2017 | Volume: 140 | Issue: 12 | Pages: 3301-3316

10.1093/brain/awx284 | PMID 29161341

Behavioral and transcriptomic analysis of Trem2-null mice: not all knockout mice are created equal

Human Molecular Genetics | October 10, 2017 | Volume: 27 | Issue: 2 | Pages: 211-223

10.1093/hmg/ddx366 | PMID 29040522

Progranulin-mediated deficiency of cathepsin D results in FTD and NCL-like phenotypes in neurons derived from FTD patients

Human Molecular Genetics | September 22, 2017 | Volume: 26 | Issue: 24 | Pages: 4861-4872

10.1093/hmg/ddx364 | PMID 29036611

Loss of clusterin shifts amyloid deposition to the cerebrovasculature via disruption of perivascular drainage pathways

Proceedings of the National Academy of Sciences | July 12, 2017 | Volume: 114 | Issue: 33 | Pages: No page available

10.1073/pnas.1701137114 | PMID 28701379

Significance Deposition of amyloid-β (Aβ) peptide in the form of parenchymal plaques and Aβ accumulation in the walls of cerebral vessels as cerebral amyloid angiopathy (CAA) are pathological hallmarks of Alzheimer’s disease (AD). The clusterin ( CLU ) gene, which confers AD risk, is associated with amyloid deposition. Here we show that loss of CLU promotes cerebrovascular CAA, yet significantly reduces the amount of parenchymal plaques by altering perivascular drainage of Aβ in the APP/PS1 mouse model of AD. The absence of CLU in these mice is associated with a lower number of hemorrhages and a decrease in inflammation. These results suggest that CLU functions as a major Aβ chaperone to maintain Aβ solubility along interstitial fluid drainage pathways and prevent CAA formation.
APOE ε4/ε4 diminishes neurotrophic function of human iPSC-derived astrocytes

Human Molecular Genetics | April 20, 2017 | Volume: 26 | Issue: 14 | Pages: 2690-2700

10.1093/hmg/ddx155 | PMID 28444230

Soluble TREM2 induces inflammatory responses and enhances microglial survival

Journal of Experimental Medicine | February 16, 2017 | Volume: 214 | Issue: 3 | Pages: 597-607

10.1084/jem.20160844 | PMID 28209725

Triggering receptor expressed on myeloid cells 2 (TREM2) is an innate immune receptor expressed in microglia in the brain. A soluble form of TREM2 (sTREM2) derived from proteolytic cleavage of the cell surface receptor is increased in the preclinical stages of AD and positively correlates with the amounts of total and phosphorylated tau in the cerebrospinal fluid. However, the physiological and pathological functions of sTREM2 remain unknown. Here, we show that sTREM2 promotes microglial survival in a PI3K/Akt-dependent manner and stimulates the production of inflammatory cytokines depending on NF-κB. Variants of sTREM2 carrying AD risk-associated mutations were less potent in both suppressing apoptosis and triggering inflammatory responses. Importantly, sTREM2 delivered to the hippocampi of both wild-type and Trem2-knockout mice elevated the expression of inflammatory cytokines and induced morphological changes of microglia. Collectively, these data indicate that sTREM2 triggers microglial activation inducing inflammatory responses and promoting survival. This study has implications for the pathogenesis of AD and provides insights into targeting sTREM2 pathway for AD therapy.
Rapid in vivo measurement of β-amyloid reveals biphasic clearance kinetics in an Alzheimer’s mouse model

Journal of Experimental Medicine | April 11, 2016 | Volume: 213 | Issue: 5 | Pages: 677-685

10.1084/jem.20151428 | PMID 27069115

Findings from genetic, animal model, and human studies support the observation that accumulation of the β-amyloid (Aβ) peptide in the brain plays a central role in the pathogenic cascade of Alzheimer’s disease (AD). Human studies suggest that one key factor leading to accumulation is a defect in brain Aβ clearance. We have developed a novel microimmunoelectrode (MIE) to study the kinetics of Aβ clearance using an electrochemical approach. This is the first study using MIEs in vivo to measure rapid changes in Aβ levels in the brains of living mice. Extracellular, interstitial fluid (ISF) Aβ levels were measured in the hippocampus of APP/PS1 mice. Baseline levels of Aβ40 in the ISF are relatively stable and begin to decline within minutes of blocking Aβ production with a γ-secretase inhibitor. Pretreatment with a P-glycoprotein inhibitor, which blocks blood–brain barrier transport of Aβ, resulted in significant prolongation of Aβ40 half-life, but only in the latter phase of Aβ clearance from the ISF.
Neuronal heparan sulfates promote amyloid pathology by modulating brain amyloid-β clearance and aggregation in Alzheimer’s disease

Science Translational Medicine | March 30, 2016 | Volume: 8 | Issue: 332 | Pages: No page available

10.1126/scitranslmed.aad3650 | PMID 27030596

Deleting neuronal heparan sulfates in a mouse model of Alzheimer’s disease results in faster Aβ clearance, reduced Aβ aggregation, and less amyloid pathology.
APOE2 eases cognitive decline during Aging: Clinical and preclinical evaluations

Annals of Neurology | March 2, 2016 | Volume: 79 | Issue: 5 | Pages: 758-774

10.1002/ana.24628 | PMID 26933942

ObjectiveApolipoprotein E (apoE), a major cholesterol carrier in the brain, is associated with a strong risk for Alzheimer disease. Compared to the risky APOE4 gene allele, the effects of the protective APOE2 gene allele are vastly understudied, and thus need to be further clarified.MethodsWe reviewed National Alzheimer's Coordinating Center clinical records and performed preclinical experiments using human apoE‐targeted replacement (apoE‐TR) mice, which do not show amyloid pathology.ResultsClinically, the APOE2 allele was associated with less cognitive decline during aging. This effect was also seen in subjects with little amyloid pathology, or after adjusting for Alzheimer disease‐related pathologies. In animal studies, aged apoE2‐TR mice also exhibited preserved memory function in water maze tests. Regardless, apoE2‐TR mice showed similar or greater age‐related changes in synaptic loss, neuroinflammation, and oxidative stress compared to apoE3‐TR or apoE4‐TR mice. Interestingly, apoE concentrations in the cortex, hippocampus, plasma, and cerebrospinal fluid (CSF) were positively correlated with memory performance across apoE isoforms, where apoE2‐TR mice had higher apoE levels. Moreover, apoE2‐TR mice exhibited the lowest levels of cholesterol in the cortex, despite higher levels in CSF and plasma. These cholesterol levels were associated with apoE levels and memory performance across apoE isoforms.InterpretationAPOE2 is associated with less cognitive decline during aging. This can occur independently of age‐related synaptic/neuroinflammatory changes and amyloid accumulation. Higher levels of apoE and associated cholesterol metabolism in APOE2 carriers might contribute to this protective effect. Ann Neurol 2016;79:758–774