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Terzioglu, G.

Publications and source records attributed to Terzioglu, G..

5 recordsLinked to original sources

The Alzheimer's disease risk gene ABCA7 regulates microglial lysosomal and lipid homeostasis and promotes phagocytosis to maintain neuronal health

Background: Loss of function mutations in the lipid transporter ABCA7 have been linked to increased risk for late onset Alzheimer's disease (AD). Although rare and common variants in ABCA7 associated with AD alter the coding sequence and are predicted to impair protein function, the precise cell-type consequences of ABCA7 deficiency remain incompletely defined. Methods: We used CRISPR/Cas9 gene editing to generate induced pluripotent stem cells (iPSCs) that were deficient for ABCA7 (ABCA7-KO) and their wild-type (ABCA7-WT) isogenic counterparts and subsequently performed unbiased proteomics on differentiated astrocytes (iAs), neurons (iNs) and microglia (iMGs). ABCA7 deficiency in iMGs produced the largest proteomic changes, so we therefore conducted additional functional analyses to define its effects on microglial lysosomal activity, phagocytosis, and lipid metabolism. In addition, we leveraged CRISPR/Cas9 to correct the ABCA7 rs3752246 AD risk variant in patient-derived iPSCs and compared proteomic and functional phenotypes between corrected iMGs and isogenic mutant carriers. Finally, we examined the functional consequence of ABCA7-deficient microglia on neurons. Results: ABCA7-KO iMGs were deficient for proteins involved in lysosome function, measured by down-regulated lysosomal proteomic signatures, as well as reduced DQ-BSA activity and reduced LAMP1+ area. Additionally, ABCA7-KO iMGs displayed impaired phagocytic capacity and increased inflammatory markers, including MHC proteins CD1A and CD1E, and IL-18. Multi-omic integration of lipidomic and proteomic profiles nominated a dysregulated metabolic network characterized by altered phospholipid steady-state metabolism and increased lipid peroxidation in ABCA7-KO iMGs. This was complemented by an accumulation of polyunsaturated triacylglycerols and lipid droplets, suggesting that ABCA7 deficiency disrupts intracellular lipid dynamics. This was supported by the alleviation of lysosomal and lipid droplet phenotypes through the inhibiting the synthesis of triacylglycerols. Concordantly, proteomic and functional analyses revealed lysosomal dysfunction in rs3752246-mutant iMGs, suggesting a shared ABCA7-dependent mechanism underlying AD risk. Tri-cultures of iNs, iAs and iMGs revealed that ABCA7 deficiency in iMGs worsened AD-relevant neuronal measures such as tau phosphorylation and synapse number. Conclusions: This work supplies evidence for the important role of ABCA7 in microglia and provides unique insights into the molecular and functional consequences of reduced ABCA7 function in lysosomal and lipid regulation, paving a path forward to a more comprehensive understanding of AD molecular subtypes and personalized therapeutics.

neuroscience↗

INPP5D/SHIP1 is a dual regulator of endo-lysosome function and selective phagocytosis in human microglia

INPP5D, which encodes SHIP1, is genetically associated with Alzheimers disease (AD) risk and regulates microglial immune function. Here we identified SHIP1 as a regulator of endo-lysosomal homeostasis in human microglia. INPP5D haploinsufficiency impaired endosome maturation and lysosomal degradation, leading to lipid droplet accumulation, lysosomal stress, and NLRP3 inflammasome activation. SHIP1-deficient microglia shifted from an immune-responsive state toward a disease-associated state with elevated cargo-selective phagocytosis. Although amyloid-{beta} uptake was unaffected, SHIP1-deficient microglia accumulated intracellular amyloid-{beta} and exhibited exacerbated lipid droplet accumulation, consistent with defective lysosomal processing. Proteomic analysis of genetically diverse human microglia revealed that the protective INPP5D rs10933431 variant is associated with elevated phosphatase-domain containing SHIP1, and protein profiles consistent with enhanced endolysosomal trafficking. In mice xenografted with SHIP1-deficient human microglia, high amyloid-{beta} burden exacerbated lysosomal, lipid droplet and inflammasome phenotypes. Together, these findings identify disrupted endo-lysosomal trafficking and degradative capacity as mechanisms linking INPP5D dysfunction to disease-associated microglial states in AD.

neuroscience↗

BAG3 coordinates astrocytic proteostasis of Alzheimer's disease-linked proteins via proteasome, autophagy, and retromer complex interactions

BackgroundBcl-2-associated athanogene 3 (BAG3) is a mediator of chaperone assisted selective autophagy, and in the brain, most highly expressed in astrocytes. However, its role in astrocytes remains poorly defined. Given the genetic and pathological links of BAG3 to proteostasis and neurodegenerative diseases, we investigated how BAG3 contributes to astrocyte function and Alzheimers disease (AD). MethodsSnRNA-seq of the human brain determined cell type expression of BAG3. CRISPR/Cas9 gene editing in human iPSCs, followed by tandem mass tag-mass spectrometry and RNA-sequencing was performed to assess proteomic and transcriptomic changes following BAG3 loss. Co-immunoprecipitation of BAG3 in human astrocytes defined the interactome, with top interactors being validated by western blot (WB), AlphaFold modeling, and proximity ligation assays. In astrocytes, autophagic flux, lysosomal phenotypes, proteasome activity, and endocytic uptake were measured in BAG3 KO and BAG3 WT. Finally, BAG3 expression was assessed in postmortem AD brain by WB and snRNA-seq, and its functional relevance to amyloid-{beta} (A{beta}) degradation was tested in co-cultures of BAG3 KO iAs with familial AD neurons. ResultsIn human brain and iPSC models, BAG3 was most highly expressed in astrocytes. Further, BAG3 loss caused greater proteomic disruption in astrocytes than in neurons. In the absence of BAG3, astrocytes showed reduced autophagy, diminished lysosome abundance and activity, and decreased proteasome function. To uncover molecular binding partners of BAG3 that might influence these phenotypes, we performed co-immunoprecipitation, revealing interactions with HSPB8 and other heat shock proteins, proteasome regulators (PSMD5, PSMF1), and the retromer component, VPS35. Integration of BAG3 KO transcriptomic and proteomic datasets pinpointed AD-relevant proteins under post-translational control of BAG3, which included GFAP, BIN1, and HSPB8. HSPB8 levels were markedly reduced in BAG3-deficient astrocytes with overexpression partially rescuing its levels. Loss of astrocytic BAG3 impaired A{beta} clearance in co-culture with APP/PSEN1 mutant neurons, directly linking BAG3 to a disease-relevant astrocyte function. Finally, analysis of postmortem brain tissue revealed BAG3 marks a stress-responsive astrocyte subtype in the brain of aged individuals with AD. ConclusionsBAG3 binds to key regulators of autophagy, proteasome activity, and retromer function to coordinate astrocyte proteostasis, lysosomal function, and A{beta} clearance. These findings position BAG3 as a potential therapeutic target and coordinator of glial protein quality control in neurodegeneration.

neuroscience↗

A proteogenomic tool uncovers protein markers for human microglial states

Human microglial heterogeneity has been largely described using transcriptomic data. Here, we introduce a microglial proteomic data resource and a Cellular Indexing of Transcriptomes and Epitopes by Sequencing panel enhanced with antibodies targeting 17 microglial cell surface proteins (mCITE-Seq). We evaluated mCITE-Seq on HMC3 microglia-like cells, induced-pluripotent stem cell-derived microglia (iMG), and freshly isolated primary human microglia. We identified novel protein microglial markers such as CD51 and relate expression of 101 cell surface proteins to transcriptional programs. This results in the identification and validation of three protein marker combinations with which to purify microglia enriched with each of 23 transcriptional programs; for example, CD49D, HLA-DR and CD32 enrich for GPNMBhigh ("disease associated") microglia. Further, we identify and validate proteins - SIRPA, PDPN and CD162 - that differentiate microglia from infiltrating macrophages. The mCITE-Seq panel enables the transition from RNA-based classification and facilitates the functional characterization and harmonization of model systems.

neuroscience↗

Contributions of genetic variation in astrocytes to cell and molecular mechanisms of risk and resilience to late onset Alzheimer's disease

Reactive astrocytes are associated with Alzheimers disease (AD), and several AD genetic risk variants are associated with genes highly expressed in astrocytes. However, the contribution of genetic risk within astrocytes to cellular processes relevant to the pathogenesis of AD remains ill-defined. Here we present a resource for studying AD genetic risk in astrocytes using a large collection of induced pluripotent stem cell (iPSC) lines from deeply phenotyped individuals with a range of neuropathological and cognitive outcomes. IPSC lines from forty-four individuals were differentiated into astrocytes followed by unbiased molecular profiling using RNA sequencing and tandem mass tag-mass spectrometry. We demonstrate the utility of this resource in examining gene- and pathway-level associations with clinical and neuropathological traits, as well as in analyzing genetic risk and resilience factors through parallel analyses of iPSC-astrocytes and brain tissue from the same individuals. Our analyses reveal that genes and pathways altered in iPSC-derived astrocytes from AD individuals are concordantly dysregulated in AD brain tissue. This includes increased prefoldin proteins, extracellular matrix factors, COPI-mediated trafficking components and reduced proteins involved in cellular respiration and fatty acid oxidation. Additionally, iPSC-derived astrocytes from individuals resilient to high AD neuropathology show elevated basal levels of interferon response proteins and increased secretion of interferon gamma. Correspondingly, higher polygenic risk scores for AD are associated with lower levels of interferon response proteins. This study establishes an experimental system that integrates genetic information with a heterogeneous set of iPSCs to identify genetic contributions to molecular pathways affecting AD risk and resilience.

neuroscience↗