---
title: "AZP2006 for Parkinson’s disease models: neuroprotection via lysosomal homeostasis and the Progranu"
id: "plos-one-16-azp2006-in-parkinson-s-disease-models-a-promising-new-neuroprotective-treatment"
canonical_url: "https://medichelpline.com/clinical-feed/plos-one-16-azp2006-in-parkinson-s-disease-models-a-promising-new-neuroprotective-treatment"
content_type: "clinical_feed_article"
specialty: "Neurology"
source_name: "PLOS ONE (Medicine)"
source_url: "https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0359269"
published_at: "2026-09-30T14:00:00.000Z"
evidence_level: "Journal Feed"
license: "CC-BY-NC-4.0 / Informational Use"
---
# AZP2006 for Parkinson’s disease models: neuroprotection via lysosomal homeostasis and the Progranu
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/plos-one-16-azp2006-in-parkinson-s-disease-models-a-promising-new-neuroprotective-treatment
- **Specialty:** [Neurology](https://medichelpline.com/clinical-feed/neurology.md)
- **Primary Source:** PLOS ONE (Medicine)
- **Source URL:** [Original Journal Publication](https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0359269)
- **Published At:** 2026-09-30T14:00:00.000Z
- **Evidence Rating:** Journal Feed
## Executive GIST (TL;DR)
- Parkinson’s disease (PD) pathology includes aggregated **alpha-synuclein** (Lewy bodies), mitochondrial stress, proteasomal dysfunction, and progressive loss of dopaminergic neurons in the substantia nigra pars compacta. - Emerging data link **lysosomal dysfunction** to PD; lysosomes and lysosomal enzymes (eg, cathepsins) are central to degradation of aggregation-prone proteins such as alpha-synuclein. - **Progranulin (PGRN)** regulates lysosomal function and enhances activity of lysosomal enzymes; its delivery to lysosomes depends on interactions with **Prosaposin (PSAP)** or sortilin. - PSAP is a lysosomal regulatory protein with neuroprotective roles; PSAP and PGRN are functionally interdependent, and deficits in either impair lysosomal homeostasis and associate with neurodegeneration. - AZP2006 (Ezeprogind) is a small lysosomotropic molecule that binds the **PGRN/PSAP complex** and was previously identified for neuroprotective activity in other proteinopathies; its effects require PGRN and PSAP. - The study evaluated AZP2006 in multiple PD-like models (cellular and animal) that reproduce mitochondrial injury, alpha-synuclein preformed fibril (PFF) toxicity and accumulation, and microglial-driven neuroinflammation. - In vitro, AZP2006 mitigated acute mitochondrial injury (6-OHDA, MPP+, rotenone) and chronic alpha-synuclein PFF–induced toxicity; effects correlated with reduced microglial activation. - In vivo, AZP2006 protected dopaminergic neurons and reduced alpha-synuclein accumulation in aged mice challenged with alpha-syn PFF. - Mechanistic evidence links AZP2006’s neuroprotection to restoration of **lysosomal homeostasis** via the PGRN/PSAP complex: effects were lost in absence of PGRN or PSAP in prior work and PGRN-KO cell lines were used here to probe dependency. - Experimental approaches included primary rat and mouse mesencephalic cultures (with/without microglia), differentiated SH-SY5Y WT and PGRN-KO cells, exposure to mitochondrial toxins and alpha-syn PFF, live- and fixed-cell immunostaining, PhenoVue lysosomal dye, automated high-content imaging and quantitative image analysis. - AZP2006 is in clinical development for tauopathies (including PSP); the project received funding from Alzprotect and Neuro-Sys, with declared competing interests related to the developer company. - The authors conclude that strategies aiming to improve **PGRN** and **PSAP** levels or activity represent promising therapeutic approaches for proteinopathies such as PD.
## Clinical Analysis & Structured Key Points
AZP2006 in Parkinson’s disease models: A promising new neuroprotective treatment involving lysosomal homeostasis and the Progranulin/Prosaposin complex | PLOS One Browse Subject Areas ? Click through the PLOS taxonomy to find articles in your field. For more information about PLOS Subject Areas, click here . Article Authors Metrics Comments Media Coverage Peer Review Reader Comments Figures Figures Abstract The pathohistological hallmarks of Parkinson’s disease are aggregated alpha-synuclein and other aggregation-prone proteins (Lewy bodies). Recent studies show mechanistic as well as genetic connections between lysosomal dysfunction and Parkinson’s disease pathology. A direct link between lysosomal function and Parkinson’s disease might be the degradation of alpha-synuclein within the lysosomal system. Progranulin is necessary for maintaining lysosomal function, facilitating the activity of several lysosomal enzymes. Progranulin’s exit from the endoplasmic reticulum and its lysosomal availability depend on an interaction with Prosaposin. AZP2006 (INN: Ezeprogind) is a small lysosomotropic neuroprotective molecule currently in clinical development in Progressive Supranuclear Palsy patients. Its neuroprotective effects involve the Progranulin/Prosaposin complex. In this study, we investigated the neuroprotective effects of AZP2006 in several Parkinson’s-like models ( vitro and vivo ). We showed that AZP2006 was able to counteract a mitochondrial injury as well as the toxicity of alpha-synuclein preformed fibril spreading. We proved that Progranulin was involved in AZP2006’s neuroprotective action, restoring lysosomal homeostasis and ultimately supporting the health of dopaminergic neurons. In light of this evidence, strategies with the aim of improving Progranulin and Prosaposin levels and activity offer a promising therapeutic approach in the context of proteinopathies such as Parkinson’s disease. Citation: Callizot N, Culley G, Flower G, Rouvière L, De Conto V, Wojcinski A, et al. (2026) AZP2006 in Parkinson’s disease models: A promising new neuroprotective treatment involving lysosomal homeostasis and the Progranulin/Prosaposin complex. PLoS One 21(9): e0359269. https://doi.org/10.1371/journal.pone.0359269 Editor: Miriam A. Hickey, University of Tartu, ESTONIA Received: August 13, 2025; Accepted: September 11, 2026; Published: September 30, 2026 Copyright: © 2026 Callizot et al. This is an open access article distributed under the terms of the Creative Commons Attribution License , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Data Availability: All relevant data are within the manuscript and its Supporting Information files. Funding: This work was funded by Alzprotect ( https://www.alzprotect.com/ ) and Neuro-Sys ( https://www.neuro-sys.com/ ). Alzprotect provided support in the form of salaries for its employees (PV and CE) who are co authors on this study and contracted Neuro Sys, a contract research organization, to perform the experimental work and data analysis. Neuro Sys employed and paid its own staff (NC, GC, GF, LR, VDC, AW, CB and AH), who are also co-authors on this study, and was compensated on a fee for service basis. Philippe Verwaerde (PV), CEO of Alzprotect, received a grant (MJFF-021163) from the Michael J. Fox Foundation ( https://www.michaeljfox.org/ ) for the project entitled “Using AZP2006 (Ezeprogind) to Stabilize Progranulin – A Novel Therapeutic Strategy for GBA1 linked Parkinson’s Disease.” The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. Competing interests: This work was funded by Alzprotect. Philippe Verwaerde is the CEO of Alprotect, the company that develops AZP2006. Introduction Parkinson’s disease (PD) is defined by the progressive, irreversible loss of dopaminergic neurons in the substantia nigra pars compacta ( SN pc). Its neuropathological hallmarks include the accumulation of misfolded, aggregated alpha-synuclein (α-syn) and other aggregation-prone proteins (Lewy bodies). Neurodegeneration in PD stems from multiple, interconnected mechanisms, such as proteasomal dysfunction-driven protein aggregation, mitochondrial stress, and impaired dopamine (DA) release. These pathways often converge, amplifying the production of reactive oxygen species (ROS) and oxidative stress, resulting in neuronal death [ 1 ]. More recent studies show mechanistic, as well as genetic, connections between lysosomal dysfunction and PD [ 2 ]. Lysosomes are acidic, membrane-enclosed organelles that degrade cellular macromolecules and participate in key processes such as endocytosis, phagocytosis and autophagy. Large protein aggregates, including α-syn, are predominately degraded via the lysosomal-autophagy system, where proteases, namely cathepsins, mediate their breakdown [ 3 ]. Lysosomal function depends on tightly regulated homeostasis mediated by lysosomal ion channels, which maintain the acidic pH required for lysosomal enzyme activity [ 4 , 5 ]. Progranulin (PGRN), is a ubiquitous growth factor which plays a role in regulating lysosomal function by enhancing the activity of lysosomal enzymes, including a critical protease, cathepsin D [ 6 , 7 ]. In the central nervous system, PGRN is highly expressed in microglia where it can be secreted as a full-length glycoprotein [ 8 , 9 ]. Once released, PGRN can interact with several signaling receptors [ 10 ] before becoming internalized and trafficked to the lysosomes of neurons and other glia [ 11 ]. PGRN deficiency disrupts microglial function and promotes neurodegeneration [ 12 ], whereas increasing PGRN levels in animal models of neurodegeneration enhances neuronal survival [ 13 , 14 ], axonal growth and regeneration after injury, and reduces oxidative stress [ 15 ]. Emerging clinical evidence links PGRN deficiency to neurodegenerative diseases whereby reduced PGRN levels have been reported in frontal temporal dementia (FTD), Alzheimer’s disease and PD [ 19 – 21 ]. The delivery of PGRN to the lysosome is dependent on the interaction with sortilin or prosaposin (PSAP) [ 11 , 16 ]. PSAP, a precursor of saposins (cofactors for glycosphingolipids hydrolases), is itself a lysosomal regulatory protein with neuroprotective properties [ 17 , 18 ]. In FTD caused by granulin (GRN) mutations [ 22 ], neuronal PSAP levels are diminished [ 23 , 24 ] — a finding that has been recapitulated in GRN-deficient mice [ 24 ]. Furthermore, PSAP supplementation has been shown to rescue lysosomal dysfunction in PGRN-deficient neurons [ 25 ], while PSAP-deficient mice exhibit reduced neuronal PGRN levels [ 25 ]. In PD, plasma PSAP levels decline with disease progression [ 21 ], further supporting the clinical relevance of this lysosomal protein. Collectively, these findings suggest that the PGRN-PSAP interaction is critical for lysosomal function and clearance of aggregation-prone proteins, such as α-syn. The PGRN/PSAP complex is therefore a compelling target in PD. AZP2006 (INN: Ezeprogind; N-3-(4-(3-(diisobutylamino)propyl)piperazin-1-yl)propyl)-1H-benzo[d]imidazol-2-amine di-sulphate salt) is a small molecule that was initially screened and selected for its ability to reduce beta-amyloid (Aβ) release, increase levels of non-amyloidogenic APP metabolites and ultimately protect against neuronal loss [ 26 ]. AZP2006 is able to bind to the PGRN/PSAP complex and its neuroprotective effects are lost in the absence of either PGRN or PSAP [ 26 , 27 ]. These findings suggest that its neuroprotective mechanism relies on restoring lysosomal function through its interaction with the PGRN/PSAP complex. AZP2006 is in development as a therapy for tauopathies, including Progressive Supranuclear Palsy (PSP), where a Phase 2a trial (NCT04008355) demonstrated favorable clinical outcomes [ 27 ]. Pre-clinical studies have also explored its potential in Alzheimer’s disease and FTD [ 26 ]. Here, we extend these investigations to PD by evaluating the neuroprotective effects of AZP2006 in multiple PD-like models (cellular and animal models) which reproduce key pathological features including mitochondrial stress, α-syn preformed fibril (PFF) toxicity and α-syn accumulation in neurons [ 28 ]. Given the critical role of microglia in PGRN secretion and activity, as well as its role in neuroinflammation, we also examined the impact of AZP2006 on microglial activation. In vitro , AZP2006 mitigated both acute mitochondrial injury, and chronic α-syn PFF-induced toxicity, which was associated with reduced microglial activation. These findings were translational in vivo , where AZP2006 protected dopaminergic neurons and reduced α-syn accumulation in aged mice injured with α-syn PFF. Using lysosomal function markers and PGRN knock-out (KO) cell lines, we provide evidence that the neuroprotective effects of AZP2006 in these PD models are mechanistically linked to the restoration of lysosomal homeostasis via the PGRN/PSAP complex. Materials and methods All experiments were carried out in accordance with the National Institutes of Health Guide for the Care and Use of Laboratory Animals and followed current European Union regulations (Directive 2010/63/EU). Animals were housed for acclimation for 1 week in Neuro-Sys facilities and were maintained in a reversed 12 h light/dark cycle. They were placed in ventilated cages and maintained in a room with controlled temperature (21–22 °C), hygrometry (40–60%) and with food and water ad libitum . Primary culture and treatment of mesencephalic neurons in presence or absence of microglial cells Pregnant female rats of 15 days gestation (Wistar rats, Janvier Labs, Le Genest-Saint-Isle, France) or mice of 14 days gestation (Swiss mice, Janvier Labs France) were sacrificed using deep anesthesia with CO 2 followed by cervical dislocation. Rat or mouse mesencephalic neurons were prepared and cultured as previously described (see [ 1 , 29 ]). Briefly, the embryonic midbrains were dissected under a stereo zoom binocular microscope and placed in ice-cold medium of Leibovitz (L15, Pan Biotech, Aidenbach, Germany) containing 2% Penicillin (10,000 U/mL) and Streptomycin (10 mg/mL) solution (PS, Pan Biotech) and 1% bovine serum albumin (BSA, Pan Biotech). The ventral portion of the mesencephalic flexure, a region of the developing brain rich in dopaminergic neurons, was isolated for the cell preparations. Midbrains were dissociated by trypsinization for 20 minutes at 37 °C (0.05% trypsin and 0.02% EDTA, Pan Biotech). The reaction was stopped by the addition of Dulbecco’s modified Eagle medium (DMEM, Dutscher, Bernolsheim, France) containing 0.2 mg/mL DNase I grade II (Pan Biotech) and 10% fetal calf serum (FCS, Thermo Fisher Scientific, Cergy Pontoise, France). Cells were then mechanically dissociated by 3 passages through a 10 mL pipette. Cells were centrifuged at 180 x g for 10 minutes at +4 °C on a layer of BSA (3.5%) in L15 medium. The supernatant was discarded and the cell pellets were re-suspended in a defined culture medium consisting of Neurobasal medium (Thermo Fisher Scientific) supplemented with: 2% B27 (Invitrogen), 2 mM L-glutamine (Pan Biotech), 2% PS solution, 10 ng/mL of Brain-derived neurotrophic factor (BDNF, Pan Biotech) and 1 ng/mL of Glial-Derived Neurotrophic Factor (GDNF, Pan Biotech). For the protocol using microglial cells, the medium was additionally supplemented with 4% heat-inactivated FCS, 1 g/L of glucose, 1 mM sodium pyruvate, and 100 µM of non-essential amino acids. Viable cells were counted using the LUNA-FL (logosbio) cell counter. The cells were seeded at a density of 40,000 cells/well (without microglial cells) or 80,000 cells/well (with microglial cells) in 96-well plates pre-coated with poly-L-lysine (Corning Biocoat, Le Pont de Claix, France) and maintained in a 5% CO 2 /95% air atmosphere humidified incubator at 37 °C. Half of the medium was replaced every 2 days with fresh medium. On day 6, rat cultures were injured with 20 µM 6-Hydroxydopamine hydrobromide (6OHDA), 4 μM 1-Methyl-4-phenylpyridinium iodide (MPP + ) or 10 nM Rotenone (all from Sigma-Aldrich, St. Louis, MO, USA), diluted in culture medium, in the presence of AZP2006 for 48 h (6OHDA and MPP + ) or for 24 h (Rotenone). Mouse cultures were treated with an anti-PGRN antibody (5 μg/mL, ref: MAB2557) or an unrelated control for antibody treatment (anti-CD206, 5 μg/mL, ref: MCA2235GA (See S3 Fig )). For the study of lysosome exocytosis, cells were treated with 100 nM AZP2006 for 96 h (total), with treatment renewal after the first 48 h (day 8 of culture) and the culture stopped on day 10. Generation of PGRN-KO SH-SY5Y cell line and treatment SH-SY5Y human neuroblastoma cells (Sigma Aldrich, 94030304) were cultured at Neuro-Sys (Gardanne, France). After a cell bank was generated, the cells were used between the 5 th and the 15 th passage. The PGRN knock-out (KO) SH-SY5Y cell line was generated by Neuro-Sys using CRISPR-Cas9 and homology directed repair approach. Briefly, CRISPR-Cas9 technology, using a non-homologous end joining approach (NHEJ), was used to generate an SH-SY5Y KO for GRN, the gene coding for PGRN protein. A single clone, selected based on the silencing of GRN gene, was characterized. SH-SY5Y cells were transfected with a plasmid coding for single-guide RNA (sgRNA), single-stranded DNA (ssDNA) and a puromycin resistance gene. Transfected cells were selected with puromycin and grown from single cells into colonies. A bank of PGRN KO cells was then generated to allow future studies. Cryoprotected wild-type (WT) and PGRN KO SH-SY5Y cells, stored in liquid nitrogen, were rapidly thawed in a water bath at 37 °C. Cells were immediately resuspended in high glucose-DMEM, (4.5 g/L, Dutscher), centrifuged at 125 x g for 7 minutes at 4 °C and the pellets resuspended in DMEM, supplemented with 10% FCS, and with 2% PS solution. Cells were seeded in 96-well plates at a density of 4,000 cells per well and cultured in a 5% CO 2 /95% air atmosphere humidified incubator at 37 °C. Cells were then cultured in DMEM, supplemented with 5% FCS and 1% PS solution. 10 μM retinoic acid (Sigma Aldrich) was added to the culture medium for 7 days to trigger cell differentiation. The culture medium was renewed every 2 days. After one week of differentiation, WT SH-SY5Y cells were injured with 1 mM MPP + , whereas PGRN KO cells were injured with 500 μM MPP + , both for 48 h. Concentrations of MPP + were chosen to achieve the same level of neuronal survival between WT and PGRN KO cell cultures after intoxication ( S5 Fig ). AZP2006 was administered in co-treatment. α-syn PFF preparation, injury and treatment of primary mesencephalic neurons (± microglia) or WT SH-SY5Y cells Rat primary mesencephalic neurons + /- microglia or SH-SY5Y cells were prepared as previously described. Three days before injury, α-syn PFF were prepared following the procedure described by Henriques et al, 2022 [ 17 ]. Briefly, human α-syn peptide (stock at 69 µM in water at −20 °C) was reconstituted at a final concentration of 50 μM in NaCl 0.9% and gently agitated for 3 days at 37 °C in the dark to generate a preparation containing; α-syn monomeric form (27%), small oligomers (from 25–42 kDa; 30%) large oligomers/PFF (50–120 kDa; 30%) and large fibrils (14%), precisely quantified as previously described [ 17 ]. On day 6 (primary culture) or day 11 (SH-SY5Y cells) were intoxicated with the α-syn preparation (250 nM), in the presence of AZP2006, dissolved in culture medium, for 48 h (with microglia) or 96 h (without microglia) for primary culture and 72 h for WT SH-SY5Y cells. Following intoxication, the cell culture medium was removed, and cells were prepared for immunostaining. Immunocytochemistry and automated image analysis Live cell imaging. To identify functional lysosomes, we incubated WT SH-SY5Y cells with PhenoVue 577 (Revvity, diluted in Hank’s Balanced Salt Solution (HBSS)), which is a fluorescent dye that accumulates in acidic vesicles. An increase in fluorescence intensity is associated with increased lysosomal function. After 72 h of intoxication with α-syn PFF, culture medium was removed from WT SH-SY5Y cells and incubated with PhenoVue 577 for 30 minutes at 37 °C. HBSS was removed and images were acquired (see below for further details). Fixed cell immunostaining. At the end of the treatment, primary mesencephalic neurons cells were washed with phosphate-buffered saline (PBS, Dutscher) and fixed with 4% paraformaldehyde (PFA) in PBS (pH = 7.3), for 20 minutes at room temperature (RT). Cells were washed twice in PBS and then permeabilized and non-specific binding sites blocked with PBS containing 0.1% saponin and 1% FCS, for 15 minutes at RT. Cells were incubated with the following primary antibodies (Ab), in PBS containing 1% FCS, 0.1 mg/mL of saponin, for 2 h at RT: mouse monoclonal anti-Tyrosine Hydroxylase (TH, 1/10000) antibody or rabbit polyclonal anti-TH (1/2000) antibody to identify dopaminergic neurons and their neurites; polyclonal anti-α-syn antibody produced in rabbit or in guinea pig (1/200); polyclonal anti-post-synaptic density 95 (PSD95, a post-synaptic marker) produced in rabbit (1/400), polyclonal anti-lysosomal associated membrane protein 2 (LAMP2, marker of lysosomes) produced in rabbit (1/200) or in mouse; rabbit monoclonal anti-OX-41 antibody (to specifically stain microglial cells to study their activation (M1 phenotype)) (1/500) or with a monoclonal anti-light chain 3 b (LC3b) antibody produced in mouse (1/100), a marker of autophagy (see Table 1 for more details). Download: PNG larger image TIFF original image Table 1. Antibodies used for in vitro investigations. https://doi.org/10.1371/journal.pone.0359269.t001 For WT and PGRN-KO SH-SY5Y cells injured with MPP + , after 48 h of intoxication, cells were fixed with methanol. After being washed twice in PBS, cell membrane permeabilization and blocking of non-specific binding sites was performed with a solution of PBS containing 5% BSA and 0.1% Triton X-100 for 10 minutes at RT. Cells were then incubated with the following primary antibodies: a polyclonal anti-α-syn antibody, produced in rabbit, at a dilution of 1/200 and mouse anti-LAMP2 antibody, at a dilution of 1/1000. Following primary antibody incubation (primary mesencephalic neurons or SH-SY5Y cells), cells were washed with PBS containing 1% FCS, 0.1% saponin, and then incubated with the appropriate secondary antibodies: Alexa Fluor conjugated antibodies, diluted 1/400 in PBS containing 1% FCS, 0.1% saponin, for 1 hour at RT. Cell nuclei were counterstained with the fluorescent Hoechst dye (1/1000, Sigma Aldrich). Automated image analysis. For each experimental condition (6 culture well replicates), images representing 80% of the total surface of the well area were automatically acquired at 10x magnification with ImageXpress® (20 photomicrographs per well, Molecular Devices, San Jose, CA, USA) or Operetta® (9 photomicrographs per well, Revvity), using the same acquisition parameters. Image analysis was performed automatically using MetaXpress® (Molecular Devices) or Harmony® (Revvity). Fluorescence detection thresholds were established based on background signal from control cultures treated only with secondary antibodies; since secondary antibodies did not produce detectable signal, this threshold was set at a low baseline level. Read-outs included: the number of TH(+) neurons (survival) and the length of their neurite network (µm); the area of cytoplasmic α-syn accumulation, the area of LAMP2(+) vesicles, the overlapping area between α-syn and LAMP2(+), LC3b(+) vesicles within the zone of interest, the overlapping area between LAMP2(+) vesicles and LC3b(+) vesicle area within TH(+) neurons (in µm²), PhenoVue 577(+) area (in µm²) within WT SH-SY5Y cells, as well as, the area of OX-41(+) staining in microglial cells. Further desc
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