• parkinson's disease
• cellular neuroscience

• Animals
• alpha-Synuclein/metabolism
• alpha-Synuclein/genetics
• Parkinson Disease/metabolism
• Parkinson Disease/pathology
• Parkinson Disease/therapy
• Parkinson Disease/genetics
• Fasting/physiology
• Disease Models, Animal
• Mice
• Dopaminergic Neurons/metabolism
• Dopaminergic Neurons/pathology
• Male
• Autophagy
• Mice, Inbred C57BL
• Dopamine/metabolism
• Humans
• Corpus Striatum/metabolism
• Corpus Striatum/pathology
• Microglia/metabolism
• Intermittent Fasting

• FA-658-3-1 Deutsche Forschungsgemeinschaft (German Research Foundation)

• Parkinson's disease
• apoptosis
• insulin‐like growth factor binding protein 2
• mitochondria dysfunction
• oxidative stress

• Animals
• Male
• Rats
• Apoptosis/drug effects
• Apoptosis/physiology
• Insulin-Like Growth Factor Binding Protein 2/metabolism
• Oxidative Stress/drug effects
• Oxidative Stress/physiology
• Oxidopamine/toxicity
• Parkinson Disease/metabolism
• Parkinson Disease/pathology
• Parkinsonian Disorders/metabolism
• Parkinsonian Disorders/chemically induced
• Parkinsonian Disorders/pathology
• PC12 Cells
• Receptor, IGF Type 1/metabolism
• Rats, Wistar

• 82271275 National Natural Science Foundation of China
• National Natural Science Foundation of China

• calcium
• daf-2
• insulin-dopamine crosstalk
• learning

• Animals
• Insulin
• Caenorhabditis elegans
• Dopaminergic Neurons
• Dopamine
• Signal Transduction

• TRC - DST funding
• University Grants Commission

• parkinson's disease

• 1191003 Fondo Nacional de Desarrollo Científico y Tecnológico (National Fund for Scientific and Technological Development)
• 1191003 Fondo Nacional de Desarrollo Científico y Tecnológico (National Fund for Scientific and Technological Development)

• FK506
• IGF-1
• IL-2
• biomarkers
• calcineurin
• neuroprotection
• α-synuclein

• R01 NS117750 NINDS NIH HHS

• CRISPR-Cas9
• Degradation
• Lysosome
• TSPAN3
• α-Synuclein

• Hcy
• IGF-1
• Levodopa and benserazide hydrochloride
• Motor function
• Parkinson’ s disease
• Rasagiline

• Humans
• Aged
• Middle Aged
• Levodopa/therapeutic use
• Parkinson Disease/drug therapy
• Benserazide/therapeutic use
• Antiparkinson Agents/therapeutic use
• Insulin-Like Growth Factor I
• Homocysteine

• 2019-YF09-00086-SN 5G communication technology supported remote diagnosis, treatment and care of patients with brain dysfunction and disability, semi-disability, and integrated prevention and control system
• 2019-YF09-00086-SN 5G communication technology supported remote diagnosis, treatment and care of patients with brain dysfunction and disability, semi-disability, and integrated prevention and control system
• 2019-YF09-00086-SN 5G communication technology supported remote diagnosis, treatment and care of patients with brain dysfunction and disability, semi-disability, and integrated prevention and control system
• 2019-YF09-00086-SN 5G communication technology supported remote diagnosis, treatment and care of patients with brain dysfunction and disability, semi-disability, and integrated prevention and control system

• Parkinson’s disease
• biomarkers
• exercise
• neuroendocrine
• neurohormone

• K23 NS123506 NINDS NIH HHS
• UL1 TR001422 NCATS NIH HHS

• Humans
• Adult
• Insulin-Like Growth Factor I/metabolism
• Neuroprotection
• Brain/metabolism
• Central Nervous System/metabolism
• Nerve Growth Factors/metabolism

• Alzheimer’s disease
• Autophagy
• Brain insulin resistance
• Epigenetics
• Parkinson’s disease

• Drug targets
• Genetic modifiers
• Lewy bodies
• Parkinson’s disease
• SNCA
• α-synuclein

• EGF
• IGF-1
• Nonmotor symptoms
• Parkinson’s disease

• Humans
• Parkinson Disease/diagnosis
• Epidermal Growth Factor
• Insulin-Like Growth Factor I/metabolism
• Cognitive Dysfunction/diagnosis
• Cognitive Dysfunction/etiology
• Cognition

• Alzheimer’s disease (AD)
• Insulin-like growth factor-1 (IGF-1)
• Metabolic syndrome (MetS)
• Neurodegeneration
• Neuroprotection

• 6-hydroxydopamine
• Parkinson’s disease
• alpha-synuclein
• insulin-like growth factor-2
• insulin-like growth factor-2 receptor
• neurodegeneration
• neuroprotection
• skin-derived precursor Schwann cells

• Anterior cingulate
• Caudate
• Insula
• Nonmotor symptoms
• Parkinson’s disease
• Plasma IGF-1

A constant metabolism and energy supply are crucial to all organs, particularly the brain. Age-dependent neurodegenerative diseases, such as Parkinson’s disease (PD), are associated with alterations in cellular metabolism. These changes have been recognized as a novel hot topic that may provide new insights to help identify risk in the pre-symptomatic phase of the disease, understand disease pathogenesis, track disease progression, and determine critical endpoints. Nuclear receptor-related factor 1 (NURR1), an orphan member of the nuclear receptor superfamily of transcription factors, is a major risk factor in the pathogenesis of PD, and changes in NURR1 expression can have a detrimental effect on cellular metabolism. In this review, we discuss recent evidence that suggests a vital role of NURR1 in dopaminergic (DAergic) neuron development and the pathogenesis of PD. The association between NURR1 and cellular metabolic abnormalities and its implications for PD therapy have been further highlighted.

• Dopaminergic neuron
• Metabolism
• Mitochondria
• NURR1
• Parkinson’s disease
• α-Synuclein

• 4-hydroxyisoleucine
• GLP-1
• IGF-1
• amyotrophic lateral sclerosis
• demyelination
• methylmercury
• motor neuron death

• Amyotrophic Lateral Sclerosis/drug therapy
• Amyotrophic Lateral Sclerosis/genetics
• Animals
• Glucagon-Like Peptide 1/metabolism
• Insulin-Like Growth Factor I/metabolism
• Isoleucine/analogs & derivatives
• Methylmercury Compounds/toxicity
• Motor Neurons
• Rats
• Rats, Wistar

• ISFCP/IAEC/CPCSEA/Meeting No.28/2020/Protocol No.455 Indo Soviet Friendship College of Pharmacy

There are several links between insulin resistance and neurodegenerative disorders such as Parkinson’s disease. However, the direct influence of insulin signaling on abnormal α-synuclein accumulation—a hallmark of Parkinson’s disease—remains poorly explored. To our best knowledge, this work is the first attempt to investigate the direct effects of insulin signaling on pathological α-synuclein accumulation induced by the addition of α-synuclein preformed fibrils in primary dopaminergic neurons. We found that modifying insulin signaling through (1) insulin receptor inhibitor GSK1904529A, (2) SHIP2 inhibitor AS1949490 or (3) PTEN inhibitor VO-OHpic failed to significantly affect α-synuclein aggregation in dopaminergic neurons, in contrast to the aggregation-reducing effects observed after the addition of glial cell line-derived neurotrophic factor. Subsequently, we tested different media formulations, with and without insulin. Again, removal of insulin from cell culturing media showed no effect on α-synuclein accumulation. We observed, however, a reduced α-synuclein aggregation in neurons cultured in neurobasal medium with a B27 supplement, regardless of the presence of insulin, in contrast to DMEM/F12 medium with an N2 supplement. The effects of culture conditions were present only in dopaminergic but not in primary cortical or hippocampal cells, indicating the unique sensitivity of the former. Altogether, our data contravene the direct involvement of insulin signaling in the modulation of α-synuclein aggregation in dopamine neurons. Moreover, we show that the choice of culturing media can significantly affect preformed fibril-induced α-synuclein phosphorylation in a primary dopaminergic cell culture.

• Cell Culture Techniques
• Dopamine
• Dopaminergic Neurons
• Humans
• Insulin/pharmacology
• Parkinson Disease/pathology
• alpha-Synuclein

• GLP-1
• Parkinson’s disease
• dopamine
• insulin
• type 2 diabetes mellitus

Insulin-like growth factor 2 (IGF2) and autophagy-related genes have been proposed as biomolecules of interest related to idiopathic Parkinson’s disease (PD). The objective of this study was to determine the IGF2 and IGF1 levels in plasma and peripheral blood mononuclear cells (PBMCs) from patients with moderately advanced PD and explore the potential correlation with autophagy-related genes in the same blood samples. IGF1 and IGF2 levels in patients' plasma were measured by ELISA, and the IGF2 expression levels were determined by real-time PCR and Western blot in PBMCs. The expression of autophagy-related genes was evaluated by real-time PCR. The results show a significant decrease in IGF2 plasma levels in PD patients compared with a healthy control group. We also report a dramatic decrease in IGF2 mRNA and protein levels in PBMCs from PD patients. In addition, we observed a downregulation of key components of the initial stages of the autophagy process. Although IGF2 levels were not directly correlated with disease severity, we found a correlation between its levels and autophagy gene profile expression in a sex-dependent pattern from the same samples. To further explore this correlation, we treated mice macrophages cell culture with α-synuclein and IGF2. While α-synuclein treatment decreased levels Atg5, IGF2 treatment reverted these effects, increasing Atg5 and Beclin1 levels. Our results suggest a relationship between IGF2 levels and the autophagy process in PD and their potential application as multi-biomarkers to determine PD patients' stages of the disease.

• IGF-1
• alpha-synuclein
• insulin
• parkinsonism
• substantia nigra

• adipokine
• apelin-13
• apelin-36
• apelinergic
• biomarker
• brain-gut peptide

• Caenorhabditis elegans
• Parkinson's disease
• alpha-synuclein
• mesenchymal stem cells
• secretome

• ALS
• Demyelination
• GLP-1
• Genetic dysfunction
• IGF-1
• Immune dysregulation
• Neuroinflammation

• ACE/angiotensin receptors/renin angiotensin system
• Angiotensin
• COVID-19
• Cell biology/structural biology
• Cell signaling/signal transduction
• Intracrine
• Mitochondria
• Nucleus
• Oxidant stress
• Oxidative stress

• Aging
• Central nervous system
• Dopamine
• Estrogens
• IGF-1
• Parkinson’s disease

• Brain
• Dopamine
• Female
• Humans
• Insulin-Like Growth Factor I
• Neurons
• Parkinson Disease

Diabetes mellitus (DM), a group of diseases characterized by defective glucose metabolism, is the most widespread metabolic disorder affecting over 400 million adults worldwide. This pathological condition has been implicated in the pathogenesis of a number of central encephalopathies and peripheral neuropathies. In further support of this notion, recent epidemiological evidence suggests a link between DM and Parkinson’s disease (PD), with hyperglycemia emerging as one of the culprits in neurodegeneration involving the nigrostriatal pathway, the neuroanatomical substrate of the motor symptoms affecting parkinsonian patients. Indeed, dopaminergic neurons located in the mesencephalic substantia nigra appear to be particularly vulnerable to oxidative stress and degeneration, likely because of their intrinsic susceptibility to mitochondrial dysfunction, which may represent a direct consequence of hyperglycemia and hyperglycemia-induced oxidative stress. Other pathological pathways induced by increased intracellular glucose levels, including the polyol and the hexosamine pathway as well as the formation of advanced glycation end-products, may all play a pivotal role in mediating the detrimental effects of hyperglycemia on nigral dopaminergic neurons. In this review article, we will examine the epidemiological as well as the molecular and cellular clues supporting the potential susceptibility of nigrostriatal dopaminergic neurons to hyperglycemia.

• dopamine
• glucotoxicity
• hyperglycemia
• mitochondrial dysfunction
• nigrostriatal pathway
• oxidative stress

The advances in medicine, together with lifestyle modifications, led to a rising life expectancy. Unfortunately, however, aging is accompanied by an alarming boost of age-associated chronic pathologies, including neurodegenerative and metabolic diseases. Interestingly, a non-negligible interplay between alterations of glucose homeostasis and brain dysfunction has clearly emerged. In particular, epidemiological studies have pointed out a possible association between Type 2 Diabetes (T2D) and Parkinson’s Disease (PD). Insulin resistance, one of the major hallmark for etiology of T2D, has a detrimental influence on PD, negatively affecting PD phenotype, accelerating its progression and worsening cognitive impairment. This review aims to provide an exhaustive analysis of the most recent evidences supporting the key role of insulin resistance in PD pathogenesis. It will focus on the relevance of insulin in the brain, working as pro-survival neurotrophic factor and as a master regulator of neuronal mitochondrial function and oxidative stress. Insulin action as a modulator of dopamine signaling and of alpha-synuclein degradation will be described in details, too. The intriguing idea that shared deregulated pathogenic pathways represent a link between PD and insulin resistance has clinical and therapeutic implications. Thus, ongoing studies about the promising healing potential of common antidiabetic drugs such as metformin, exenatide, DPP IV inhibitors, thiazolidinediones and bromocriptine, will be summarized and the rationale for their use to decelerate neurodegeneration will be critically assessed.

• Parkinson’s disease
• dopamine
• insulin resistance
• neurodegeneration
• type 2 diabetes mellitus

Parkinson’s disease (PD) is a neurodegenerative disease characterized by motor impairments and resulting from progressive degenerative loss of midbrain dopaminergic (DAergic) neurons in the substantia nigra. Although the main cause of the loss of DAergic neurons is still unknown, various etiopathogenic mechanisms are distinguished, including release and accumulation of endogenous excitotoxic mediators along with the production of oxidative free radicals. Several neurotrophic and growth factors are known to increase DAergic neuronal survival and enhance antioxidant mechanisms. In this context, the micro-immunotherapy (MI) approach consists to regulate the immune system in order to protect DAergic neurons and control oxidative stress.

The aim of the present study was to investigate the effect of the MI medicine (MIM), 2LPARK^® (Labo’Life), on oxidative stress and on the number of neurons positive for tyrosine hydroxylase (TH), in an in vitro model of PD.

Rat primary mesencephalic DAergic neurons cultures were pre-treated for 1 hr with the MIM (10 μM and 10 mM), placebo (10 μM and 10 mM) or brain-derived neurotrophic factor (BDNF; 3.3 μM) and then intoxicated with 6-hydroxydopamine (6-OHDA; 20 μM) for 48 hrs. After incubation, cells were incubated 30 mins at 37°C with CellROX green reagent and number of labeled cells were quantified. Then, cells were fixed and incubated with anti-TH antibody and the number of TH⁺ neurons was evaluated.

We showed that, contrary to placebo, MIM was able to reduce oxidative stress and protect DAergic neurons from 6-OHDA-induced cell death.

Our results demonstrate the in vitro efficacy of MIM on two essential mechanisms of PD and propose the MI approach as a new ally in the regulation of neuroinflammation and in the treatment of this degenerative disease.

• growth factors
• immune system
• low dose
• micro-immunotherapy
• neurotrophic factors

Background: Insulin-like growth factor-1 (IGF-1) function is impaired in Parkinson disease. Cyclic glycine-proline (cGP), a metabolite of IGF-1, is neuroprotective through improving IGF-1 function. Parkinson disease patients score lower on Hospital-associated Anxiety and Depression Scale after supplementing blackcurrant anthocyanins (BCA), which may be associated with IGF-1 function. We evaluated the changes of cGP and IGF-1 before and after the supplementation. Methods: Plasma and cerebrospinal fluid (CSF) were collected from 11 male patients before and after 28 day supplementation of BCA. The concentrations of IGF-1, IGF binding protein (IGFBP)-3, and cGP were measured using ELISA and HPLC-MS assays. The presence of cGP in the BCA was evaluated. Results: cGP presented in the BCA. BCA supplementation increased the concentration of cGP (p < 0.01), but not IGF-1 and IGFBP-3 in the CSF. CSF concentration of cGP was correlated with plasma concentration of cGP (R = 0.68, p = 0.01) and cGP/IGF-1 molar ratio (R = 0.66, p = 0.01). The CSF/plasma ratio was high in cGP and low in IGF-1 and IGFBP-3. Conclusion: cGP is a natural nutrient to the BCA. The increased CSF cGP in Parkinson disease patients may result from the central uptake of plasma cGP. Given neurotrophic function, oral availability, and effective central uptake of cGP, the BCA has the potential to be developed to treat neurological conditions with IGF-1 deficiency.

• Parkinson disease
• autocrine regulation
• bioavailability of insulin-like growth factor-1 (IGF-1)
• blackcurrant anthocyanins
• central uptake
• cerebrospinal fluid
• cyclic Glycine-Proline (cGP)

• Aged
• Aged, 80 and over
• Anthocyanins/isolation & purification
• Anthocyanins/therapeutic use
• Antiparkinson Agents/isolation & purification
• Antiparkinson Agents/therapeutic use
• Biomarkers/blood
• Biomarkers/cerebrospinal fluid
• Fruit/chemistry
• Humans
• Insulin-Like Growth Factor Binding Protein 3/cerebrospinal fluid
• Insulin-Like Growth Factor I/cerebrospinal fluid
• Insulin-Like Growth Factor I/deficiency
• Male
• Middle Aged
• New Zealand
• Parkinson Disease/blood
• Parkinson Disease/cerebrospinal fluid
• Parkinson Disease/drug therapy
• Parkinson Disease/physiopathology
• Peptides, Cyclic/blood
• Peptides, Cyclic/cerebrospinal fluid
• Ribes/chemistry
• Time Factors
• Treatment Outcome

Dementia, a condition that frequently afflicts patients in advanced stages of Parkinson's disease (PD), results in decreased quality of life and survival time. Nevertheless, the pathological mechanisms underlying Parkinson's disease dementia (PDD) are not completely understood. The symptoms characteristic of PDD may be the result of functional and structural deficiencies. The present study implicates the accumulation of Lewy bodies in the cortex and limbic system as a potent trigger in the development of PDD. In addition, significant Alzheimer-type pathologies, including amyloid-β (Aβ) plaques and NFTs, are observed in almost half of PDD patients. Interestingly, links between PDD pathogenesis and the mechanisms underlying the development of insulin resistance have begun to emerge. Furthermore, previous studies have demonstrated that insulin treatment reduces amyloid plaques in Alzheimer's disease (AD), and normalizes the production and functionality of dopamine and ameliorates motor impairments in 6-OHDA-induced rat PD models. GSK3β, a downstream substrate of PI3K/Akt signaling following induction by insulin and IGF-1, exerts an influence on AD and PD physiopathology. The genetic overexpression of GSK3β in cortex and hippocampus results in signs of neurodegeneration and spatial learning deficits in in vivo models (Lucas et al., 2001), whereas its inhibition results in improvements in cognitive impairment in these rodents, including AD and PD. Accordingly, insulin- or IGF-1-activated PI3K/Akt/GSK3β signaling may be involved in PDD pathogenesis, at least in the pathology of PD-type + AD-type.

• Akt
• Glycogen synthase kinase β (GSK3β)
• Insulin-like growth factor (IGF-I)
• Parkinson's disease dementia (PDD)
• insulin
• phosphoinositide 3 kinase (PI3k)
• tau
• α-synuclein

• Parkinson's disease
• amyloid
• connectometry
• diffusion tensor imaging
• dopamine
• insulin-like growth factor-1
• synuclein
• tau

The local renin-angiotensin system (RAS) and insulin-like growth factor 1 (IGF-1) have been involved in longevity, neurodegeneration and aging-related dopaminergic degeneration. However, it is not known whether IGF-1 and angiotensin-II (AII) activate each other. In the present study, AII, via type 1 (AT1) receptors, exacerbated neuroinflammation and dopaminergic cell death. AII, via AT1 receptors, also increased the levels of IGF-1 and IGF-1 receptors in microglial cells. IGF-1 inhibited RAS activity in dopaminergic neurons and glial cells, and also inhibited the AII-induced increase in markers of the M1 microglial phenotype. Consistent with this, IGF-1 decreased dopaminergic neuron death induced by the neurotoxin MPP⁺ both in the presence and in the absence of glia. Intraventricular administration of AII to young rats induced a significant increase in IGF-1 expression in the nigral region. However, aged rats showed decreased levels of IGF-1 relative to young controls, even though RAS activity is known to be enhanced in aged animals. The study findings show that IGF-1 and the local RAS interact to inhibit or activate neuroinflammation (i.e. transition from the M1 to the M2 phenotype), oxidative stress and dopaminergic degeneration. The findings also show that this mechanism is impaired in aged animals.

• Gerotarget
• IGF-1
• Parkinson
• longevity
• microglia
• neurodegeneration

• Parkinson's disease
• gene polymorphism
• insulin-like growth factor 1
• rs972936

• Adult
• Aged
• Aged, 80 and over
• Cognition Disorders/blood
• Cognition Disorders/complications
• Female
• Humans
• Insulin-Like Growth Factor I/metabolism
• Male
• Middle Aged
• Parkinson Disease/blood
• Parkinson Disease/complications

• Michael J. Fox Foundation for Parkinson's Research

• Disease modification
• Insulin resistance
• Neurodegeneration
• Parkinson’s disease

• Autophagy
• ER stress, aggregation, neurodegenerative disease
• IGFs
• UPR

• Acanthopanax senticosus Harms
• Parkinson's disease
• lncRNA
• neurodegeneration
• α-synuclein

Long-acting glucagon-like peptide-1 (GLP-1) analogues marketed for type 2 diabetes (T2D) treatment have been showing positive and protective effects in several different tissues, including pancreas, heart or even brain. This gut secreted hormone plays a potent insulinotropic activity and an important role in maintaining glucose homeostasis. Furthermore, growing evidences suggest the occurrence of several commonalities between T2D and neurodegenerative diseases, insulin resistance being pointed as a main cause for cognitive decline and increased risk to develop dementia. In this regard, it has also been suggested that stimulation of brain insulin signaling may have a protective role against cognitive deficits. As GLP-1 receptors (GLP-1R) are expressed throughout the central nervous system and GLP-1 may cross the blood-brain-barrier, an emerging hypothesis suggests that they may be promising therapeutic targets against brain dysfunctional insulin signaling-related pathologies. Importantly, GLP-1 actions depend not only on the direct effect mediated by its receptor activation, but also on the gut-brain axis involving an exchange of signals between both tissues via the vagal nerve, thereby regulating numerous physiological functions (e.g., energy homeostasis, glucose-dependent insulin secretion, as well as appetite and weight control). Amongst the incretin/GLP-1 mimetics class of anti-T2D drugs with an increasingly described neuroprotective potential, the already marketed liraglutide emerged as a GLP-1R agonist highly resistant to dipeptidyl peptidase-4 degradation (thereby having an increased half-life) and whose systemic GLP-1R activity is comparable to that of native GLP-1. Importantly, several preclinical studies showed anti-apoptotic, anti-inflammatory, anti-oxidant and neuroprotective effects of liraglutide against T2D, stroke and Alzheimer disease (AD), whereas several clinical trials, demonstrated some surprising benefits of liraglutide on weight loss, microglia inhibition, behavior and cognition, and in AD biomarkers. Herein, we discuss the GLP-1 action through the gut-brain axis, the hormone’s regulation of some autonomic functions and liraglutide’s neuroprotective potential.

• Type 2 diabetes
• Glucagon-like peptide-1
• Gut
• Brain
• Insulin
• Liraglutide
• Alzheimer disease
• Neuroprotection

• Alzheimer's Disease
• Clinical studies
• IGF-1
• Incretins
• Insulin
• Synucleinopathies

• Amyloid beta-Peptides/toxicity
• Blotting, Western
• Cell Death
• Cell Line, Tumor
• Cell Survival
• Cytoplasm/drug effects
• Cytoplasm/metabolism
• Dose-Response Relationship, Drug
• Forkhead Box Protein O3
• Forkhead Transcription Factors/metabolism
• Hexokinase/metabolism
• Humans
• Insulin/pharmacology
• Membrane Potential, Mitochondrial
• Mitochondria/drug effects
• Mitochondria/metabolism
• Neurons/drug effects
• Neurons/metabolism
• Oxidative Stress
• Peptide Fragments/toxicity
• Phosphorylation
• Protein Transport
• Proto-Oncogene Proteins c-akt/metabolism
• Reactive Oxygen Species/metabolism
• Receptor, Insulin/metabolism
• Recombinant Proteins/toxicity
• Signal Transduction
• Time Factors
• bcl-Associated Death Protein/metabolism

• Aged
• Alzheimer Disease/genetics
• Humans
• Lewy Body Disease/genetics
• Neurodegenerative Diseases/genetics
• Parkinson Disease/genetics
• alpha-Synuclein/genetics
• alpha-Synuclein/physiology
• beta-Synuclein/genetics
• beta-Synuclein/physiology

• parkinson’s disease
• akt
• neurodegeneration
• neuroprotection

• Animals
• Cell Death/physiology
• Humans
• Neurons/cytology
• Neurons/pathology
• Neurons/physiology
• Parkinson Disease/genetics
• Parkinson Disease/physiopathology
• Parkinson Disease/therapy
• Proto-Oncogene Proteins c-akt/genetics
• Proto-Oncogene Proteins c-akt/metabolism
• Signal Transduction/physiology

• K08 NS070608 NINDS NIH HHS
• P50 NS038370 NINDS NIH HHS
• R01 NS072050 NINDS NIH HHS