Cited by 195Metabolism and Genetic DisordersLysosomal Storage Disorders ResearchNeurological diseases and metabolism

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Peroxisomes in brain development and function

Open access
Berger, Johannes, Dorninger, Fabian, Forss-Petter, Sonja, Kunze, Markus·2016·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Abstract

Peroxisomes contain numerous enzymatic activities that are important for mammalian physiology. Patients lacking either all peroxisomal functions or a single enzyme or transporter function typically develop severe neurological deficits, which originate from aberrant development of the brain, demyelination and loss of axonal integrity, neuroinflammation or other neurodegenerative processes. Whilst correlating peroxisomal properties with a compilation of pathologies observed in human patients and mouse models lacking all or individual peroxisomal functions, we discuss the importance of peroxisomal metabolites and tissue- and cell type-specific contributions to the observed brain pathologies. This enables us to deconstruct the local and systemic contribution of individual metabolic pathways to specific brain functions. We also review the recently discovered variability of pathological symptoms in cases with unexpectedly mild presentation of peroxisome biogenesis disorders. Finally, we explore the emerging evidence linking peroxisomes to more common neurological disorders such as Alzheimer's disease, autism and amyotrophic lateral sclerosis.

Overview

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Written from the paper’s full text.

TL;DR

This review synthesizes how peroxisomal metabolic pathways contribute to brain development and function, using inherited peroxisomal disorders and mouse models to link specific pathways to neuronal migration, myelination, axonal integrity, neuroinflammation, and neurodegeneration. It also discusses emerging evidence connecting peroxisomes to more common neurological disorders such as Alzheimer’s disease, autism, amyotrophic lateral sclerosis, and schizophrenia.

Key findings

  • Peroxisome biogenesis disorders (PBD) and single peroxisomal enzyme/transporter deficiencies cause major brain pathology grouped into neuronal migration/differentiation defects, white matter formation/maintenance defects, and post-developmental neuronal degeneration. Zellweger syndrome features cortical malformations such as centrosylvian pachygyria and polymicrogyria, heterotopic Purkinje cells, and white matter abnormalities; in a study of 19 patients aged 16–35 years with mild Zellweger spectrum disorder, MRI showed white matter abnormalities in 9 patients, restricted to the cerebellar hilus of the dentate nucleus and/or peridentate region.
  • Cell-type-specific mouse studies indicate that in the murine brain peroxisomes are most crucial for oligodendrocytes and the myelin compartment: oligodendrocyte-selective Pex5 knockout caused progressive subcortical demyelination, axonal degeneration, neuroinflammation, impaired motor function, and premature death starting at 2–6 months, whereas Pex5 deletion in projection neurons or astrocytes had no obvious deleterious effect on brain development or function despite VLCFA accumulation and reduced plasmalogen levels in astrocytes.
  • X-linked adrenoleukodystrophy (X-ALD) is the most common peroxisomal disorder, with estimated combined male and female incidence between 1:16,800 and 1:30,000; about 60% of male X-ALD patients develop cerebral ALD, and adrenal insufficiency affects 80% of male patients before adulthood. ABCD1 deficiency causes VLCFA accumulation, AMN with distal dying-back axonopathy, and in CALD an inflammatory demyelinating process with blood–brain barrier permeability, macrophage/T-cell infiltration, and loss of oligodendrocytes.
  • Ether phospholipid deficiency in RCDP causes rhizomelia, chondrodysplasia punctata, cataracts, growth/developmental retardation, variable brain involvement including white matter abnormalities, delayed myelination, cerebellar atrophy with Purkinje cell loss, and peripheral neuropathy; RCDP incidence is estimated at about 1:100,000. Peroxisomal links are also reported for autism (PEX7 mutations, reduced plasmalogens), Alzheimer’s disease (plasmalogen depletion, altered VLCFA, catalase, DHA, peroxisome distribution), ALS (DAO mutation, D-serine), and schizophrenia (DAO activity, D-serine/NMDA signaling).

Methods

  • Narrative review of mammalian peroxisomal functions in the nervous system, focusing on human physiology/pathophysiology supplemented by mouse models.
  • Evidence base includes human inherited peroxisomal disorders (PBD, X-ALD, Refsum disease, RCDP, single enzyme/transporter deficiencies) and genetically engineered mouse models, including global and conditional Pex knockouts, Acox1−/−, Mfp2−/−, Abcd1−/−, Phyh−/−, and ether lipid-deficient models.
  • Main analysis is qualitative synthesis comparing biochemical, neuropathological, imaging, and cell-type-specific findings across disorders and models; no systematic review, meta-analysis, or new primary data are reported.

Limitations

  • The paper states that many studies examined the presence/abundance of a single peroxisomal protein, thus possibly detecting only a subset of peroxisome-positive cells, so different investigations must be combined to infer accurate distribution and abundance.
  • The paper states that peroxisome-related metabolite levels in plasma may not reflect tissue accumulation, and that some mild PBD patients can have normal plasma VLCFA or plasmalogen levels, limiting diagnostic and pathophysiological interpretation.
  • The paper notes that mouse models differ from human disease—for example, Abcd1-deficient mice do not develop brain inflammation/demyelination as in CALD, and Mfp2-deficient mice differ markedly from human DBP deficiency—so mechanisms and phenotypes cannot always be directly translated. As an evident limitation, this is a narrative review without systematic search or quantitative synthesis.

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Integrity signals

Registry

Crossref · 10.1016/j.bbamcr.2015.12.005

Cites

344 of 344 references verified0 citation errors · 0 not checkable

Statistics

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Figures

Fig.1 Schematic drawing linking peroxisomal disease-related proteins to individual metabolic pathways. Upper part: Proteins are grouped according to their function in biosynthetic or degradative metabolic pathways, ROS homeostasis, proteolytic activity, transport of metabolites across the peroxisomal membrane (ABCD and PMP proteins), and the import of matrix and membrane proteins (PEX proteins). Ovals represent proteins that are involved in peroxisomal functions (not complete); gray ovals, proteins for which mutations have been linked to a human disease (for full name see Table 1). The degradation of various fatty acids and bile acid precursors is symbolized by the frame depicting the homodimeric transporters (ABCD1–3) and the terms α- and β-oxidation, illustrated in more detail below. Lower part: Proteins are grouped into the degradation pathways for different activated fatty acids (fatty acyl-CoA: saturated, unsaturated, dicarboxylic, branched-chain) and the side chain shortening of di- and trihydroxycholestanoic acid (DHCA/THCA) during bile acid biosynthesis (all via β-oxidation) and the oxidative removal of one carbon unit from branched-chain fatty acids (α-oxidation). Several proteins are involved in the subsequent modification of the β-oxidation products, either by thiolytic cleavage (thioesterases, ACOT), substitution of CoA for carnitine (carnitine transferases, CRAT and CROT) or amidation of the CoA-activated side chain of bile acids (amino transferase, BAAT). FALDH*, two isoforms are known residing in peroxisomes and the ER, respectively, which precludes attribution of the linked disease, Sjögren–Larsson syndrome, to a particular variant. Synthetase, CoA-activation is essential for the link between α- and β-oxidation, but the exact enzyme has not yet been assigned. PEX, peroxin; cargo-PTS1 and PTS2-cargo, representative peroxisomal matrix proteins harboring a PTS1 or PTS2 motif, respectively; mPTS-cargo, representative peroxisomal membrane protein harboring a motif for targeting of peroxisomal membrane proteins (mPTS). 4,8-DMN-CoA, 4,8-dimethylnonanoyl-CoA. Proteins not included in Table 1: 2-HACL, 2-hydroxyacyl-CoA lyase; ABCD2, ATP-binding cassette transporter D2; ACAA1, acetyl-CoA acyltransferase 1; ACOT4, acyl-CoA thioesterase 4; ACOT8, acyl-CoA thioesterase 8; ACOX2, acyl-CoA oxidase 2; CRAT, carnitine O-acetyltransferase; CROT, carnitine O-octanoyltransferase; DDO, D-aspartate oxidase; DECR2, dienoyl-CoA reductase 2; ECH1, enoyl-CoA hydratase 1; EPHX2, epoxide hydroxylase 2; GSTK1, glutathione S-transferase kappa-1, IDE, insulin-degrading enzyme; LONP2, lon peptidase 2; PAO, polyamine oxidase; PIPOX, pipecolic acid oxidase; PECI, peroxisomal D3,D2-enoyl-CoA isomerase; PMP22, peroxisomal membrane protein of 22 kDa; PMP34, peroxisomal membrane protein of 34 kDa; PRDX1, peroxiredoxin 1; PRDX5, peroxiredoxin 5; SOD1, superoxide dismutase 1; TYSND1, trypsin domain-containing 1
Fig.1 Schematic drawing linking peroxisomal disease-related proteins to individual metabolic pathways. Upper part: Proteins are grouped according to their function in biosynthetic or degradative metabolic pathways, ROS homeostasis, proteolytic activity, transport of metabolites across the peroxisomal membrane (ABCD and PMP proteins), and the import of matrix and membrane proteins (PEX proteins). Ovals represent proteins that are involved in peroxisomal functions (not complete); gray ovals, proteins for which mutations have been linked to a human disease (for full name see Table 1). The degradation of various fatty acids and bile acid precursors is symbolized by the frame depicting the homodimeric transporters (ABCD1–3) and the terms α- and β-oxidation, illustrated in more detail below. Lower part: Proteins are grouped into the degradation pathways for different activated fatty acids (fatty acyl-CoA: saturated, unsaturated, dicarboxylic, branched-chain) and the side chain shortening of di- and trihydroxycholestanoic acid (DHCA/THCA) during bile acid biosynthesis (all via β-oxidation) and the oxidative removal of one carbon unit from branched-chain fatty acids (α-oxidation). Several proteins are involved in the subsequent modification of the β-oxidation products, either by thiolytic cleavage (thioesterases, ACOT), substitution of CoA for carnitine (carnitine transferases, CRAT and CROT) or amidation of the CoA-activated side chain of bile acids (amino transferase, BAAT). FALDH*, two isoforms are known residing in peroxisomes and the ER, respectively, which precludes attribution of the linked disease, Sjögren–Larsson syndrome, to a particular variant. Synthetase, CoA-activation is essential for the link between α- and β-oxidation, but the exact enzyme has not yet been assigned. PEX, peroxin; cargo-PTS1 and PTS2-cargo, representative peroxisomal matrix proteins harboring a PTS1 or PTS2 motif, respectively; mPTS-cargo, representative peroxisomal membrane protein harboring a motif for targeting of peroxisomal membrane proteins (mPTS). 4,8-DMN-CoA, 4,8-dimethylnonanoyl-CoA. Proteins not included in Table 1: 2-HACL, 2-hydroxyacyl-CoA lyase; ABCD2, ATP-binding cassette transporter D2; ACAA1, acetyl-CoA acyltransferase 1; ACOT4, acyl-CoA thioesterase 4; ACOT8, acyl-CoA thioesterase 8; ACOX2, acyl-CoA oxidase 2; CRAT, carnitine O-acetyltransferase; CROT, carnitine O-octanoyltransferase; DDO, D-aspartate oxidase; DECR2, dienoyl-CoA reductase 2; ECH1, enoyl-CoA hydratase 1; EPHX2, epoxide hydroxylase 2; GSTK1, glutathione S-transferase kappa-1, IDE, insulin-degrading enzyme; LONP2, lon peptidase 2; PAO, polyamine oxidase; PIPOX, pipecolic acid oxidase; PECI, peroxisomal D3,D2-enoyl-CoA isomerase; PMP22, peroxisomal membrane protein of 22 kDa; PMP34, peroxisomal membrane protein of 34 kDa; PRDX1, peroxiredoxin 1; PRDX5, peroxiredoxin 5; SOD1, superoxide dismutase 1; TYSND1, trypsin domain-containing 1CC BY · PubMed Central
Fig.2 Schematic representation of neuronal migration defects in peroxisomal biogenesis disorders. (A) In the cerebral cortex (neocortex) of a healthy individual (left panel), the cell bodies of cortical neurons are localized in discrete layers. In comparison, the cortical lamination is severely disturbed and the border to the white matter in microgyric (middle panel) and pachygyric (right panel) brains of cases with Zellweger Syndrome is indicated (horizontal line). Similar abnormalities can also be found in cases of severe D-bifunctional protein deficiency. Roman numerals to the left correspond to normal cortical layers. WM, white matter. (B) In the cerebellum of a healthy individual (left panel), the Purkinje cells (blue triangles) are strictly arranged into a single cell-thick layer at the border of the molecular (outermost) layer and the thick granule cell layer. In Zellweger patients (right panel), many Purkinje cells are mislocalized to the granule cell layer and cerebellar white matter.
Fig.2 Schematic representation of neuronal migration defects in peroxisomal biogenesis disorders. (A) In the cerebral cortex (neocortex) of a healthy individual (left panel), the cell bodies of cortical neurons are localized in discrete layers. In comparison, the cortical lamination is severely disturbed and the border to the white matter in microgyric (middle panel) and pachygyric (right panel) brains of cases with Zellweger Syndrome is indicated (horizontal line). Similar abnormalities can also be found in cases of severe D-bifunctional protein deficiency. Roman numerals to the left correspond to normal cortical layers. WM, white matter. (B) In the cerebellum of a healthy individual (left panel), the Purkinje cells (blue triangles) are strictly arranged into a single cell-thick layer at the border of the molecular (outermost) layer and the thick granule cell layer. In Zellweger patients (right panel), many Purkinje cells are mislocalized to the granule cell layer and cerebellar white matter.CC BY · PubMed Central
Fig.3 Schematic representation of abnormalities of myelinated axons and synaptic transmission in peroxisomal deficiencies. (A) The left panel shows a myelinated axon at the level of a node of Ranvier in a healthy control. The myelin sheath of oligodendrocytes (in the CNS) or Schwann cells (in the PNS) surrounds and isolates the axon, except at the node of Ranvier allowing depolarization of the neuronal membrane and propagation of electrical signals. Note that a multitude of ion channels and Na+/K+-ATPases (not indicated) are located at the node of Ranvier and entail a high energy demand. In the right panel, different pathological features are indicated that may contribute to the axonal degeneration frequently observed in peroxisomal disorders, for example, adrenomyeloneuropathy (the late-onset variant of X-ALD). A scenario can be envisaged, where peroxisomal dysfunction and abnormal accumulation of lipid metabolites in myelinating cells lead to unstable paranodal loops and a loss of axonal support resulting in energy deficits and oxidative damage in the axons and progressive axonal degeneration. (B) A normal synapse with the surrounding astrocytes is depicted (left panel), representative for a synapse of any neurotransmitter. D-Amino acid oxidase is indicated for its role in D-serine degradation at e.g. glutamatergic synapses. The right panel shows several possible disturbances of synaptic function (red text) that could lead to altered neurotransmission, as predominantly described in ether lipid deficiency. NT, neurotransmitter; DAO, D-amino acid oxidase
Fig.3 Schematic representation of abnormalities of myelinated axons and synaptic transmission in peroxisomal deficiencies. (A) The left panel shows a myelinated axon at the level of a node of Ranvier in a healthy control. The myelin sheath of oligodendrocytes (in the CNS) or Schwann cells (in the PNS) surrounds and isolates the axon, except at the node of Ranvier allowing depolarization of the neuronal membrane and propagation of electrical signals. Note that a multitude of ion channels and Na+/K+-ATPases (not indicated) are located at the node of Ranvier and entail a high energy demand. In the right panel, different pathological features are indicated that may contribute to the axonal degeneration frequently observed in peroxisomal disorders, for example, adrenomyeloneuropathy (the late-onset variant of X-ALD). A scenario can be envisaged, where peroxisomal dysfunction and abnormal accumulation of lipid metabolites in myelinating cells lead to unstable paranodal loops and a loss of axonal support resulting in energy deficits and oxidative damage in the axons and progressive axonal degeneration. (B) A normal synapse with the surrounding astrocytes is depicted (left panel), representative for a synapse of any neurotransmitter. D-Amino acid oxidase is indicated for its role in D-serine degradation at e.g. glutamatergic synapses. The right panel shows several possible disturbances of synaptic function (red text) that could lead to altered neurotransmission, as predominantly described in ether lipid deficiency. NT, neurotransmitter; DAO, D-amino acid oxidaseCC BY · PubMed Central

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  • The paper relies on this without support.

    Observations in mouse models of peroxisomal disorders are informative about human brain development and function.

    “with a specific focus on human physiology and pathophysiology supplemented by observations made in various mouse models”
    “genetically engineered mouse models with tissue- or cell type-specific inactivation of peroxisome biogenesis demonstrate the importance of peroxisomes for the different brain cell types”
  • The paper relies on this without support.

    The brain pathologies observed in inherited peroxisomal disorders reveal the normal functions of peroxisomes in brain development and maintenance.

    “correlating peroxisomal properties with a compilation of pathologies observed in human patients and mouse models lacking all or individual peroxisomal functions”
    “the observed pathology cannot be attributed to individual peroxisomal metabolic pathways but rather reflects the importance of the entire organelle for brain development and maintenance”
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  1. Nave, 2006, Oligodendrocytes and Schwann cells support axon function and survival independent of their role in myelination: implications for multiple sclerosis, J. Neuroimmunol., 178, 36-36

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Metadata

Authors
Berger, J., Dorninger, F., Forss-Petter, S., & Kunze, M.
Affiliations
Medical University of Vienna (AT)
Corresponding author
Berger, Johannes
Venue
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher
Elsevier BV
Published
2016-05
Volume
1863
Issue
5
Pages
934-955
ISSN
0167-4889 (ISSN-L)
OpenAlex
W2194234530
Cited by
194
References
352
Citations by year
2026: 13 · 2025: 20 · 2024: 19 · 2023: 16 · 2022: 27 · 2021: 10 · 2020: 22 · 2019: 26 · 2018: 16 · 2017: 16 · 2016: 9
FWCI
11.30
Type
journal article
Language
en
Open access
Locations
  • Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion, cc-by)
  • PubMed Central (acceptedVersion, cc-by)
Funders
Austrian Science Fund (FWF) (P26112-B19,, P24843-B24, I2738-B26)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
  • Health Sciences › Medicine › Genetics (clinical) › Lysosomal Storage Disorders Research
  • Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
Keywords
peroxisomes, peroxisome biogenesis disorders, brain development, demyelination, axonal integrity, neuroinflammation, neurodegeneration, Alzheimer's disease, autism spectrum disorder, amyotrophic lateral sclerosis, neurological disorders
MeSH terms
ATPases Associated with Diverse Cellular Activities, Animals, Brain, Disease Models, Animal, Gene Expression Regulation, Humans, Membrane Proteins, Mutation, Synaptic Transmission, Peroxisomal Disorders, Protein Isoforms, Peroxisomes, Protein Transport, Mice, Metabolic Networks and Pathways

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