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Cited by 51Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsDementia and Cognitive Impairment Research

Lipoprotein Lipase (LPL) is Associated with Neurite Pathology and Its Levels Are Markedly Reduced in the Dentate Gyrus of Alzheimer’s Disease Brains

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Gong, Huilin, Dong, Weijiang, Rostad, Steven W., Marcovina, Santica M., Albers, John J., Brunzell, John D., Vuletic, Simona·2013·Journal of Histochemistry & Cytochemistry
DOI 10.1369/0022155413505601PMC PMC3840745
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Abstract

Lipoprotein lipase (LPL) is involved in regulation of fatty acid metabolism, and facilitates cellular uptake of lipoproteins, lipids and lipid-soluble vitamins. We evaluated LPL distribution in healthy and Alzheimer’s disease (AD) brain tissue and its relative levels in cerebrospinal fluid. LPL immunostaining is widely present in different neuronal subgroups, microglia, astrocytes and oligodendroglia throughout cerebrum, cerebellum and spinal cord. LPL immunoreactivity is also present in leptomeninges, small blood vessels, choroid plexus and ependymal cells, Schwann cells associated with cranial nerves, and in anterior and posterior pituitary. In vitro studies have shown presence of secreted LPL in conditioned media of human cortical neuronal cell line (HCN2) and neuroblastoma cells (SK-N-SH), but not in media of cultured primary human astrocytes. LPL was present in cytoplasmic and nuclear fractions of neuronal cells and astrocytes in vitro. LPL immunoreactivity strongly associates with AD-related pathology, staining diffuse plaques, dystrophic and swollen neurites, possible Hirano bodies and activated glial cells. We observed no staining associated with neurofibrillary tangles or granulovacuolar degeneration. Granule cells of the dentate gyrus and the associated synaptic network showed significantly reduced staining in AD compared to control tissue. LPL was also reduced in AD CSF samples relative to those in controls.

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  • Microglial LPL expression has been implicated in brain development, damage, and disease.

    “Moreover, microglial LPL expression has been implicated in brain development, damage, and disease [25,26,27].”

    From Lipoprotein Lipase Regulates Microglial Lipid Droplet Accumulation (2021) · cites this paper as [27]

    The Discussion (page unavailable) reports extensive microglial LPL staining and stronger staining in reactive glial cells from Alzheimer’s disease brains, implicating it in disease-related inflammation. It discusses LPL in embryonic brain development and after ischemia-reperfusion injury, but does not specifically link microglial LPL expression to development or injury. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • Patients with AD show reduced LPL abundance in the hippocampus and reduced LPL enzymatic activity in their cerebrospinal fluid.

    “For example, patients with AD show reduced LPL abundance in the hippocampus, and reduced LPL enzymatic activity in their cerebrospinal fluid (CSF) [27].”

    From Lipoprotein Lipase Regulates Microglial Lipid Droplet Accumulation (2021) · cites this paper as [27]

    The Results report reduced LPL immunoreactivity in the dentate gyrus of AD hippocampal tissue and reduced LPL levels in AD cerebrospinal fluid. The Methods describe antibody-based staining and Western blotting, not a CSF enzymatic-activity assay; reduced CSF LPL activity is therefore not supported. The hippocampal finding is also specific to the dentate gyrus, rather than the hippocampus as a whole. (LLM, conf=0.90)

    Experimental — accuracy not yet measured

  • LPL is strongly expressed in the hypothalamus, hippocampus, and striatum.

    “LPL hydrolyzes circulating chylomicrons and very-low-density lipoprotein, is a regulator of brain energy balance, is strongly expressed in the hypothalamus, hippocampus, and striatum, and LPL variants are associated with neurite pathology and Alzheimer disease [96–98].”

    From Sterol and lipid analyses identifies hypolipidemia and apolipoprotein disorders in autism associated with adaptive functioning deficits (2021) · cites this paper as [97]

    The Results (page unavailable) report robust LPL staining in the hippocampal dentate gyrus and strong staining in striatal neurons. The passages do not report strong expression in the hypothalamus, so the three-region claim is only partly supported. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • LPL variants are associated with neurite pathology and Alzheimer disease.

    “LPL hydrolyzes circulating chylomicrons and very-low-density lipoprotein, is a regulator of brain energy balance, is strongly expressed in the hypothalamus, hippocampus, and striatum, and LPL variants are associated with neurite pathology and Alzheimer disease [96–98].”

    From Sterol and lipid analyses identifies hypolipidemia and apolipoprotein disorders in autism associated with adaptive functioning deficits (2021) · cites this paper as [97]

    The Results (page unavailable) associate LPL immunostaining with neurite pathology in Alzheimer’s disease. The Discussion mentions a reported association between an LPL polymorphism and neurofibrillary tangle density in AD, but this paper does not establish that LPL variants are associated with neurite pathology or Alzheimer’s disease generally. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • There are reduced levels of LPL in the dentate gyrus of patients with Alzheimer's disease.

    “Since LD accumulation is a component of AD [67,68], and there are reduced levels of LPL in the dentate gyrus of patients with AD [27], it is plausible that reduced LPL in AD could contribute to LDAM physiology, increased CE load, microglial dysfunction, and disease progression.”

    From Lipoprotein Lipase Regulates Microglial Lipid Droplet Accumulation (2021) · cites this paper as [27]

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Authors
Gong, H., Dong, W., Rostad, S. W., Marcovina, S. M., Albers, J. J., Brunzell, J. D., & Vuletic, S.
Affiliations
University of Washington (US)
Corresponding author
Vuletic, Simona
ORCID
Venue
Journal of Histochemistry & Cytochemistry
Publisher
SAGE Publications
Published
2013-09-04
Volume
61
Issue
12
Pages
857-868
ISSN
  • 0022-1554 (ISSN-L)
  • 1551-5044
DOI
10.1369/0022155413505601
PMC
PMC3840745
OpenAlex
W2009955079
Cited by
51
References
77
Citations by year
2026: 3 · 2025: 4 · 2024: 6 · 2023: 5 · 2022: 1 · 2021: 6 · 2020: 5 · 2019: 4 · 2018: 4 · 2017: 3 · 2016: 3 · 2015: 5 · 2014: 1
FWCI
2.09
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Histochemistry & Cytochemistry (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • University of Washington
  • National Institute on Aging (AG006781, AG 05136, U01AG006781, P50AG005136)
  • National Institute of Neurological Disorders and Stroke (P50NS062684)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
  • Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords
lipoprotein lipase, Alzheimer's disease, dentate gyrus, amyloid plaques, Hirano bodies, cerebrospinal fluid, fatty acid metabolism, astrocytes, microglia, oligodendroglia, neurofibrillary tangles, granule cells, synaptic networks
MeSH terms
Aged, Aged, 80 and over, Alzheimer Disease, Female, Humans, Lipoprotein Lipase, Male, Middle Aged, Neurites, Dentate Gyrus

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