Glycosaminoglycans from aged human hippocampus have altered capacities to regulate trophic factors activities but not Aβ42 peptide toxicity

Huynh, Minh Bao; Villares, Joào; Díaz, Julia; Christiaans, Stephy; Carpentier, Gilles; Ouidja, Mohand Ouidir; Ludmilla, Sissoeff; Raisman‐Vozari, Rita; Papy-García, Dulce

doi:10.1016/j.neurobiolaging.2011.09.030

Cited by 23 publications

(34 citation statements)

References 49 publications

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“…Another study of HS expression in the hippocampus of aged (mean age 66 years) versus adult (mean age 28 years) subjects demonstrated structural changes in HS in the hippocampus of aged subjects. These changes included decreased 2- O -sulfation, and increased N- and 3- O sulfation, but no difference in 6- O -sulfation [30]. Compared to GAGs from adult brains, GAGs from aged brains had decreased binding to growth factors, and decreased ability to enhance growth factor proliferative activity.…”

Section: Discussionmentioning

confidence: 99%

“…With suppression of endogenous BDNF, aged hippocampus GAGs promoted neuritogenesis in neuroblastoma cells. However, there was no difference in the ability of aged versus adult HSPGs to protect cells against amyloid-β toxicity [30]. …”

Section: Discussionmentioning

confidence: 99%

“…Higher levels of HSGAGs but not CSGAGs have been found in aged versus adult human hippocampal cells, particularly in regions with amyloid plaques [30]. Our previous work has also shown that certain genes differentially expressed in correlation with SULF2 are associated with AD and Lewy body dementia [24].…”

Section: Introductionmentioning

confidence: 99%

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Decreased Expression of Sulfatase 2 in the Brains of Alzheimer’s Disease Patients: Implications for Regulation of Neuronal Cell Signaling

Roberts

Kang

et al. 2017

ADR

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Background The human sulfatase 1 (SULF1) and sulfatase 2 (SULF2) genes modulate cell signaling and homeostasis in many tissues. Gene expression analyses have implicated SULF2 in disease pathogenesis, including Alzheimer’s disease (AD), but changes in brain SULF2 expression have not been directly established. Objective To investigate the expression of SULF1 and SULF2 in brain tissues from AD cases and cognitively normal controls. Methods Autopsy tissue from AD cases (n = 20) and age-and gender-matched cognitively normal controls (n = 20) were identified from the Mayo Clinic Alzheimer’s Disease Patient Registry neuropathology database. Tissue slides were stained for SULF1 and SULF2 protein expression in the hippocampus and frontal lobe and an expression score computed from the proportion of cells stained and the intensity of staining (range 0 [no expression] to 9 [marked expression]). Results SULF2 expression was reduced in AD cases. Compared to cognitively normal controls, SULF2 expression in AD cases was significantly decreased in the hippocampal Cornu Ammonis (CA) (mean score of 6.5 in cases versus 8.3 in controls; p = 0.003), in the gray matter of the parahippocampal gyrus (5.6 in cases versus 7.6 in controls; p = 0.003), and in the frontal lobe gray matter (5.4 in cases versus 7.4 in controls; p = 0.002). There was no difference in SULF1 expression in the hippocampus or frontal lobe of AD cases and controls. As expected there were no differences in SULF1 or SULF2 expression in white matter in AD cases compared to cognitively normal controls. Conclusion Decresed SULF2 in specific regions of the brain occurs in AD.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Decreased Expression of Sulfatase 2 in the Brains of Alzheimer’s Disease Patients: Implications for Regulation of Neuronal Cell Signaling

Roberts

Kang

et al. 2017

ADR

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“…Thus, depending on the expression of the HS metabolic machinery in each particular cell type or tissue, HS chains can carry different sulfate signatures (Fig. ), which can vary as a consequence of aging, tissue injury or disease . Accordingly, HS can interact with a large number of proteins or peptides, known under the generic name of heparin binding proteins (HBP) .…”

Section: Heparan Sulfatesmentioning

confidence: 99%

“…HS chains can participate in both the nucleation or latency phase (‘lag phase’), and in the polymerization phase (growth phase). In the first stage, they allow the formation of a nucleus of monomers, and in the second phase they promote a rapid extension of protofibrils and formation of amyloid fibrils .…”

Section: Protein Aggregationmentioning

confidence: 99%

The role of heparan sulfates in protein aggregation and their potential impact on neurodegeneration

et al. 2018

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Neurodegenerative disorders, such as Alzheimer's, Parkinson's, and prion diseases, are directly linked to the formation and accumulation of protein aggregates in the brain. These aggregates, principally made of proteins or peptides that clamp together after acquisition of β-folded structures, also contain heparan sulfates. Several lines of evidence suggest that heparan sulfates centrally participate in the protein aggregation process. In vitro, they trigger misfolding, oligomerization, and fibrillation of amyloidogenic proteins, such as Aβ, tau, α-synuclein, prion protein, etc. They participate in the stabilization of protein aggregates, protect them from proteolysis, and act as cell-surface receptors for the cellular uptake of proteopathic seeds during their spreading. This review focuses attention on the importance of heparan sulfates in protein aggregation in brain disorders including Alzheimer's, Parkinson's, and prion diseases. The presence of these sulfated polysaccharides in protein inclusions in vivo and their capacity to trigger protein aggregation in vitro strongly suggest that they might play critical roles in the neurodegenerative process. Further advances in glyco-neurobiology will improve our understanding of the molecular and cellular mechanisms leading to protein aggregation and neurodegeneration.

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Protective effect of extractive and biotechnological chondroitin in insulin amyloid and advanced glycation end product‐induced toxicity

Iannuzzi

Borriello

D’Agostino

et al. 2018

Journal Cellular Physiology

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Glycosaminoglycans are extracellular matrix components related to several biological functions and diseases. Chondroitin sulfate is a sulphated glycosaminoglycan synthesized as part of proteoglycan molecules. They are frequently associated with amyloid deposits and possess an active role in amyloid fibril formation. Recently, a neuroprotective effect of extracellular matrix components against amyloid toxicity and oxidative stress has been reported. Advanced glycation end products (AGEs), the end products of the glycation reaction, have been linked to amyloid-based neurodegenerative disease as associated with oxidative stress and inflammation. In this study we have analyzed the effect of chondroitin sulfate isolated from different species, in comparison with a new biotechnological unsulfated chondroitin, in the amyloid aggregation process of insulin, as well as the ability to prevent the formation of AGEs and related toxicity. The results have showed a determining role of chondroitin sulfate groups in modulating insulin amyloid aggregation. In addition, both sulfated and unsulfated chondroitins have shown protective properties against amyloid and AGEs-induced toxicity. These data are very relevant as a protective effect of these glycosaminoglycans in the AGE-induced toxicity was never observed before. Moreover, considering the issues related to the purity and safety of chondroitin from natural sources, this study suggests a new potential application for the biotechnological chondroitin.

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Glycosaminoglycans from aged human hippocampus have altered capacities to regulate trophic factors activities but not Aβ42 peptide toxicity

Cited by 23 publications

References 49 publications

Decreased Expression of Sulfatase 2 in the Brains of Alzheimer’s Disease Patients: Implications for Regulation of Neuronal Cell Signaling

Decreased Expression of Sulfatase 2 in the Brains of Alzheimer’s Disease Patients: Implications for Regulation of Neuronal Cell Signaling

The role of heparan sulfates in protein aggregation and their potential impact on neurodegeneration

Protective effect of extractive and biotechnological chondroitin in insulin amyloid and advanced glycation end product‐induced toxicity

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