Ovocystatin Induced Changes in Expression of Alzheimer’s Disease Relevant Proteins in APP/PS1 Transgenic Mice

Stańczykiewicz, Bartłomiej; Gburek, Jakub; Rutkowská, M; Lemieszewska, Marta; Gołąb, Krzysztof; Juszczyńska, Katarzyna; Piotrowska, Aleksandra; Trziszka, Tadeusz; Dzięgiel, Piotr; Podhorska‐Okołów, Marzenna; Zabłocka, Agnieszka; Rymaszewska, Joanna

doi:10.3390/jcm11092372

Cited by 3 publications

(4 citation statements)

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“…It has been shown up until now, that ovocystatin has a beneficial impact on cognitive function in young rats, and might prevent aging-related cognitive impairment in older animals [ 21 ] and reduce memory decline in APP/PS1 mice model [ 23 , 24 ]. However, its potential molecular mechanism of action is not explained and needs to be examined in detail.…”

Section: Discussionmentioning

confidence: 99%

“…However, its potential molecular mechanism of action is not explained and needs to be examined in detail. It was determined by us in our latest paper that ovoC induced changes in the expression of Alzheimer’s disease—Aβ and tau proteins in APP/PS1 mice model [ 24 ]. Therefore, in this study, we focused our attention on examining the ability of ovoC to interact with Aβ42, inhibit fibrils, or control oligomer growth into non-toxic species.…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, recently published studies showed that the administration of ovoC in drinking water might be effective in the prevention of cognitive deterioration in APP/PS1 mice [ 23 ]. Additionally, ovoC could also be applied as a useful factor against Aβ oligomerization and consequent amyloid fibril formation and tau protein deposition [ 24 ]. OvoC is a small protein inhibitor of cysteine proteinases and the best model protein under study representing the cystatin superfamily [ 25 ].…”

Section: Introductionmentioning

confidence: 99%

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Effect of Ovocystatin on Amyloid β 1-42 Aggregation—In Vitro Studies

Stańczykiewicz

Goszczyński

Migdał

et al. 2023

IJMS

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Amyloid β peptides (Aβ) aggregating in the brain have a potential neurotoxic effect and are believed to be a major cause of Alzheimer’s disease (AD) development. Thus, inhibiting amyloid polypeptide aggregation seems to be a promising approach to the therapy and prevention of this neurodegenerative disease. The research presented here is directed at the determination of the inhibitory activity of ovocystatin, the cysteine protease inhibitor isolated from egg white, on Aβ42 fibril genesis in vitro. Thioflavin-T (ThT) assays, which determine the degree of aggregation of amyloid peptides based on fluorescence measurement, circular dichroism spectroscopy (CD), and transmission electron microscopy (TEM) have been used to assess the inhibition of amyloid fibril formation by ovocystatin. Amyloid beta 42 oligomer toxicity was measured using the MTT test. The results have shown that ovocystatin possesses Aβ42 anti-aggregation activity and inhibits Aβ42 oligomer toxicity in PC12 cells. The results of this work may help in the development of potential substances able to prevent or delay the process of beta-amyloid aggregation—one of the main reasons for Alzheimer’s disease.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Effect of Ovocystatin on Amyloid β 1-42 Aggregation—In Vitro Studies

Stańczykiewicz

Goszczyński

Migdał

et al. 2023

IJMS

Self Cite

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“…Nevertheless, toxicological studies are warranted to confirm this hypothesis [ 113 ]. In order to ascertain the underlying molecular mechanisms, a histopathological examination was conducted, revealing that both β-amyloid and tau protein deposits were significantly reduced in the hippocampi of the APP/PS1 mice treated intraperitoneally with ovocystatin [ 114 ]. With limited evidence for ovocystatin passage through the blood-brain barrier to the brain compartment, it is also possible that the observed effects were exerted peripherally and indirectly led to the changes in the brain tissue.…”

Section: Cystatin Cmentioning

confidence: 99%

Cystatins: unravelling the biological implications for neuroprotection

Stańczykiewicz,

Łuc,

Banach

et al. 2023

Arch Med Sci

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Cystatins, a family of proteins known for their inhibitory role against cysteine proteases, have garnered significant attention in the field of neurodegeneration. Numerous genetic, experimental and clinical studies concerning cystatin C suggest it plays an important role in the course of neurodegenerative diseases. Its beneficial effects are associated with cysteine protease inhibition, impact on β-amyloid aggregation as well as regulation of cell proliferation, autophagy and apoptosis. Cystatin isolated from chicken egg white, called Ovocystatin, has been widely used in medical and pharmaceutical research due to its structural and biological similarities to human cystatin C. This article focuses on the potential use of cystatins, with special emphasis on easily-obtained Ovocystatin, in the treatment of neurodegenerative diseases, such as dementia. The current evidence on cystatin use has been portrayed shedding light on their mechanisms of action and therapeutic implications for neuroprotection and maintenance of cognitive functions.

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LRP1 and RAGE Genes Transporting Amyloid and Tau Protein in the Hippocampal CA3 Area in an Ischemic Model of Alzheimer’s Disease with 2-Year Survival

Pluta,

Kocki,

Bogucki

et al. 2023

Cells

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Explaining changes at the gene level that occur during neurodegeneration in the CA3 area is crucial from the point of view of memory impairment and the development of post-ischemic dementia. An ischemic model of Alzheimer’s disease was used to evaluate changes in the expression of genes related to amyloid transport in the CA3 region of the hippocampus after 10 min of brain ischemia with survival of 2, 7 and 30 days and 12, 18 and 24 months. The quantitative reverse transcriptase PCR assay revealed that the expression of the LRP1 and RAGE genes involved in amyloid transport was dysregulated from 2 days to 24 months post-ischemia in the CA3 area of the hippocampus. LRP1 gene expression 2 and 7 days after ischemia was below control values. However, its expression from day 30 to 24 months, survival after an ischemic episode was above control values. RAGE gene expression 2 days after ischemia was below control values, reaching a maximum increase 7 and 30 days post-ischemia. Then, after 12, 18 and 24 months, it was again below the control values. The data indicate that in the CA3 area of the hippocampus, an episode of brain ischemia causes the increased expression of the RAGE gene for 7–30 days during the acute phase and that of LRP1 from 1 to 24 months after ischemia during the chronic stage. In other words, in the early post-ischemic stage, the expression of the gene that transport amyloid to the brain increases (7–30 days). Conversely, in the late post-ischemic stage, amyloid scavenging/cleaning gene activity increases, reducing and/or preventing further neuronal damage or facilitating the healing of damaged sites. This is how the new phenomenon of pyramidal neuronal damage in the CA3 area after ischemia is defined. In summary, post-ischemic modification of the LRP1 and RAGE genes is useful in the study of the ischemic pathways and molecular factors involved in the development of Alzheimer’s disease.

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Ovocystatin Induced Changes in Expression of Alzheimer’s Disease Relevant Proteins in APP/PS1 Transgenic Mice

Cited by 3 publications

References 54 publications

Effect of Ovocystatin on Amyloid β 1-42 Aggregation—In Vitro Studies

Effect of Ovocystatin on Amyloid β 1-42 Aggregation—In Vitro Studies

Cystatins: unravelling the biological implications for neuroprotection

LRP1 and RAGE Genes Transporting Amyloid and Tau Protein in the Hippocampal CA3 Area in an Ischemic Model of Alzheimer’s Disease with 2-Year Survival

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