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Article ; Online: Involvement of calcium ions in amyloid-β-induced lamin fragmentation.

Hossain, Md Selim / Ramasamy, Vijay Sankar / Park, Il-Seon

Biochimica et biophysica acta. Molecular cell research

2022 Volume 1870, Issue 1, Page(s) 119383

Abstract: Amyloid-β (Aβ) peptide, the main pathogenic peptide in Alzheimer's disease, has been shown to induce an increase in cytoplasmic calcium concentration (CCC). In the current study, we explored the cytotoxic signal transduction pathway in 42-amino-acid Aβ ( ... ...

Abstract	Amyloid-β (Aβ) peptide, the main pathogenic peptide in Alzheimer's disease, has been shown to induce an increase in cytoplasmic calcium concentration (CCC). In the current study, we explored the cytotoxic signal transduction pathway in 42-amino-acid Aβ (Aβ42)-treated HeLa cells in relation to the increase in CCC. The increase in CCC was prominent in cells treated twice with oligomeric Aβ42. We previously showed that double treatment also promoted Aβ-induced lamin fragmentation (AILF), which appears to be mediated by cathepsin L. Apoptotic caspase activation was a downstream event of AILF. The Ca
MeSH term(s)	Humans ; Calcium ; Cathepsin L ; Peptide Fragments/pharmacology ; Peptide Fragments/metabolism ; HeLa Cells ; Lamins ; Neuroblastoma/pathology ; Amyloid beta-Peptides/pharmacology ; Amyloid beta-Peptides/metabolism ; Caspases/metabolism ; Ions
Chemical Substances	Calcium (SY7Q814VUP) ; Cathepsin L (EC 3.4.22.15) ; Peptide Fragments ; Lamins ; 1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester (139890-68-9) ; Amyloid beta-Peptides ; Caspases (EC 3.4.22.-) ; Ions
Language	English
Publishing date	2022-10-24
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2022.119383
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Article: Amyloid β cytotoxicity is enhanced or reduced depending on formation of amyloid β oligomeric forms

Shahnawaz, Md / Bilkis, Tahmina / Park, Il-Seon

Biotechnology letters. 2021 Jan., v. 43, no. 1

2021

Abstract: OBJECTIVES: We explored the underlying mechanisms that facilitate reducing and enhancing effects of exogenous proteins on cytotoxicity of amyloid β (Aβ), a main pathogen of Alzheimer’s disease, by using an Escherichia coli chaperonin DnaK. RESULTS: DnaK ... ...

Abstract	OBJECTIVES: We explored the underlying mechanisms that facilitate reducing and enhancing effects of exogenous proteins on cytotoxicity of amyloid β (Aβ), a main pathogen of Alzheimer’s disease, by using an Escherichia coli chaperonin DnaK. RESULTS: DnaK was chosen as a tool, because it, easily available and functionally stable, reduced or enhanced Aβ cytotoxicity depending on its concentration. Cytotoxicity was enhanced when the molar ratio of DnaK to Aβ42, at 20 μM Aβ42, was 0.01–0.5, while reduced cytotoxicity was observed at higher ratios (> 1) at 1 μM Aβ42. Significant amounts of oligomeric Aβ42 species accumulated concomitantly with enhanced cytotoxicity, whereas the oligomers appeared to form complexes with DnaK in conditions of reduced cytotoxicity. CONCLUSIONS: The difference in cytotoxicity was due to variations in the toxic oligomeric Aβ species and DnaK is a useful tool for the study of the Aβ ultrastructure formation and toxicity of Aβ peptide.
Keywords	Escherichia coli ; amyloid ; biotechnology ; chaperonins ; cytotoxicity ; pathogens ; peptides ; ultrastructure
Language	English
Dates of publication	2021-01
Size	p. 165-175.
Publishing place	Springer Netherlands
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	423853-9
ISSN	1573-6776 ; 0141-5492
ISSN (online)	1573-6776
ISSN	0141-5492
DOI	10.1007/s10529-020-03015-8
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Article ; Online: Evidence for a Strong Relationship between the Cytotoxicity and Intracellular Location of β-Amyloid

Md. Aminul Haque / Md. Selim Hossain / Tahmina Bilkis / Md. Imamul Islam / Il-Seon Park

Life, Vol 12, Iss 4, p

2022 Volume 577

Abstract: β-Amyloid (Aβ) is a hallmark peptide of Alzheimer’s disease (AD). Herein, we explored the mechanism underlying the cytotoxicity of this peptide. Double treatment with oligomeric 42-amino-acid Aβ (Aβ42) species, which are more cytotoxic than other ... ...

Abstract	β-Amyloid (Aβ) is a hallmark peptide of Alzheimer’s disease (AD). Herein, we explored the mechanism underlying the cytotoxicity of this peptide. Double treatment with oligomeric 42-amino-acid Aβ (Aβ42) species, which are more cytotoxic than other conformers such as monomers and fibrils, resulted in increased cytotoxicity. Under this treatment condition, an increase in intracellular localization of the peptide was observed, which indicated that the peptide administered extracellularly entered the cells. The cell-permeable peptide TAT-tagged Aβ42 (tAβ42), which was newly prepared for the study and found to be highly cell-permeable and soluble, induced Aβ-specific lamin protein cleavage, caspase-3/7-like DEVDase activation, and high cytotoxicity (5–10-fold higher than that induced by the wild-type oligomeric preparations). Oligomeric species enrichment and double treatment were not necessary for enhancing the cytotoxicity and intracellular location of the fusion peptide. Taiwaniaflavone, an inhibitor of the cytotoxicity of wild-type Aβ42 and tAβ42, strongly blocked the internalization of the peptides into the cells. These data imply a strong relationship between the cytotoxicity and intracellular location of the Aβ peptide. Based on these results, we suggest that agents that can reduce the cell permeability of Aβ42 are potential AD therapeutics.
Keywords	β-amyloid ; Alzheimer’s disease ; cytotoxicity ; cell permeability ; oligomeric species ; tAβ42 ; Science ; Q
Subject code	571
Language	English
Publishing date	2022-04-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: Differential involvement of caspase-6 in amyloid-β-induced fragmentation of lamin A and B.

Islam, Md Imamul / Hossain, Md Selim / Park, Il-Seon

Biochemistry and biophysics reports

2020 Volume 24, Page(s) 100839

Abstract: Amyloid-β (Aβ), a peptide implicated in Alzheimer's disease, was shown to cause specific fragmentation of lamin proteins, which was mediated by an unidentified protease named nuclear scaffold protease (NSP) independently of caspase-6. Because caspase-6 ... ...

Abstract	Amyloid-β (Aβ), a peptide implicated in Alzheimer's disease, was shown to cause specific fragmentation of lamin proteins, which was mediated by an unidentified protease named nuclear scaffold protease (NSP) independently of caspase-6. Because caspase-6 is responsible for the fragmentation process in many other damage-induced apoptosis, here we further investigated possible involvement of caspase-6 in Aβ-induced lamin fragmentation under various conditions. We found that lamin A fragment generated by NSP (named fragment b) disappeared in cells incubated with Aβ42 for prolonged periods and this product was preserved by a caspase-6 inhibitor. Furthermore, caspase-6 could remove fragment b in nuclei isolated from Aβ42-treated cells (ANU). Lamin B in ANU was fragmented by caspase-6 only after treatment with an alkaline phosphatase. The caspase-mediated fragmentation of lamin B was also achieved with nuclei isolated from cells incubated with Aβ42 plus a Cdk5 inhibitor. The results indicate that Aβ42 induces NSP-mediated fragmentation of lamin A and the following removal process of fragment b by caspase-6 and an Aβ-induced phosphorylation prevents the fragmentation of lamin B by caspase-6. The pathway leading to lamin protein fragmentation in this investigation appears to be specific for Aβ and thus the data will provide novel insights into the toxicity of the peptide.
Language	English
Publishing date	2020-10-26
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2831046-9
ISSN	2405-5808 ; 2405-5808
ISSN (online)	2405-5808
ISSN	2405-5808
DOI	10.1016/j.bbrep.2020.100839
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Article ; Online: Amyloid β cytotoxicity is enhanced or reduced depending on formation of amyloid β oligomeric forms.

Shahnawaz, Md / Bilkis, Tahmina / Park, Il-Seon

Biotechnology letters

2020 Volume 43, Issue 1, Page(s) 165–175

Abstract: Objectives: We explored the underlying mechanisms that facilitate reducing and enhancing effects of exogenous proteins on cytotoxicity of amyloid β (Aβ), a main pathogen of Alzheimer's disease, by using an Escherichia coli chaperonin DnaK.: Results: ... ...

Abstract	Objectives: We explored the underlying mechanisms that facilitate reducing and enhancing effects of exogenous proteins on cytotoxicity of amyloid β (Aβ), a main pathogen of Alzheimer's disease, by using an Escherichia coli chaperonin DnaK. Results: DnaK was chosen as a tool, because it, easily available and functionally stable, reduced or enhanced Aβ cytotoxicity depending on its concentration. Cytotoxicity was enhanced when the molar ratio of DnaK to Aβ42, at 20 μM Aβ42, was 0.01-0.5, while reduced cytotoxicity was observed at higher ratios (> 1) at 1 μM Aβ42. Significant amounts of oligomeric Aβ42 species accumulated concomitantly with enhanced cytotoxicity, whereas the oligomers appeared to form complexes with DnaK in conditions of reduced cytotoxicity. Conclusions: The difference in cytotoxicity was due to variations in the toxic oligomeric Aβ species and DnaK is a useful tool for the study of the Aβ ultrastructure formation and toxicity of Aβ peptide.
MeSH term(s)	Alzheimer Disease ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Peptides/toxicity ; Cell Line, Tumor ; Cell Survival/drug effects ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/metabolism ; HSP70 Heat-Shock Proteins/chemistry ; HSP70 Heat-Shock Proteins/metabolism ; Humans ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Peptide Fragments/toxicity ; Protein Aggregation, Pathological
Chemical Substances	Amyloid beta-Peptides ; Escherichia coli Proteins ; HSP70 Heat-Shock Proteins ; Peptide Fragments ; amyloid beta-protein (1-42) ; dnaK protein, E coli (EC 3.6.1.-)
Language	English
Publishing date	2020-10-06
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	423853-9
ISSN	1573-6776 ; 0141-5492
ISSN (online)	1573-6776
ISSN	0141-5492
DOI	10.1007/s10529-020-03015-8
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Article: Evidence for a Strong Relationship between the Cytotoxicity and Intracellular Location of β-Amyloid.

Haque, Md Aminul / Hossain, Md Selim / Bilkis, Tahmina / Islam, Md Imamul / Park, Il-Seon

Life (Basel, Switzerland)

2022 Volume 12, Issue 4

Abstract: β-Amyloid (Aβ) is a hallmark peptide of Alzheimer's disease (AD). Herein, we explored the mechanism underlying the cytotoxicity of this peptide. Double treatment with oligomeric 42-amino-acid Aβ (Aβ42) species, which are more cytotoxic than other ... ...

Abstract	β-Amyloid (Aβ) is a hallmark peptide of Alzheimer's disease (AD). Herein, we explored the mechanism underlying the cytotoxicity of this peptide. Double treatment with oligomeric 42-amino-acid Aβ (Aβ42) species, which are more cytotoxic than other conformers such as monomers and fibrils, resulted in increased cytotoxicity. Under this treatment condition, an increase in intracellular localization of the peptide was observed, which indicated that the peptide administered extracellularly entered the cells. The cell-permeable peptide TAT-tagged Aβ42 (tAβ42), which was newly prepared for the study and found to be highly cell-permeable and soluble, induced Aβ-specific lamin protein cleavage, caspase-3/7-like DEVDase activation, and high cytotoxicity (5-10-fold higher than that induced by the wild-type oligomeric preparations). Oligomeric species enrichment and double treatment were not necessary for enhancing the cytotoxicity and intracellular location of the fusion peptide. Taiwaniaflavone, an inhibitor of the cytotoxicity of wild-type Aβ42 and tAβ42, strongly blocked the internalization of the peptides into the cells. These data imply a strong relationship between the cytotoxicity and intracellular location of the Aβ peptide. Based on these results, we suggest that agents that can reduce the cell permeability of Aβ42 are potential AD therapeutics.
Language	English
Publishing date	2022-04-13
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2662250-6
ISSN	2075-1729
ISSN	2075-1729
DOI	10.3390/life12040577
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Article ; Online: Differential involvement of caspase-6 in amyloid-β-induced fragmentation of lamin A and B

Md Imamul Islam / Md Selim Hossain / Il-Seon Park

Biochemistry and Biophysics Reports, Vol 24, Iss , Pp 100839- (2020)

2020

Abstract	Amyloid-β (Aβ), a peptide implicated in Alzheimer's disease, was shown to cause specific fragmentation of lamin proteins, which was mediated by an unidentified protease named nuclear scaffold protease (NSP) independently of caspase-6. Because caspase-6 is responsible for the fragmentation process in many other damage-induced apoptosis, here we further investigated possible involvement of caspase-6 in Aβ-induced lamin fragmentation under various conditions. We found that lamin A fragment generated by NSP (named fragment b) disappeared in cells incubated with Aβ42 for prolonged periods and this product was preserved by a caspase-6 inhibitor. Furthermore, caspase-6 could remove fragment b in nuclei isolated from Aβ42-treated cells (ANU). Lamin B in ANU was fragmented by caspase-6 only after treatment with an alkaline phosphatase. The caspase-mediated fragmentation of lamin B was also achieved with nuclei isolated from cells incubated with Aβ42 plus a Cdk5 inhibitor. The results indicate that Aβ42 induces NSP-mediated fragmentation of lamin A and the following removal process of fragment b by caspase-6 and an Aβ-induced phosphorylation prevents the fragmentation of lamin B by caspase-6. The pathway leading to lamin protein fragmentation in this investigation appears to be specific for Aβ and thus the data will provide novel insights into the toxicity of the peptide.
Keywords	Amyloid β ; Alzheimer's disease ; Lamin ; Nuclear scaffold protease ; Caspase-6 ; Phosphorylation ; Biology (General) ; QH301-705.5 ; Biochemistry ; QD415-436
Subject code	570
Language	English
Publishing date	2020-12-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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Article: α-Klotho levels in girls with central precocious puberty: potential as a diagnostic and monitoring marker.

Park, Jun-Hong / Noh, Eu-Seon / Hwang, Il Tae

Frontiers in endocrinology

2024 Volume 15, Page(s) 1383812

Abstract: Background: Recent studies suggest a link between the Klotho protein, sex hormones, and insulin-like growth factor-1 (IGF-1), indicating that α-Klotho levels may rise during puberty, including in central precocious puberty (CPP) cases. This study aimed ... ...

Abstract	Background: Recent studies suggest a link between the Klotho protein, sex hormones, and insulin-like growth factor-1 (IGF-1), indicating that α-Klotho levels may rise during puberty, including in central precocious puberty (CPP) cases. This study aimed to explore α-Klotho levels in girls with CPP to assess its potential as a diagnostic and monitoring tool for this condition. Methods: In total, 139 girls, comprising 82 patients diagnosed with CPP and 57 healthy prepubertal controls, were enrolled in this study. From March 2020 to May 2023, we assessed both α-Klotho levels and clinical parameters. α-Klotho concentrations were measured using an α-Klotho ELISA kit. For the girls with CPP, we additionally analyzed samples taken 6 months after GnRH agonist treatment. Results: α-Klotho levels were higher in the CPP group compared with the control (CPP group: 2529 ± 999 ng/mL; control group: 1802 ± 675 pg/mL) (P < 0.001), and its level modest decreased after 6 months of GnRH agonist treatment (2147± 789 pg/mL) (P < 0.001). The association between α-Klotho and IGF-1 SDS, follicular stimulating hormone and baseline luteinizing hormone was assessed by partial correlation after adjusting for age, BMI SDS (r= 0.416, p= <0.001; r= 0.261, p= 0.005; r= 0.278, p= 0.002), respectively. Receiver operating characteristic curve analysis identified an α-Klotho cut-off differentiating CPP from controls, with a cut-off of 1914 pg/mL distinguishing girls with CPP from controls with a sensitivity of 69.5% and specificity of 70.2%; the area under the curve was 0.723. Conclusion: The findings of our study are the first step towards deciphering the role of α-Klotho in puberty induction. With additional data and further research, α-Klotho could potentially be utilized as a significant diagnostic and monitoring tool for CPP.
Language	English
Publishing date	2024-04-08
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2592084-4
ISSN	1664-2392
ISSN	1664-2392
DOI	10.3389/fendo.2024.1383812
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Article ; Online: Successful retrieval of ruptured stent balloon catheter during percutaneous coronary intervention.

Son, Byeng-Ju / Park, Jong-Seon / Kim, Ung / Choi, Kang-Un / Park, Jong-Il

The Journal of invasive cardiology

2024

Abstract: An 82-year-old woman was admitted for non-ST elevation myocardial infarction. ...

Abstract	An 82-year-old woman was admitted for non-ST elevation myocardial infarction.
Language	English
Publishing date	2024-03-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	1154372-3
ISSN	1557-2501 ; 1042-3931
ISSN (online)	1557-2501
ISSN	1042-3931
DOI	10.25270/jic/24.00043
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Article: Anti-inflammatory of disenecionyl

Park, Ji Hyeon / Kim, Jang Hoon / Jang, Seon Il / Cho, Byoung Ok

Heliyon

2023 Volume 9, Issue 10, Page(s) e21032

Abstract: The objective of the present study was to investigate anti-inflammatory effects of ... ...

Abstract	The objective of the present study was to investigate anti-inflammatory effects of disenecionyl
Language	English
Publishing date	2023-10-14
Publishing country	England
Document type	Journal Article
ZDB-ID	2835763-2
ISSN	2405-8440
ISSN	2405-8440
DOI	10.1016/j.heliyon.2023.e21032
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