The intrinsic amyloidogenic propensity of cofilin-1 is aggravated by Cys-80 oxidation : A possible link with neurodegenerative diseases
Copyright © 2021 Elsevier Inc. All rights reserved..
Cofilin-1, an actin dynamizing protein, forms actin-cofilin rods, which is one of the major events that exacerbates the pathophysiology of amyloidogenic diseases. Cysteine oxidation in cofilin-1 under oxidative stress plays a crucial role in the formation of these rods. Others and we have reported that cofilin-1 possesses a self-oligomerization property in vitro and in vivo under physiological conditions. However, it remains elusive if cofilin-1 itself forms amyloid-like structures. We, therefore, hypothesized that cofilin-1 might form amyloid-like assemblies, with a potential to intensify the pathophysiology of amyloid-linked diseases. We used various in silico and in vitro techniques and examined the amyloid-forming propensity of cofilin-1. The study confirms that cofilin-1 possesses an intrinsic tendency of aggregation and forms amyloid-like structures in vitro. Further, we studied the effect of cysteine oxidation on the stability and structural features of cofilin-1. Our data show that oxidation at Cys-80 renders cofilin-1 unstable, leading to a partial loss of protein structure. The results substantiate our hypothesis and establish a strong possibility that cofilin-1 aggregation might play a role in cofilin-mediated pathology and the progression of several amyloid-linked diseases.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:569 |
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| Enthalten in: |
Biochemical and biophysical research communications - 569(2021) vom: 10. Sept., Seite 187-192 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Kaushik, Vibha [VerfasserIn] |
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| Links: |
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| Themen: |
Actin dynamics |
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| Anmerkungen: |
Date Completed 22.11.2021 Date Revised 22.11.2021 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.bbrc.2021.07.013 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM328018708 |
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| 520 | |a Copyright © 2021 Elsevier Inc. All rights reserved. | ||
| 520 | |a Cofilin-1, an actin dynamizing protein, forms actin-cofilin rods, which is one of the major events that exacerbates the pathophysiology of amyloidogenic diseases. Cysteine oxidation in cofilin-1 under oxidative stress plays a crucial role in the formation of these rods. Others and we have reported that cofilin-1 possesses a self-oligomerization property in vitro and in vivo under physiological conditions. However, it remains elusive if cofilin-1 itself forms amyloid-like structures. We, therefore, hypothesized that cofilin-1 might form amyloid-like assemblies, with a potential to intensify the pathophysiology of amyloid-linked diseases. We used various in silico and in vitro techniques and examined the amyloid-forming propensity of cofilin-1. The study confirms that cofilin-1 possesses an intrinsic tendency of aggregation and forms amyloid-like structures in vitro. Further, we studied the effect of cysteine oxidation on the stability and structural features of cofilin-1. Our data show that oxidation at Cys-80 renders cofilin-1 unstable, leading to a partial loss of protein structure. The results substantiate our hypothesis and establish a strong possibility that cofilin-1 aggregation might play a role in cofilin-mediated pathology and the progression of several amyloid-linked diseases | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Actin dynamics | |
| 650 | 4 | |a Actin-cofilin rods | |
| 650 | 4 | |a Alzheimer's disease | |
| 650 | 4 | |a Amyloids | |
| 650 | 4 | |a Cofilin-1 | |
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| 700 | 1 | |a Brünnert, Daniela |e verfasserin |4 aut | |
| 700 | 1 | |a Hanschmann, Eva-Maria |e verfasserin |4 aut | |
| 700 | 1 | |a Sharma, Phulwanti Kumari |e verfasserin |4 aut | |
| 700 | 1 | |a Anand, Bibin G |e verfasserin |4 aut | |
| 700 | 1 | |a Kar, Karunakar |e verfasserin |4 aut | |
| 700 | 1 | |a Kateriya, Suneel |e verfasserin |4 aut | |
| 700 | 1 | |a Goyal, Pankaj |e verfasserin |4 aut | |
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