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A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2
Akkermansia muciniphila can produce various mucin-degrading proteins. However, the functional characteristics of these proteins and their role in mucin degradation are unclear. Of the predicted protein-coding genes, Amuc_1434, which encodes for a hypothetical protein, is the focus in this study. A r...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6982040/ https://www.ncbi.nlm.nih.gov/pubmed/31861919 http://dx.doi.org/10.3390/ijms21010072 |
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author | Meng, Xin Wang, Wencheng Lan, Tianqi Yang, Wanxin Yu, Dahai Fang, Xuexun Wu, Hao |
author_facet | Meng, Xin Wang, Wencheng Lan, Tianqi Yang, Wanxin Yu, Dahai Fang, Xuexun Wu, Hao |
author_sort | Meng, Xin |
collection | PubMed |
description | Akkermansia muciniphila can produce various mucin-degrading proteins. However, the functional characteristics of these proteins and their role in mucin degradation are unclear. Of the predicted protein-coding genes, Amuc_1434, which encodes for a hypothetical protein, is the focus in this study. A recombinant enzyme Amuc_1434 containing the 6× His-tag produced in Escherichia coli (hereinafter termed Amuc_1434*) was isolated to homogeneity and biochemically characterised. Results showed that the enzyme can hydrolyse hemoglobin with an activity of 17.21 U/μg. The optimal pH and temperature for hemoglobin hydrolysis of Amuc_1434* were found to be around 8.0 and 40 °C, respectively. Amuc_1434* is identified as a member of the aspartic protease family through the action of inhibitor pepstatin A. Amuc_1434* promotes the adhesion of colon cancer cell line LS174T, which can highly express Muc2. Significantly Amuc_1434* can degrade Muc2 of colon cancer cells. Amuc_1434 is mainly located in the colon of BALB/c mice. These results suggest that the presence of Amuc_1434 from Akkermansia muciniphila may be correlated with the restoration of gut barrier function by decreasing mucus layer thickness. |
format | Online Article Text |
id | pubmed-6982040 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-69820402020-02-07 A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2 Meng, Xin Wang, Wencheng Lan, Tianqi Yang, Wanxin Yu, Dahai Fang, Xuexun Wu, Hao Int J Mol Sci Article Akkermansia muciniphila can produce various mucin-degrading proteins. However, the functional characteristics of these proteins and their role in mucin degradation are unclear. Of the predicted protein-coding genes, Amuc_1434, which encodes for a hypothetical protein, is the focus in this study. A recombinant enzyme Amuc_1434 containing the 6× His-tag produced in Escherichia coli (hereinafter termed Amuc_1434*) was isolated to homogeneity and biochemically characterised. Results showed that the enzyme can hydrolyse hemoglobin with an activity of 17.21 U/μg. The optimal pH and temperature for hemoglobin hydrolysis of Amuc_1434* were found to be around 8.0 and 40 °C, respectively. Amuc_1434* is identified as a member of the aspartic protease family through the action of inhibitor pepstatin A. Amuc_1434* promotes the adhesion of colon cancer cell line LS174T, which can highly express Muc2. Significantly Amuc_1434* can degrade Muc2 of colon cancer cells. Amuc_1434 is mainly located in the colon of BALB/c mice. These results suggest that the presence of Amuc_1434 from Akkermansia muciniphila may be correlated with the restoration of gut barrier function by decreasing mucus layer thickness. MDPI 2019-12-20 /pmc/articles/PMC6982040/ /pubmed/31861919 http://dx.doi.org/10.3390/ijms21010072 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Meng, Xin Wang, Wencheng Lan, Tianqi Yang, Wanxin Yu, Dahai Fang, Xuexun Wu, Hao A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2 |
title | A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2 |
title_full | A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2 |
title_fullStr | A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2 |
title_full_unstemmed | A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2 |
title_short | A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2 |
title_sort | purified aspartic protease from akkermansia muciniphila plays an important role in degrading muc2 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6982040/ https://www.ncbi.nlm.nih.gov/pubmed/31861919 http://dx.doi.org/10.3390/ijms21010072 |
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