Altered polyadenylation site usage in SERPINA1 3’UTR in response to cellular stress affects A1AT protein expression

Abstract Alternative polyadenylation results in different 3’ isoforms of messenger RNA (mRNA) transcripts. Alternative polyadenylation in the 3’ untranslated region (3’UTR) can alter RNA localization, stability and translational efficiency. The SERPINA1 mRNA has two distinct 3’ UTR isoforms, both of...

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Main Authors: F. N. U. Jiamutai, Abigail Hatfield, Austin Herbert, Debarati Majumdar, Vijay Shankar, Lela Lackey
Format: Article
Language:English
Published: Nature Portfolio 2025-07-01
Series:Scientific Reports
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Online Access:https://doi.org/10.1038/s41598-025-07569-3
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author F. N. U. Jiamutai
Abigail Hatfield
Austin Herbert
Debarati Majumdar
Vijay Shankar
Lela Lackey
author_facet F. N. U. Jiamutai
Abigail Hatfield
Austin Herbert
Debarati Majumdar
Vijay Shankar
Lela Lackey
author_sort F. N. U. Jiamutai
collection DOAJ
description Abstract Alternative polyadenylation results in different 3’ isoforms of messenger RNA (mRNA) transcripts. Alternative polyadenylation in the 3’ untranslated region (3’UTR) can alter RNA localization, stability and translational efficiency. The SERPINA1 mRNA has two distinct 3’ UTR isoforms, both of which express the protease inhibitor α-1-antitrypsin (A1AT). A1AT is an acute phase protein that is expressed and secreted from liver hepatocytes and upregulated during inflammation. Low levels of A1AT in the lung contributes to chronic obstructive pulmonary disease, while misfolding of A1AT in the liver contributes to liver cirrhosis. We analyzed the dynamics of alternative polyadenylation during cellular stress by treating the liver cell line HepG2 with the cytokine interleukin 6 (IL-6), ethanol or peroxide. SERPINA1 is transcriptionally upregulated after IL-6 treatment and has altered polyadenylation, resulting in an increase in long 3’UTR isoforms. We find that the long 3’UTR represses endogenous A1AT protein expression even with high levels of SERPINA1 mRNA. SERPINA1 expression and 3’ end processing are not affected by ethanol or peroxide. IL-6-induced changes in transcriptome-wide transcriptional regulation suggest changes to the endoplasmic reticulum and in secretory protein processing. Our data shows that inflammation influences polyA site choice for SERPINA1 transcripts, resulting in reduced A1AT protein expression.
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spelling doaj-art-337f9b6c503d46d2a7e70ebf5bc62e1f2025-08-20T03:03:32ZengNature PortfolioScientific Reports2045-23222025-07-0115111410.1038/s41598-025-07569-3Altered polyadenylation site usage in SERPINA1 3’UTR in response to cellular stress affects A1AT protein expressionF. N. U. Jiamutai0Abigail Hatfield1Austin Herbert2Debarati Majumdar3Vijay Shankar4Lela Lackey5Department of Genetics and Biochemistry, Center for Human Genetics, Clemson UniversityDepartment of Genetics and Biochemistry, Center for Human Genetics, Clemson UniversityDepartment of Genetics and Biochemistry, Center for Human Genetics, Clemson UniversityDepartment of Genetics and Biochemistry, Center for Human Genetics, Clemson UniversityDepartment of Genetics and Biochemistry, Center for Human Genetics, Clemson UniversityDepartment of Genetics and Biochemistry, Center for Human Genetics, Clemson UniversityAbstract Alternative polyadenylation results in different 3’ isoforms of messenger RNA (mRNA) transcripts. Alternative polyadenylation in the 3’ untranslated region (3’UTR) can alter RNA localization, stability and translational efficiency. The SERPINA1 mRNA has two distinct 3’ UTR isoforms, both of which express the protease inhibitor α-1-antitrypsin (A1AT). A1AT is an acute phase protein that is expressed and secreted from liver hepatocytes and upregulated during inflammation. Low levels of A1AT in the lung contributes to chronic obstructive pulmonary disease, while misfolding of A1AT in the liver contributes to liver cirrhosis. We analyzed the dynamics of alternative polyadenylation during cellular stress by treating the liver cell line HepG2 with the cytokine interleukin 6 (IL-6), ethanol or peroxide. SERPINA1 is transcriptionally upregulated after IL-6 treatment and has altered polyadenylation, resulting in an increase in long 3’UTR isoforms. We find that the long 3’UTR represses endogenous A1AT protein expression even with high levels of SERPINA1 mRNA. SERPINA1 expression and 3’ end processing are not affected by ethanol or peroxide. IL-6-induced changes in transcriptome-wide transcriptional regulation suggest changes to the endoplasmic reticulum and in secretory protein processing. Our data shows that inflammation influences polyA site choice for SERPINA1 transcripts, resulting in reduced A1AT protein expression.https://doi.org/10.1038/s41598-025-07569-3PolyadenylationRNA processingInterleukin 6 (IL-6)CirrhosisSERPINA1Alpha1 anti-trypsin (A1AT)
spellingShingle F. N. U. Jiamutai
Abigail Hatfield
Austin Herbert
Debarati Majumdar
Vijay Shankar
Lela Lackey
Altered polyadenylation site usage in SERPINA1 3’UTR in response to cellular stress affects A1AT protein expression
Scientific Reports
Polyadenylation
RNA processing
Interleukin 6 (IL-6)
Cirrhosis
SERPINA1
Alpha1 anti-trypsin (A1AT)
title Altered polyadenylation site usage in SERPINA1 3’UTR in response to cellular stress affects A1AT protein expression
title_full Altered polyadenylation site usage in SERPINA1 3’UTR in response to cellular stress affects A1AT protein expression
title_fullStr Altered polyadenylation site usage in SERPINA1 3’UTR in response to cellular stress affects A1AT protein expression
title_full_unstemmed Altered polyadenylation site usage in SERPINA1 3’UTR in response to cellular stress affects A1AT protein expression
title_short Altered polyadenylation site usage in SERPINA1 3’UTR in response to cellular stress affects A1AT protein expression
title_sort altered polyadenylation site usage in serpina1 3 utr in response to cellular stress affects a1at protein expression
topic Polyadenylation
RNA processing
Interleukin 6 (IL-6)
Cirrhosis
SERPINA1
Alpha1 anti-trypsin (A1AT)
url https://doi.org/10.1038/s41598-025-07569-3
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