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Alternative Splicing of the Porcine Glycogen Synthase Kinase 3β (GSK-3β) Gene with Differential Expression Patterns and Regulatory Functions
BACKGROUND: Glycogen synthase kinase 3 (GSK3α and GSK3β) are serine/threonine kinases involved in numerous cellular processes and diverse diseases including mood disorders, Alzheimer’s disease, diabetes, and cancer. However, in pigs, the information on GSK3 is very limited. Identification and charac...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3391277/ https://www.ncbi.nlm.nih.gov/pubmed/22792253 http://dx.doi.org/10.1371/journal.pone.0040250 |
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author | Wang, Linjie Zuo, Bo Xu, Dequan Ren, Zuqing Zhang, Hongping Li, Xuewei Lei, Minggang Xiong, Yuanzhu |
author_facet | Wang, Linjie Zuo, Bo Xu, Dequan Ren, Zuqing Zhang, Hongping Li, Xuewei Lei, Minggang Xiong, Yuanzhu |
author_sort | Wang, Linjie |
collection | PubMed |
description | BACKGROUND: Glycogen synthase kinase 3 (GSK3α and GSK3β) are serine/threonine kinases involved in numerous cellular processes and diverse diseases including mood disorders, Alzheimer’s disease, diabetes, and cancer. However, in pigs, the information on GSK3 is very limited. Identification and characterization of pig GSK3 are not only important for pig genetic improvement, but also contribute to the understanding and development of porcine models for human disease prevention and treatment. METHODOLOGY: Five different isoforms of GSK3β were identified in porcine different tissues, in which three isoforms are novel. These isoforms had differential expression patterns in the fetal and adult of the porcine different tissues. The mRNA expression level of GSK3β isoforms was differentially regulated during the course of the insulin treatment, suggesting that different GSK3β isoforms may have different roles in insulin signaling pathway. Moreover, GSK3β5 had a different role on regulating the glycogen synthase activity, phosphorylation and the expression of porcine GYS1 and GYS2 gene compared to other GSK3β isoforms. CONCLUSIONS: We are the first to report five different isoforms of GSK3β identified from the porcine different tissues. Splice variants of GSK3β exhibit differential activity towards glycogen synthase. These results provide new insight into roles of the GSK3β on regulating glycogen metabolism. |
format | Online Article Text |
id | pubmed-3391277 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-33912772012-07-12 Alternative Splicing of the Porcine Glycogen Synthase Kinase 3β (GSK-3β) Gene with Differential Expression Patterns and Regulatory Functions Wang, Linjie Zuo, Bo Xu, Dequan Ren, Zuqing Zhang, Hongping Li, Xuewei Lei, Minggang Xiong, Yuanzhu PLoS One Research Article BACKGROUND: Glycogen synthase kinase 3 (GSK3α and GSK3β) are serine/threonine kinases involved in numerous cellular processes and diverse diseases including mood disorders, Alzheimer’s disease, diabetes, and cancer. However, in pigs, the information on GSK3 is very limited. Identification and characterization of pig GSK3 are not only important for pig genetic improvement, but also contribute to the understanding and development of porcine models for human disease prevention and treatment. METHODOLOGY: Five different isoforms of GSK3β were identified in porcine different tissues, in which three isoforms are novel. These isoforms had differential expression patterns in the fetal and adult of the porcine different tissues. The mRNA expression level of GSK3β isoforms was differentially regulated during the course of the insulin treatment, suggesting that different GSK3β isoforms may have different roles in insulin signaling pathway. Moreover, GSK3β5 had a different role on regulating the glycogen synthase activity, phosphorylation and the expression of porcine GYS1 and GYS2 gene compared to other GSK3β isoforms. CONCLUSIONS: We are the first to report five different isoforms of GSK3β identified from the porcine different tissues. Splice variants of GSK3β exhibit differential activity towards glycogen synthase. These results provide new insight into roles of the GSK3β on regulating glycogen metabolism. Public Library of Science 2012-07-06 /pmc/articles/PMC3391277/ /pubmed/22792253 http://dx.doi.org/10.1371/journal.pone.0040250 Text en Wang et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Wang, Linjie Zuo, Bo Xu, Dequan Ren, Zuqing Zhang, Hongping Li, Xuewei Lei, Minggang Xiong, Yuanzhu Alternative Splicing of the Porcine Glycogen Synthase Kinase 3β (GSK-3β) Gene with Differential Expression Patterns and Regulatory Functions |
title | Alternative Splicing of the Porcine Glycogen Synthase Kinase 3β (GSK-3β) Gene with Differential Expression Patterns and Regulatory Functions |
title_full | Alternative Splicing of the Porcine Glycogen Synthase Kinase 3β (GSK-3β) Gene with Differential Expression Patterns and Regulatory Functions |
title_fullStr | Alternative Splicing of the Porcine Glycogen Synthase Kinase 3β (GSK-3β) Gene with Differential Expression Patterns and Regulatory Functions |
title_full_unstemmed | Alternative Splicing of the Porcine Glycogen Synthase Kinase 3β (GSK-3β) Gene with Differential Expression Patterns and Regulatory Functions |
title_short | Alternative Splicing of the Porcine Glycogen Synthase Kinase 3β (GSK-3β) Gene with Differential Expression Patterns and Regulatory Functions |
title_sort | alternative splicing of the porcine glycogen synthase kinase 3β (gsk-3β) gene with differential expression patterns and regulatory functions |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3391277/ https://www.ncbi.nlm.nih.gov/pubmed/22792253 http://dx.doi.org/10.1371/journal.pone.0040250 |
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