A Set of Proximal Regulatory Elements Contribute to the Transcriptional Activity of the Human Lipoprotein Lipase Promoter
Lipoprotein lipase (LPL) is a multifunctional protein that catalyzes the hydrolysis of plasma triglycerides, releasing free fatty acids, which play critical roles in the metabolism and transport of lipids. The transcription of <i>LPL</i> in response to cell types and regulatory factors i...
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2024-11-01
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| author | Nasmah K. Bastaki Taybha A. Albarjes Afnan K. Mohamed Noorhan H. Sabri Suzanne A. Al-Bustan |
| author_facet | Nasmah K. Bastaki Taybha A. Albarjes Afnan K. Mohamed Noorhan H. Sabri Suzanne A. Al-Bustan |
| author_sort | Nasmah K. Bastaki |
| collection | DOAJ |
| description | Lipoprotein lipase (LPL) is a multifunctional protein that catalyzes the hydrolysis of plasma triglycerides, releasing free fatty acids, which play critical roles in the metabolism and transport of lipids. The transcription of <i>LPL</i> in response to cell types and regulatory factors is a complex process that starts with its promoter. In previous studies, several proximal regulatory elements within the human <i>LPL</i> promoter were individually characterized. This study was designed to characterize the effect of 12 proximal regulatory elements as a combined unit on the transcriptional activity of the <i>LPL</i> promoter. The hypothesis was that these proximal regulatory elements collectively result in the optimal transcriptional activity of the human <i>LPL</i> promoter. Full and partial <i>LPL</i> promoter sequences, which contained and excluded the 12 regulatory elements, respectively, were cloned and inserted into a promoterless luciferase reporter vector. The functional activities of these constructs were tested in vitro using a dual-luciferase reporter assay. Our results showed that HEK-293 cells transfected with the full <i>LPL</i> promoter exhibited significantly greater luciferase activity than cells transfected with partial <i>LPL</i> promoters. Our results indicate that the proximal regulatory elements within the <i>LPL</i> promoter, including four TATA boxes, two Oct-1 sites, one CT element, two C/EBPα sites, one SP1 site, and two cis-acting regions (LP-α and LP-β), are essential for its transcriptional activity. |
| format | Article |
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| institution | OA Journals |
| issn | 1467-3037 1467-3045 |
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| spelling | doaj-art-93d6befd6fe74a65a708f532f72f798a2025-08-20T01:53:53ZengMDPI AGCurrent Issues in Molecular Biology1467-30371467-30452024-11-014611132091322210.3390/cimb46110788A Set of Proximal Regulatory Elements Contribute to the Transcriptional Activity of the Human Lipoprotein Lipase PromoterNasmah K. Bastaki0Taybha A. Albarjes1Afnan K. Mohamed2Noorhan H. Sabri3Suzanne A. Al-Bustan4Department of Biological Science, Faculty of Science, Kuwait University, Kuwait City 13060, KuwaitDepartment of Biological Science, Faculty of Science, Kuwait University, Kuwait City 13060, KuwaitDepartment of Biological Science, Faculty of Science, Kuwait University, Kuwait City 13060, KuwaitDepartment of Biological Science, Faculty of Science, Kuwait University, Kuwait City 13060, KuwaitDepartment of Biological Science, Faculty of Science, Kuwait University, Kuwait City 13060, KuwaitLipoprotein lipase (LPL) is a multifunctional protein that catalyzes the hydrolysis of plasma triglycerides, releasing free fatty acids, which play critical roles in the metabolism and transport of lipids. The transcription of <i>LPL</i> in response to cell types and regulatory factors is a complex process that starts with its promoter. In previous studies, several proximal regulatory elements within the human <i>LPL</i> promoter were individually characterized. This study was designed to characterize the effect of 12 proximal regulatory elements as a combined unit on the transcriptional activity of the <i>LPL</i> promoter. The hypothesis was that these proximal regulatory elements collectively result in the optimal transcriptional activity of the human <i>LPL</i> promoter. Full and partial <i>LPL</i> promoter sequences, which contained and excluded the 12 regulatory elements, respectively, were cloned and inserted into a promoterless luciferase reporter vector. The functional activities of these constructs were tested in vitro using a dual-luciferase reporter assay. Our results showed that HEK-293 cells transfected with the full <i>LPL</i> promoter exhibited significantly greater luciferase activity than cells transfected with partial <i>LPL</i> promoters. Our results indicate that the proximal regulatory elements within the <i>LPL</i> promoter, including four TATA boxes, two Oct-1 sites, one CT element, two C/EBPα sites, one SP1 site, and two cis-acting regions (LP-α and LP-β), are essential for its transcriptional activity.https://www.mdpi.com/1467-3045/46/11/788lipoprotein lipasehumanpromotorluciferaseregulatory elements |
| spellingShingle | Nasmah K. Bastaki Taybha A. Albarjes Afnan K. Mohamed Noorhan H. Sabri Suzanne A. Al-Bustan A Set of Proximal Regulatory Elements Contribute to the Transcriptional Activity of the Human Lipoprotein Lipase Promoter Current Issues in Molecular Biology lipoprotein lipase human promotor luciferase regulatory elements |
| title | A Set of Proximal Regulatory Elements Contribute to the Transcriptional Activity of the Human Lipoprotein Lipase Promoter |
| title_full | A Set of Proximal Regulatory Elements Contribute to the Transcriptional Activity of the Human Lipoprotein Lipase Promoter |
| title_fullStr | A Set of Proximal Regulatory Elements Contribute to the Transcriptional Activity of the Human Lipoprotein Lipase Promoter |
| title_full_unstemmed | A Set of Proximal Regulatory Elements Contribute to the Transcriptional Activity of the Human Lipoprotein Lipase Promoter |
| title_short | A Set of Proximal Regulatory Elements Contribute to the Transcriptional Activity of the Human Lipoprotein Lipase Promoter |
| title_sort | set of proximal regulatory elements contribute to the transcriptional activity of the human lipoprotein lipase promoter |
| topic | lipoprotein lipase human promotor luciferase regulatory elements |
| url | https://www.mdpi.com/1467-3045/46/11/788 |
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