Please use this identifier to cite or link to this item:
doi:10.22028/D291-38684
Title: | Protein Kinase CK2 Contributes to Glucose Homeostasis by Targeting Fructose-1,6-Bisphosphatase 1 |
Author(s): | Pack, Mandy Gulde, Tim Nikolai Völcker, Michelle Victoria Boewe, Anne S. Wrublewsky, Selina Ampofo, Emmanuel Montenarh, Mathias Götz, Claudia |
Language: | English |
Title: | International Journal of Molecular Sciences |
Volume: | 24 (2023) |
Issue: | 1 |
Publisher/Platform: | MDPI |
Year of Publication: | 2022 |
Free key words: | protein kinase CK2 fructose-1,6-bisphosphatase gluconeogenesis diabetes-associated genes |
DDC notations: | 610 Medicine and health |
Publikation type: | Journal Article |
Abstract: | Glucose homeostasis is of critical importance for the survival of organisms. It is under hormonal control and often coordinated by the action of kinases and phosphatases. We have previously shown that CK2 regulates insulin production and secretion in pancreatic β-cells. In order to shed more light on the CK2-regulated network of glucose homeostasis, in the present study, a qRT-PCR array was carried out with 84 diabetes-associated genes. After inhibition of CK2, fructose-1,6-bisphosphatase 1 (FBP1) showed a significant lower gene expression. Moreover, FBP1 activity was down-regulated. Being a central enzyme of gluconeogenesis, the secretion of glucose was decreased as well. Thus, FBP1 is a new factor in the CK2-regulated network implicated in carbohydrate metabolism control. |
DOI of the first publication: | 10.3390/ijms24010428 |
Link to this record: | urn:nbn:de:bsz:291--ds-386843 hdl:20.500.11880/34885 http://dx.doi.org/10.22028/D291-38684 |
ISSN: | 1422-0067 |
Date of registration: | 16-Jan-2023 |
Faculty: | M - Medizinische Fakultät |
Department: | M - Chirurgie M - Medizinische Biochemie und Molekularbiologie |
Professorship: | M - Prof. Dr. Robert Ernst M - Prof. Dr. Michael D. Menger |
Collections: | SciDok - Der Wissenschaftsserver der Universität des Saarlandes |
Files for this record:
File | Description | Size | Format | |
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ijms-24-00428.pdf | 1,86 MB | Adobe PDF | View/Open |
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