Mirela Delibegovic

Last updated
Mirela Delibegovic
FRSE
Born
Tuzla
Alma mater University of Dundee
University of Edinburgh
Scientific career
Institutions GlaxoSmithKline
Harvard Medical School
University of Aberdeen
Thesis In vivo effects of insulin on the glycogen targeted forms of protein phosphatase 1  (2003)

Mirela Delibegovic, FRSE is a Bosnian-British pharmacologist/biochemist who is Dean for Industrial Engagement in Research & Knowledge Transfer and Director of Aberdeen Cardiovascular and Diabetes Centre. She is also Regius Professor of Physiology at the University of Aberdeen. During the COVID-19 pandemic, Delibegovic used artificial intelligence to develop technologies that would allow mass-screening for coronavirus disease 2019.

Contents

Early life and education

Delibegovic is from Tuzla in Bosnia and Herzegovina. [1] She grew up during the Bosnian War, which forced her family apart. In the early nineties, she moved to Scotland and finished her secondary school education at George Heriot's School in Edinburgh. [2] Delibegovic studied pharmacology at the University of Edinburgh. [3] In the final year of her undergraduate degree Delibegovic moved to Essex, where she did her undergraduate final year project at GlaxoSmithKline on novel anti-diabetes drugs. [3] She completed her doctoral research with Prof Dame Patricia Cohen at the University of Dundee Medical Research Council Protein Phosphorylation Unit. [4] Here she studied the way that enzymes such as protein phosphatase 1 influenced diabetes development. She was supported by the Royal Society studentship. She has said that she was interested in diabetes because of family history and prevalence of Type 2 diabetes in Bosnia and Herzegovina. [3] During her doctoral research, Delibegovic worked closely with pharmaceutical companies to translate her research to the read world. [4] In 2003 she was awarded the American Heart Association personal fellowship to study the role of PTPN1 in glucose homeostasis at the Harvard Medical School in Boston, USA. She spent four years in Boston, working with Prof Benjamin Neel on mouse models of insulin resistance. [5]

Research and career

In 2007 Delibegovic returned to the United Kingdom, where she was awarded the Research Councils UK 5-year tenure track fellowship to investigate obesity and ageing at the University of Aberdeen. She was made Professor in Diabetes Physiology in 2015 at the age of 38. The field of her research has focussed on the PTP1B phosphatase, the molecular mechanisms that cause diabetes and what the relationship is between diabetes and Alzheimer's disease. [2] She has demonstrated that PTP1B can be used for targeted treatments, reaching the cells of specific organs without causing any side effects. [4] [6] In 2017 Delibegovic demonstrated a novel pharmaceutical, Trodusquemine, that could be used to treat type 2 diabetes and breast cancer. She went on to show that a single dose of Trodusquemine, the PTP1B inhibitor, could be used to reverse the effects of atherosclerosis. [7]

During the COVID-19 pandemic, Delibegovic, in collaboration with an SME Vertebrate Antibodies Ltd and the NHS Grampian, obtained funding from the Scottish Government/ Chief Scientist office to develop a diagnostic test that could support mass screening for coronavirus disease. [8] Her long-term aim was to use artificial intelligence [9] [10] to identify which parts of the severe acute respiratory syndrome coronavirus 2 activated the body's immune system. [8] [11] At the time, other coronavirus disease tests available in the United Kingdom would not support rapid deployment, and several were unreliable. [12] [13] In May 2020, the tests developed by Delibegovic and her team were in development. [14] In March 2021, the tests were developed and available. https://www.abdn.ac.uk/news/14759/

In June 2024 she was appointed Regius Professor of Physiology at the University of Aberdeen. [15]

Awards and honours

Selected publications

Personal life

Delibegovic met her husband whilst a graduate student at the University of Dundee. [4]

Related Research Articles

A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein. Protein phosphorylation is one of the most common forms of reversible protein posttranslational modification (PTM), with up to 30% of all proteins being phosphorylated at any given time. Protein kinases (PKs) are the effectors of phosphorylation and catalyse the transfer of a γ-phosphate from ATP to specific amino acids on proteins. Several hundred PKs exist in mammals and are classified into distinct super-families. Proteins are phosphorylated predominantly on Ser, Thr and Tyr residues, which account for 79.3, 16.9 and 3.8% respectively of the phosphoproteome, at least in mammals. In contrast, protein phosphatases (PPs) are the primary effectors of dephosphorylation and can be grouped into three main classes based on sequence, structure and catalytic function. The largest class of PPs is the phosphoprotein phosphatase (PPP) family comprising PP1, PP2A, PP2B, PP4, PP5, PP6 and PP7, and the protein phosphatase Mg2+- or Mn2+-dependent (PPM) family, composed primarily of PP2C. The protein Tyr phosphatase (PTP) super-family forms the second group, and the aspartate-based protein phosphatases the third. The protein pseudophosphatases form part of the larger phosphatase family, and in most cases are thought to be catalytically inert, instead functioning as phosphate-binding proteins, integrators of signalling or subcellular traps. Examples of membrane-spanning protein phosphatases containing both active (phosphatase) and inactive (pseudophosphatase) domains linked in tandem are known, conceptually similar to the kinase and pseudokinase domain polypeptide structure of the JAK pseudokinases. A complete comparative analysis of human phosphatases and pseudophosphatases has been completed by Manning and colleagues, forming a companion piece to the ground-breaking analysis of the human kinome, which encodes the complete set of ~536 human protein kinases.

<span class="mw-page-title-main">Phosphatase</span> Enzyme which catalyzes the removal of a phosphate group from a molecule

In biochemistry, a phosphatase is an enzyme that uses water to cleave a phosphoric acid monoester into a phosphate ion and an alcohol. Because a phosphatase enzyme catalyzes the hydrolysis of its substrate, it is a subcategory of hydrolases. Phosphatase enzymes are essential to many biological functions, because phosphorylation and dephosphorylation serve diverse roles in cellular regulation and signaling. Whereas phosphatases remove phosphate groups from molecules, kinases catalyze the transfer of phosphate groups to molecules from ATP. Together, kinases and phosphatases direct a form of post-translational modification that is essential to the cell's regulatory network.

In biochemistry, dephosphorylation is the removal of a phosphate group from an organic compound by hydrolysis. It is a reversible post-translational modification. Dephosphorylation and its counterpart, phosphorylation, activate and deactivate enzymes by detaching or attaching phosphoric esters and anhydrides. A notable occurrence of dephosphorylation is the conversion of ATP to ADP and inorganic phosphate.

<span class="mw-page-title-main">Protein tyrosine phosphatase</span> Class of enzymes

Protein tyrosine phosphatases (EC 3.1.3.48, systematic name protein-tyrosine-phosphate phosphohydrolase) are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins:

<i>PTEN</i> (gene) Tumor suppressor gene

Phosphatase and tensin homolog (PTEN) is a phosphatase in humans and is encoded by the PTEN gene. Mutations of this gene are a step in the development of many cancers, specifically glioblastoma, lung cancer, breast cancer, and prostate cancer. Genes corresponding to PTEN (orthologs) have been identified in most mammals for which complete genome data are available.

<span class="mw-page-title-main">Tyrosin-protein kinase Lck</span> Lymphocyte protein

Tyrosin-protein kinase Lck is a 56 kDa protein that is found inside lymphocytes and encoded in the human by the LCK gene. The Lck is a member of Src kinase family (SFK) and is important for the activation of T-cell receptor (TCR) signaling in both naive T cells and effector T cells. The role of Lck is less prominent in the activation or in the maintenance of memory CD8 T cells in comparison to CD4 T cells. In addition, the constitutive activity of the mouse Lck homolog varies among memory T cell subsets. It seems that in mice, in the effector memory T cell (TEM) population, more than 50% of Lck is present in a constitutively active conformation, whereas less than 20% of Lck is present as active form in central memory T cells. These differences are due to differential regulation by SH2 domain–containing phosphatase-1 (Shp-1) and C-terminal Src kinase.

<span class="mw-page-title-main">Receptor tyrosine kinase</span> Class of enzymes

Receptor tyrosine kinases (RTKs) are the high-affinity cell surface receptors for many polypeptide growth factors, cytokines, and hormones. Of the 90 unique tyrosine kinase genes identified in the human genome, 58 encode receptor tyrosine kinase proteins. Receptor tyrosine kinases have been shown not only to be key regulators of normal cellular processes but also to have a critical role in the development and progression of many types of cancer. Mutations in receptor tyrosine kinases lead to activation of a series of signalling cascades which have numerous effects on protein expression. The receptors are generally activated by dimerization and substrate presentation. Receptor tyrosine kinases are part of the larger family of protein tyrosine kinases, encompassing the receptor tyrosine kinase proteins which contain a transmembrane domain, as well as the non-receptor tyrosine kinases which do not possess transmembrane domains.

<span class="mw-page-title-main">PTPN11</span> Protein-coding gene in humans

Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) also known as protein-tyrosine phosphatase 1D (PTP-1D), Src homology region 2 domain-containing phosphatase-2 (SHP-2), or protein-tyrosine phosphatase 2C (PTP-2C) is an enzyme that in humans is encoded by the PTPN11 gene. PTPN11 is a protein tyrosine phosphatase (PTP) Shp2.

<span class="mw-page-title-main">PTPRC</span> Mammalian protein found in Homo sapiens

Protein tyrosine phosphatase, receptor type, C also known as PTPRC is an enzyme that, in humans, is encoded by the PTPRC gene. PTPRC is also known as CD45 antigen, which was originally called leukocyte common antigen (LCA).

<span class="mw-page-title-main">LYN</span> Mammalian protein found in Homo sapiens

Tyrosine-protein kinase Lyn is a protein that in humans is encoded by the LYN gene.

<span class="mw-page-title-main">PTPN1</span> Protein-coding gene in the species Homo sapiens

Tyrosine-protein phosphatase non-receptor type 1 also known as protein-tyrosine phosphatase 1B (PTP1B) is an enzyme that is the founding member of the protein tyrosine phosphatase (PTP) family. In humans it is encoded by the PTPN1 gene. PTP1B is a negative regulator of the insulin signaling pathway and is considered a promising potential therapeutic target, in particular for treatment of type 2 diabetes. It has also been implicated in the development of breast cancer and has been explored as a potential therapeutic target in that avenue as well.

<span class="mw-page-title-main">PTPN22</span> Protein-coding gene in the species Homo sapiens

Protein tyrosine phosphatase non-receptor type 22 (PTPN22) is a cytoplasmatic protein encoded by gene PTPN22 and a member of PEST family of protein tyrosine phosphatases. This protein is also called "PEST-domain Enriched Phosphatase" ("PEP") or "Lymphoid phosphatase" ("LYP"). The name LYP is used strictly for the human protein encoded by PTPN22, but the name PEP is used only for its mouse homolog. However, both proteins have similar biological functions and show 70% identity in amino acid sequence. PTPN22 functions as a negative regulator of T cell receptor (TCR) signaling, which maintains homeostasis of T cell compartment.

<span class="mw-page-title-main">PTPRN</span> Protein-coding gene in the species Homo sapiens

Receptor-type tyrosine-protein phosphatase-like N, also called "IA-2", is an enzyme that in humans is encoded by the PTPRN gene.

<span class="mw-page-title-main">PTPRM</span> Protein-coding gene in the species Homo sapiens

Receptor-type tyrosine-protein phosphatase mu is an enzyme that in humans is encoded by the PTPRM gene.

<span class="mw-page-title-main">Protein phosphorylation</span> Process of introducing a phosphate group on to a protein

Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or otherwise modifying its function. Approximately 13,000 human proteins have sites that are phosphorylated.

<span class="mw-page-title-main">PTPRN2</span> Protein-coding gene in the species Homo sapiens

Receptor-type tyrosine-protein phosphatase N2 (R-PTP-N2) also known as islet cell autoantigen-related protein (ICAAR) and phogrin is an enzyme that in humans is encoded by the PTPRN2 gene. PTPRN and PTPRN2 are both found to be major autoantigens associated with insulin-dependent diabetes mellitus.

mir-210 microRNA

In molecular biology mir-210 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms.

<span class="mw-page-title-main">Trodusquemine</span> Chemical compound

Trodusquemine is an aminosterol that inhibits protein tyrosine phosphatase 1B (PTP1B) activity. The compound exhibits broad-spectrum antimicrobial activity and numerous regenerative, neuroprotective, anti-atherosclerotic, antitumor, antiangiogenic, antiobesity, and anxiolytic properties. Phase I clinical trials of trodusquemine have demonstrated good tolerability, but several planned phase II trials were halted due to financial difficulties of the developer.

<span class="mw-page-title-main">Protein arginine phosphatase</span> Enzyme that catalyzes the dephosphorylation of phosphoarginine residues in proteins

Protein Arginine Phosphatase (PAPs), also known as Phosphoarginine Phosphatase, is an enzyme that catalyzes the dephosphorylation of phosphoarginine residues in proteins. Protein phosphatases (PPs) are "obligatory heteromers" made up of two maximum catalytic subunits attached to a non-catalytic subunit. Arginine modification is a post-translational protein modification in gram-positive bacteria. McsB and YwIE were recently identified as phosphorylating enzymes in Bacillus Subtilis (B.Subtilis). YwIE was thought to be a protein-tyrosine-phosphatase, and McsB a tyrosine-kinase, however in 2012 Elsholz et al. showed that McsB is a protein-arginine-kinase (PAK) and YwlE is a phosphatase-arginine-phosphatase (PAP).

<span class="mw-page-title-main">Alexei Kharitonenkov</span> Russian biochemist

Alexei Kharitonenkov is a Russian-American researcher best known for his discoveries of endocrine functions of Fibroblast Growth Factor 21 (FGF21) and its prospects in developing novel therapies for metabolic diseases. He is also known for his landmark identification of the signal-regulatory family of proteins (SIRPs), and their corresponding protein-tyrosine phosphatases, which helped unveil the molecular machinery of immune self-recognition and their potential for the development of drugs to fight cancer.

References

  1. ↑ "Doctor Mirjana Delibegovic from Tuzla invented a Medicine used in the Treatment of Diabetes and Breast Cancer". Sarajevo Times. 2017-11-07. Retrieved 2020-05-12.
  2. 1 2 "Professor Mirela Delibegovic | Staff Profile | The Institute of Medical Sciences | The University of Aberdeen". www.abdn.ac.uk. Retrieved 2020-05-12.
  3. 1 2 3 "Science Scotland". www.sciencescotland.org. Retrieved 2020-05-12.
  4. 1 2 3 4 Lambert, Hazel. "Alumni Interview | Mirela Delibegovic" . Retrieved 2020-05-12.
  5. 1 2 Delibegovic, Mirela; Zimmer, Derek; Kauffman, Caitlin; Rak, Kimberly; Hong, Eun-Gyoung; Cho, You-Ree; Kim, Jason K.; Kahn, Barbara B.; Neel, Benjamin G.; Bence, Kendra K. (2009-03-01). "Liver-Specific Deletion of Protein-Tyrosine Phosphatase 1B (PTP1B) Improves Metabolic Syndrome and Attenuates Diet-Induced Endoplasmic Reticulum Stress". Diabetes. 58 (3): 590–599. doi: 10.2337/db08-0913 . ISSN   0012-1797. PMC   2646057 . PMID   19074988.
  6. ↑ Grant, Louise; Shearer, Kirsty D.; Czopek, Alicja; Lees, Emma K.; Owen, Carl; Agouni, Abdelali; Workman, James; Martin-Granados, Cristina; Forrester, John V.; Wilson, Heather M.; Mody, Nimesh (2014-02-01). "Myeloid-Cell Protein Tyrosine Phosphatase-1B Deficiency in Mice Protects Against High-Fat Diet and Lipopolysaccharide-Induced Inflammation, Hyperinsulinemia, and Endotoxemia Through an IL-10 STAT3-Dependent Mechanism". Diabetes. 63 (2): 456–470. doi: 10.2337/db13-0885 . hdl: 2164/4556 . ISSN   0012-1797. PMID   24186864.
  7. ↑ McCann, Lee (16 November 2016). "Aberdeen researchers find breast cancer drug can 'melt away' fat inside arteries". Evening Express. Retrieved 2020-05-14.
  8. 1 2 theorkneynews (2020-05-08). "Fast Tracking Tests for Covid19 Mass Screening". The Orkney News. Retrieved 2020-05-12.
  9. ↑ Puttick, Helen. "Coronavirus in Scotland: Pledge to mass test for immunity by winter". The Times . ISSN   0140-0460 . Retrieved 2020-05-12.
  10. ↑ Easton, Kaitlin (6 May 2020). "Aberdeen University will use innovative approach to tackle Covid-19". Press and Journal. Retrieved 2020-05-14.
  11. ↑ "University of Aberdeen Portfolio – Chief Scientist Office". www.cso.scot.nhs.uk. Retrieved 2020-05-12.
  12. ↑ "Škotska: Tuzlanka Mirela Delibegović razvija test za masovni skrining na Covid-19". BHDINFODESK. 2020-05-09. Retrieved 2020-05-12.
  13. ↑ McKee, Selina (2020-05-06). "Aberdeen Uni proceeds with COVID-19 mass screening research". PharmaTimes. Retrieved 2020-05-12.
  14. ↑ Puttick, Helen. "Coronavirus in Scotland: Pledge to mass test for immunity by winter". The Times . ISSN   0140-0460 . Retrieved 2020-05-12.
  15. ↑ "No. 64452". The London Gazette . 8 July 2024. p. 13158.
  16. ↑ "Royal Society of Edinburgh (RSE) Young Academy of Scotland". The University of Aberdeen. Retrieved 2020-05-12.
  17. ↑ "Principal's Prize for Public Engagement with Research | Public Engagement with Research | The University of Aberdeen". www.abdn.ac.uk. Retrieved 2020-05-12.
  18. ↑ "(FOTO) ŽENE DONIJELE JEDNOGLASNU ODLUKU: Razija Mujanović je dobitnica priznanja "Super žena 2017."". Kameleon M&M (in Bosnian). 2018-04-21. Retrieved 2020-05-12.
  19. ↑ Thomas, James (2022-03-22). "Academic and artistic minds honoured as RSE Fellows". Royal Society of Edinburgh. Retrieved 2022-12-15.
  20. ↑ Bence, Kendra K.; Delibegovic, Mirela; Xue, Bingzhong; Gorgun, Cem Z.; Hotamisligil, Gokhan S.; Neel, Benjamin G.; Kahn, Barbara B. (2006). "Neuronal PTP1B regulates body weight, adiposity and leptin action". Nature Medicine. 12 (8): 917–924. doi:10.1038/nm1435. ISSN   1546-170X. PMID   16845389. S2CID   10654045.
  21. ↑ Delibegovic, Mirela; Bence, Kendra K.; Mody, Nimesh; Hong, Eun-Gyoung; Ko, Hwi Jin; Kim, Jason K.; Kahn, Barbara B.; Neel, Benjamin G. (2007-11-01). "Improved Glucose Homeostasis in Mice with Muscle-Specific Deletion of Protein-Tyrosine Phosphatase 1B". Molecular and Cellular Biology. 27 (21): 7727–7734. doi: 10.1128/MCB.00959-07 . ISSN   0270-7306. PMC   2169063 . PMID   17724080.
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