High throughput drug discovery in prostate cancer:

Our lab has been able to obtain a NIH grant for a collaborative project between Professor Bruce Zetter lab and Assistant Professor Michael S. Rogers (both from Boston Children’s Hospital, Harvard Medical School). The project is based on previous finding from the Zetter lab about the role of Antizyme Inhibitor (AZIN1) as a tumor growth stimulator. Dr. Zetter found that AZIN1 promotes tumor growth by binding and suppressing the activity of antizyme, a known tumor suppressor. They have shown that silencing AZI in tumor cells leads to reduced tumor growth and extended survival in experimental animals. In this project, we are currently aiming to develop assays that can be used to screen small molecule libraries for antagonists of AZI binding to antizyme. The goal of the project is to identifies novel drug candidates that can restore tumor suppression.

Discovering new targets for medulloblastoma treatment:

Recently, Dr. Ghalali has been funded by the Swedish Childhood Cancer fond for a project aiming to discover targets for medulloblastoma treatment. Medulloblastoma is the most common children brain cancer and is divided into four main subtypes, each with distinct molecular and clinical features. Molecules targeted by the tumor suppressor antizyme are found in each subtype. Increased levels of antizyme inhibitor (AZIN1) in medulloblastoma, along with the recent demonstration of an edited AZIN1 isoform in certain cancers, highlight the importance of this molecule in that disease. In preliminary experiments, we have seen dramatic increase of AZIN1 (the endogenous antizyme inhibitor) expression in medulloblastoma. In this project, we are aiming to validate expression/localization for some oncoproteins as a marker for pediatric brain tumors, which may predict therapeutic efficacy. Our work may also lead to development of tests that predict recurrence and progression of child brain tumors. We also aiming to correlate those oncoproteins to the outcome of medulloblastoma. That may directly benefit patients by allowing physicians to predict which children with medulloblastoma will require more intensive treatment.


Dr. Aram Ghalali has a Bachelor of Science in chemical engineering as well as Bachelor of Science in biotechnology. Furthermore, he has earned multiple Master of Science degrees, one in quality assessment in pharmaceuticals sciences/biotechnology and another in cancer prevention and pharmacy design. Dr. Ghalali also holds a degree in Civil Engineering, that was earned at Mälardalens (méé-lar daal-ens) University (Sweden).

He has completed his Ph.D. in field of medicine at the Karolinska Institutet (Sweden), focusing on cellular signaling pathways. Where he also obtained his first postdoctoral research fellowship, in the field of toxicology investigating the role of environmental pollutants on occupational health. He has completed his second postdoctoral fellowship in Boston Children’s Hospital at Harvard Medical school. He is a part of Vascular Biology Program at the department of Surgery. His research at Harvard is focused on oncometabolites and drug development targeting late stage/aggressive (metastatic) cancer. Recently, he has been promoted by Harvard Medical School to Instructor of Surgery / Faculty. His interests beside of science includes geopolitics, applied history, arts, sports, languages, poetry and writing.


Publications powered by Harvard Catalyst Profiles

  1. Nonsurgical mouse model of endometriosis-associated pain that responds to clinically active drugs. Pain. 2020 06; 161(6):1321-1331. View abstract
  2. PTEN and PHLPP crosstalk in cancer cells and in TGFß-activated stem cells. Biomed Pharmacother. 2020 Jul; 127:110112. View abstract
  3. Human Peripheral Blood Eosinophils Express High Levels of the Purinergic Receptor P2X4. Front Immunol. 2019; 10:2074. View abstract
  4. The Water Extract of Juniperus communis L. Induces Cell Death and Sensitizes Cancer Cells to Cytostatic Drugs through p53 and PI3K/Akt Pathways. Int J Mol Sci. 2019 Apr 26; 20(9). View abstract
  5. Developing a novel FRET assay, targeting the binding between Antizyme-AZIN. Sci Rep. 2019 03 15; 9(1):4632. View abstract
  6. Clusterin enhances AKT2-mediated motility of normal and cancer prostate cells through a PTEN and PHLPP1 circuit. J Cell Physiol. 2019 07; 234(7):11188-11199. View abstract
  7. CXADR-Mediated Formation of an AKT Inhibitory Signalosome at Tight Junctions Controls Epithelial-Mesenchymal Plasticity in Breast Cancer. Cancer Res. 2019 01 01; 79(1):47-60. View abstract
  8. Toluene diisocyanate exposure and autotaxin-lysophosphatidic acid signalling. Toxicol Appl Pharmacol. 2018 09 15; 355:43-51. View abstract
  9. Atorvastatin Decreases HBx-Induced Phospho-Akt in Hepatocytes via P2X Receptors. Mol Cancer Res. 2017 06; 15(6):714-722. View abstract
  10. Phosphatase and tensin homolog deleted on chromosome 10 (PTEN) and PH domain and leucine-rich repeat phosphatase cross-talk (PHLPP) in cancer cells and in transforming growth factor ß-activated stem cells. J Biol Chem. 2017 01 13; 292(2):760. View abstract
  11. Toluene diisocyanate: Induction of the autotaxin-lysophosphatidic acid axis and its association with airways symptoms. Toxicol Appl Pharmacol. 2015 Sep 15; 287(3):222-31. View abstract
  12. Phosphatase and tensin homolog deleted on chromosome 10 (PTEN) and PH domain and leucine-rich repeat phosphatase cross-talk (PHLPP) in cancer cells and in transforming growth factor ß-activated stem cells. J Biol Chem. 2014 Apr 25; 289(17):11601-11616. View abstract
  13. Atorvastatin prevents ATP-driven invasiveness via P2X7 and EHBP1 signaling in PTEN-expressing prostate cancer cells. Carcinogenesis. 2014 Jul; 35(7):1547-55. View abstract
  14. Differential role of thiopurine methyltransferase in the cytotoxic effects of 6-mercaptopurine and 6-thioguanine on human leukemia cells. Biochem Biophys Res Commun. 2013 Jul 26; 437(2):280-6. View abstract
  15. Silencing p110ß prevents rapid depletion of nuclear pAkt. Biochem Biophys Res Commun. 2011 Dec 02; 415(4):613-8. View abstract
  16. Purinergic receptor-mediated rapid depletion of nuclear phosphorylated Akt depends on pleckstrin homology domain leucine-rich repeat phosphatase, calcineurin, protein phosphatase 2A, and PTEN phosphatases. J Biol Chem. 2010 Sep 03; 285(36):27900-10. View abstract