Research Overview

Dr. Aram Ghalali is a biomedical researcher dedicated to improving the diagnosis and treatment of serious brain and vascular diseases, with a special focus on children. His research aims to develop non-invasive biomarkers (tests that can be done using blood or other body fluids) and new, targeted treatments for pediatric brain tumors and complex cerebrovascular conditions. These include diseases such as moyamoya disease, brain aneurysms, arteriovenous malformations, and cavernous malformations—conditions that can be difficult to diagnose and treat effectively.

A central goal of Dr. Ghalali’s work is to help doctors make earlier diagnoses, choose more effective treatments, and better predict how a disease may progress. By understanding the underlying biology of these conditions, his research strives to improve both survival and quality of life for patients and their families.

Cancer Research and New Treatment Strategies

Dr. Ghalali has devoted his career to cancer research and has extensive experience studying aggressive and advanced cancers, including prostate, lung, and liver cancer, as well as childhood brain tumors such as medulloblastoma, diffuse midline glioma, and glioblastoma. His current research focuses on understanding the biological and metabolic changes that cause cancers to develop, grow, and become resistant to treatment.

At the same time, his laboratory works to identify weak points in cancer cells that can be targeted with new drugs. Several promising treatment compounds discovered through this research are now being tested in preclinical studies, an important step toward future clinical use.

Developing New Drugs Through Translational Research

An important part of Dr. Ghalali’s research focuses on translational science, which means turning discoveries made in the laboratory into potential treatments for patients. One major effort involves developing new therapies for prostate cancer. This work builds on the discovery that a protein called Antizyme Inhibitor 1 (AZIN1) helps cancer cells grow by blocking the action of the body’s natural tumor-suppressing mechanisms. Dr. Ghalali is developing advanced laboratory tests that allow thousands of drug candidates to be screened efficiently, with the goal of identifying compounds that can block AZIN1, restore tumor suppression, and slow cancer growth.

In parallel, Dr. Ghalali’s team is working to develop new treatment strategies for aggressive pediatric brain tumors, including diffuse midline glioma (DMG). His laboratory has recently identified a previously unknown receptor that plays a critical role in DMG tumor invasiveness—the ability of cancer cells to spread into surrounding brain tissue. Building on this discovery, the team is actively searching for highly selective inhibitors that can block this receptor and limit tumor spread. This approach represents a promising new therapeutic direction for a disease that currently has very limited treatment options.

Several of the discoveries arising from these translational research efforts have strong potential for clinical application, and multiple patent applications are currently under development to protect these innovations and support their future translation into patient therapies.

Improving Care for Children with Medulloblastoma

Dr. Ghalali also leads research projects aimed at improving treatment for medulloblastoma, the most common malignant brain tumor in children. These projects are supported by organizations including the Swedish Childhood Cancer Fund, the Sweden–America Foundation, and the Dubai–Harvard Foundation for Medical Research.

Medulloblastoma is not a single disease but includes several subtypes that respond differently to treatment. Dr. Ghalali’s team has discovered that levels of AZIN1 are dramatically increased in medulloblastoma tumors. This finding suggests that AZIN1 plays an important role in how these tumors grow and respond to therapy.

The research aims to identify proteins that can serve as biomarkers—biological signals that help predict how aggressive a tumor is, how it may respond to treatment, and whether it is likely to come back. This information could allow doctors to better tailor treatment plans, helping some children avoid unnecessary side effects while ensuring that others receive more intensive therapy when needed.

Environmental Health Research

In addition to his work on cancer and brain disease, Dr. Ghalali is deeply interested in environmental health. At Karolinska Institutet, he leads a large, collaborative research effort to study traces of environmental pollutants and their potential effects on human health. This research seeks to better understand how long-term exposure to environmental factors may contribute to disease risk, particularly in vulnerable populations.

Research Background

Dr. Aram Ghalali holds a Bachelor of Science in Chemical Engineering as well as a Bachelor of Science in Biotechnology. He has also earned multiple Master of Science degrees, including one in Quality Assessment in Pharmaceutical Sciences/Biotechnology and another in Cancer Prevention and Pharmacy Design. In addition, Dr. Ghalali holds a degree in Civil Engineering from Mälardalen (méé-lar daal-ens) University (Sweden).

He completed his Ph.D. in the field of medicine at the Karolinska Institutet (Sweden), where his research focused on cellular signaling pathways. He subsequently obtained his first postdoctoral research fellowship at Karolinska Institutet in the field of toxicology, investigating the role of environmental pollutants in occupational health. Dr. Ghalali then completed a second postdoctoral fellowship at Boston Children’s Hospital, Harvard Medical School, where he is part of the Vascular Biology Program within the Department of Surgery.

His research at Harvard focuses on oncometabolites and drug development targeting late-stage and aggressive (metastatic) cancers. Currently, Dr. Ghalali holds multiple affiliations: he serves as faculty at Harvard Medical School, as an Instructor in Surgery at Boston Children’s Hospital, and as an Assistant Professor affiliated with the Karolinska Institutet.

Publications

  1. AZIN1 level is increased in medulloblastoma and correlates with c-Myc activity and tumor phenotype. J Exp Clin Cancer Res. 2025 Feb 17; 44(1):56. View Abstract
  2. Lectin-type oxidized LDL receptor-1 as a potential therapeutic target for cerebral cavernous malformations treatment. Front Neurosci. 2024; 18:1442110. View Abstract
  3. Contrasting effects of intracellular and extracellular human PCSK9 on inflammation, lipid alteration and cell death. Commun Biol. 2024 08 13; 7(1):985. View Abstract
  4. Discovery and Characterization of Ephrin B2 and EphB4 Dysregulation and Novel Mutations in Cerebral Cavernous Malformations: In Vitro and Patient-Derived Evidence of Ephrin-Mediated Endothelial Cell Pathophysiology. Cell Mol Neurobiol. 2023 Dec 27; 44(1):12. View Abstract
  5. Disease specific urinary biomarkers in the central nervous system. Sci Rep. 2023 11 07; 13(1):19244. View Abstract
  6. Inhibition of Wnt Signaling in Colon Cancer Cells via an Oral Drug that Facilitates TNIK Degradation. Mol Cancer Ther. 2023 01 03; 22(1):25-36. View Abstract
  7. AZIN1 RNA editing alters protein interactions, leading to nuclear translocation and worse outcomes in prostate cancer. Exp Mol Med. 2022 10; 54(10):1713-1726. View Abstract
  8. Nonsurgical mouse model of endometriosis-associated pain that responds to clinically active drugs. Pain. 2020 06; 161(6):1321-1331. View Abstract
  9. PTEN and PHLPP crosstalk in cancer cells and in TGFß-activated stem cells. Biomed Pharmacother. 2020 Jul; 127:110112. View Abstract
  10. Human Peripheral Blood Eosinophils Express High Levels of the Purinergic Receptor P2X4. Front Immunol. 2019; 10:2074. View Abstract
  11. 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
  12. Developing a novel FRET assay, targeting the binding between Antizyme-AZIN. Sci Rep. 2019 03 15; 9(1):4632. View Abstract
  13. 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
  14. 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
  15. Toluene diisocyanate exposure and autotaxin-lysophosphatidic acid signalling. Toxicol Appl Pharmacol. 2018 09 15; 355:43-51. View Abstract
  16. Atorvastatin Decreases HBx-Induced Phospho-Akt in Hepatocytes via P2X Receptors. Mol Cancer Res. 2017 06; 15(6):714-722. View Abstract
  17. 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
  18. 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
  19. 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
  20. 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
  21. 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
  22. Silencing p110ß prevents rapid depletion of nuclear pAkt. Biochem Biophys Res Commun. 2011 Dec 02; 415(4):613-8. View Abstract
  23. 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

Contact Aram Ghalali

Phone: 617-919-2326
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