Dominique Bollino, PhD

Research Assistant Professor

Organization:

West Virginia University WVU Cancer Institute

Department:

Department of Medical Oncology

Classification:

Faculty

• BS, Frostburg State University, 2008
• PhD, University of Maryland, 2015

1. Colunga, A., Bollino, D., Schech, A. and Aurelian, L. “Calpain-dependent clearance of the autophagy protein p62/SQSTM1 is a contributor to ΔPK oncolytic activity in melanoma.”  Gene Therap. 2014; 21: 371-378.
2. Bollino D, Balan I, Aurelian LA. “Valproic acid induces neuronal cell death through a novel calpain-dependent necroptosis pathway.” J Neurochem. 2015; 133 (2):174-86.
3.  June HL, Liu J, Warnock KT, Bell KA, Balan I, Bollino D, Puche A, Aurelian L. “CRF-Amplified Neuronal TLR4/MCP-1 Signaling Regulates Alcohol Self-Administration.” Neuropsychopharmacology. 2015; 40(6):1549-59.
4. Bollino D, Colunga A, Li B, Aurelian, LA. “ΔPK oncolytic activity includes modulation of the tumour cell milieu.” J Gen Virol. 2016; 97(2):496-508.
5. Aurelian L, Bollino D, Colunga A. “The oncolytic virus ∆PK has multi-modal anti-tumor activity” Pathogens and Disease. 2016; 74(5). pii: ftw050. doi: 10.1093/femspd/ftw050.
6. Webb TJ, Carey GB, East JE, Sun W, Bollino DR, Kimball AS, Brutkiewicz RR. “Alterations in cellular metabolism modulate CD1d-mediated NKT cell responses”. Pathogens and Disease. 2016; 74 (6): ftw055. doi: 10.1093/femspd/ftw055.
7. Shissler SC, Bollino DR, Tiper IV, Bates JP, Derakhshandeh R, Webb TJ. “Immunotherapeutic strategies targeting natural killer T cell responses in cancer.” Immmunogenetics. 2016; 68 (8), 623-638.
8. Bollino D, Webb TJ. Chimeric antigen receptor-engineered natural killer and natural killer T cells for cancer immunotherapy. Trans Res. 2017; 187:32-43.
9. Emadi A, Kapadia B, Bollino D, Bhandary B, Baer MR, Niyongere S, Strovel ET, Kaizer H, Chang E, Choi EY, Ma X, Tighe KM, Carter-Cooper B, Moses BS, Civin CI, Mahurkar A, Shetty AC, Gartenhaus RB, Kamangar F, Lapidus RG. Venetoclax and pegcrisantaspase for complex karyotype acute myeloid leukemia. Leukemia. 2020 Nov 16. doi: 10.1038/s41375-020-01080-6. Epub ahead of print. PMID: 33199836.
10. Ferraris D, Lapidus R, Truong P, Bollino D, Carter-Cooper B, LeeM, Chang E, LaRossa-Garcia M, Dash S, Gartenhaus R, Choi EY, Kipe O, Lam V, Mason K, Palmer R, Williams E, Ambulos N, Kamangar F, Zhang Y, Kapadia B, Jing Y, Emadi A. Pre-Clinical Activity of Amino-Alcohol Dimeric Naphthoquinones as Potential Therapeutics for Acute Myeloid Leukemia. Anticancer Agents Med Chem. 2022;22(2):239-253. PMID: 34080968.
11. Kapadia B, Shetty AC, Bollino D, Bhandary B, Lapidus RG, Mahmood K, Mahurkar A, Gartenhaus RB, Eckert RL, Emadi A. “Translatome changes in acute myeloid leukemia cells post exposure to pegcrisantaspase and Venetoclax”. Exp Hematol. 2022 Apr;108:55-63.
12. Bollino D, Claiborne JP, Mahmood K. Ma X, Tighe KM, Carter-Cooper B, Lapidus RG, Strovel ET, Emadi A.  Erwinia asparaginase (crisantaspase) increases plasma levels of serine and glycine. Frontiers in Oncology. 12. 1035537. 10.3389/fonc.2022.1035537.
13. Bollino D, Woodard N, Tighe KM, Ma X, Casildo A, D'Adamo CR, Emadi A, Knott CL. Community-engaged basic science in an NCI-designated comprehensive cancer center: antioxidants and chemotherapeutic efficacy. Cancer Causes Control. 2023 Oct 9;. doi: 10.1007/s10552-023-01806-8.
14. Hameed KM, Bollino DR, Shetty AC, Carter-Cooper B, Lapidus RG, Emadi A. Dual targeting of glutamine and serine metabolism in acute myeloid leukemia. Front Oncol. 2024 Apr 16;14:1326754. doi: 10.3389/fonc.2024.1326754. PMID: 38690164; PMCID: PMC11059989. Bollino D, Hameed KM, Bhatt A, Zarrabi A, Strovel E, Casildo A, Ma X, Tighe K, Carter-Cooper B, Lapidus R, Emadi A. Pegcrisantaspase does not potentiate chemotherapy and induces alternate amino acid biosynthetic pathways in a preclinical model of pancreatic ductal adenocarcinoma. Cancer Metab 12, 19 (2024). https://doi.org/10.1186/s40170-024-00346-2.

Dr. Dominique Bollino received her undergraduate degree in Biology from Frostburg State University and completed her PhD in Molecular Medicine at the University of Maryland Baltimore (UMB). Her dissertation research focused on uncovering the mechanistic pathways of oncolysis of the HSV-2 mutant ΔPK, particularly the molecular signaling involved in programmed cell death pathways as well as the induction of inflammation by oncolytic viruses. During her postdoctoral research fellowship in the laboratory of Dr. Tonya Webb at UMB, she investigated the immunosuppressive mechanisms of ovarian cancer. Dr. Bollino then joined the Department of Medicine at UMB as a Research Associate in the laboratory of Dr. Ashkan Emadi, and her work focused on targeting metabolic liabilities in both hematological and solid malignancies to enhance current therapeutic modalities. In 2024, she was recruited to the Department of Medical Oncology at West Virginia University School of Medicine as a Research Assistant Professor. Her current research is centered around using asparaginase-based combinations for the treatment of pancreatic cancer, glioma, and other malignancies that are sensitive to glutamine and asparagine depletion.

Alexander B. Osborn Hematopoietic Malignancy and Transplantation Program

Metabolic reprogramming contributes to tumor development but can, in some cases, introduce specific metabolic liabilities that can be exploited to treat cancer. All cells need the amino acids asparagine and glutamine for protein synthesis and growth, and while normal healthy cells can obtain most of their needs through synthesis, cancer cells cannot produce enough to meet cellular demands and must therefore rely on circulating blood levels. Depletion of asparagine and glutamine has emerged as a therapeutic approach for cancers that are dependent on an exogenous (e.g. blood) amino acid supply for survival and proliferation. L-asparaginases are enzymes that primarily catalyze the hydrolysis of asparagine to aspartate and through their simultaneous glutaminase activity, glutamine to glutamate; thereby reducing circulating levels of asparagine and glutamine. Clinically available asparaginase is derived from 2 bacterial sources: Escherichia coli and Erwinia chrysanthemi (called crisantaspase), with higher glutaminase activity reported for crisantaspase. The use of asparaginase is well-established as part of multi-agent chemotherapeutic regimens in pediatric and adult acute lymphoblastic leukemia (ALL) but is also being investigated in additional hematological and solid malignancies with asparagine and glutamine dependencies.  In our laboratory, we are investigating the potential of asparaginases to target glutamine and asparagine metabolic pathways in several cancer models. Our research aims to identify effective asparaginase-based combinations that can be rapidly translated into clinical applications, offering new therapeutic avenues for cancer treatment.

- Investigating the impact of asparaginase-mediated amino acid depletion on the anti-cancer effects of other chemotherapeutic, targeted, or immunotherapeutic agents in various cancer models.

- Identifying novel therapeutic strategies to combat asparaginase resistance mechanisms.

Laboratory techniques:

- Adherent and suspension cell culture (murine and human cancer cell lines)

- Cell proliferation/cell death assays

- Dose-response curves/Drug synergy assays

- Western blotting

- Quantitative PCR

- Plasma amino acid analysis

- Real-time metabolic analysis (Seahorse XF Analyzer)

- Flow cytometry

- Mouse cancer models