Bio

Received her undergraduate degree from Williams College, after which she spent one year conducting research at the NIH National Cancer Institute. She then attended medical school at the University of Michigan, where she also completed a PhD in Molecular and Cellular Pathology as part of the Medical Scientist Training Program. She completed residency at UCSF prior to starting Hematology and Oncology fellowship training at Stanford. Her prior research has focused on the transcription factor biology and deregulated signaling pathways in hematologic malignancies. She is currently a postdoctoral fellow in Dr. Ravi Majeti's lab studying clonal hematopoiesis and preleukemic stem cells.

Clinical Focus

  • Malignant Hematology
  • Clonal Hematopoiesis
  • Fellow

Contact

  • Academic
    collinsc@stanford.edu
    University - Scholar Department: School of Medicine Position: Medical Fellow

Additional Info

  • Mail Code: 5151

All Publications

  • Engineering Sequential Mutations into Human HSPCs Yields an Aggressive Myeloid Malignancy Allowing for Interrogation of Preleukemic Transformation Collins, C. T., Nakauchi, Y., Koehnke, T., Chavez, J. S., Choi, S., Sharma, R., Zhao, F., Majeti, R. AMER SOC HEMATOLOGY. 2023

    View details for DOI 10.1182/blood-2023-187422

    View details for Web of Science ID 001159306703222

  • BCOR Loss Confers Increased Stemness and Partially Rescues RUNX1-Deficient Phenotypes in Human Hematopoietic Stem and Progenitor Cells Jackson, K. K., Fan, A. C., Karigane, D., Zhao, F., Collins, C. T., Nakauchi, Y., Kayamori, K., Rangavajhula, A. S., Koehnke, T., Majeti, R. AMER SOC HEMATOLOGY. 2023

    View details for DOI 10.1182/blood-2023-187865

    View details for Web of Science ID 001159306703215

  • Gene Correction of DNMT3A:R882H in Primary Human AML Demonstrates That This Mutation Is Not Required for Disease Maintenance, but Is Associated with Increased Leukemia Stem Cell Frequency Koehnke, T., Karigane, D., Hilgart, E., Kayamori, K., Fan, A. C., Collins, C. T., Suchy, F. P., Rangavajhula, A. S., Feng, Y., Nakauchi, Y., Martinez-Montes, E., Koldobskiy, M., Feinberg, A., Majeti, R. AMER SOC HEMATOLOGY. 2023

    View details for DOI 10.1182/blood-2023-186440

    View details for Web of Science ID 001159306702092

  • Gilteritinib Clinical Activity in Relapsed/Refractory FLT3 Mutated AML Previously Treated with FLT3 inhibitors. American journal of hematology Numan, Y., Abdel Rahman, Z., Grenet, J., Boisclair, S., Bewersdorf, J. P., Collins, C., Barth, D., Fraga, M., Bixby, D. L., Zeidan, A. M., Yilmaz, M., Desai, P., Mannis, G., Deutsch, Y. E., Abaza, Y., Dinner, S., Frankfurt, O., Litzow, M., Al-Kali, A., Foran, J. M., Sproat, L. Z., Jovanovic, B., Daver, N., Perl, A. E., Altman, J. K. 2022

    Abstract

    Gilteritinib is approved for the treatment of relapsed/refractory (R/R) acute myeloid leukemia (AML) with a FLT3-mutation (FLT3mut+ ). However, the gilteritinib phase 3 ADMIRAL study (Perl et al NEJM 2019) was conducted prior to widespread adoption of either midostaurin as a component of standard intensive induction and consolidation or post-transplant FLT3 inhibitor maintenance. We performed a retrospective analysis using data from 11 US centers and where we identified 113 patients who received gilteritinib alone or as combination therapy for the treatment of R/R FLT3mut+ AML. The composite CR rate (CRc, defined as CR + CRi + CRp) was 48.7% (n= 55). The CRc rate after treatment with gilteritinib in patients who were treated with only prior 7+3 and midostaurin with or without consolidation was 58% with a median survival of 7.8 months. Survival was longest in patients who obtained a CR, particularly a cMRD (Clinical minimal or measurable residual disease) negative response; this remained significant after censoring at the time of SCT. MAPK pathway activating mutations that are known for gilteritinib resistance (NRAS, KRAS, and PTPN11) had lower CRc (35% vs 60.5%) and lower mOS than patients' whose leukemia did not express these mutations (4.9 months vs 7.8 months) (HR 2.4- 95% CI 1.1-5.4) p value <0.01. This article is protected by copyright. All rights reserved.

    View details for DOI 10.1002/ajh.26447

    View details for PubMedID 34981560

  • Deregulation of the HOXA9/MEIS1 axis in acute leukemia CURRENT OPINION IN HEMATOLOGY Collins, C. T., Hess, J. L. 2016; 23 (4): 354-361

    Abstract

    HOXA9 is a homeodomain transcription factor that plays an essential role in normal hematopoiesis and acute leukemia, in which its overexpression is strongly correlated with poor prognosis. The present review highlights recent advances in the understanding of genetic alterations leading to deregulation of HOXA9 and the downstream mechanisms of HOXA9-mediated transformation.A variety of genetic alterations including MLL translocations, NUP98-fusions, NPM1 mutations, CDX deregulation, and MOZ-fusions lead to high-level HOXA9 expression in acute leukemias. The mechanisms resulting in HOXA9 overexpression are beginning to be defined and represent attractive therapeutic targets. Small molecules targeting MLL-fusion protein complex members, such as DOT1L and menin, have shown promising results in animal models, and a DOT1L inhibitor is currently being tested in clinical trials. Essential HOXA9 cofactors and collaborators are also being identified, including transcription factors PU.1 and C/EBPα, which are required for HOXA9-driven leukemia. HOXA9 targets including IGF1, CDX4, INK4A/INK4B/ARF, mir-21, and mir-196b and many others provide another avenue for potential drug development.HOXA9 deregulation underlies a large subset of aggressive acute leukemias. Understanding the mechanisms regulating the expression and activity of HOXA9, along with its critical downstream targets, shows promise for the development of more selective and effective leukemia therapies.

    View details for DOI 10.1097/MOH.0000000000000245

    View details for Web of Science ID 000378017500009

    View details for PubMedID 27258906

    View details for PubMedCentralID PMC5653247

  • Characterization of the Molecular Interplay Between HOXA9 and Ogt in Leukemia Rual, J. M., Xu, T., Collins, C., Zhang, H., Wang, J., Kuick, R., Bronstein, J., Basrur, V., Park, S., Ha, K., Chen, L., Elenitoba-Johnson, K. J., Muntean, A. G., Hess, J. L. AMER SOC HEMATOLOGY. 2014

    View details for Web of Science ID 000349242708031

  • C/EBP alpha is an essential collaborator in Hoxa9/Meis1-mediated leukemogenesis PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA Collins, C., Wang, J., Miao, H., Bronstein, J., Nawer, H., Xu, T., Figueroa, M., Muntean, A. G., Hess, J. L. 2014; 111 (27): 9899-9904

    Abstract

    Homeobox A9 (HOXA9) is a homeodomain-containing transcription factor that plays a key role in hematopoietic stem cell expansion and is commonly deregulated in human acute leukemias. A variety of upstream genetic alterations in acute myeloid leukemia (AML) lead to overexpression of HOXA9, almost always in association with overexpression of its cofactor meis homeobox 1 (MEIS1) . A wide range of data suggests that HOXA9 and MEIS1 play a synergistic causative role in AML, although the molecular mechanisms leading to transformation by HOXA9 and MEIS1 remain elusive. In this study, we identify CCAAT/enhancer binding protein alpha (C/EBPα) as a critical collaborator required for Hoxa9/Meis1-mediated leukemogenesis. We show that C/EBPα is required for the proliferation of Hoxa9/Meis1-transformed cells in culture and that loss of C/EBPα greatly improves survival in both primary and secondary murine models of Hoxa9/Meis1-induced leukemia. Over 50% of Hoxa9 genome-wide binding sites are cobound by C/EBPα, which coregulates a number of downstream target genes involved in the regulation of cell proliferation and differentiation. Finally, we show that Hoxa9 represses the locus of the cyclin-dependent kinase inhibitors Cdkn2a/b in concert with C/EBPα to overcome a block in G1 cell cycle progression. Together, our results suggest a previously unidentified role for C/EBPα in maintaining the proliferation required for Hoxa9/Meis1-mediated leukemogenesis.

    View details for DOI 10.1073/pnas.1402238111

    View details for Web of Science ID 000338514800049

    View details for PubMedID 24958854

    View details for PubMedCentralID PMC4103350

  • Mechanisms of Transcriptional Regulation and Transformation by HOXA9 Hess, J. L., Collins, C., Bronstein, J., Sun, Y., Nagaraja, S. AMER SOC HEMATOLOGY. 2012

    View details for Web of Science ID 000313838900060

  • Identification and characterization of Hoxa9 binding sites in hematopoietic cells BLOOD Huang, Y., Sitwala, K., Bronstein, J., Sanders, D., Dandekar, M., Collins, C., Robertson, G., MacDonald, J., Cezard, T., Bilenky, M., Thiessen, N., Zhao, Y., Zeng, T., Hirst, M., Hero, A., Jones, S., Hess, J. L. 2012; 119 (2): 388-398

    Abstract

    The clustered homeobox proteins play crucial roles in development, hematopoiesis, and leukemia, yet the targets they regulate and their mechanisms of action are poorly understood. Here, we identified the binding sites for Hoxa9 and the Hox cofactor Meis1 on a genome-wide level and profiled their associated epigenetic modifications and transcriptional targets. Hoxa9 and the Hox cofactor Meis1 cobind at hundreds of highly evolutionarily conserved sites, most of which are distant from transcription start sites. These sites show high levels of histone H3K4 monomethylation and CBP/P300 binding characteristic of enhancers. Furthermore, a subset of these sites shows enhancer activity in transient transfection assays. Many Hoxa9 and Meis1 binding sites are also bound by PU.1 and other lineage-restricted transcription factors previously implicated in establishment of myeloid enhancers. Conditional Hoxa9 activation is associated with CBP/P300 recruitment, histone acetylation, and transcriptional activation of a network of proto-oncogenes, including Erg, Flt3, Lmo2, Myb, and Sox4. Collectively, this work suggests that Hoxa9 regulates transcription by interacting with enhancers of genes important for hematopoiesis and leukemia.

    View details for DOI 10.1182/blood-2011-03-341081

    View details for Web of Science ID 000299268900016

    View details for PubMedID 22072553

    View details for PubMedCentralID PMC3257007