Sol Schulman, MD, PhD
Assistant Professor of Medicine
Harvard Medical School
Division of Hemostasis and Thrombosis
Beth Israel Deaconess Medical Center
3 Blackfan Circle, Room 950, Boston MA 02215
Dr. Schulman is a physician-scientist in the Division of Hemostasis and Thrombosis at Beth Israel Deaconess Medical Center and Harvard Medical School. After receiving B.S. and M.S. degrees in biochemistry from Brandeis University, he earned M.D. and Ph.D. degrees in the joint Harvard-MIT Medical Scientist Training Program. His graduate thesis research in the laboratory of Professor Tom Rapoport provided important insights into human vitamin K metabolism and the mechanisms of warfarin resistance. He subsequently completed internal medicine residency training at the Brigham and Women’s Hospital and hematology/oncology fellowship training at Beth Israel Deaconess Medical Center, where he performed his research in the Division of Hemostasis and Thrombosis under the mentorship of Drs. Bruce Furie and Robert Flaumenhaft.
Dr. Schulman’s research program is focused on integrating human genetics, functional genomics, and cell biology to identify new mechanisms that regulate the initiation of blood coagulation. He is particularly interested in understanding genetic modifiers of the tissue factor pathway relevant to human bleeding and thrombotic risk. Dr. Schulman’s research is supported by grants from the National Hemophilia Foundation, Hemostasis and Thrombosis Research Society, American Society of Hematology, the National Heart, Lung, and Blood Institute, and the NIH Director’s Early Independence Award (https://commonfund.nih.gov/earlyindependence/awardrecipients). Dr. Schulman’s research has also been recognized with a Future Leader in Hematology Award (Celgene), the Professor Heimburger Award (CSL Behring), and the James Tolbert Shipley Prize (Harvard Medical School). Dr. Schulman maintains a focused clinical practice in non-malignant hematology with particular expertise in the diagnosis and treatment of patients with rare bleeding and clotting disorders. Beyond the hospital, he is a proud father, avid hiker, and an increasingly rusty trumpet player.
Tissue factor (TF) binds blood coagulation factor VII/VIIa to initiate blood coagulation in humans. Inappropriate TF procoagulant activity underlies substantial human suffering, including that due to myocardial infarction, venous thromboembolism, cancer-associated thrombosis, and stroke. TF expression and activity must therefore be carefully regulated in vascular tissues to enable hemostasis following injury but prevent pathologic thrombosis. Despite decades of close investigation, the mechanisms by which TF expression and procoagulant activity are regulated on the vascular cell surface remain incompletely understood. We combine functional genomics, human and rodent genetics, cell biology, and protein biochemistry to dissect the TF-dependent initiation of blood coagulation. Because the contribution of cellular TF is not captured by clinical coagulation testing, these critical modifiers of human bleeding and thrombotic risk remain undetected in human populations.
Current and Recent Grants
NIH Director’s Early Independence Award
Functional Genetics of Tissue Factor in Bleeding and Thrombotic Risk
This project integrates functional genetics with human population data to identify new sources of tissue factor-dependent bleeding and thrombotic risk.
Modifiers of Tissue Factor Procoagulant Activity
This project seeks to use a functional genetic screen to understand the biochemical mechanisms regulating tissue factor activation on the endothelial cell surface.
Scholar Award (Schulman)
American Society of Hematology
This project seeks to use a functional genetic screen to elucidate the biochemical mechanisms regulating tissue factor expression and procoagulant activity.
Mentored Research Award (Schulman)
Hemostasis and Thrombosis Research Society
Role of Protein Disulfide Isomerase in Prothrombin Activation
This project seeks to characterize the role of protein disulfide isomerase in prothrombin activation and use protein disulfide isomerase as an hemostatic agent.