Peter Brooks, Ph.D.
Maine Medical Center Research Institute
81 Research Dr
Scarborough ME, 04074
Phone: (207) 396-8239
Lab Phone: (207) 396-8239
Fax: (207) 396-8179
Dr Brooks obtained his PhD in Cell and Developmental Biology from the State University of New York at Stony Brook in 1993. In 1994 he discovered a role for integrin avb3 in blood vessel development. These studies resulted in the development of two anti-angiogenic drugs (Vitaxin/AbegrinTM and CilengitideTM), which are currently being evaluated in several clinical trials. He received the Wilson S. Stone Memorial Award for outstanding contributions in biomedical research in 1997 and joined USC School of Medicine as an Assistant Professor. Dr Brooks co-founded Cell Matrix Incorporated (CMI) a biotech company based in Los Angeles that focused on anti-angiogenic drugs targeting cryptic ECM epitopes and in 2000, joined NYU School of Medicine as Associate Professor and Director of Angiogenesis and Radiation Research. Dr Brooks’s studies have lead to a recent clinical trial to evaluate the affects of D93; a humanized antibody directed to a cryptic collagen epitope for the treatment of malignant tumors. While studying integrins, proteases and ECM molecules, he recently discovered a vitamin-like compound and several organic analogs that enhanced the anti-tumor activity of chemotherapy and radiation. Dr Brooks recently joined the Maine Medical Center Research Institute and continues his studies on the mechanisms that regulate angiogenesis, tumor growth and metastasis.
Our laboratory is primarily interested in studying how integrin-mediated cellular communication with the extracellular matrix (ECM) regulates angiogenesis, tumor growth and metastasis. In particular, we study the cellular and molecular mechanisms by which the cooperative interactions between integrin receptors and proteolytic enzymes regulate the exposure of cryptic ECM epitopes that modulate endothelial and tumor cell behavior. We are currently characterizing these unique cryptic ECM regulatory elements in an attempt to understanding how integrin receptor binding to these control sites regulate signaling pathways that contribute to angiogenesis and tumor progression. Surprisingly, inhibition of cellular interactions with one of these cryptic ECM control elements significantly increased expression of insulin-like growth factor binding protein-4 (IGFBP-4) as well as the well-known endogenous angiogenesis inhibitor TSP-1. In this regard, we have recently demonstrated the possibility that targeting these non-cellular cryptic epitopes may represent a unique clinical strategy for controlling malignant cell behavior. In summary, we utilize a combination of in vitro cellular, molecular and biochemical assays in conjunction with several in vivo models in attempts to develop novel strategies for the treatment of pathological angiogenesis and malignant tumor growth progression.