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Department
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Vascular Biology Program
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Hospital Title
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Senior Research Associate, Surgery
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Academic Title
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Professor of Surgery
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Phone
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617-919-2207
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Fax
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617-730-0231
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Email
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Marsha Moses
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Location
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300 Longwood Avenue
Karp-12.214
Boston MA 02115
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The Moses Lab has had a long-standing interest in identifying and characterizing the biochemical and molecular mechanisms underlying the regulation of angiogenesis during tumor progression, from the angiogenic switch through metastasis. Dr. Moses and her group have discovered five different angiogenesis inhibitors, three of which are in clinical development for use against a variety of cancers.
Significant efforts are now underway in the lab to identify the genes and proteins that they encode, that are responsible for the ''angiogenic switch''. This critical checkpoint, during which time a tiny benign, avascular tumor acquires the vascular phenotype, is a prerequisite for subsequent tumor growth and progression. The Moses Lab has recently identified and validated a number of genes which are differentially expressed during the angiogenic switch and is currently developing molecular and biochemical interventions to prevent the switch from occurring by targeting some of these genes.
In addition, the Moses Lab has, as part of their long term Urinary Proteomics Initiative, developed a number of sensitive and specific non-invasive urine tests for different cancers. These cancer tests are based on the lab's work focused on the detection of biomarker proteins purified from the urine of cancer patients. A number of these urine tests are currently in clinical testing as potential cancer diagnostics and prognostics.
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Marsha A. Moses received a PhD from Boston University and completed a National Institutes of Health postdoctoral fellowship at Children's Hospital and MIT. She is the recipient of a number of NIH and foundation grants. Her awards and honors include the Cancer Research Foundation Award, American Cancer Society Research Award, the CaPCURE Research Award and the Science Scholar Fellowship Award, from The Mary Ingraham Bunting Institute of Radcliffe College. She is currently the Chair of the Cell Structure and Metastasis Peer Review Committee of the American Cancer Society.
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- Roy R, Wewer UM, Zurakowski D, Pories SE, Moses MA. ADAM 12 cleaves ECM proteins: correlation with breast cancer status and stage. J. Biol. Chem.2004; 279(49):51323-30. (Epub 2004 Sep 20)
- Fernandez CA, Butterfield C, Jackson G, Moses MA. Structural and functional uncoupling of the enzymatic and angiogenic inhibitory activities of TIMP-2: Loop 6 is a novel angiogenesis inhibitor. J. Biol. Chem. 2003;278:40989-40995.
- Yan I, Borregaard N, Kjeldsen L and Moses MA. The high molecular weight urinary matrix metalloproteinase (MMP) activity is a complex of gelatinase B/MMP-9 and neutrophil gelatinase-associated lipocalin (NGAL). J. Biol. Chem. 2001;276:37258-37265
- Fang JM, Shing Y, Wiederschain D, Yan L, Butterfield C, Jackson G, Harper J, Tamvakopoulos G, Moses MA. Matrix metalloproteinase-2 is required for the switch to the angiogenic phenotype in a tumor model. Proceedings of the National Academy of Sciences 2000; 97: 3884-3889.
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