Digestive Disease Center
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Lucy Tompkins

Academic Appointments

Contact Information

  • Clinical Offices
    300 Pasteur Dr S101F; MC 5107 Stanford, CA 94305
    Tel Work (650) 725-6542 Fax (650) 723-3474

Professional Snapshot

Clinical Focus

  • Infectious Diseases
  • Internal Medicine
  • hospital epidemiology

Administrative Appointments

  • Medical Director, Hospital Epidemiolgy and Infection Control Dept, Stanford Hospital and Clinics (1989 - present)
  • Associate Dean for Academic Affairs, School of Medicine (2001 - present)
  • Chief, Division of Infectious Diseases and Geographic Medicine; Associate Dean for Academic Affairs, Department of Medicine/Stanford U. Medical School (2001 - 2008)

Honors and Awards

  • Fellow, Infectious Dis Soc of America (1987)
  • Member, Western Assoc. Physicians (1990)
  • Member, Am. Assoc Physicians (1995)
  • Fellow, Am.Academy Microbiology (1997)
  • Fellow, AAAS (2001)

Professional Education

Fellowship: University of Washington School of Medicine-GME, WA (1979)
Board Certification: Internal Medicine, American Board of Internal Medicine (1976)
Residency: University of Washington School of Medicine-GME, WA (1976)
Residency: Dartmouth Hitchcock Medical Center, NH (1975)
Internship: Dartmouth Hitchcock Medical Center, NH (1974)
View All 8

Graduate & Fellowship Program Affiliations

Scientific Focus

Research Interests

Molecular and cellular basis of pathogenicity of Helicobacter pylori infection and the relationship to gastric malignancy. We are studying the interaction between Helicobacter pylori, the causative agent of peptic ulcers and gastric cancer, and gastric epithelial cells. Genes encoded by a pathogenicity island in H. pylori comprise a secretory apparatus that secretes bacterial CagA protein into target gastric epithelial cells. CagA is phosphorylated on tyrosine residues by host cell kinases and is associated with signal transduction and changes in the cytoskeleton and motility. Cells that have received CagA develop an elongated phenotype and become motile. Further studies suggest that the full-length protein localizes to junctional adhesion sites and acts as an oncoprotein to stimulate the cMET receptor, leading to changes in cell polarity, motility and differentiation, changes which may be related to the development of gastric cancer. We have used an animal model of infection to study gastric lymphoma (MALT lymphoma), including the cellular response.

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