Overview
RESEARCH ABSTRACT
Studies from this laboratory identified cell surface expression of the molecular chaperone GRP78 as a major factor in prostate cancer and other malignancies. Cell surface GRP78 functions as a signaling receptor promoting tumor proliferation and suppressing apoptosis. Patients with a number of malignancies mount an autoimmune response to GRP78 and these antibodies, which bind to the NH2 terminal domains of GRP78, are receptor agonists whose appearance is a marker of poor prognosis. More recently, we have shown that antibodies directed against the COOH-terminal domain of GRP78 are receptor antagonists which may have therapeutic potential for treating patients whose tumors express GRP78 on the cell surface.
Studies from this laboratory identified cell surface expression of the molecular chaperone GRP78 as a major factor in prostate cancer and other malignancies. Cell surface GRP78 functions as a signaling receptor promoting tumor proliferation and suppressing apoptosis. Patients with a number of malignancies mount an autoimmune response to GRP78 and these antibodies, which bind to the NH2 terminal domains of GRP78, are receptor agonists whose appearance is a marker of poor prognosis. More recently, we have shown that antibodies directed against the COOH-terminal domain of GRP78 are receptor antagonists which may have therapeutic potential for treating patients whose tumors express GRP78 on the cell surface.
Current Appointments & Affiliations
Professor Emeritus of Pathology
·
2025 - Present
Pathology,
Clinical Science Departments
Recent Publications
Inhibition of cell surface GRP78 and activated α2M interaction attenuates kidney fibrosis.
Journal Article JCI Insight · December 22, 2025 We recently showed that cell surface translocation of the endoplasmic reticulum-resident protein GRP78, when bound by activated α 2-macroglobulin (α2M*), induces pro-fibrotic responses in glomerular mesangial cells in response to high glucose and regulates ... Full text Link to item CiteCorrection: Autoantibodies against the cell surface-associated chaperone GRP78 stimulate tumor growth via tissue factor.
Journal Article J Biol Chem · September 2025 Full text Link to item CiteAuthor Correction: Activated α2-macroglobulin binding to cell surface GRP78 induces trophoblastic cell fusion.
Journal Article Sci Rep · August 6, 2025 Full text Link to item CiteRecent Grants
Serum pro-N-cadherin as an early biomarker of radiation-induced heart disease
ResearchCo-Principal Investigator · Awarded by National Institutes of Health · 2025 - 2030Development of an Optimized Human Antibody to a Novel Target for the Treatment of Fibrotic Diseases
ResearchPrincipal Investigator · Awarded by North Carolina Biotechnology Center · 2019 - 2020Tension-Stat3-miR-mediated Metastasis
ResearchInvestigator · Awarded by City of Hope · 2015 - 2017View All Grants
Education, Training & Certifications
Duke University ·
1973
M.D.
Duke University ·
1972
Ph.D.