Northwestern University Feinberg School of Medicine
Faculty Profiles
Charles V Clevenger, MD, PhD

Charles V Clevenger, MD, PhD

Adjunct Professor of Pathology

Focus of Work

Bio

Prolactin and Breast Cancer



The research focus in Dr. Clevenger’s lab is the characterization of prolactin (PRL) receptor signal transduction and function as it relates to breast cancer and mammary gland development. The PRL receptor (PRLr) is a member of the growth factor/cytokine receptor family, which includes the receptors for interleukin 2-7, GM-CSF, EPO, and GH. Within humans, PRL functions at the endocrine and autocrine/paracrine levels as a growth, differentiation, and motility ...[Read full text]
Prolactin and Breast Cancer



The research focus in Dr. Clevenger’s lab is the characterization of prolactin (PRL) receptor signal transduction and function as it relates to breast cancer and mammary gland development. The PRL receptor (PRLr) is a member of the growth factor/cytokine receptor family, which includes the receptors for interleukin 2-7, GM-CSF, EPO, and GH. Within humans, PRL functions at the endocrine and autocrine/paracrine levels as a growth, differentiation, and motility factor within the breast, a hypothesis first postulated by our laboratory. Therefore, one of our major aims is the characterization of those mechanisms that regulate PRL/PRLr expression and action in both normal and neoplastic tissues. PRL action in human tissues is mediated by the PRLr. The molecular dissection of PRLr isoform structure/function is a research focus, utilizing both biochemical and biophysical approaches to examine PRL-PRLr binding and the interaction of the PRLr with its associated transduction pathways that include JAK/Stat, Nek3/Vav2/Rac, Fyn, SIRPa, NFAT, and c-myb. We have also recently identified a direct genomic action of PRL on gene expression. This action is mediated by the prolyl isomerase cyclophilin B (CypB), which retrotransports endocytosed ligand into the nucleus, where the PRL/CypB complex directly interacts with and activates the Stat5 transcription factor. Additional research by our lab on prolyl isomerases has found that cyclophilin A (CypA) is required for proximal PRLr transduction, functioning as the “molecular switch” facilitating ligand-induced conformational change of the PRLr enabling Jak2 activation. As such our findings present vantage points in the development of novel therapies aimed at modulating PRL action during the differentiation of the human breast and the pathogenesis of malignancy in this tissue.[Shorten text]

Keywords


Education and Certification

  • MD, PhD: Northwestern University Feinberg School of Medicine (1987)
  • Residency: Hospital of the University of Pennsylvania (1990)
  • Fellowship: Hospital of the University of Pennsylvania (1991)
  • Board Certification: Anatomic Pathology, Cytopathology

Contact

804-828-0183

Ward Building Room 3-140
303 E Chicago Avenue
Chicago IL 60611