The Lencer laboratory studies the cell and molecular biology of vesicular transport in polarized epithelial cells and regulation of ion transport in the intestine. These studies relate to how intestinal epithelial cells interact with the luminal and sub-epithelial micro-environment, and to the biology of bacterial pathogenesis and host defense at mucosal surfaces.
The lab has discovered how some enteric bacterial toxins breech the intestinal epithelial barrier and enter host epithelial cells to cause disease. These toxins hijack the cellular and molecular mechanisms of retrograde membrane transport to move from the luminal cell surface into the endoplasmic reticulum (ER) of affected cells, the total reverse of protein biosynthesis.
In another project, the lab studies the cell and molecular biology of the MHC Class I-like IgG receptor FcRn. FcRn transports IgG across mucosal surfaces where it may function in immune surveillance and host defense.
In a third area of interest, the lab aims to understand the mechanisms and regulation of intestinal Cl- secretion, the initial ion transport event in secretory diarrhea.
The Lencer Lab is also conducting research projects on oral and pulmonary delivery of protein therapeutics and on clotrimazole for the treatment of inflammatory bowel disease.
About Wayne Lencer
Wayne Lencer received his MD degree from Boston University School of Medicine. He completed an internship and residency at Boston City Hospital, a clinical and research fellowship at Harvard Medical School/Boston Children's Hospital and a fellowship in cell biology and biophysics at Massachusetts General Hospital, HMS and University of California San Francisco.
Dr. Lencer is the recipient of the Samuel J. Meltzer Basic Research Award from the American Digestive Health Foundation and a Harvard Medical School Teaching Award.
- Cho JA, Lee AH, Platzer B, Cross BC, Gardner BM, De Luca H, Luong P, Harding HP, Glimcher LH, Walter P, Fiebiger E, Ron D, Kagan JC, Lencer WI. The Unfolded Protein Response Element IRE1alpha Senses Bacterial Proteins Invading the ER to Activate RIG-I and Innate Immune Signaling. Cell host & microbe. 2013;13(5):558-69. Epub 2013/05/21. doi: 10.1016/j.chom.2013.03.011. PubMed PMID: 23684307; PubMed Central PMCID: PMC3766372.
- Chinnapen DJ, Hsieh WT, Te Welscher YM, Saslowsky DE, Kaoutzani L, Brandsma E, D'Auria L, Park H, Wagner JS, Drake KR, Kang M, Benjamin T, Ullman MD, Costello CE, Kenworthy AK, Baumgart T, Massol RH, Lencer WI. Lipid Sorting by Ceramide Structure from Plasma Membrane to ER for the Cholera Toxin Receptor Ganglioside GM1. Developmental cell. 2012;23(3):573-86. Epub 2012/09/15. doi: 10.1016/j.devcel.2012.08.002. PubMed PMID: 22975326.
- Lencer WI, von Andrian UH. Eliciting mucosal immunity. The New England journal of medicine. 2011;365(12):1151-3. Epub 2011/10/14. doi: 10.1056/NEJMcibr1107816. PubMed PMID: 21992128.
- Saslowsky DE, Cho JA, Chinnapen H, Massol RH, Chinnapen DJ, Wagner JS, De Luca HE, Kam W, Paw BH, Lencer WI. Intoxication of zebrafish and mammalian cells by cholera toxin depends on the flotillin/reggie proteins but not Derlin-1 or -2. The Journal of clinical investigation. 2010;120(12):4399-409. Epub 2010/11/03. doi: 42958 [pii]
10.1172/JCI42958. PubMed PMID: 21041954.
- Tzaban S, Massol RH, Yen E, Hamman W, Frank SR, Lapierre LA, Hansen SH, Goldenring JR, Blumberg RS, Lencer WI. The recycling and transcytotic pathways for IgG transport by FcRn are distinct and display an inherent polarity. Journal Of Cell Biology. 2009;185(4):673-84. PubMed PMID: 19451275.
- Lencer WI. Patching a leaky intestine. N Engl J Med. 2008;359(5):526-8. PubMed PMID: 18669433.