Developmental Glycobiology Section
Building 30, Room 407
30 Convent Dr, MSC 4370
Bethesda, MD 20892-4370
Cells of the body are decorated with a variety of carbohydrates (sugars) that serve diverse functions. Alterations in the presence of these sugars are associated with a number of human diseases, including familial tumoral calcinosis and various cancers. To better understand how alterations in glycosylation contribute to disease onset and progression, Dr. Ten Hagen’s group studies how sugar addition (O-glycosylation) is regulated and how it influences basic biological processes. Using Drosophila models, the group has demonstrated that O-glycosylation is an essential modification that is required in specific cells and tissues during development. Current research is directed at further defining the role this protein modification plays in secretion, secretory vesicle formation, cell adhesion, and cell signaling in both Drosophila and mammals. Ultimately, the aim is to elucidate how O-glycosylation regulates key cellular processes during development and disease.
Dr. Kelly Ten Hagen received a BS from Cornell University and earned a PhD at Stanford University. She served as a research assistant professor at the University of Rochester from 1992-2001, and then as a senior research fellow at the National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK), from 2001-2004. She was appointed chief of the Developmental Glycobiology Unit at NIDCR in 2004 and was promoted to senior investigator and chief in 2012. Dr. Ten Hagen has served as an editorial board member for The Journal of Biological Chemistry and on the Board of Directors for the Society for Glycobiology. She currently serves on the Promotion and Tenure Committee for NIDCR, the Woman Scientist Advisors Executive Committee for the NIH, the steering committees for the NIH Glycobiology and Developmental Biology Scientific Interest Groups, and as an editorial board member for the journal Glycobiology.
- Tran DT, Ten Hagen KG. Real-time insights into regulated exocytosis. J Cell Sci. 2017 Apr 15;130:1355-63.Tran DT, Zhang L, Zhang Y, Tian E, Earl L, Ten Hagen KG. Multiple members of the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase family are essential for viability in Drosophila. J Biol Chem. 2012 Feb 17;287(8):5243-52.
- Revoredo L, Wang S, Bennett EP, Clausen H, Moremen KW, Jarvis DL, Ten Hagen KG, Tabak LA, Gerken TA. Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family. Glycobiology. 2016 Apr;26(4):360-76.Kakani S, Yardeni T, Poling J, Ciccone
- Tian E, Stevens SR, Guan Y, Anderson SA, Springer DA, Starost MF, Patel V, Ten Hagen KG, Tabak L. Galnt1 is required for normal heart valve development and cardiac function. PLoS One. 2015 Jan 23;10(1): e0115861.
- Tran DT, Masedunskas A, Weigert W, Ten Hagen KG. Arp2/3-mediated F-actin formation controls regulated exocytosis in vivo. Nat Commun. 2015 Dec 7;6:10098.
- C, Niethamer T, Klootwijk RD, Manoli I, Darvish D, Hoogstraten-Miller S, Zerfas P, Speranksy V, Tian E, Ten Hagen KG, Kopp JB, Gahl WA, Huizing M. The Gne M712T mouse as a model for human glomerulopathy. Am J Pathol. 2012 Apr;180(4):1431-40.
- Tian E, Hoffman MP, Ten Hagen KG. 2012. O-glycosylation modulates integrin and FGF signaling by influencing the secretion of basement membrane components. Nat Commun. 2012 May 29;3:869
- Tran DT, Lim JM, Liu M, Stalnaker SH, Wells L, Ten Hagen KG, Live D. Glycosylation of α-dystroglycan: O-mannosylation influences the subsequent addition of GalNAc by the UDP-GalNAc polypeptide N-acetylgalactosaminyltransferases. J Biol Chem. 2012 Jun 15;287(25):20967-74.
- Tran DT, Ten Hagen KG. Mucin-type O-glycosylation during development. J Biol Chem. 2013 Mar 8;288(10):6921-9.
- Zhang L, Syed ZA, van Dijk Härd I, Lim J-M, Wells L, Ten Hagen KG. O-glycosylation regulates polarized secretion by modulating Tango1 stability. Proc Natl Acad Sci U S A. 2014 May 20;111(20):7296-301.