Judith White        Professor of Cell Biology             (and Microbiology) Phone: (434)924-2593 Fax: (434)982-3912 Mail: UVA Health System,          School of Medicine,          Box 800732 Email: jw7g@virginia.edu Homepage: Click Here

Research Interest

As an outgrowth of studies on sperm-egg binding and fusion, my laboratory discovered the ADAM family of proteins (Blobel et al., 1992. Nature. 356:248; Wolfsberg et al. 1993. Proc. Nat'l. Acad. Sci. 90:10783). ADAMs acquired their acronym because they contain A Disintegrin and A Metalloprotease domain. They also contain a cysteine-rich domain (on their extracellular side) and a cytoplasmic tail (on their intracellular side); many of the cytoplasmic tails contain signaling motifs. ADAMs thus represent a large and widely expressed family of multidomain proteins. They have been implicated in a variety of important processes and diseases (e.g., fertilization, neurogenesis, myoblast fusion, inflammatory responses, and asthma). ADAM metalloproteases are involved in two very important classes of cell surface proteolytic events: ectodomain shedding and remodeling of extracellular matrices. A long-term goal of our work is to understand how the downstream disintegrin, cysteine-rich, and signaling domains affect ADAM proteolytic activity in vivo. In the past we have studied the role of ADAMs in sperm-egg interactions. Our recent focus, developed in collaboration with Dr. Douglas DeSimone, is on ADAMs in neural crest cell migration. We have shown that ADAM disintegrin domains can interact with integrins and that the cysteine-rich domain plays a key role in regulating ADAM proteolytic activity. Current work addresses the detailed mechanism of ADAM-mediated cell migration.

Representative Recent Publications

1. White, J.M. and T.G. Wolfsberg. 2003. Table of the ADAMs. http://www.people.virginia.edu/~jw7g/Table_of_the_ADAMs.html

2. Smith, K.M., A. Gaultier, H. Cousin, D. Alfandari, J.M. White, and D. DeSimone. 2002. The cysteine-rich domain regulates ADAM protease function in vivo. J. Cell Biol.: 159: 893-902.

3. Alfandari, D., H. Cousin, A. Gaultier, K. Smith, J.M. White, T. Darribere, and D.W. DeSimone. 2001. Xenopus ADAM 13 is a metalloprotease required for cranial neural crest-cell migration. Curr. Biol. 11:918-930.

4. Takahashi, Y., D. Bigler, Y. Ito, and J.M. White. 2001. Sequence-specific interaction between the disintegrin domain of mouse ADAM 3 and murine eggs: role of the b1 integrin associated proteins CD9, CD81 and CD98. Mol. Biol. Cell. 12:809-820.

5. Bigler, D., Y. Takahashi, M.S. Chen, E.A.C. Almeida, L. Osbourne, and J.M. White. 2000. Sequence-specific interaction between the disintegrin domain of mouse ADAM 2 (fertilin b) and murine eggs: Role of the a6 integrin subunit. J. Biol. Chem. 275:11576-11584.
   

   
   

For more information email jw7g@virginia.edu.