Arthur Veis
Title: Professor Emeritus
Research Area: Extracellular matrix proteins: Assembly, Interactions, and Functions
Degree: Ph.D., Northwestern University
Voice: 312.503.1355
Fax: 312.503.2544
e-mail: aveis@northwestern.edu

Detailed research description:
The connective tissues and skeletal tissues are comprised of a mixture of cells and extracellular matrix (ECM) components. The ECM provides the form and structural stability to the tissues and organs, provides protective barriers between the organism and its external environment, and translates the forces involved in muscular contraction into mechanical motion. Normal growth and development requires controlled remodeling of the structural components. Thus, it is crucial to understand these structures and how the remodeling processes are regulated, as well as how they provide such a wide variety of tissue elements.

Our studies are focused on three principal areas: the formation of the collagen fibril matrix; the mechanisms of mineralization of the matrix to form bone and dentin; and the epithelial-mesenchymal signaling interactions that guide craniofacial development. Current studies on collagen focus on the assembly of the heterotrimeric type I molecule within the endoplasmic reticulum via interactions between the C-terminal pro-alpha 1 and pro-alpha 2 domains. The specific structural domains have been prepared as recombinant proteins. These are being crystallized for X-ray structure determination, and their interactions are being studied. Collagen-ECM protein interactions are being examined by rotary shadowing electron microscopy to locate the specific interaction domains, and are being quantitated by dynamic and Rayleigh light scattering analysis. These are linked to the deposition of mineral within collagenous domains. Finally, unique regulatory proteins from the mineralized dentin matrix have been isolated, sequenced and produced by recombinant means. These proteins, in vitro and in vivo, direct the late stages of both amelogenesis and odontogenesis in tooth germs.

Representative publications:

Alvares, K., Siddiqui, F, Malone, J.P., and Veis, A.  Assembly of the type I procollagen molecule: Selectivity of the interactions between the pro-a1(I) and pro-a2(I)-carboxyl propeptides. Biochemistry 38: 5401-5411 (1999).

Stock, S. R., Nagaraja, S., Barss, J., Dahl, T., and Veis, A.  X-rayMicroCT study of the pyramids of the sea urchin Lytechinus variegatus. J. Struct. Biol. 141:9-21 (2003).

Veis, A. Amelogenin gene splice products: Potential Signaling Molecules. Cell Mol. Life Sci. 60:38-55 (2003).