Artlett Hall
Cook College
Rutgers University
New Brunswick, NJ 08903

(732) 932-8354
FAX: (732) 932-6996

Research studies are aimed at isolating, characterizing and understanding the function of proteolytic enzymes and various factors which regulate protein turnover in animal cells. More specifically, we work on 1) proteases and their role in growth and development and in the intracellular removal of normal and abnormal proteins in physiological and pathological states; and 2) the identification of agents which selectively inhibit or stimulate the protein synthetic and the protein degradative process. In addition to finding novel functions for previously described proteases, we have isolated novel enzymes and factors which affect the rate of breakdown of cellular proteins. We are also studying several compounds which accelerate or retard the rate of protein synthesis and degradation in mammalian cells and tissues. These compounds may be useful for the treatment/prevention of certain disease states (e.g., cancer, heart disease) or to accelerate growth in domestic animals.

For complete list: PubMed

Fagan, J.M., Ganguly, M., Tiao, G., Fischer, J.E., and Hasselgren, P.O. (1996).
Sepsis increases oxidatively damaged proteins in skeletal muscle.
Archives of Surgery. 131(12):1326-31; discussion 1331-2.

Strack, P.R., Waxman, L., and Fagan, J.M. (1996).
Activation of the multicatalytic endopeptidase by oxidants. Effects on enzyme structure.
Biochemistry. 35(22):7142-9

Strack, P.R., Waxman, L., and Fagan, J.M. (1996).
ATP-stimulated degradation of oxidatively modified superoxide dismutase b cathepsin D in cardiac tissue extracts.
Biochemical & Biophysical Research Communications. 219(2):348-53.