SCD1 is a Novel Molecular Target in Human Carcinomas
Stearoyl-CoA desaturase 1 (SCD1), a lipid metabolism enzyme, was first observed in Dr. Copland's Cancer Biology and Translational Lab to be abnormally expressed in clear cell renal cell carcinoma (ccRCC) and has since been explored in other cancer types.
Genetic and molecular targeting of SCD1 activity results in tumor-specific inhibition of cell growth and induction of apoptosis both in vitro and in vivo.
Through in silico drug modeling, Dr. Copland's lab has created novel SCD1-specific inhibitors that are being developed for clinical trials in various cancers.
SCD1 is an iron-containing enzyme belonging to a family of fatty acyl desaturases whose role is to catalyze the biosynthesis of monounsaturated fatty acids (MUFAs), oleic acid and palmitoleic acids from saturated fatty acids (SFAs), including stearic acid and palmitic acid.
MUFAs are involved in many biological processes, are a major constituent of biological structures such as membranes, and can also function as or modify signaling molecules.
Review poster presentations related to Dr. Copland's research on the SCD1 novel molecular target (these documents are PDF files requiring Adobe Reader):