Home > Research > Research Faculty > Craniofacial Biology Faculty

School of Dental Medicine Faculty

MARY E. REYLAND Associate Professor Craniofacial Biology Mail Stop 8120, RC1-S, Rm L18 11113 12801 E. 17th Ave P.O. Box 6511 Aurora, CO 80045 Phone: 303-724-4572 Fax: 303-724-4580 Email: Mary.Reyland@uchsc.edu

Education:    
Ph.D. Medical College of Virginia
Postdoctoral Training: University of Washington, Seattle, WA           

Honors and Awards:
Irving H. Page Award for Young Investigators, American Heart Association
Outstanding Basic Science Instructor, Dental Hygiene, University of Colorado Denver School of Dental Medicine

Research Interests: 

Phosphorylation of cellular proteins by protein kinases is utilized widely as a mechanism to relay information within the cell, a process known as "signal transduction." Signal transduction pathways are essential for the regulation of diverse cellular functions, including programmed cell death, or apoptosis. My laboratory is interested in how specific members of the protein kinase C family function to modulate apoptosis in salivary acinar epithelial cells. We have shown that PKCd is essential for apoptosis induced by a diverse group of cell toxins which target the mitochondria-dependent apoptotic pathway. Inhibition of PKCd blocks apoptosis at, or prior to, the mitochondria, resulting in suppression of DNA fragmentation and caspase activation. This argues that PKCd functions upstream of the mitochondria as an integrator of diverse death signals. Using techniques to localize PKCd in cells undergoing apoptosis, we show that nuclear translocation of PKCd occurs early in the apoptotic pathway, and that mutations of PKCd which prevent its nuclear translocation inhibit apoptosis. Thus, PKCd may function in the nucleus to initiate apoptosis. Our goal now is to identify nuclear phosphorylation targets of PKCd and to understand the mechanism by which PKCd regulates the apoptotic pathway. A second project in the laboratory is to understand how PKCa protects against apoptosis. Inhibition of PKCa using a dominant negative PKCa, induces apoptosis in parotid acinar cells. Interestingly, apoptosis induced by inhibition of PKCa requires PKCd, suggesting that PKCa lies upstream of PKCd in the apoptotic pathway. PKC is a potentially exciting therapeutic target since the expression of anti-apoptotic PKC isoforms may protect the salivary gland against destruction in patients undergoing cancer chemotherapy or X-radiation. Conversely, expression of pro-apoptotic PKC isoforms may be useful in the treatment of salivary gland tumors and other tumors of epithelial origin.

Selected Publications:

DeVries TA, Neville MC, Reyland ME. Nuclear import of PKCdelta is required for apoptosis: identification of a novel nuclear import sequence. EMBO J. 2002 Nov 15;21(22):6050-6060.

Shizukuda Y, Reyland ME, Buttrick PM. Protein kinase C-delta modulates apoptosis induced by hyperglycemia in adult ventricular myocytes. Am J Physiol Heart Circ Physiol. 2002 May;282(5):H1625-34.

Helt CE, Hoernig GR, Albeck DS, Gerhardt GA, Ickes B, Reyland ME, Quissell DO, Stromberg I, Granholm AC. Neuroprotection of grafted neurons with a GDNF/caspase inhibitor cocktail. Exp Neurol. 2001 Aug;170(2):258-69.

Matassa AA, Carpenter L, Biden TJ, Humphries MJ, Reyland ME. PKCdelta is required for mitochondrial-dependent apoptosis in salivary epithelial cells. J Biol Chem. 2001 Aug 10;276(32):29719-28.

Reyland ME, Barzen KA, Anderson SM, Quissell DO, Matassa AA. Activation of PKC is sufficient to induce an apoptotic program in salivary gland acinar cells. Cell Death Differ. 2000 Dec;7(12):1200-9.

Latest Publications in PubMed

TOP