Email Address: jdunlevy@medicine.nodak.edu

Phone: (701) 777-2575

FAX: (701) 777-2477

Education/Training:

Teaching:

Undergraduate:

• Anatomy 490: Directed studies in Anatomy

Graduate:

• BIMD 500: Foundations in Biomedical Sciences, Lecturer
• ANAT 515: Histology, Course Director and Lecturer
• ANAT 518: Developmental Biology, Lecturer
• ANAT 590: Readings in Anatomy and Cell Biology

Medical School:

• Lecturer in Cell Biology, Histology and Human Embryology - year 1
• Laboratory Instructor in Histology – year 1
• Facilitator for Patient Center Learning (PCL) - year 2

Scholarly Activity and Research Interests:

There are three avenues of research and scholarship that I am currently pursuing:

1. The molecular and cellular biology of oxidative stress in retinal pigment epithelial cells. This project involves investigating the molecular changes that occur during oxidative stress in retinal pigment epithelial cells (RPE) and how this influences the cellular pathways of apoptosis, necrosis and autophagy. This project also involves a collaboration with Paul W. Wong, Ph.D. Reunette Harris Professor of Ophthalmology at Emory University to further examine genetic changes associated with these cellular processes.

SH3BP4 is a unique protein with both endocytosis and apoptosis domains and may play a critical role in RPE cells which are very active in phagocytosis (Figure 1). The role of SH3BP4 in RPE cell biology and stress events is a continuing focus of the laboratory (Figure 2).

Figure 1: The SH3BP4 protein domains that are encoded by the various constructs. A) The domains of SH3BP4 are shown. “Full” refers to encoding for the full length SH3BP4 protein starting at amino acid 6 (BamH1 site), amino acids 6-963. There are 2 Full constructs, one encoding for GFP (B) and the other encoding for the c-myc epitope tag (C). The myc-DD construct encodes for the c-myc epitope tag followed by amino acids 521-963 of SH3BP4 (D).

Consensus sequences identified in BOG 25 protein. (cDNA=5.2 kb, ORF=963 amino acids)
SH3 = Src Homology 3 domain involved in intracellular protein-protein binding.
N-P-F = (Asn-Pro-Phe) involved in binding to EH domains of proteins in the EH-network.
P-X-X-P = (Pro-X-X-Pro where X=any amino acid) binds SH3 domains.
pat7 = nuclear targeting sequence
Bipartite nuclear targeting = best known sequence for targeting proteins to the nucleus.
Tyr Phosph. = tyrosine phosphorylation sequence, common use in intracellular signaling.
Death Domain (DD) = domain identified in proteins involved in apoptotic protease cascade.

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Figure 2: Photomicrographs of APRE-19 transfected with SH3BP4-GFP, GFP-SH3BP4 and myc-SH3BP4 constructs. The top panel shows plasma membrane and nuclear periphery localization of the SH3BP4 fusion proteins (A). Membrane spiking and a drastic alteration in cell morphology in cells expressing the SH3BP4 fusion proteins were also observed (B). Nuclei from ARPE-19 transfected with GFP-SH3BP4 for 24 hrs were purified using NE-PER reagent. Confocal and epifluorescence microscopy show GFP-SH3BP4 at the nuclear periphery. The corresponding phase microscopy image for the epifluorescent nuclei is also shown (C). Confocal photomicrographs of APRE-19 transfected with GFP-SH3BP4 for 24 hrs and stained with the plasma membrane marker CM-DiI. GFP-SH3BP4 at the cell periphery co-localizes with the plasma membrane marker CM-DiI seen in yellow in the merged image (D). Bars=20 om

2. Alteration of cell biological processes in the transition of human proximal tubule and bladder cells from a mesenchymal to an epithelial cell type. This project examines changes in cytoskeletal and cell-cell interactions that occur relative to metallothionein-3 expression and cadmium transformation during the transition of epithelial to mesenchymal cell types and vice versa in bladder and human proximal tubule cells. This project involves collaboration with Don Sens, Ph.D. and Seema Somji, Ph.D. in the Department of Pathology at UND.

3. The use of virtual slide technology in medical and health science education. I have been interested and active in advancing the use of virtual slide technology in medical and graduate education since 2002. This project involves a collaboration with Mary Ann Sens, M.D., Ph.D., Dept of Pathology, Office of Medical Education, and Computer Services where UND has one of the largest virtual slides for education in the nation. This collection includes ~200 histology and developmental anatomy slides which are currently maintained on a 2 TB server.

Peer Reviewed Publications: