Elimelda Ongeri

TitleAssistant Professor





OfficeBarnes Hall
Room: 215

1601 East Market Street
Greensboro, NC 27411

Elimelda Ongeri


Other: Ovarian Gene Regulation, Pennsylvania State University, College of Medicine, Hershey, PA, 2005

Ph D: Animal Physiology, Purdue University-Main Campus, 2001

MS: Basic Medical Sciences, Purdue University, 1999

MS: Animal Physiology, University of Nairobi, 1994

BS: Animal Sciences, Egerton University, 1991

Research Interests

Research in the Ongeri lab focuses on understanding the cellular and molecular mechanisms underlying acute and chronic kidney disease. We work with in vitro cell culture systems, animal models, and human patients. Of specific interest to my research group is determining the role of meprin metalloproteases in the progression of kidney injury. To this end we utilize surgical procedures for induction of acute kidney injury in mouse models which include ischemia/reperfusion-induced acute kidney injury, unilateral ureteric obstruction (UUO), and cecal-ligation and puncture (CLP)-induced sepsis. In addition to working with mouse models, for diabetic kidney disease (DKD), we are interested in understanding the basis for health disparities in DKD in African Americans, and in identifying biomarkers of kidney injury which could be used to develop diagnostic and therapeutic tools. We use an interdisciplinary team approach with collaborators at NC A&T and other research institutions.

Recent Publications

Ongeri, Elimelda  Niyitegeka, Jean-Marie  (2016).  The Anti-Inflammatory Peptide Ac-SDKP is Released from Thymosin β4 by Renal Meprin  and Prolyl Oligopeptidase.  No  (1,  308,  pp. F56-68).  American Journal of Physiology - Renal.

Niyitegeka, Jean-Marie  Bastidas, Adam  Newman, Robert  Taylor, Susan  Bond, Judith  Ongeri, Elimelda  (2014).  Isoform-specific interactions between meprin metalloproteases and the catalytic subunit of protein kinase A.  (28,  pp. 690.613).  The FASEB Journal.

Boyd, Sada  Newman, Robert  Ongeri, Elimelda  (2014).  Protein kinase C alpha is a target for the meprin B metalloproteinase.  (28,  pp. 690.614).  The FASEB Journal.