Yong Ran, M.D., Ph.D.

Ran, YongAssistant Scientist
Department of Neuroscience
Center for Translational Research in Neurodegenerative (CTRND)
1275 Center Drive
PO Box 100159
Gainesville, FL  32610-0159

Email:  yran@ufl.edu
Office phone: (352) 273-9690
Website:  Ran Research

Education

1993-2001 M.D. Tongji Medical University
Wuhan, China
2001-2005 Ph.D.
(Bioengineering/Biophysics)
Huazhong University of Science & Technology
Wuhan, China
2005-2006 Postdoctoral Associate
(Physiology & Functional Genomics)
Department of Pysiology & Functional Genomics
University of Florida
Gainesville, Florida
2006-2011 Postdoctoral Associate
(Chemistry)
Department of Chemistry
University of Florida
Gainesville, Florida
2011-2012 Postdoctoral Associate
(Neuroscience)
Department of Neuroscience
Center for Translational Research in Neurodegenerative Disease (CTRND)
University of Florida
Gainesville, Florida
Key Words: Gamma-secretase, signal peptide peptidase, intramembrane proteolysis
Research Summary:
A protease is any enzyme that conducts cleavage of a protein or peptide into shorter protein, peptide or amino acid. Proteases are involved in many physiological activities, from the digestion of food to cell signaling transduction. Gamma-secretase (a complex of many components) controls many transmembrane proteins, among them are the well-studied the amyloid precursor protein and Notch receptor. The most notable member of the Gamma-secretase complex is presenillin, the catalytic component responsible for the initiation of substrate cleavage.   The activity of the gamma secretase plays a key role in the pathology of Alzheimer’s disease. Similar in function to presenillin is signal peptide peptidase (SPP), an intramembrane protease that processes signal peptide. SPP plays important role in immune surveillance and virus maturation.  SPP is implicated in malaria and its characterization may be useful in the design of a drug target for this rampant disease.
Our research focused on the cleavage mechanism of gamma secretase, signal peptide peptidase (SPP) and signal peptide peptidase like proteins (SPPLs). We have established a multi-substrate cleavage monitoring platform based on cell models and in vitro assay systems. This platform can help us to gain a better understanding of how gamma secretase works and how it reacts to various types of inhibitors and modulators. For the SPP and SPPLs project, we are working establish an accelerated screening method.  These methods enable us to comprehensively and efficiently screen for drugs active against gamma secretase and SPP in a fraction of the time used in current gamma secretase activity assays.
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