Graduate School
University of Michigan-Ann Arb (2000)

Research Interest

  • Identification of the physiological functions of paraoxonases (PONs), a family of calcium dependent esterases. Investigation of the protective functions of the PONs as they relate to cardiovascular diseases, bacterial pathogenesis and organophosphate toxicity.


Featured Publications LegendFeatured Publications

Paraoxonase 2 is down-regulated by the Pseudomonas aeruginosa quorumsensing signal N-(3-oxododecanoyl)-L-homoserine lactone and attenuates oxidative stress induced by pyocyanin.
Horke S, Witte I, Altenhöfer S, Wilgenbus P, Goldeck M, Förstermann U, Xiao J, Kramer GL, Haines DC, Chowdhary PK, Haley RW, Teiber JF Biochem. J. 2010 Feb 426 1 73-83
Dominant Role of Paraoxonases in Inactivation of the Pseudomonas aeruginosa Quorum-Sensing Signal N-(3-Oxododecanoyl)-L-Homoserine Lactone
John F. Teiber, Sven Horke, Donovan C. Haines, Puneet K. Chowdhary, Junhui Xiao, Gerald L. Kramer, Robert W. Haley, and Dragomir I. Draganov Infection and Immunity June 2008 76 2512-2519
Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities.
Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN. J. Lipid Res. June 2005 46 1239-1247
Purified human serum PON1 does not protect LDL against oxidation in the in vitro assays initiated with copper or AAPH.
Teiber JF, Draganov DI, La Du BN. J. Lipid Res. December 2004 45 2260-2268