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Yi Jin, Ph.D.

DECEASED

Yi Jin, Ph.D.

faculty photo
Department: Pharmacology

Contact information
Department of Pharmacology
Room 1310
BRB 2/3
421 Curie Blvd
Philadelphia, PA 19104
Office: 215.573.6191
Fax: 215.573.0200
Lab: 215.898.1144
Education:
BS (Chemistry)
Peking University, 1990.
MS (Chemistry: Protein Crystallography)
Peking University, 1993.
PhD (Chemistry: Biological)
University of Minnesota, 2000.
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Description of Research Expertise

The general interests of Dr. Jin's research lie in the study of structure/function of enzymes and their involvement in human diseases, particularly in the study of enzymes involved in steroid biosynthesis and metabolism.

1.Function of Cytochrome P450 NADPH Oxidoreductase (POR) Genetic Variants.

POR provides electrons for the catalysis of all 50 human microsomal P450 enzymes which include the hepatic drug-metabolizing and the steroidogenic P450s. POR genetic variations can result in severe symptoms characterized by bone malformation, disordered steroidogenesis and sex development, and can also alter metabolism of xenoibiotics. Effects of POR mutations/ polymorphisms on the electron transfer function of POR and in turn the catalysis of key P450 enzymes are investigated by a combination of biochemical and biophysical approaches, such as binding analysis, steady state and transient state kinetics, coupled assays, liposome reactions, etc.

2.Role of Steroid Transform Enzymes of the Aldo-Keto Reductase (AKR) Family in Synthetic Steroid Hormone Metabolism and Action.

Role of AKR in pharmacological effects of synthetic glucocorticoids for asthma (i.e., systemic side-effects and drug resistance) and the cardiovascular effects of progestins in hormonal therapy for women are studied by characterizing enzyme and cell-based steroid metabolism, enzyme inhibition, hormone receptor activity, and enzyme expression levels in relevant cells, etc.

3.Structure and Function of Steroid Transform Enzymes of AKR Family and Their Role in Steroid Metabolism.

Steroid transforming AKRs play important roles in steroid metabolism. Kinetic behavior, substrate recognition, and stereospecificity of these enzymes are studied by a combination of biochemical and structural approaches, such as steady state and transient state kinetics, crystallography, and molecular modeling. Functional basis of bile acid deficiency caused by naturally occurring mutations in AKR1D1 is investigated.

Selected Publications

Liedtke AJ, Adeniji AO, Chen M, Byrns MC, Jin Y, Christianson DW, Marnett LJ, Penning TM.: Development of potent and selective indomethacin analogues for the inhibition of AKR1C3 (Type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase) in castrate-resistant prostate cancer. J. Med. Chem. 56(6): 2429-46, 2013.

Jin Y*, Duan L, Chen M, Penning TM, Kloosterboer HJ.: Metabolism of the synthetic progestogen norethynodrel by human ketosteroid reductases of the aldo-keto reductase superfamily. J. Steroid Biochem. Mol. Biol. 129: 139-44, 2012.

Adeniji AO, Twenter BM, Byrns MC, Jin Y, Chen M, Winkler JD, Penning TM. : Development of potent and selective inhibitors of aldo-keto reductase 1C3 (type 5 17β-hydroxysteroid dehydrogenase) based on N-phenyl-aminobenzoates and their structure-activity relationships. J. Med. Chem. 55(5): 2311-23, 2012 Notes: Epub.

Jin Y, Mesaros CA, Blair IA, Penning TM: Stereospecific reduction of 5β-reduced steroids by human ketosteroid reductases of the aldo-keto reductase (AKR) superfamily: role of AKR1C1-AKR1C4 in the metabolism of testosterone and progesterone via the 5β-reductase pathway. Biochem J 437(1): 53-61, 2011.

Jin Y, Byrns MC, Penning TM [co-first author]: Inhibitors of type 5 17β-hydroxysteroid dehydrogenase (AKR1C3): Overview and structural insights. J Steroid Biochem Mol Biol 125(1-2): 95-104, 2011.

Jin Y: Activities of aldo-keto reductase 1 enzymes on two inhaled corticosteroids: Implications for the pharmacological effects of inhaled corticosteroids. Chem Biol Interact 191(1-3): 234-238, 2011.

Adeniji AO, Twenter BM, Byrns MC, Jin Y, Winkler JD, Penning TM: Discovery of substituted 3-(phenylamino)benzoic acids as potent and selective inhibitors of type 5 17β-hydroxysteroid dehydrogenase (AKR1C3). Bioorg Med Chem Lett 21(5): 1464-1468, 2011.

Zhang L, Jin Y, Chen M, Huang M, Harvey RG, Blair IA, Penning TM. : Detoxication of structurally diverse polycyclic aromatic hydrocarbon (PAH) o-quinones by human recombinant catechol-O-methyltransferase (COMT) via O-methylation of PAH catechols. J. Biol. Chem. 286(29): 25644-54, 2011.

Penning TM, Lee SH, Jin Y, Gutierrez A, Blair IA: Liquid chromatography-mass spectrometry (LC-MS) of steroid hormone metabolites and its applications. J Steroid Biochem Mol Biol 121(3-5): 546-555, 2010.

Jin Y, Duan L, Lee S-H, Kloosterboer HJ, Blair IA, Penning TM: Human cytosolic hydroxysteroid dehydrogenases of the aldo-ketoreductase superfamily catalyze reduction of conjugated steroids: implications for phase I and phase II steroid hormone metabolism. J Biol Chem 284(15): 10013-10022, 2009.

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Last updated: 01/02/2014
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