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Jian Fu, B.Med., Ph.D.

Contact Information

Phone Numbers

Administrative: (585) 276-7698

Office: (585) 276-7724

Fax: (585) 276-1530

Research Labs

Hypoxia-inducible factor a heterodimeric transcription factor composed of HIFa subunit and b/ARNT subunit. While HIF b expressed, HIF a subunit is degraded at normoxia by ubiquitin-proteasome pathway.

Lab: (585) 276-7724

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Research Network

Biography

Hypoxia-inducible factor (HIF) is a heterodimeric transcription factor composed of a HIF alpha subunit and a beta/ARNT subunit. While HIF beta subunit is constitutively expressed, HIF alpha subunit is rapidly degraded at normoxia by the ubiquitin-proteasome pathway. Importantly, it has been shown recently that the prolyl hydroxylation of HIF alpha subunit is required for its ubiquitination and subsequent destruction. The a subunit becomes hydroxylated by a family of newly identified prolyl-4-hydroxylases. Three prolyl hydroxylases namely EGLN1, 2, 3 have been identified to date.

My research focus is on elucidating of the biochemical and biological roles of SM20, the orthologue of EGLN-3, with a specific emphasis on deciphering the effect of SM20 on the differentiation and development of skeletal muscle. Towards this end, we have been using pharmalogical inhibitors to repress the activity of the prolyl hydroxylase, siRNAs to knock down SM20 expression level, and transient transfection strategy to overexpress SM20 to reveal a role for SM20 in the differentiation of cultured skeletal myoblasts. Strikingly, our preliminary results suggest that SM20 is involved in myogenesis. Our intriguing finding prompts us to dissect the underlying mechanism(s). It has been well documented that the myogenic differentiation is mainly orchestrated by a family of muscle regulatory factors (MRFs) including MyoD, myogenin, Myf-5, and MRF4. As a first step, work is in progress to explore the impact of SM20 on these master muscle-specific molecules. Further efforts will be made to identify more complicated molecular basis of SM20 on myogenesis by employing a broad variety of approaches such as (but not limited to) cDNA microarray and proteomics methodologies. In addition, we set out to create the SM20 knock-out mice to obtain more complex picture of how SM20 regulates myogenesis and development. Our study will improve the understanding of the biochemical and biological relevance of SM20 and provide novel insights into the regulation of myogenic differentiation.

Research

Hypoxia-inducible factor (HIF) is a heterodimeric transcription factor composed of a HIF alpha subunit and a beta/ARNT subunit. While HIF beta subunit is constitutively expressed, HIF alpha subunit is rapidly degraded at normoxia by the ubiquitin-proteasome pathway. Importantly, it has been shown recently that the prolyl hydroxylation of HIF alpha subunit is required for its ubiquitination and subsequent destruction. The a subunit becomes hydroxylated by a family of newly identified prolyl-4-hydroxylases. Three prolyl hydroxylases namely EGLN1, 2, 3 have been identified to date.

My research focus is on elucidating of the biochemical and biological roles of SM20, the orthologue of EGLN-3, with a specific emphasis on deciphering the effect of SM20 on the differentiation and development of skeletal muscle. Towards this end, we have been using pharmalogical inhibitors to repress the activity of the prolyl hydroxylase, siRNAs to knock down SM20 expression level, and transient transfection strategy to overexpress SM20 to reveal a role for SM20 in the differentiation of cultured skeletal myoblasts. Strikingly, our preliminary results suggest that SM20 is involved in myogenesis. Our intriguing finding prompts us to dissect the underlying mechanism(s). It has been well documented that the myogenic differentiation is mainly orchestrated by a family of muscle regulatory factors (MRFs) including MyoD, myogenin, Myf-5, and MRF4. As a first step, work is in progress to explore the impact of SM20 on these master muscle-specific molecules. Further efforts will be made to identify more complicated molecular basis of SM20 on myogenesis by employing a broad variety of approaches such as (but not limited to) cDNA microarray and proteomics methodologies. In addition, we set out to create the SM20 knock-out mice to obtain more complex picture of how SM20 regulates myogenesis and development. Our study will improve the understanding of the biochemical and biological relevance of SM20 and provide novel insights into the regulation of myogenic differentiation.

Credentials

Faculty Appointments

  • Research Assistant Professor (Part-Time) - Department of Medicine, Aab Cardiovascular Research Institute (SMD) - Primary

Education

1989
B. Med | Hubei University of Medicine
Medicine

1995
PhD | Peking University School of Medicine

Awards

2002
Travel Award
Sponsor: Annual Meeting of ASBMB and Experiental Biology

2002
Paul E. Strandjord Young Investigator Award
Sponsor: Annual Mtg of Academy of Clinical Lab. Physicians & Scientists

1994
Guanghua Outstanding Graduate Award
Location: Peking University

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Publications

Journal Articles

2010
Fu, J.; Taubman, M.B. "Prolyl hydroxylase EGLN3 regulates skeletal myoblast differentiation through an NF-kappaB-dependent pathway." J Biol Chem. 2010; 285(12): 8927-8935.

2009
Kirby, R.J.; Jin, Y.; Fu, J.; Cubillos, J.; Swertfeger, D.; Arend, L.J. "Dynamic regulation of sphingosine-1-phosphate homeostasis during development of the mouse metanephric kidney." Am J Physiol Renal Physiol. 2009; 296(3): F634-641.

4/27/2007
Fu J, Menzies K, Freeman RS, Taubman MB. "EGLN3 prolyl hydroxylase regulates skeletal muscle differentiation and myogenin protein stability." The Journal of biological chemistry.. 2007 Apr 27; 282(17):12410-8. Epub 2007 Mar 06.

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