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Faculty Detail    
Name JON DANIEL SHARER
 
Campus Address KAUL 640B
Phone  (20-5) -206
E-mail  dsharer@uab.edu
Other websites UAB Biochemical Genetics Laboratory
     

Education
Graduate  Rutgers University    1994  PhD in Biochemistry and Molecular Biology 
Fellowship  Emory University School of Medicine    2005  Board certification in Clinical Biochemical Genetics 

Certifications
American Board of Medical Genetics (Clinical Biochemical Genetics)  2005 


Faculty Appointment(s)
Appointment Type Department Division Rank
Primary  Genetics   Clinical Genetics Professor
Center  Civitan International Research Center  Civitan International Research Center Professor
Center  General Clinical Research Center  Ctr for Clinical & Translational Sci Professor
Center  General Clinical Research Center  Nephrology Research & Training Center Professor

Graduate Biomedical Sciences Affiliations
Genetics and Genomic Sciences 
Integrative Genetics Graduate Program 

Biographical Sketch 
Daniel Sharer received his PhD in Biochemistry and Molecular Biology from Rutgers University in 1994. Dr. Sharer performed postdoctoral research at the National Cancer Institute and Emory University from 1996 - 2001. He then completed American Board of Medical Genetics (ABMG) training in Clinical Biochemical Genetics from 2002 - 2004, becoming board-certified in this specialty in 2005. Dr. Sharer is currently a Professor of Genetics and has been Director of the UAB Biochemical Genetics and Metabolic Disease Laboratory since 2005. Dr. Sharer is also the Director of the UAB Laboratory Genetics Fellowship Training Program, a member of the ACGME Residency Review Committee, the ABMG Board of Directors, and President of the Southeast Regional Genetics Group (SERGG).

Society Memberships
Organization Name Position Held Org Link
Accrediatation Council for Graduate Medical Education (ACGME)  Medical Genetics Residency Review Committee   
American Board of Medical Genetics and Genomics (ABMGG)  Board of Directors   
American College of Medical Genetics (ACMG)  Active Member   
American Society of Human Genetics (ASHG)  Past Member   
Association of Professors of Human and Medical Genetics (APHMG)  Workgroup Chair   
Southeast Regional Genetics Group (SERGG)  President   



Research/Clinical Interest
Title
Clinical Biochemical Genetics
Description
The primary goal of the Biochemical Genetics Laboratory (BGL) is to provide diagnostic services focusing on inborn errors of metabolism (IEM). These genetic disorders commonly present in neonates or young children and may rapidly cause irreversible brain damage or death if not identified and treated in a timely fashion. The advantage of biochemical analysis in these cases is the ability to quickly measure levels of genetically determined metabolites, such as amino acids, which may lead to rapid identification and treatment of an otherwise catastrophic condition. It is estimated that at least 1% of all cases of sudden infant death syndrome (SIDS) are caused by undiagnosed IEMs, several of which can be treated by nothing more than a specialized diet. Biochemical methods are now being widely employed for expanded newborn screening, which can identify affected infants before symptoms appear. The BGL is equipped with three core technologies: gas chromatography/mass spectrometry (GC/MS), automated amino acid ion exchange liquid chromatography, and liquid chromatography/tandem mass spectrometry (LC/MS/MS). Utilizing these instruments it is possible to identify a significant number of IEMs, including defects in amino and organic acid metabolism (including urea cycle disorders) and fatty acid oxidation disorders. The lab is also one of the few in the country that offers testing for creatine deficiency syndromes, a significant metabolic cause of MR and autism, as well as polyol analysis for disorders of the pentose phosphate pathway. Future diagnostic capabilities will include lysosomal storage disorders and galactosemia.

Selected Publications 
Publication PUBMEDID
Sharer, J. D. (2015) Amino Acids and Disorders of Amino Acid Metabolism. pp. 136 – 147. In Encyclopedia of Neurological Sciences, 2nd edition (M.J. Aminoff and R.B. Daroff, eds). Elsevier.   
Kim, T., Moore, J. F., Sharer, J. D., Yang, K., Wood, P. A., and Yang, Q. (2014) Carnitine palmitoyltransferase 1b deficient mice develop severe insulin resistance after prolonged high fat diet feeding. J. Diabetes Metab. 5: 1000401    
Askenazi, D. J., Moore, J. F., Fineberg, N., Koralkar, R., Clevenger, S., and Sharer, J. D. (2014) Comparison of methods, storage conditions and time to analysis of serum and urine creatinine measured from microsamples by liquid chromatography mass spectrometry (LC/MS) vs. Jaffe. J. Clin. Lab Anal. 0, 1 – 4   
Kim, T., He, L., Johnson, M. S., Ding, Y., Long, Q., Moore, J. F., Sharer, J. D., Nagy, T. R., Young, M. E., Wood, P. A., and Yang, Q. (2014) Carnitine Palmitoyltransferase1b deficiency protects mice from diet-induced insulin resistance. J. Diabetes Metab. 5, 361-372   
Prasain, J. K., Arabshahi, A., Taub, P. R., Sweeney, S., Moore, R., Sharer, J. D., and Barnes, S. (2013) A validated method for measurement of urinary F2-isoprostanes and prostaglandins by LC-MS/MS. J Chromatogr B Analyt Technol Biomed Life Sci. 913-914, 161-168   
Reardon, R. R. and Sharer, J. D. (2012) Teaching mitochondrial genetics and disease: a GENA Project curriculum intervention. The American Biology Teacher 74, 224-230   
Sharer, J.D. (2009) Mechanisms of toxicity in fatty acid oxidation disorders. pp. 317 – 348. In Endogenous Toxins: Targets for Disease Treatment and Prevention (P. O’Brien and R. Bruce, eds). Wiley-VCH, Weinheim

Ji S, You Y, Kerner J, Hoppel CL, Schoeb TR, Chick WSH, Hamm DA, Sharer JD, Wood PA. (2007) Homozygous carnitine palmitoyltransferase 1b (muscle isoform) deficiency is lethal in the mouse. Mol Genet Metab 93, 314-322

Buhimschi, C. S., Buhimschi, I. A., Yu, C., Wang, H., Sharer, J. D., Diamond, M. P., Petkova, A. P., Garfield, R. E., Saade, G. R., and Wiener, C. P. (2006) The effect of dystocia and previous cesarean uterine scar tissue on the tensile properties of the lower uterine segment. Am J Obstet Gynecol 194, 873-883

Bowzard JB, Sharer JD, Kahn RA. (2005) Assays used in the analysis of Arl2 and its binding partners. Methods Enzymol. 404:453-67.

Sharer JD. (2005) The adenine nucleotide translocase type 1 (ANT1): a new factor in mitochondrial disease. IUBMB Life. 57(9):607-14.

Sharer, J. D. (2005) An Overview of Biochemical Genetics. In Current Protocols in Human Genetics, Unit 17.1 (N. C. Dracopoli, J. L. Haines, B. R. Korf, C. C. Morton, C. E. Seidman, J.G. Seidman, and D. R. Smith, eds.) John Wiley & Sons, Inc.

Tolwani RJ, Hamm DA, Tian L, Sharer JD, Vockley J, Rinaldo P, Matern D, Schoeb TR, Wood PA. (2005) Medium-Chain Acyl-CoA Dehydrogenase Deficiency in Gene-Targeted Mice. PLoS Genet. 1: 205-212

Shern, J. F., Sharer, J. D., Pallas, D. C., Bartolini, F., Cowan, N. J., Reed, M. S., Pohl, J., and Kahn, R. A. (2003) Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A. J Biol Chem. 278: 40829-36.

Sharer, J. D., Shern, J., Van Valkenberg, H., Wallace, D., and Kahn, R. A. (2002) ARL2 and BART enter mitochondria and bind the Adenine Nucleotide Transporter. Mol. Biol. Cell 13, 71-83

Van Valkenburgh, H., Shern, J. F., Sharer, J. D., Zhu, X., and Kahn, R. A. (2001) ADP-ribosylation factors (Arfs) and Arf-like 1 (Arl1) have both specific and shared effectors: characterizing Arl1 binding proteins. J. Biol. Chem. 276, 22826-22837

Sharer, J. D., Koosha, H., Church, W. B., and March, P. E. (1999) The function of conserved amino acid residues adjacent to the effector domain in Elongation Factor G. Proteins: Structure, Function, and Genetics 37, 293-302

Sharer, J. D. and Kahn, R. A. (1999) The Arf-like 2 (ARL2) binding protein, BART: purification, cloning, and initial characterization. J. Biol. Chem. 274, 27553-27561

Pillutla, R. C., Sharer, J. D., Gulati, P. S., Wu, E., Yamashita, Y., Lerner, C. G., Inouye, M., and March, P. E. (1995) Cross-species complementation of the indispensable Escherichia coli era gene highlights amino acid regions essential for activity. J. Bacteriol. 177, 2194-2196

Hou, Y., Lin, Y., Sharer, J. D., and March, P. E. (1994). In vivo selection of conditional-lethal mutations in the gene encoding Elongation Factor G in Escherichia coli. J. Bacteriol. 176, 123-129

Lin, Y., Sharer, J. D., and March, P. E. (1994). GTPase-dependent signaling in bacteria: characterization of a membrane binding site for Era in Escherichia coli. J. Bacteriol. 176, 44-49
 
 

Keywords
Biochemical genetics, inherited metabolic disorders, biomarkers, metabolites, tandem mass spectrometry, regulatory mechanisms