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Faculty Detail     Name JON DANIEL SHARER   Campus Address KAUL 652 Zip 0024 Phone 205-996-4799 E-mail dsharer@uab.edu Other websites UAB Biochemical Genetics Laboratory

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

Faculty Appointment(s) Appointment Type Department Division Rank Primary  Genetics   Clinical Genetics Associate Professor Center  General Clinical Research Center  Ctr for Clinical & Translational Sci Associate Professor Center  Medicine  Nephrology Res & Trng Ctr Associate Professor

Graduate Biomedical Sciences Affiliations Medical Scientist Training Program

Biographical Sketch  Daniel Sharer received his PhD in Biochemistry and Molecular Biology from the University of Medicine and Dentistry of New Jersey 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 ABMG board-certified in this specialty in 2005. Dr. Sharer is currently an Associate Professor of Genetics and has been Director of the UAB Biochemical Genetics Laboratory since 2005.

Society Memberships Organization Name Position Held Org Link American College of Medical Genetics  Laboratory Quality Assurance Committee    American Society of Human Genetics  Active Member    Society for Inherited Metabolic Disorders  Active Member    Southeast Regional Genetics Group  Board of Directors

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 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

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