Chad Borges

BDA L130G
BIODESIGN
TEMPE
Assistant Professor
Faculty
TEMPE Campus
Mailcode
6401

Biography

Chad Borges is an assistant professor with joint appointments in the School of Molecular Sciences and The Biodesign Institute. He received a B.S. in chemistry from Walla Walla College (WA) in 1997. He went on to complete a Ph.D. in Analytical Toxicology (2001) at the University of Utah under Professor Douglas Rollins, the medical director in charge of doping control for the 2002 Olympic Games. His dissertation research focused on the role of hair pigments and cellular transport in drug incorporation into hair. He continued his education as a postdoctoral fellow at Michigan State University under pioneering mass spectrometrist J. Throck Watson, where he studied protein mass spectrometry with an emphasis on characterizing protein posttranslational modifications. In 2003, he returned to Utah where he helped establish the Olympic-level certified Sports Medicine Research and Testing Laboratory. Following successful laboratory accreditation, he transitioned to the Biodesign Institute at ASU in 2007 where he worked for several years as a research faculty member with Dr. Randall Nelson before joining the Department of Chemistry & Biochemistry (now School of Molecular Sciences) in 2013. Professor Borges’ research interests include development and application of a new form of bottom-up glycomics recently developed by his group; developing molecular markers of biospecimen integrity; and characterization of protein posttranslational modifications as indicators of disease and physiological function.

Education

Ph.D. Analytical Toxicology, University of Utah 2001

B.S. Chemistry, Walla Walla College, WA 1997

Research Interests

1. Analysis of Protein and Lipid Glycosylation

For many years cancer biologists have recognized that, as a general rule, tumor cells display aberrant glycan (sugar polymer) structures. This means that if glycans can be analyzed in the right way(s), they should serve as excellent markers for the presence and progression of cancer. Altered activity of the enzymes that build glycans (glycotransferases, GTs) is the immediate upstream cause of abnormal glycan production. GTs build glycans in an opportunistic non-template driven, first-come-first-build way, with each type of GT adding a specific sugar residue to a specific position of a growing glycan "tree". Thus increased expression of a particular GT results in an increased number of specific glycan polymer branch points (or linear linkages) and a highly diverse set of final glycan structures. We have invented a new gas chromatography-mass spectrometry (GC-MS) based technique to quantify N-, O-, and lipid-linked glycans in whole biofluids and tissues on the basis of these specific glycan polymer branch points and linkages rather than on the basis of intact glycan structure. This provides a means for condensing interesting glycan features into single analytical signals as well as a direct surrogate readout for GT activity. As such, it represents a promising new angle by which to leverage glycans as cancer biomarkers.

2. Protein Posttranslational Modifications (PTMs)

Many if not most proteins are molecularly modified after translation. Abnormal protein modification may exist as either a cause or an effect of disease; it therefore warrants exploration as a potentially rich source of disease markers. In combination with optimized sample preparation techniques, modern bioanalytical tools such as mass spectrometry are now capable of routinely characterizing and quantifying the relative abundance of most protein PTMs.  Yet caution is warranted as certain protein modifications-oxidative PTMs in particular-may arise as artifacts of less-than-optimal sample handling, potentially confounding their use as disease markers and interfering with conventional clinical laboratory tests based on binding interactions (e.g., ELISAs where protein quantification is based on interaction of the target protein with an antibody). We are interested in tracking protein modifications due to artifactual oxidation, determining how they affect conventional clinical laboratory tests, and figuring out how to prevent them from occurring.

Publications

Ferdosi, S., Rehder, D.S., Maranian, P., Castle, E.P., Ho, T.H., Pass, H.I., Cramer, D.W., Hollingsworth, M.A., Anderson, K.S., Fu, L., Cole, D.E.C., Le, T., Wu, X., Borges, C.R.: Stage Dependence, Cell-Origin Independence and Prognostic Capacity of Serum Glycan Fucosylation, β1-4 Branching, β1-6 Branching and α2-6 Sialylation in Cancer. J Proteome Res, 17: 543-558, 2018.

Deb, A., Johnson, W.A., Kline, A.P., Scott, B.J., Meador, L.R., Srinivas, D., Martin-Garcia, J.M., Dorner, K., Borges, C.R., Misra, R., Hogue, B.G., Fromme, P., Mor, T.S.: Bacterial expression, correct membrane targeting and functional folding of the HIV-1 membrane protein Vpu using a periplasmic signal peptide. PLoS One, 12:e0172529, 2017.

Ingram, T., Zuck, J., Borges, C.R., Redig, P., Sweazea, K.: Variations in native protein glycation and plasma antioxidants in several birds of prey. Comparative Biochemistry & Physiology Part B, 210: 18-28, 2017.

Hu, Y. and Borges, C.R.: A spin column-free approach to sodium hydroxide-based glycan permethylation. Analyst, 142: 2748-2759, 2017.

Jeffs, J.W., Ferdosi, S., Yassine, H.N., Borges, C.R.: Ex vivo instability of glycated albumin: A role for autoxidative glycation. Arch Biochem Biophys, 629: 36-42, 2017.

Biswas, S., Sen, S., Im, J., Biswas, S., Krstic, P., Ashcroft, B., Borges, C., Zhao, Y., Lindsay, S., Zhang, P.: Universal Readers Based on Hydrogen Bonding or π-π Stacking for Identification of DNA Nucleotides in Electron Tunnel Junctions. ACS Nano, 10: 11304-11316, 2016

Fu L, Borges CR, Rehder DS, Wong BY, Williams R, Carpenter TO, Cole DE.: Characterization of Additional Vitamin D Binding Protein Variants. J Steroid Biochem Mol Biol., 159: 54-59, 2016.

Zaare, S., Aguilar, J., Hu, Y., Ferdosi, S., Borges, C.R.: Glycan Node Analysis: A Bottom-Up Approach
to Glycomics. J Vis Exp (In Press)

Fu L, Borges CR, Rehder DS, Wong BY, Williams R, Carpenter TO, Cole DE. Characterization of Additional Vitamin D Binding Protein Variants. J Steroid Biochem Mol Biol. 2016 Feb 23. pii: S0960-0760(16)30036-X. doi: 10.1016/j.jsbmb.2016.02.022.

Borges C.R., Jeffs J.W., Kapuruge E.P.: Impact of Artifactual, Ex Vivo Oxidation on Biochemical
Research. In: Oxidative Stress: Diagnostics and Therapy Volume 2. Edited by Hepel M, Andreescu S:
American Chemical Society Books; pgs. 375-413, 2015. doi: 10.1021/bk-2015-1200.ch016 (Hardcopy In
Press)

Biswas S., Song W., Borges C.R., Lindsay S., Zhang P.: Click Addition of a DNA Thread to the N-termini
of Peptides for Their Translocation through Solid-State Nanopores. ACS Nano, 9(10): 9652-9664, 2015.

Hanavan, P.D., Borges, C.R., Katchman, B.A., Faigel, D.O., Ho, T.H., Meurice, N., Petit, J.L., Ma, C.-T.,
Sergienko, E.A., Lake, D.F. Ebselen inhibits QSOX1 enzymatic activity and suppresses invasion of pancreatic
and renal cancer cell lines. Oncotarget, 6(21): 18418-28, 2015.

Ho, T. H., Nateras, R. N., Yan, H., Park, J. G., Jensen, S., Borges, C., Lee, J. H., Champion, M. D., Tibes,
R., Bryce, A. H., Carballido, E. M., Todd, M. A., Joseph, R. W., Wong, W. W., Parker, A. S., Stanton, M. L.,
Castle, E. P. A Multidisciplinary Biospecimen Bank of Renal Cell Carcinomas Compatible with Discovery
Platforms at Mayo Clinic, Scottsdale, Arizona. PloS One 10(7):e0132831, 2015.

Rehder, D.S., Gundberg, C.M., Booth, S.L., Borges, C.R. Gamma-Carboxylation and Fragmentation of Osteocalcin in Human Serum Defined by Mass Spectrometry. Mol Cell Proteomics 14(6): 1546-1555, 2015.

Yassine, H.N., Trenchevska, O., He, H., Borges, C.R., Nedelkov, D., Mack, W., Kono, N., Koska, J., Reaven, P.D., Nelson, R.W. Serum Amyloid A Truncations in Type 2 Diabetes Mellitus. PLoS One, 10(1):e0115320, 2015.

Sherma N.D., Borges C.R., Trenchevska O., Jarvis J.W., Rehder D.S., Oran P.E., Nelson R.W., Nedelkov D.  Mass Spectrometric Immunoassay for the Qualitative and Quantitative Analysis of the Cytokine Macrophage Migration Inhibitory Factor (MIF). Proteome Science 12(1):52, 2014.

Borges C.R. and Lake D.F. Oxidative Protein Folding: Nature’s Knotty Challenge. Antioxid Redox Signal 21(3): 392-395, 2014.

Borges C.R., Rehder D.S., Jensen S., Schaab M.R., Sherma N.D., Yassine H., Nikolova B., Breburda C. Elevated Plasma Albumin and Apolipoprotein A-I Oxidation under Suboptimal Specimen Storage Conditions. Mol Cell Proteomics 13(7):1890-1899, 2014.

Zhao, Y., Ashcroft, B., Zhang, P., Liu, H., Sen, S., Song, W., Im, J., Gyarfas, B., Manna, S., Biswas, S., Borges, C., Lindsay, S. Single-molecule spectroscopy of amino acids and peptides by recognition tunneling. Nat Nanotechnol 9(6): 466-473, 2014.

Oran P.E., Trenchevska O., Nedelkov D., Borges C.R., Schaab M.R., Rehder D.S., Jarvis J.W., Sherma N.D., Shen L., Krastins B., Lopez M.F., Schwenke D.C., Reaven P.D., Nelson R.W. Parallel workflow for high-throughput (>1,000 samples/day) quantitative analysis of human insulin-like growth factor 1 using mass spectrometric immunoassay.  PLoS One, 9(3): e92801, 2014. doi: 10.1371/journal.pone.0092801.

Borges C.R., Sherma N.D. Techniques for the Analysis of Cysteine Sulfhydryls and Oxidative Protein Folding. Antioxid Redox Signal, 21(3): 511-531, 2014.

Yassine H.N., Jackson A.M., Borges C.R., Billheimer D., Koh H., Smith D., Reaven P., Lau S.S., Borchers C.H. The application of multiple reaction monitoring and multi-analyte profiling to HDL proteins. Lipids Health Dis 13(1): 8, 2014.

Yassine, H., Borges, C.R., Schaab, M.R., Billheimer, D., Stump, C., Reaven, P., Lau, S.S., Nelson, R.W. Mass Spectrometric Immunoassay and Multiple Reaction Monitoring as Targeted MS-based Quantitative Approaches in Biomarker Development: Potential Applications to Cardiovascular Disease and Diabetes. Proteomics Clin Appl, 7(7-8): 528-540, 2013.

Borges, C.R., Rehder, D.S., Boffetta, P. Multiplexed surrogate analysis of glycotransferase activity in whole biospecimens. Anal Chem, 85: 2927-2936, 2013.

Orsak, T., Smith, T.L., Eckert, D., Lindsley, J.E., Borges, C.R., Rutter, J. Revealing the Allosterome: Systematic Identification of Metabolite/Protein Interactions. Biochemistry, 51(1):225-32, 2012.

Bley, C.J., Qi, X., Rand, D.P., Borges, C.R., Nelson, R.W., Chen, J.J.L. RNA-protein binding interface in the telomerase ribonucleoprotein. PNAS, 108(51): 20333-8, 2011.

Oran, P.E., Jarvis, J.W., Borges, C.R., Sherma, N.D., Nelson, R.W. Mass Spectrometric Immunoassay of Intact Insulin and Related Variants for Population Proteomics Studies. Proteomics Clin Appl 5: 454-9, 2011.

Borges, C.R., Oran, P.E., Buddi, S., Jarvis, J.W., Schaab, M.R., Rehder, D.S., Rogers, S. P., Taylor, T. and Nelson, R.W. Building Multidimensional Biomarker Views of Type 2 Diabetes Based on Protein Microheterogeneity. Clin.Chem 57: 719-728, 2011.

Nelson, R.W., Borges, C.R. Mass spectrometric immunoassay revisited. J Am Soc Mass Spectrom 22: 960-968, 2011.

Rehder, D. S., Borges, C. R. Cysteine Sulfenic Acid as an Intermediate in Disulfide Bond Formation and Nonenzymatic Protein Folding, Biochemistry 49: 7748-7755, 2010.

Oran, P.E., Sherma, N.D., Borges, C.R., Jarvis, J.W., Nelson, R.W. Intrapersonal and Populational Heterogeneity of the Chemokine RANTES. Clin Chem 56: 1432-1441, 2010.

Rehder, D. S., Borges, C. R. Possibilities and pitfalls in quantifying the extent of cysteine sulfenic acid modification of specific proteins within complex biofluids. BMC Biochemistry 11: 25, 2010.

Lopez, M.F., Rezai, T., Sarracino, D.A., Prakash, A., Krastins, B., Athanas, M., Singh, R.J., Barnidge, D.R., Oran, P.E., Borges, C.R., Nelson, R.W.  Selected Reaction Monitoring–Mass Spectrometric Immunoassay Responsive to Parathyroid Hormone and Related Variants Clin Chem 56: 281-290, 2010.

Borges, C.R., Rehder, D.S., Jarvis, J.W., Schaab, M.S., Oran, P.E., Nelson, R.W. Full length characterization of proteins in human populations Clin Chem 56: 202-211, 2010.

Oran, P.E., Jarvis, J.W., Borges, C.R., Nelson, R.W. C-peptide Microheterogeneity in Type 2 Diabetes Populations Proteomics Clin Appl 4: 1-6, 2010.

Rehder, D. S., Nelson, R. W., Borges, C. R. Glycosylation status of vitamin D binding protein in cancer patients. Protein Sci 18: 2036-2042, 2009.

Borges, C.R., Jarvis, J.W., Oran, P.E., Rogers, S.P., Nelson, R.W.  “Population Studies of Vitamin D Binding Protein Microheterogeneity by Mass Spectrometry Lead to Characterization of its Genotype Dependent O-glycosylation Patterns” J. Proteom. Res. 7:4143-53, 2008.

Borges, C.R., Jarvis, J.W., Oran, P.E., Rogers, S.P., Nelson, R.W. “Population studies of intact Vitamin D binding protein by affinity capture ESI-TOF-MS” J Biomolecular Techniques 19(3): 167-176, 2008.

Hoggan, A.M., Shelby, M.K., Crouch, D.J., Borges, C.R., Slawson, M.H. “Detection of bumetanide in an over-the-counter dietary supplement” J. Anal. Toxicol. 31(9):601-4, 2007.

Borges C.R., “Concept for facilitating analyst-mediated interpretation of qualitative chromatographic-mass spectral data: an alternative to manual examination of extracted ion chromatograms.” Anal. Chem. 79(13):4805-13, 2007.

Borges C.R., Miller N., Shelby M., Hansen M., White C., Slawson M.H., Monti K., and Crouch D.J. “Analysis of a challenging subset of World Anti-Doping Agency-banned steroids and anti-estrogens by LC/MS/MS” J. Anal. Toxicol. 31(3):125-31, 2007.

Borges C.R., Taccogno J., Crouch D.J., Le L., Truong T.N. “Structure and Mechanism of Formation of an Important Ion in Doping Control.” Int. J. Mass Spectrom. 247: 48-54, 2005.

Borges C.R., Qi J., Wu W, Torng E., Hinck A.P., and Watson J.T. “Algorithm-Assisted Elucidation of Disulfide Structure: Application of the Negative Signature Mass Algorithm to Mass-Mapping the Disulfide Structure of the 12-Cysteine Transforming Growth Factor β Type II Receptor Extracellular Domain.” Anal Biochem. 329(1):91-103, 2004.

Rollins, D.E., Wilkins, D.G., Krueger, G.G., Augsburger, M.P., Mizuno, A., O’neal, C., Borges, C.R., Slawson, M.H.  “The Effect of Hair Color on the Incorporation of Codeine into Hair.” J. Anal. Toxicol. 27: 545-551, 2003.

Qi, J., Hang, D., Rupp, M., Borges, C.R., Wu, W., Torng E., and Watson, J.T.  “Automated Data Interpretation Based on the Concept of ‘Negative Signature Mass’ for Mass-Mapping Disulfide Structures of Cystinyl Proteins.” J. Amer. Soc. Mass Spectrom. 14(9): 1032-1038, 2003.

Borges, C.R., and Watson, J.T., “Recognition of Cysteine-Containing Peptides through Prompt Fragmentation of the 4-Dimethylaminophenylazophenyl-4’-maleimide Derivative During Analysis by MALDI-MS” Protein Sci. 12(7): 1567-72, 2003.

Borges, C.R., Kuhn, D.M., and Watson, J.T. “Mass Mapping Sites of Nitration in Tyrosine Hydroxylase: Random versus Selective Nitration of Three Tyrosine Residues” Chem. Res. Toxicol. 16(4): 536-40, 2003.

Borges, C.R., Roberts, J.C., Wilkins, D.G., and Rollins, D.E. “Cocaine, Benzoylecgonine, Amphetamine, and N-acetylamphetamine Binding to Melanin Subtypes.” J. Anal. Toxicol. 27(3): 125-34, 2003.

Wilkins, D.G., Mizuno, A., Borges, C.R., Slawson, M.H., and Rollins, D.E., “Ofloxacin as a reference marker in hair of various colors.” J. Anal. Toxicol. 27(3): 149-55, 2003.

Borges, C.R., Geddes, T., Watson, J.T., and Kuhn, D.M. “Dopamine biosynthesis is regulated by S-glutathionylation: Potential mechanism of tyrosine hydroxylase inhibition during oxidative stress.” J. Biol. Chem. 277(50): 48295-302, 2002.

Kuhn D.M., Sadidi M., Lu X., Kriepke C., Geddes T., Borges C., Watson J.T. “Peroxynitrite-induced nitration of tyrosine hydroxylase: identification of tyrosines 423, 428, and 432 as sites of modification by MALDI-TOF mass spectrometry and tyrosine-scanning mutagenesis.” J. Biol. Chem. 277(16): 14336-42, 2002.

Borges, C.R., Martin, S.D., Meyer, L.J., Wilkins, D.G., and Rollins, D.E. “Influx and Efflux of Amphetamine and N-acetylamphetamine in Keratinocytes, Pigmented Melanocytes, and Non-Pigmented Melanocytes.” J. Pharm. Sci. 91(6): 1523-35, 2002.

Borges, C.R., Wilkins, D.G., and Rollins, D.E. “Amphetamine and N-acetylamphetamine incorporation into hair: an investigation of the potential role of drug basicity in hair color bias.” J. Anal. Toxicol. 25: 221-227, 2001.

Borges, C.R., Roberts, J.C., Wilkins, D.G., and Rollins, D.E. “Relationship of melanin degradation products to actual melanin content: Application to human hair.” Anal. Biochem. 290: 116-125, 2001.

Denkinger, D.J., Borges, C.R., Butler, C.L., Cushman, A.M., and Kawahara, R.S. "Genomic organization and regulation of the vav proto-oncogene." Biochim. Biophys. Acta 1491: 253-262, 2000.

Hold, K.M., Borges, C.R., Wilkins, D.G., Rollins, D.E., and Joseph, R.E. Jr. "Detection of nandrolone, testosterone and their esters in rat and human hair samples." J. Anal. Toxicol. 23: 416-423, 1999

Research Activity

Courses

Spring 2018
Course NumberCourse Title
CHM 328Instrumental Analysis Lab
CHE 492Honors Directed Study
MBB 495Undergraduate Research
Fall 2017
Course NumberCourse Title
MBB 495Undergraduate Research
CHE 498Pro-Seminar
Spring 2017
Course NumberCourse Title
CHM 494Special Topics
CHM 598Special Topics
Fall 2016
Course NumberCourse Title
CHM 325Analytical Chemistry
Spring 2016
Course NumberCourse Title
CHM 327Instrumental Analysis
Fall 2015
Course NumberCourse Title
CHM 326Advanced Analytical Chem Lab
Spring 2015
Course NumberCourse Title
CHM 494Special Topics
CHM 598Special Topics
Fall 2014
Course NumberCourse Title
CHM 325Analytical Chemistry
CHM 501Current Topics in Chemistry
Fall 2013
Course NumberCourse Title
CHM 326Advanced Analytical Chem Lab