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Martyn Sharpe, PhD

Associate Research Professor of Neurosurgery, Institute for Academic Medicine
Associate Research Member, Research Institute
Houston Methodist


masharpe@houstonmethodist.org
Biography

Martyn A. Sharpe is a classically trained biochemist and bioenergeticist with a strong background in chemistry and the reactions of both reactive oxygen and nitrogen species. He has had more than a decade’s worth of experience in examining the cell proliferation/death mechanisms, and has examined the growth and characteristics of many different cell types including astrocytes, neurons and neuronal/astrocyte co-cultures.

Dr. Sharpe enjoys a large number of collaborations/friendships with scientists worldwide and has published papers with 85 co-authors over the last 15 years. He is often asked to participate in projects where there is an overlap of chemistry/cell physiology; especially in the areas of reactive oxygen/nitrogen species.

Dr. Sharpe switched from classical biochemistry/bioenergetics into related pathologies, especially of the brain, a decade ago following the death of his uncle from glioblastoma multiforme, soon after diagnosis. He has used the knowledge he acquired to develop drugs and drug delivery systems to target gliomas.
In addition to nanosyringes Sharpe & Baskin have been developing prodrugs to target gliomas that are based on their maturation by monoamine oxidase B (MAOB).

Martyn is deeply committed to neuro-oncology and is determined to develop a therapy to treat the 220,000 people, worldwide, who develop gliomas each year.

Description of Research

Dr Sharpe main areas of research have been the following:
-Design, synthesis and testing in vitro and in vivo MAOB activated pro-drugs and retention dyes for the treatment of glioma.
-Development of targeted nanosyringes for chemotherapy
-Examination of the sensitivity of human brain cells, astrocytes and neuron’s, toward organomercury
-Development of assays for identifying specific lesions in DNA

Areas Of Expertise

Drug design Nanotechnology
Publications

Monoamine oxidase B levels are highly expressed in human gliomas and are correlated with the expression of HiF-1a and with transcription factors Sp1 and Sp3
Sharpe, MA & Baskin, DS 2016, Oncotarget, vol 7, no. 3, pp. 3379-3393.

Successful Treatment of Intracranial Glioblastoma Xenografts With a Monoamine Oxidase B-Activated Pro-Drug
Sharpe, MA, Livingston, AD, Gist, TL, Ghosh, P, Han, J & Baskin, DS 2015, EBioMedicine, vol 2, no. 9, pp. 1122-1132. DOI:

Design and synthesis of a MAO-B-selectively activated prodrug based on MPTP: a mitochondria-targeting chemotherapeutic agent for treatment of human malignant gliomas
Sharpe, MA, Han, J, Baskin, AM & Baskin, DS 2015, ChemMedChem, vol 10, no. 4, pp. 621-628. DOI:

Monoamine oxidase B levels are highly expressed in human gliomas and are correlated with the expression of HiF-1a and with transcription factors Sp1 and Sp3
Sharpe, MA & Baskin, DS 2016, Oncotarget, vol 7, no. 3, pp. 3379-3393. DOI:

Regulation of the pentose phosphate pathway by an androgen receptor-mTOR-mediated mechanism and its role in prostate cancer cell growth
Tsouko, E, Khan, AS, White, MA, Han, JJ, Shi, Y, Merchant, FA, Sharpe, MA, Xin, L & Frigo, DE 2014, Oncogenesis, vol 3, no. 5, e103. DOI:

Alterations in sensitivity to estrogen, dihydrotestosterone, and xenogens in b-lymphocytes from children with autism spectrum disorder and Their Unaffected Twins/Siblings
Sharpe, MA, Gist, TL & Baskin, DS 2013, Journal of Toxicology, vol 2013, 159810. DOI:

B-lymphocytes from a population of children with autism spectrum disorder and their unaffected siblings exhibit hypersensitivity to thimerosal
Sharpe, MA, Gist, TL & Baskin, DS 2013, Journal of Toxicology, vol 2013, 801517. DOI:

Thimerosal-derived ethylmercury is a mitochondrial toxin in human astrocytes: Possible role of fenton chemistry in the oxidation and breakage of mtDNA
Sharpe, MA, Livingston, AD & Baskin, DS 2012, Journal of Toxicology, vol 2012, 373678. DOI:

Antibody-targeted nanovectors for the treatment of brain cancers
Sharpe, MA, Marcano, DC, Berlin, JM, Widmayer, MA, Baskin, DS & Tour, JM 2012, ACS Nano, vol 6, no. 4, pp. 3114-3120. DOI:

Quantification and calibration of images in fluorescence microscopy
Baskin, DS, Widmayer, MA & Sharpe, MA 2010, Analytical Biochemistry, vol 404, no. 2, pp. 118-126. DOI:

Quantification of DNase type I ends, DNase type II ends, and modified bases using fluorescently labeled ddUTP, terminal deoxynucleotidyl transferase, and formamidopyrimidine-DNA glycosylase
Baskin, DS, Widmayer, MA & Sharpe, MA 2010, BioTechniques, vol 49, no. 1, pp. 505-512. DOI:

Lipotoxicity in renal proximal tubular cells: Relationship between endoplasmic reticulum stress and oxidative stress pathways
Katsoulieris, E, Mabley, JG, Samai, M, Sharpe, MA, Green, IC & Chatterjee, PK 2010, Free Radical Biology and Medicine, vol 48, no. 12, pp. 1654-1662. DOI:

Steady state redox levels in cytochrome oxidase: Relevance for in vivo near infrared spectroscopy (NIRS)
Cooper, CE, Sharpe, MA, Mason, MG & Nicholls, P 2009, . in Advances in Experimental Medicine and Biology. vol. 645, Advances in Experimental Medicine and Biology, vol. 645, pp. 123-128. DOI:

EPR evidence of cyanide binding to the Mn(Mg) center of cytochrome c oxidase: Support for Cu a-Mg involvement in proton pumping
Sharpe, MA, Krzyaniak, MD, Xu, S, McCracken, J & Ferguson-Miller, S 2009, Biochemistry, vol 48, no. 2, pp. 328-335. DOI:

Proton-dependent electron transfer from CuA to heme a and altered EPR spectra in mutants close to heme a of cytochrome oxidase
Mills, DA, Xu, S, Geren, L, Hiser, C, Qin, L, Sharpe, MA, McCracken, J, Durham, B, Millett, F & Ferguson-Miller, S 2008, Biochemistry, vol 47, no. 44, pp. 11499-11509. DOI:

A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases
Sharpe, MA & Ferguson-Miller, S 2008, Journal of Bioenergetics and Biomembranes, vol 40, no. 5, pp. 541-549. DOI:

Comparison of the effects of the superoxide dismutase mimetics EUK-134 and tempol on paraquat-induced nephrotoxicity
Samai, M, Sharpe, MA, Gard, PR & Chatterjee, PK 2007, Free Radical Biology and Medicine, vol 43, no. 4, pp. 528-534. DOI:

Conserved lipid-binding sites in membrane proteins: a focus on cytochrome c oxidase
Qin, L, Sharpe, MA, Garavito, RM & Ferguson-Miller, S 2007, Current Opinion in Structural Biology, vol 17, no. 4, pp. 444-450. DOI:

Storage of an excess proton in the hydrogen-bonded network of the D-pathway of cytochrome c oxidase: Identification of a protonated water cluster
Xu, J, Sharpe, MA, Qin, L, Ferguson-Miller, S & Voth, GA 2007, Journal of the American Chemical Society, vol 129, no. 10, pp. 2910-2913. DOI:

Fibrillar beta-amyloid peptide Aß1-40 activates microglial proliferation via stimulating TNF-a release and H2O2 derived from NADPH oxidase: A cell culture study
Jekabsone, A, Mander, PK, Tickler, A, Sharpe, M & Brown, GC 2006, Journal of Neuroinflammation, vol 3, 24. DOI: