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Dr Adam Benham, BA (Oxon), PhD

Contact Dr Adam Benham (email at adam.benham@durham.ac.uk)

Media Contacts

Available for media contact about:

• Medical and health research topics: I am in interested in how proteins get made properly. Examples include proteins necessary for fertility (sperm binding to the egg) and proteins that are important in autoimmune/inflammatory disease (such as rheumatoid arthritis).
• Biological and Biomedical Sciences: I am in interested in how proteins get made properly. Examples include proteins necessary for fertility (sperm binding to the egg) and proteins that are important in autoimmune/inflammatory disease (such as rheumatoid arthritis).
• Bioactive chemistry: I am in interested in how proteins get made properly. Examples include proteins necessary for fertility (sperm binding to the egg) and proteins that are important in autoimmune/inflammatory disease (such as rheumatoid arthritis).
• Stem cells and regenerative medicine: I am in interested in how proteins get made properly. Examples include proteins necessary for fertility (sperm binding to the egg) and proteins that are important in autoimmune/inflammatory disease (such as rheumatoid arthritis).

Biography

I graduated from St. Catherine's College, Oxford, with first class honours in Biochemistry and obtained my PhD in transplantation immunology with Prof. John Fabre at the Institute of Child Health, University College, London. I received an EU postdoctoral fellowship to study the biochemistry of antigen presentation with Prof. Jacques Neefjes at the Netherlands Cancer Institute in Amsterdam and then joined Prof. Ineke Braakman's laboratory at Utrecht University, Netherlands, to research mechanisms of protein quality control in the endoplasmic reticulum.

Since establishing my laboratory at Durham University, I have been interested in both the quality control of proteins involved in antigen presentation and in the machinery that controls oxidative protein folding. My laboratory is particularly interested in how these fundamentally important biological pathways relate to human and animal health. For example, our work on a novel member of the Protein Disulfide Isomerase family called PDILT has shown that this protein is required for sperm:egg binding (in collaboration with Prof. Masaru Okabe and Prof. Masahito Ikawa, Osaka University, Japan). This may lead to the development of new tests and cures for unexplained male infertility. Our work on MHC class I and class II molecules seeks to explain how oxidative protein folding and ER chaperones contribute to the rheumatic disease ankylosing spondylitis, and to susceptibility to rheumatoid arthritis and other autoimmune conditions. Recent studies in my laboratory have also shown that there may be a link between the oxidative protein folding machinery and gastrointestinal disease (in collaboration with clinical colleagues at James Cook University Hospital, Middlesbrough). A selection of our peer-reviewed research publications can be found below.

Along with my research commitments, I am academic co-ordinator for Level 3 undergraduate teaching, I am the module co-ordinator for undergraduate Level 2 Immunology and I am a Departmental International co-ordinator for the Science Faculty. I am on the editorial board of the journal "Antioxidants and Redox Signaling" and I serve on the committee for the Society for Experimental Biology (Cell section).

Research Interests

• Oxidative folding of proteins in the Endoplasmic Reticulum

Publications

• 1: Battle, D.M., Dias-Gunasekara, S., Watson, G.R. , Mohamed Ahmed, E., Saysell, C.G., Altaf, N., Munipalle, P., Sanusi, A., Scoones, D., Walker, J., Viswanath, Y. & Benham, A.M. (2013). Expression of the Endoplasmic Reticulum Oxidoreductase Ero1α in gastro-intestinal cancer reveals a link between homocysteine and oxidative protein folding. Antioxidants and Redox Signaling in press.
• 2: Benham, A.M., van Lith, M., Sitia, R. & Braakman, I. (2013). Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum. Philosophical Transactions of the Royal Society B: Biological Sciences 368(1617): 20110403.
• 3: Tokuhiro, K., Ikawa, M., Benham, AM. & Okabe, M. (2012). Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility. Proceedings of the National Academy of Sciences of the United States of America 109(10): 3850-3855.
• 4: Benham, A.M (2012). Protein secretion and the endoplasmic reticulum. In Protein Synthesis and Translational Control. Hershey, JWB, Sonenberg, N & Mathews, MB Cold Spring Harbor Press. 4: 147-162.
• 5: Benham, AM (2012). The protein disulfide isomerase family: key players in health and disease. Antioxidants & Redox Signaling 16(8): 781.
• 6: Ikawa, M., Tokuhiro, K., Yamaguchi, R., Benham, AM., Tamura, T., Wada, I., Satouh, Y., Inoue, N. & Okabe, M. (2011). Calsperin is a testis-specific chaperone required for sperm fertility. Journal of Biological Chemistry 286(7): 5639-5646.
• 7: van Lith, M., McEwen-Smith, RM. & Benham, AM. (2010). HLA-DP, HLA-DQ and HLA-DR have different requirements for invariant chain and HLA-DM. Journal of Biological Chemistry 285(52): 40800-40808.
• 8: Ikawa, M., Inoue, N., Benham, AM. & Okabe, M. (2010). Fertilization: a sperm's journey to and interaction with the oocyte. Journal Clinical Investigation 120(4): 984-994.
• 9: Benham, AM. (2009). Protein folding and disulfide bond formation in the eukaryotic cell. FEBS Journal 276(23): 6905-11.
• 10: van Lith, M., Karala, A., Bown, D., Gatehouse, J., Ruddock, L., Saunders, P & Benham, AM. (2007). A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells. Molecular Biology of the Cell 18(8): 2795-2804.
• 11: Lemin, A., Saleki, K., van Lith, M. & Benham, AM. (2007). Activation of the unfolded protein response and alternative splicing of ATF6α in HLA-B27 positive lymphocytes. FEBS Letters 581: 1819-1824.
• 12: van Lith, M. & Benham, AM. (2006). The DMalpha and DMbeta chain co-operate in the oxidation and folding of HLA-DM. Journal of Immunology 177(8): 5430-5439.
• 13: Dias-Gunasekara, S., van Lith, M., Williams, JAG., Kataky, R. & Benham, AM. (2006). Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1b. Journal of Biological Chemistry 281(35): 25018-25025.
• 14: Saleki, K, Hartigan, N, van Lith, M, Bulleid, N & Benham, AM (2006). Differential oxidation of HLA-B2704 and HLA-B2705 in lymphoblastoid and transfected adherent cell lines. Antioxidants and Redox Signaling 8: 292-299.
• 15: van Lith M, Hartigan N, Hatch J & Benham AM (2005). PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum. Journal of Biological Chemistry 280(2): 1376-1383.
• 16: Dias-Gunasekara S, Gubbens J, van Lith M, Dunne C, Williams JA, Kataky R, Scoones D, Lapthorn A, Bulleid NJ & Benham AM (2005). Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Erolb. Journal of Biological Chemistry 280(38): 33066-33075.
• 17: Dixon DP, van Lith M, Edwards R & Benham AM (2003). Cloning and initial characterization of the Arabidopsis thaliana Endoplasmic Reticulum Oxidoreductins. Antioxidants and Redox Signaling 4: 389-396.
• 18: Mezghrani A, Fassio A, Benham AM, Simmen T, Braakman I & Sitia R (2001). Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J 20: 6288-6296.
• 19: Benham AM, Cabibbo A, Fassio A, Bulleid N, Sitia R & Braakman I (2000). The CXXCXXC motif determines the folding, structure and stability of human Ero1-La. EMBO J 19: 4493-4502.