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Durham University

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Staff Profile

Prof Roy Andrew Quinlan, BSc hons; PhD

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Professor in the Department of Biosciences
Telephone: +44 (0) 191 33 41331
Fax: +44 191 334 1201

Contact Prof Roy Andrew Quinlan (email at


This image shows an epithelial cell that has been stained with antibodies  to the small heat shock protein, HSP27.

Professor Roy Quinlan joined the University of Durham in 2001 and was one of those responsible for founding the Biophysical Sciences Institute, which was then established in 2007. He is a Biochemistry graduate and PhD from the University of Kent where he worked on microtubules with Professor Keith Gull FRS, before taking up an Alexander von Humboldt fellowship at the German Cancer Research Centre to work on Intermediate Filaments with Professor Werner Franke in 1981. He joined Dr Murray Stewart at the LMB Cambridge determining the coiled coil pitch of myosin LS2, but continued to investigate structural aspects of GFAP and lamins. In 1988, he was appointed as a lecturer to the Department of Biochemistry in Dundee. Here his interest in the cytoskeleton and particularly intermediate filaments in astrocytes, cardiomyocytes and the lens led to the discovery of the functionally important interaction of the small heat shock protein chaperones with intermediate filaments and its role in mediating the biomechanical properties of cells. In the lens, these proteins are key to its function as an optical element the eye. The strong correlation between structure and function in this tissue provides the platform for current research interests to model lens cell organization in 3 and 4 dimensions and integrating the cytoskeletal and chaperone functions into a scaled model of this tissue.

The eye lens is a tissue in which its cell structure and cell organisation is intimately linked to function. The lens epithelium is a single layer of cells covering the anterior portion of the lens and underlying the anterior lens capsule. It is the cells of the lens epithelium that cause complications after cataract surgery and it is also those that are damaged by ionising radiation and this damage then manifests itself as lens opacities and eventually cataract. The lens epithelial cells form the lens fibre cells by cell differentiation. This is restricted to those epithelial cells at the very equator of the lens. The lens grows, albeit slowly, throughout life. To ensure that there is a continual supply of lens epithelial cells to differentiate into fibre cells, a cell proliferation zone is adjacent to the lens equator. The geometrical order of the lens originates in the epithelium and is manifested in fibre cell differentiation. The differentiating lens fibre cells undergo massive (~1000X) elongation so that eventually the ends of these cells from opposing lens quadrants touch to form the lens sutures. This exemplifies the precise arrangement of the lens fibre cells required to produce a functional lens that is capable of refracting focused images onto the retina. The epithelial cells outside of the equatorial and proliferative zones have the potential to proliferate, but they appear quiescent. This is called the central zone. The epithelial cells retain the potential for proliferation. We are investigating how ionising radiation causes lens opacities and cataract. We predict that it is damage to the cells in the lens epithelium and disturbance to their patterns of cell proliferation and differentiation, but important questions remain. For instance: Are some cells more sensitive than others to (low dose) ionising radiation? Is there a threshold dose? How does radiation damage to the lens epithelium cause the posterior subcapsular cataract that is so typical of radiation damage to the lens? 

The mouse is an excellent animal model because of the wealth of genetic and molecular tools to dissect out the mechanistic detail of low dose radiation effects. The lens is very accessible and easy to dissect. My laboratory has developed both mounting techniques and lens explant culturing techniques that has allowed us to link cell position in the epithelium to metric data (length, cross-sectional area; proliferation and apoptotic status). We can therefore detect the earliest signs of ionising radiation damage to the lens epithelium through changes in cell proliferation, cell death or cell metrics. Real time imaging of the developing eye lens would also be helpful to populate our knowledge base in terms of cell positioning, division planes and other organelle dynamics within the developing lens, but this is more easily achieved using zebrafish. With colleagues (Professor John Girkin, Dr Robert Pal, Dr Boguslaw Obara, Dr Junjie Wu) in Durham University Biophysical Sciences Institute, we are using multidisciplinary approaches to reach this goal so that in future, mouse and zebrafish systems can complement each other. This has led also to important research collaborations with Dr Kislon Voitchovsky and Dr Margarita Staykova (Physics), Dr John Sanderson and Dr Jackie Mosely (Chemistry) on lens membranes, their lipids and associated proteins, so that we connect our studies on the mechanistic details of lens function and cataractogenesis with our modelling of the lens.

We are currently investigating Electronic Lab Notebooks to standardise protocols, communicate results with collaborators and favour SciNote for ease of use and accessibility (

Research Groups

Department of Biosciences

  • Animal Cells and Systems
  • Durham Centre for Bioimaging Technology

Research Interests

  • Animal cell biology
  • Aquaporin 0 structure and function
  • Cataract and amyloidosis
  • Inherited human diseases caused by mutant cytoskeletal proteins, particularly cataract, cardiomyopathy and neuropathies
  • Membrane domains and their association with protein chaperones and intermediate filaments
  • Motor neurone disease
  • Protein chaperones
  • The cytoskeleton
  • The eye lens and the ageing process

Teaching Areas

  • Contributor to the module Age and Age Related Diseases

  • Module organiser for Advanced Cell Biology

Selected Publications

Chapter in book

  • Perng, M.D., Huang, Y.S. & Quinlan R.A. (2016). Purification of Protein Chaperones and Their Functional Assays with Intermediate Filaments. In Intermediate Filament Associated Proteins. Sonnenberg, A. & Wilson, K. Elsevier. 569: 155-175.

Journal Article

  • Tapodi, Antal, Clemens, Daniel, Uwineza, Alice, Goldberg, Martin, Thinon, Emmanuelle, Heal, William, Tate, Edward, Nemeth-Cahalan, Karinne, Vorontsova, Irene, Jarrin, Miguel, Hall, James & Quinlan, Roy (2019). BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability. Experimental Eye Research 185: 107585.
  • Uwineza, Alice, Kalligeraki, Alexia A., Hamada, Nobuyuki, Jarrin, Miguel & Quinlan, Roy A. (2019). Cataractogenic load – a concept to study the contribution of ionizing radiation to accelerated aging in the eye lens. Mutation Research/Reviews in Mutation Research 779: 68-81.
  • Barnard, SGR , McCarron, R, Moquet, J, Quinlan, RA & Ainsbury, E (2019). Inverse dose-rate effect of ionising radiation on residual 53BP1 foci in the eye lens. Scientific Reports 9: 10418.
  • Gorter, Rianne P., Nutma, Erik, Jahreiβ, Marie-Christina, de Jonge, Jenny C., Quinlan, Roy, van der Valk, Paul, van Noort, Johannes M., Baron, Wia & Amor, Sandra (2018). Heat shock proteins are differentially expressed in brain and spinal cord: implications for multiple sclerosis. Clinical & Experimental Immunology 194(2): 137-152.
  • Young, L.K., Jarrin, M., Saunter, C.D., Quinlan, R.A. & Girkin, J.M. (2018). Non-invasive in vivo quantification of the developing optical properties and graded index of the embryonic eye lens using SPIM. Biomedical Optics Express 9(5): 2176-2188.
  • Sharma, S., Conover, G., Elliott, J.E., Perng, M.D., Herrmann, H. & Quinlan, R.A. (2017). αB-crystallin is a sensor for assembly intermediates and for the subunit topology of desmin intermediate filaments. Cell Stress and Chaperones 22(4): 613-626.
  • Quinlan, R.A., Schwartz, N., Windoffer, R., Richardson, C., Hawkins, T., Broussard, J.A., Green, K.J. & Leube, R. (2017). A Rim and Spoke Hypothesis to explain the biomechanics roles for intermediate filament networks. Journal of Cell Science 130(20): 3437-3445.
  • Ricci, M., Quinlan, R. A. & Voïtchovsky, K. (2017). Sub-nanometre mapping of the aquaporin-water interface with multifrequency atomic force microscopy. Soft Matter 13(1): 187-195.
  • Carver, J.A., Grosas, A.B., Ecroyd, H. & Quinlan, R.A. (2017). The functional roles of the unstructured N- and C-terminal regions in alphaB-crystallin and other mammalian small heat-shock proteins. Cell Stress and Protein Chaperones 22(4): 627-638.
  • Forssell-Aronsson, E. & Quinlan, R.A. (2017). The impact of circadian rhythms on medical imaging and radiotherapy regimes for the paediatric patient. Radiation Protection Dosimetry 173(1-3): 16-20.
  • Barnard, S., Ainsbury, E.A., Quinlan, R.A. & Buffler, S. (2016). Radiation protection of the eye lens in medical workers—basis and impact of the ICRP recommendations. The British Journal of Radiology 89(1060): 20151034.
  • Barnes, S. & Quinlan, R.A. (2016). Small molecules, both dietary and endogenous, influence the onset of lens cataracts. Experimental Eye Research 156: 87-94.
  • Ismail, Vian S., Mosely, Jackie A., Tapodi, Antal Quinlan, Roy A. & Sanderson, John M. (2016). The Lipidation Profile of Aquaporin-0 Correlates with The Acyl Composition of Phosphoethanolamine Lipids in Lens Membranes. Biochimica et Biophysica Acta (BBA) - Biomembranes 1858(11): 2763-2768.
  • Wu, J.J., Wu, W., Tholozan, F.M., Saunter, C.D., Girkin, J.M. & Quinlan, R.A. (2015). A dimensionless ordered pull-through model of the mammalian lens epithelium evidences scaling across species and explains the age-dependent changes in cell density in the human lens. Journal of The Royal Society Interface 12(108): 20150391.
  • Quinlan, R.A. (2015). A new dawn for cataracts. Science 350(6261): 636-637.
  • Quinlan, R.A., Bromley, E.H. & Pohl, E. (2015). A silk purse from a sow’s ear – bioinspired materials based on α-helical coiled coils. Current opinion in cell biology 32: 131-137.
  • Markiewicz, Ewa, Barnard, Stephen, Haines, Jackie, Coster, Margaret, Geel, Orry van, Wu, Weiju, Richards, Shane, Ainsbury, Elizabeth, Rothkamm, Kai, Bouffler, Simon & Quinlan, Roy A. (2015). Nonlinear ionizing radiation-induced changes in eye lens cell proliferation, cyclin D1 expression and lens shape. Open biology 5: 150011.
  • Bouffler, S., Peters, S., Gilvin, P., Slack, K., Markiewicz, E.M., Quinlan, R.A., Gillan, J., Coster, M., Barnard, S., Rothkamm, K. & Ainsbury, E. (2015). The lens of the eye: exposures in the UK medical sector and mechanistic studies of radiation effects. Annals of the ICRP 44(1 Suppl): 84-90.
  • Wu, W., Tholozan, F.M., Goldberg, M.W., Bowen, L., Wu, J.J. & Quinlan, R.A (2014). A gradient of matrix-bound FGF-2 and perlecan is available to lens epithelial cells. Experimental Eye Research 120: 10-14.
  • Chen, M.H., Hagemann, T.L., Quinlan, R.A., Messing, A. & Perng, M.-D. (2013). Caspase cleavage of GFAP produces an assembly-compromised proteolytic fragment that promotes filament aggregation. ASN Neuro 5(5): 293-308.
  • Quinlan, R.A., Zhang, Y., Lansbury, A., Williamson, I., Pohl, E. & Sun, F. (2013). Changes in the quaternary structure and function of MjHSP16.5 attributable to deletion of the I–X–I motif and introduction of the substitution, R107G in the a-crystallin domain. Philosophical Transactions of the Royal Society B: Biological Sciences 368(1617): 20120327.
  • Quinlan, R.A. & Ellis, R.J. (2013). Chaperones: needed for both the good times and the bad times. Philosophical Transactions of the Royal Society B: Biological Sciences 368(1617): 20130091.
  • Elliott, J.L., Der Perng, M., Prescott, A.R., Jansen, K.A., Koenderink, G.H. & Quinlan, R.A. (2013). The specificity of the interaction between αB-crystallin and desmin filaments and its impact on filament aggregation and cell viability. Philosophical Transactions of the Royal Society B: Biological Sciences 368(1617): 20120375.
  • Qu, Bo, Landsbury, Andrew, Schoenthaler, Helia Berrit, Dahm, Ralf, Liu, Yizhi, Clark, John I., Prescott, Alan R. & Quinlan, Roy A. (2012). Evolution of the vertebrate beaded filament protein, Bfsp2; comparing the in vitro assembly properties of a “tailed” zebrafish Bfsp2 to its “tailless” human orthologue. Experimental Eye Research 94(1): 192-202.
  • Chen, Yi-Song, Lim, Suh-Ciuan, Chen, Mei-Hsuan, Quinlan, Roy A. & Perng, Ming-Der (2011). Alexander disease causing mutations in the C-terminal domain of GFAP are deleterious both to assembly and network formation with the potential to both activate caspase 3 and decrease cell viability. EXPERIMENTAL CELL RESEARCH 317(16): 2252-2266.
  • Dahm, Ralf, van Marle, Jan, Quinlan, Roy A., Prescott, Alan R. & Vrensen, Gijs F. J. M. (2011). Homeostasis in the vertebrate lens: mechanisms of solute exchange. Philosophical Transactions of the Royal Society B: Biological Sciences 366(1568): 1265-1277.
  • Houck, Scott A., Landsbury, Andrew, Clark, John I. & Quinlan, Roy A. (2011). Multiple Sites in alpha B-Crystallin Modulate Its Interactions with Desmin Filaments Assembled In Vitro. PLOS ONE 6(11): e25859.
  • Tang, G., Perng, M.D., Wilk, S., Quinlan, R. & Goldman, J.E. (2010). Oligomers of mutant glial fibrillary acidic protein (GFAP) Inhibit the proteasome system in alexander disease astrocytes, and the small heat shock protein αB-crystallin reverses the inhibition. Journal of Biological Chemistry 285(14): 10527-10537.
  • Sugiyama, Yuki, Akimoto, Kazunori, Robinson, Michael L., Ohno, Shigeo & Quinlan, Roy A. (2009). A cell polarity protein aPKCλ is required for eye lens formation and growth. Developmental Biology 336(2): 246-256.
  • Quinlan, P. R., Sreseli, R., Quinlan, R. A., Hadad, S., Bray, S. E., Kernohan, N., Kellock, D., Baker, L., Purdie, C., Jordan, L. & Thompson, A. M. (2009). alpha B-crystallin, vimentin and increased p53 expression levels in breast cancer is associated with poor prognosis. Cancer Research 69(2 Suppl): 321S-322S.
  • Sreseli, R., Quinlan, P. R., Quinlan, R. A., Hadad, S., Bray, S., Kellock, D., Baker, L., Purdie, C., Jordan, L. & Thompson, A. M. (2009). ASSOCIATION OF AB-CRYSTALLIN, VIMENTIN WITH POOR PROGNOSIS IN PRIMARY BREAST CANCER. ANNALS OF ONCOLOGY 20: 53.
  • Song, Shuhua, Landsbury, Andrew, Dahm, Ralf, Liu, Yizhi, Zhang, Qingjiong & Quinlan, Roy A. (2009). Functions of the intermediate filament cytoskeleton in the eye lens. JOURNAL OF CLINICAL INVESTIGATION 119(7): 1837-1848.
  • Middeldorp, Jinte, Kamphuis, Willem, Sluijs, Jacqueline A., Achoui, Dalila, Leenaars, Cathalijn H. C., Feenstra, Matthijs G. P., van Tijn, Paula, Fischer, David F., Berkers, Celia, Ovaa, Huib, Quinlan, Roy A. & Hol, Elly M. (2009). Intermediate filament transcription in astrocytes is repressed by proteasome inhibition. FASEB JOURNAL 23(8): 2710-2726.
  • Gorog, Diana A., Jabr, Rita I., Tanno, Masaya, Sarafraz, Negin, Clark, James E., Fisher, Simon G., Cao, Xou Bin, Bellahcene, Mohamed, Dighe, Kushal, Kabir, Alamgir M. N., Quinlan, Roy A., Kato, Kanefusa, Gaestel, Matthias, Marber, Michael S. & Heads, Richard J. (2009). MAPKAPK-2 modulates p38-MAPK localization and small heat shock protein phosphorylation but does not mediate the injury associated with p38-MAPK activation during myocardial ischemia. CELL STRESS \& CHAPERONES 14(5): 477-489.
  • Sreseli, R., Quinlan, P. R., Quinlan, R. A., Bray, S. E., Kellok, D. B., Baker, L., Jordan, L., Purdie, C. & Thompson, A. M. (2009). NF-kB Complex Activation and Association of alpha B-Crystallin and Vimentin with Poor Prognosis in Primary Breast Cancer. CANCER RESEARCH 69(24): 2143.
  • Saunter, Christopher D., Perng, Ming Der, Love, Gordon D. & Quinlan, Roy A. (2009). Stochastically determined directed movement explains the dominant small-scale mitochondrial movements within non- neuronal tissue culture cells. FEBS LETTERS 583(8): 1267-1273.
  • Sugiyama, Yuki, Prescott, Alan R., Tholozan, Frederique M. D., Ohno, Shigeo & Quinlan, Roy A. (2008). Expression and localisation of apical junctional complex proteins in lens epithelial cells. Experimental Eye Research 87(1): 64-70.
  • Perng, Ming-Der, Wen, Shu-Fang, Gibbon, Terry, Middeldorp, Jinte, Sluijs, Jacqueline, Hol, Elly M. & Quinlan, Roy A. (2008). Glial Fibrillary Acidic Protein Filaments Can Tolerate the Incorporation of Assembly-compromised GFAP-delta, but with Consequences for Filament Organization and alpha B-Crystallin Association. Molecular Biology of the Cell 19(10): 4521-4533.
  • Hayes, Victoria H., Devlin, Glyn & Quinlan, Roy A. (2008). Truncation of αB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells. Journal of Biological Chemistry 283(16): 10500-10512.
  • Perng, M.D., Su, M. Wen, S.F., , Li, R., Gibbon, T., , Prescott, A.R., Brenner, M. & Quinlan, R.A. (2006). The Alexander disease-causing Glial Fibrillary Acidic Protein mutant, R416W, accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of alphaB-crystallin and HSP27. American Journal of Human Genetics 79(2): 197-213.
  • Perng, MD, Wen, SF, van den Ijssel, P, Prescott, AR & Quinlan, RA (2004). Desmin aggregate formation by R120G alpha B-crystallin is caused by altered filament interactions and is dependent upon network status in cells. Molecular Biology Of The Cell 15(5): 2335-2346.
  • Sandilands, A, Hutcheson, AM, Long, HA, Prescott, AR, Vrensen, G, Löster, J, Klopp, N, Lutz, RB, Graw, J, Masaki, S, Dobson, CM, MacPhee, CE & Quinlan, RA (2002). Altered aggregation properties of mutant gamma-crystallins cause inherited cataract. EMBO Journal 21(22): 6005-6014.
  • Der Perng, M., Muchowski, P.J., van den IJssel, P., Wu, G.J.S., Hutcheson, A.M., Clark, J.I. & Quinlan, R.A. (1999). The cardiomyopathy and lens cataract mutation in αB-crystallin alters its protein structure, chaperone activity, and interaction withintermediate filaments in vitro. Journal of Biological Chemistry 274(47): 33235-33243.
  • Eyers, PA, van den Ijssel, P, Quinlan, RA, Goedert, M & Cohen, P (1999). Use of a drug-resistant mutant of stress-activated protein kinase2a/p38 to validate the in vivo specificity of SE 203580. Febs Letters 451(2): 191-196.

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