Dr John Parrington
MRC Senior Non-Clinical Fellow
Fellow and Tutor in Physiological Sciences
Fellow and College Lecturer at Worcester
Molecular basis of egg activation. Role of phospholipase C enzymes in sperm. Calcium signalling and early embryogenesis. In vivo gene transfer into the testis and sperm. Identification and characterisation of the NAADP receptor. Molecular components of calcium signalling in sea urchin gametes
Dr John Parrington
Dr Parrington was educated at Downing College, Cambridge and received a BA in Natural Sciences (Zoology) in 1986. He obtained his PhD in 1992 from the Imperial Cancer Research Fund and London University, having worked on the molecular mechanisms underlying the interferon signalling pathway in Ian Kerr's laboratory. Dr Parrington moved to the MRC National Institute for Medical Research where he begun studying the molecular events underlying fertilization, a theme which he continued at University College London as an MRC Career Development Fellow. He currently holds an MRC Senior Non-Clinical Fellowship. Dr Parrington was elected to a joint Tutorial Fellowship and College Lectureship at Worcester and Exeter Colleges, respectively, in 2002 and will take up a University Lectureship in Pharmacology in 2006.
Since joining the Department, Dr Parrington's principal research interest has been in studying how calcium signalling governs key physiological events. He has been centrally involved in demonstrating that the physiological agent of egg activation in mammals appears to be a novel, sperm-derived phospholipase C with distinctive properties - PLCzeta. Recently he has identified an avian orthologue of PLCzeta, which suggests that this signalling protein may play a universal role in vertebrate egg activation. Dr Parrington is also studying how signalling molecules of the phosphoinositide pathway are involved in gametogenesis and development of the early embryo. He is currently involved in identifying and characterising the NAADP receptor and other components of the cADPR and NAADP signalling pathways at the molecular level. A strong theme of Dr Parrington’s research is in using biochemical and molecular strategies within a multidisciplinary approach. Most recently, his group have been developing a way to express recombinant proteins in the sperm using in vivo gene transfer, which could provide a novel way to study testis and sperm function.
Dr Parrington is General Secretary of the Society for Reproduction and Fertility, upon whose Education Committee he also sits, and a Member of the British Society for Andrology and the US Society for the Study of Reproduction. He also has a diploma with distinction in Science Communication from Birkbeck College, London. He has written articles about science for The Guardian and New Scientist as well as preparing reports about scientific issues for the public for the Wellcome Trust, the Royal Society and the British Council. He presented the Charles Darwin Award Lecture at the BA Festival of Science 2003 at the University of Salford.
- NAADP activates two-pore channels on T cell cytolytic granules to stimulate exocytosis and killing.
- Davis, LC, Morgan, AJ, Chen, J, Snead, CM, Bloor-Young, D, Shenderov, E, Stanton-Humphreys, MN, Conway, SJ, Churchill, GC, Parrington, J, Cerundolo, V, and Galione, A
Curr Biol, 22(24):2331-7.
- Photoaffinity labeling of high affinity nicotinic acid adenine dinucleotide phosphate (NAADP)-binding proteins in sea urchin egg.
- Walseth, TF, Lin-Moshier, Y, Jain, P, Ruas, M, Parrington, J, Galione, A, Marchant, JS, and Slama, JT
J Biol Chem, 287(4):2308-15.
- The luminal Ca(2+) chelator, TPEN, inhibits NAADP-induced Ca(2+) release.
- Morgan, AJ, Parrington, J, and Galione, A
Cell Calcium, 52(6):481-7.
- Loss of activity mutations in phospholipase C zeta (PLCzeta) abolishes calcium oscillatory ability of human recombinant protein in mouse oocytes.
- Kashir, J, Jones, C, Lee, HC, Rietdorf, K, Nikiforaki, D, Durrans, C, Ruas, M, Tee, ST, Heindryckx, B, Galione, A, De Sutter, P, Fissore, RA, Parrington, J, and Coward, K
Hum Reprod, 26(12):3372-87.
- Two-pore channels form homo- and heterodimers.
- Rietdorf, K, Funnell, TM, Ruas, M, Heinemann, J, Parrington, J, and Galione, A
J Biol Chem, 286(43):37058-62.
- NAADP as an intracellular messenger regulating lysosomal calcium-release channels.
- Galione, A, Morgan, AJ, Arredouani, A, Davis, LC, Rietdorf, K, Ruas, M, and Parrington, J
Biochem Soc Trans, 38(6):1424-31.
- Purified TPC isoforms form NAADP receptors with distinct roles for Ca(2+) signaling and endolysosomal trafficking.
- Ruas, M, Rietdorf, K, Arredouani, A, Davis, LC, Lloyd-Evans, E, Koegel, H, Funnell, TM, Morgan, AJ, Ward, JA, Watanabe, K, Cheng, X, Churchill, GC, Zhu, MX, Platt, FM, Wessel, GM, Parrington, J, and Galione, A
Curr Biol, 20(8):703-9.
- TPC2 is a novel NAADP-sensitive Ca2+ release channel, operating as a dual sensor of luminal pH and Ca2+.
- Pitt, SJ, Funnell, TM, Sitsapesan, M, Venturi, E, Rietdorf, K, Ruas, M, Ganesan, A, Gosain, R, Churchill, GC, Zhu, MX, Parrington, J, Galione, A, and Sitsapesan, R
J Biol Chem, 285(45):35039-46.
- TPC2 proteins mediate nicotinic acid adenine dinucleotide phosphate (NAADP)- and agonist-evoked contractions of smooth muscle.
- Tugba Durlu-Kandilci, N, Ruas, M, Chuang, K, Brading, A, Parrington, J, and Galione, A
J Biol Chem, 285(32):24925-32.
- Two-pore channels for integrative Ca signaling.
- Zhu, MX, Evans, AM, Ma, J, Parrington, J, and Galione, A
Commun Integr Biol, 3(1):12-7.