Peter R. Dunkley

Riverside

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Phillip W. Dickson

Hunter Medical Research Institute

Larisa Bobrovskaya

University of South Australia

Lin Kooi Ong

Monash University Malaysia

John A.P. Rostas

University of Newcastle Australia

Paula E. Jarvie

University of Newcastle Australia

Phillip J. Robinson

Children's Medical Research Institute

Stephen J. Bunn

University of Otago

Alistair T.R. Sim

Compass (United States)

Rodrigo Bainy Leal

Universidade Federal de Santa Catarina

Daniel Pens Gelain

Universidade Federal do Rio Grande do Sul

Cooperative Institutions

University of Newcastle Australia

Hunter Medical Research Institute

Universidade Federal do Rio Grande do Sul

Universidade Federal de Santa Catarina

University of Sydney

University of Melbourne

Monash University

Universidade Federal do Rio de Janeiro

UNSW Sydney

Universidade Federal de Ciências da Saúde de Porto Alegre

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The effect of social stress on tyrosine hydroxylase phosphorylation

Larisa Bobrovskaya Lin Kooi Ong Rebecca Alison Walker Trevor A. Day Phillip W. Dickson

Tyrosine 3-Monooxygenase

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Whigs and Paupers: The Reform of the English Poor Laws, 1830-1834

Journal of British Studies (1981)

Peter R. Dunkley

In 1832, a royal commission was appointed to investigate the operation of the poor laws in England and Wales, and two years later legislation was adopted on the basis of the commission's recommendations. For most contemporaries the passage of this measure, the so-called New Poor Law, seemed to promise significant, perhaps even radical, change in the administration of poor relief. An ancient system of parochial government was to be supplanted in the localities by a series of larger poor law unions and boards of guardians, whose discretion was to be limited by responsibility to a national bureaucratic authority in London. No less dramatic was the relief policy that the new law envisioned. It was generally understood that the poor law commissioners appointed under the act were to direct their main efforts to the establishment of a system of workhouses, wherein relief could be accorded under conditions that rendered the pauper's lot “less eligible,” that is, less attractive, than that of the poorest independent laborer. Through such means, it was hoped, an end might be made to what was seen as a long-established and widespread practice of supplementing the inadequate wages of the laboring poor out of the poor rates. While the tendency of recent work has been to question the practical effect of this legislation on the actual distribution of aid, the problem remains of explaining the motivations and intentions of the men who promoted a measure of such seemingly abundant and far-reaching implications.

Bureaucracy

Poor law

Poor relief

Poorhouse

Law reform

Royal Commission

10.1086/385776

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Citations (46)

Expression of Tyrosine Hydroxylase Increases the Resistance of Human Neuroblastoma Cells to Oxidative Insults

Toxicological Sciences (2009)

Jeferson Luís Franco Thaís Posser Sarah L. Gordon Larisa Bobrovskaya Jennifer Schneider

In this study, we demonstrate that human neuroblastoma SH-SY5Y cells transfected with human tyrosine hydroxylase isoform 1 (SH + TH cells) were substantially more resistant to cell death induced by hydrogen peroxide and 6-hydroxydopamine when compared to wild-type SH-SY5Y cells (SH cells). SH + TH cells exhibit increased levels of dopamine (DA) compared to SH cells. Incubation with hydrogen peroxide or 6-hydroxydopamine (10–100μM) for 24 h caused a significant reduction in cell viability and increased apoptosis in both cell types. However, these effects were significantly reduced in the SH + TH cells when compared to the SH cells. The SH + TH cells showed an improved ability to detoxify peroxide, which correlated with an increase in glutathione peroxidase and glutathione reductase activities, while catalase activity was unchanged. Our data suggest that a preconditioning-like mechanism linked to higher DA levels increased the resistance of SH + TH cells against oxidative insults, which is at least in part related to an augmentation in the activity of glutathione-related antioxidant enzymes.

Glutathione reductase

SH-SY5Y

10.1093/toxsci/kfp245

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Citations (21)

Tetanus Toxin Inhibits Depolarization‐Stimulated Protein Phosphorylation in Rat Cortical Synaptosomes: Effect on Synapsin I Phosphorylation and Translocation

Journal of Neurochemistry (1992)

Peter Presek Sönke Jessen Florian Dreyer Paula E. Jarvie Duygu Fındık

Abstract: Synapsin I, a prominent phosphoprotein in nerve terminals, is proposed to modulate exocytosis by interaction with the cytoplasmic surface of small synaptic vesicles and cytoskeletal elements in a phosphorylation‐dependent manner. Tetanus toxin (TeTx), a potent inhibitor of neurotransmitter release, attenuated the depolarization‐stimulated increase in synapsin I phosphorylation in rat cortical particles and in synaptosomes. TeTx also markedly decreased the translocation of synapsin I from the small synaptic vesicles and the cytoskeleton into the cytosol, on depolarization of synaptosomes. The effect of TeTx on synapsin I phosphorylation was both time and TeTx concentration dependent and required active toxin. One‐ and two‐dimensional peptide maps of synapsin I with V8 proteinase and trypsin, respectively, showed no differences in the relative phosphorylation of peptides for the control and TeTx‐treated synaptosomes, suggesting that both the calmodulin‐and the cyclic AMP‐dependent kinases that label this protein are equally affected. Phosphorylation of synapsin IIb and the B‐50 protein (GAP43), a known substrate of protein kinase C, was also inhibited by TeTx. TeTx affected only a limited number of phosphoproteins and the calcium‐dependent decrease in dephosphin phosphorylation remained unaffected. In vitro phosphorylation of proteins in lysed synaptosomes was not influenced by prior TeTx treatment of the intact synaptosomes or by the addition of TeTx to lysates, suggesting that the effect of TeTx on protein phosphorylation was indirect. Our data demonstrate that TeTx inhibits neurotransmitter release, the phosphorylation of a select group of phosphoproteins in nerve terminals, and the translocation of synapsin I. These findings contribute to our understanding of the basic mechanism of TeTx action.

Synapsin

Synapsin I

Synaptic vesicle recycling

10.1111/j.1471-4159.1992.tb08445.x

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Citations (27)

Advances in Second Messenger and Phosphoprotein Research, Vol. 27 : Model Systems in Signal Transduction edited by S. Shenolikar and A. C. Nairn. Raven Press, New York, 1993, ISBN 0‐88167‐975‐5, 224 pp., $95.00

Journal of Neurochemistry (1994)

Peter R. Dunkley

Phosphoprotein

10.1046/j.1471-4159.1994.t01-2-62052061.x

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P3.061 Differential distribution of tyrosine hydroxylase isoforms in the human brain

Parkinsonism & Related Disorders (2009)

Jacqueline Shehadeh Kay L. Double Karen E. Murphy Larisa Bobrovskaya Stefanie Reyes

Tyrosine 3-Monooxygenase

10.1016/s1353-8020(09)70625-x

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Histamine-stimulated phosphorylation of tyrosine hydroxylase in bovine adrenal medullary cells

Neurochemistry International (1992)

Stephen J. Bunn Peter R. Dunkley

Tyrosine 3-Monooxygenase

10.1016/0197-0186(92)92182-4

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Pre-incubation of subcellular fractions from rat cerebral cortex inactivates protein phosphorylation

Biochemical Journal (1981)

Peter R. Dunkley Phillip J. Robinson

Pre-incubation of various subcellular fractions from rat brain caused a significant decrease in the phosphorylation of individual polypeptides. The rate and extent of this loss of labelling was not uniform and polypeptides whose phosphorylation was independent of cyclic AMP were primarily affected, whereas substrate availability remained unaltered. It is recommended that pre-incubation effects must be carefully monitored if valid conclusions are to be made about the physiological relevance of changes in protein phosphorylation observed in vitro.

Incubation period

10.1042/bj1990269

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Citations (15)

Commoners: Common Right, Enclosure and Social Change in England, 1700-1820.

The American Historical Review (1995)

Peter R. Dunkley J. M. Neeson

Enclosure

10.2307/2169935

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Citations (16)

Characterisation of tryptic peptides of phosphorylated tyrosine hydroxylase by high-pressure liquid chromatography electrospray ionisation mass spectrometry