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, M. Harrer, , , H. Vogelsang,
Published: 15 October 2013
by Wiley
Alimentary Pharmacology & Therapeutics, Volume 18, pp 1113-1120; doi:10.1046/j.1365-2036.2003.01793.x

Abstract:
Background : Antibiotics and thiopurines have been employed in the management of fistulizing Crohn's disease, although evidence of their efficacy is rare. Aim : To evaluate, in a prospective, open‐label study, the influence of antibiotics and azathioprine on the clinical outcome of perianal fistulas in patients with Crohn's disease. Methods : Fifty‐two patients entered the study, starting with an 8‐week regimen of ciprofloxacin (500–1000 mg/day) and/or metronidazole (1000–1500 mg/day). Seventeen patients had already received daily azathioprine (2–2.5 mg/kg) at enrolment, whereas in 14 patients azathioprine was initiated after 8 weeks of antibiotic treatment. Outcome was evaluated by Fistula Drainage Assessment and the Perianal Disease Activity Index at weeks 8 and 20. Results : Overall, 26 patients (50%) responded to antibiotic treatment, with complete healing in 25% of patients at week 8. The Perianal Disease Activity Index decreased significantly from 8.4 ± 2.9 to 6.0 ± 4.0 (P < 0.0001). At week 20, the outcome was assessed in 49 patients (94%), 29 of whom (59%) had received azathioprine. Response was noted in 17 of the 49 patients (35%), with complete healing in nine patients (18%). Patients who received azathioprine were more likely to achieve a response (48%) than those without immunosuppression (15%) (P = 0.03). The Perianal Disease Activity Index was closely associated with treatment response and perianal disease activity. Conclusion : Antibiotics are useful to induce a short‐term response in perianal Crohn's disease, and may provide a bridging strategy to azathioprine, which seems to be essential for the maintenance of fistula improvement.
Pierre-Marc Bouloux, Salvatore Corsello, Michael Besser, Ashley Grossman
Published: 12 December 2012
by Wiley
British Journal of Clinical Pharmacology, Volume 42, pp 225-232; doi:10.1046/j.1365-2125.1996.41421.x

Abstract:
Intravenous bolus doses of thyrotrophin releasing hormone (TRH, 50–1000 μg) caused statistically significant, non-dose dependent and transient rises in blood pressure, heart rate and plasma catecholamines in healthy young males. Mean peak incremental rises in systolic blood pressure (mean ± s.e. mean) following 50, 200 and 500 μg TRH were 14.3 ± 2.9 mmHg, 15.7 ± 3.2 mmHg and 17.1 ± 3.9 mmHg respectively (all P < 0.05 vs placebo). Mean incremental rises in heart rate for the three doses of TRH were 8.2 ± 2.2 beats min−1, 7.1 ± 1.8 beats min−1, and 1O.7 ± 2.9 beats min−1 respectively (all P < 0.05 vs placebo). Following the 50 μg and 1000 μg doses of TRH, plasma noradrenaline and adrenaline rose significantly (P < 0.05) between 4 and 8 min. Mean ± s.e. mean incremental plasma noradrenaline rise following 50, 200 and 1000 μg TRH were 0.4 ± O.13 nmol 1−1, 0.37 ± 0.21 nmol 1−1 and 0.41 ± 0.18 nmol 1−1 respectively. Mean ± s.e. mean incremental rise in adrenaline for the 50, 200 and 1000 μg dose were 0.13 ± 0.04 nmol 1−1, 0.08 ± 0.03 nmol 1−1, and 0.11 ± 0.05 nmol l−1 respectively. Following administration of the ganglion blocking drug pentolinium (5 mg) the incremental systolic blood pressure and heart rate rises following 500 μg TRH alone 16.6 ± 2.8 mmHg and 1O.4 ± 3.1 beats min−1 respectively. The rises in plasma noradrenaline and adrenaline following TRH were attenuated by prior ganglion blockade. α-adrenoceptor blockade with thymoxamine (0.3 mg kg−1 bolus + 0.3 mg kg−1 h−1 infusion), singly and combined with intravenous propranolol (10 mg i.v. over 10 min), did not alter the pressor or tachycardic effects of 500 μg TRH. In conclusion, although plasma noradrenaline rises following i.v. TRH, suggesting activation of the sympathetic nervous system, this effect is not responsible for the pressor response to TRH, which appears to be due to either a direct vasoconstrictive effect on the peripheral resistance vessels or a direct inotropic/chronotropic effect on the heart.
Published: 21 February 2012
by Wiley
Histopathology, Volume 60, pp 675-677; doi:10.1046/j.1365-2559.2003.04239.x

, , K. Hibbit
Published: 13 September 2010
by Wiley
Journal of Intellectual Disability Research, Volume 43, pp 380-392; doi:10.1046/j.1365-2788.1999.043005380.x

The publisher has not yet granted permission to display this abstract.
, John C. Wingfield
Published: 10 June 2010
by Wiley
Journal of Neuroendocrinology, Volume 10, pp 593-599; doi:10.1046/j.1365-2826.1998.00238.x

The publisher has not yet granted permission to display this abstract.
R. Meliconi, L. Pulsatelli, C. Melchiorri, L. Frizziero, C. Salvarani, P. Macchioni, M. Uguccioni, M. C. Focherini, A. Facchini
Published: 23 October 2009
by Wiley
Clinical & Experimental Immunology, Volume 107, pp 494-500; doi:10.1046/j.1365-2249.1997.00294.x

The publisher has not yet granted permission to display this abstract.
Paul D. Mintz
Published: 20 October 2009
by Wiley
Transfusion, Volume 31, pp 382-382; doi:10.1046/j.1537-2995.1976.16176130843.x-i1

Mark A. Popovsky
Published: 20 October 2009
by Wiley
Transfusion, Volume 35, pp 180-181; doi:10.1046/j.1537-2995.1981.21381201817.x-i1

Published: 18 September 2009
by Wiley
Development, Growth & Differentiation, Volume 43; doi:10.1046/j.1440-169x.2001.00006-authorindex.x

Comment
P. J. S. Dunn
Published: 18 September 2009
by Wiley
Cytopathology, Volume 9, pp 138-138; doi:10.1046/j.1365-2303.1998.0137a.x

Journal of Veterinary Emergency and Critical Care, Volume 13, pp 200-200; doi:10.1046/j.1435-6935.2003.00109.x

Journal of Veterinary Emergency and Critical Care, Volume 13, pp 197-198; doi:10.1046/j.1435-6935.2003.00107.x

Journal of Veterinary Emergency and Critical Care, Volume 13, pp 199-199; doi:10.1046/j.1435-6935.2003.00108.x

, Hanno L. Tan
Published: 14 September 2009
by Wiley
Journal of Cardiovascular Electrophysiology, Volume 14, pp 1258-1258; doi:10.1046/j.1540-8167.2003.03328a.x

Suneet Mittal, Bruce B. Lerman
Published: 10 September 2009
by Wiley
Journal of Cardiovascular Electrophysiology, Volume 15, pp 615-616; doi:10.1046/j.1540-8167.2004.04013.x

Adam E. Saltman, Stephen J. Lahey, Nicola A. Francalancia, E. Victor Tselentakis
Published: 10 September 2009
by Wiley
Journal of Cardiovascular Electrophysiology, Volume 14, pp 786-786; doi:10.1046/j.1540-8167.2003.03201.x

Alejandro Perez‐Lugones, James T. McMahon,
Published: 10 September 2009
by Wiley
Journal of Cardiovascular Electrophysiology, Volume 15, pp 122-123; doi:10.1046/j.1540-8167.2004.03525_3.x

Comment
Published: 10 September 2009
by Wiley
Journal of Cardiovascular Electrophysiology, Volume 15, pp 616-616; doi:10.1046/j.1540-8167.2004.03700.x

Comment
Attilio Del Rosso, Angelo Bartoletti, Michele Brignole
Published: 10 September 2009
by Wiley
Journal of Cardiovascular Electrophysiology, Volume 15, pp 615-615; doi:10.1046/j.1540-8167.2004.03697.x

Comment
Josef Kautzner, Robert Cihá, , Robert Čihák
Published: 10 September 2009
by Wiley
Journal of Cardiovascular Electrophysiology, Volume 15, pp 617-618; doi:10.1046/j.1540-8167.2004.04008.x

Comment
Published: 9 September 2009
by Wiley
Journal of Cardiovascular Electrophysiology, Volume 16, pp 678-678; doi:10.1046/j.1540-8167.2005.50047.x

Per Insulander, Hans Vallin
Published: 9 September 2009
by Wiley
Journal of Cardiovascular Electrophysiology, Volume 16, pp 679-680; doi:10.1046/j.1540-8167.2005.50060.x

, Julie Milland, Peter Kyriakou, Bruce R. Thorley, Dale Christiansen, Marc B. Lanteri, Mark Regensburg, Maureen Duffield, Andrew J. French, Lindsay Williams, et al.
Published: 13 August 2009
by Wiley
Xenotransplantation, Volume 11, pp 171-183; doi:10.1046/j.1399-3089.2003.00103_11_2.x

The publisher has not yet granted permission to display this abstract.
Published: 30 July 2009
by Wiley
BJU International, Volume 91, pp 428-428; doi:10.1046/j.1464-410x.2002.04121.x

Published: 30 July 2009
by Wiley
BJU International, Volume 91, pp 431-431; doi:10.1046/j.1464-410x.2002.02988.x-i3

Published: 23 July 2009
by Wiley
Journal of Neurochemistry, Volume 87, pp 86-88; doi:10.1046/j.1474-1644.2003.2170_11.x

Published: 23 July 2009
by Wiley
Journal of Neurochemistry, Volume 70, pp 440-440; doi:10.1046/j.1471-4159.1998.7001440a.x

Published: 16 July 2009
by Wiley
Journal of Neurochemistry, Volume 66, pp 440-440; doi:10.1046/j.1471-4159.1996.6601440a.x

Published: 16 July 2009
by Wiley
Journal of Neurochemistry, Volume 69, pp 887-888; doi:10.1046/j.1471-4159.1997.6902887a.x

Published: 16 July 2009
by Wiley
Journal of Neurochemistry, Volume 84; doi:10.1046/j.1471-4159.2002.00835.x-1

Published: 15 July 2009
by Wiley
Xenotransplantation, Volume 10, pp 637-638; doi:10.1046/j.1399-3089.2003.00102_1.x

Published: 2 July 2009
by Wiley
BJU International, Volume 91, pp 127-127; doi:10.1046/j.1464-410x.2002.02988_91_1.x

Richard A. Wennberg, Luis Felipe Quesney
Published: 11 May 2009
by Wiley
Epilepsia, Volume 42, pp 704-705; doi:10.1046/j.1528-1157.2001.0420057042.x

Theodore H. Schwartz, Carl Bazil, Mennato Forgione, Jeffrey N. Bruce, Robert R. Goodman
Published: 11 May 2009
by Wiley
Epilepsia, Volume 42, pp 704-705; doi:10.1046/j.1528-1157.2001.0420057043.x

International Journal of Paediatric Dentistry, Volume 11, pp 387-395; doi:10.1046/j.1365-263x.2001.00297.x

, M. Cammarota, V. A. Brent,
Published: 22 April 2009
by Wiley
Journal of Neurochemistry, Volume 76, pp 149-154; doi:10.1046/j.1471-4159.2001.00058.x

The publisher has not yet granted permission to display this abstract.
H. F. Dovey, V. John, J. P. Anderson, L. Z. Chen, P. De Saint Andrieu, L. Y. Fang, S. B. Freedman, B. Folmer, E. Goldbach, E. J. Holsztynska, et al.
Published: 22 April 2009
by Wiley
Journal of Neurochemistry, Volume 76, pp 173-181; doi:10.1046/j.1471-4159.2001.00012.x

Abstract:
Converging lines of evidence implicate the beta‐amyloid peptide (Aβ) as causative in Alzheimer's disease. We describe a novel class of compounds that reduce Aβ production by functionally inhibiting γ‐secretase, the activity responsible for the carboxy‐terminal cleavage required for Aβ production. These molecules are active in both 293 HEK cells and neuronal cultures, and exert their effect upon Aβ production without affecting protein secretion, most notably in the secreted forms of the amyloid precursor protein (APP). Oral administration of one of these compounds, N‐[N‐(3,5‐difluorophenacetyl)‐l‐alanyl]‐S‐phenylglycine t‐butyl ester, to mice transgenic for human APPV717F reduces brain levels of Aβ in a dose‐dependent manner within 3 h. These studies represent the first demonstration of a reduction of brain Aβin vivo. Development of such novel functional γ‐secretase inhibitors will enable a clinical examination of the Aβ hypothesis that Aβ peptide drives the neuropathology observed in Alzheimer's disease.
Hee‐Sun Kim, Seok Jong Hong, Mark S. LeDoux, Kwang-Soo Kim
Published: 22 April 2009
by Wiley
Journal of Neurochemistry, Volume 76, pp 280-294; doi:10.1046/j.1471-4159.2001.00044.x

The publisher has not yet granted permission to display this abstract.
Claire L. Standen, Janet Brownlees, , Sashi Kesavapany, , ,
Published: 22 April 2009
by Wiley
Journal of Neurochemistry, Volume 76, pp 316-320; doi:10.1046/j.1471-4159.2001.00102.x

Abstract:
Threonine(668) (thr(668)) within the carboxy-terminus of the Alzheimer's disease amyloid precursor protein (APP) is a known in vivo phosphorylation site. Phosphorylation of APPthr(668) is believed to regulate APP function and metabolism. Thr(668) precedes a proline, which suggests that it is targeted for phosphorylation by proline-directed kinase(s). We have investigated the ability of four major neuronally active proline-directed kinases, cyclin dependent protein kinase-5, glycogen synthase kinase-3 beta, p42 mitogen-activated protein kinase and stress-activated protein kinase-1b, to phosphorylate APPthr(668) and report here that SAPK1b induces robust phosphorylation of this site both in vitro and in vivo. This finding provides a molecular framework to link cellular stresses with APP metabolism in both normal and disease states.
Published: 22 April 2009
by Wiley
Journal of Neurochemistry, Volume 76, pp 302-306; doi:10.1046/j.1471-4159.2001.00060.x

Abstract:
Deficiency of complex I in the respiratory chain and oxidative stress induced by hydrogen peroxide occur simultaneously in dopaminergic neurones in Parkinson's disease. Here we demonstrate that the membrane potential of in situ mitochondria (ΔΨm), as measured by the fluorescence change of JC‐l (5,5′,6,6′‐tetrachloro‐1,1,3,3′‐tetraethylbenzimidazolyl‐carbocyanine iodide), collapses when isolated nerve terminals are exposed to hydrogen peroxide (H2O2,100 and 500 µm) in combination with the inhibition of complex I by rotenone (5 nm−1 µm). H2O2 reduced the activity of complex I by 17%, and the effect of H2O2 and rotenone on the enzyme was found to be additive. A decrease in ΔΨm induced by H2O2 was significant when the activity of complex I was reduced to a similar extent as found in Parkinson's disease (26%). The loss of ΔΨm observed in the combined presence of complex I deficiency and H2O2 indicates that when complex I is partially inhibited, mitochondria in nerve terminals become more vulnerable to H2O2‐induced oxidative stress. This mechanism could be crucial in the development of bioenergetic failure in Parkinson's disease.
Randy Krainock,
Published: 22 April 2009
by Wiley
Journal of Neurochemistry, Volume 76, pp 312-315; doi:10.1046/j.1471-4159.2001.00089.x

Abstract:
Heregulin plays key roles in regulating cell number, determining fate and establishing pattern in the developing nervous system via specific receptors (ErbBs), including ErbB4. Two recent reports have shown that ErbB4 forms a complex with postsynaptic density proteins, which are, in turn, known to complex with nitric oxide synthase (NOS)-1. To reveal whether heregulin might regulate the expression of NOS-1, cultures enriched in cerebellar granule cells were exposed to heregulin for 72 h. This treatment resulted in an increase in NOS-1 protein (> 70%), an effect mediated by the ErbB4 receptor. While nitric oxide might mediate some of the downstream effects of heregulin in the nervous system, heregulin treatment neither enhanced granule cell survival, nor protected neurons from acute glutamate excitotoxicity.
Published: 22 April 2009
by Wiley
Journal of Neurochemistry, Volume 76, pp 307-311; doi:10.1046/j.1471-4159.2001.00073.x

Abstract:
CNS precursors derived from E12 rat mesencephalon proliferate in the presence of basic fibroblast growth factor and differentiate in vitro into functional dopaminergic neurons, which upon transplantation alleviate behavioral symptoms in a rat model of Parkinson's disease. Here we show that the efficiency of dopaminergic differentiation decreases in the mesencephalic precursors that were proliferated or passaged for extended periods in vitro. Ascorbic acid treatment restored dopaminergic differentiation in these precursors and led to a greater than 10‐fold increase in dopamine neuron yield compared with untreated cultures. The effect of ascorbic acid was stereospecific and could not be mimicked by any other antioxidants. The expression of sodium‐dependent vitamin C transporter, a recently identified stereospecific ascorbic acid transporter, was maintained in mesencephalic precursors for extended in vitro periods. Pre‐treatment of in vitro expanded mesencephalic precursors with ascorbic acid might facilitate the large‐scale generation of dopaminergic neurons for clinical transplantation.
, J. Ren, M. H. O'regan
Published: 22 April 2009
by Wiley
Journal of Neurochemistry, Volume 76, pp 247-257; doi:10.1046/j.1471-4159.2001.00050.x

Abstract:
A rat four vessel occlusion model was utilized to examine the effects of ischemia/reperfusion on cortical window superfusate levels of amino acids, glucose, and lactate. Superfusate aspartate, glutamate, phosphoethanolamine, taurine, and GABA were significantly elevated by cerebral ischemia, then declined during reperfusion. Other amino acids were affected to a lesser degree. Superfusate lactate rose slightly during the initial ischemic period, declined during continued cerebral ischemia and then was greatly elevated during reperfusion. Superfusate glucose levels declined to near zero levels during ischemia and then rebounded beyond basal levels during the reperfusion period. Inhibition of neuronal lactate uptake with alpha-cyano-4-hydroxycinnamate dramatically elevated superfusate lactate levels, enhanced the ischemia/reperfusion evoked release of aspartate but reduced glutamine levels. Topical application of an alternative metabolic fuel, glutamine, had a dose dependent effect. Glutamine (1 mM) elevated basal superfusate glucose levels, diminished the decline in glucose during ischemia, and accelerated its recovery during reperfusion. Lactate levels were elevated during ischemia and reperfusion. These effects were not evident at 5 mM glutamine. At both concentrations, glutamine significantly elevated the superfusate levels of glutamate. Topical application of sodium pyruvate (20 mM) significantly attenuated the decline in superfusate glucose during ischemia and enhanced the levels of both glucose and lactate during reperfusion. However, it had little effect on the ischemia-evoked accumulation of amino acids. Topical application of glucose (450 mg/dL) significantly elevated basal superfusate levels of lactate, which continued to be elevated during both ischemia and reperfusion. The ischemia-evoked accumulations of aspartate, glutamate, taurine and GABA were all significantly depressed by glucose, while phosphoethanolamine levels were elevated. These results support the role of lactate in neuronal metabolism during ischemia/reperfusion. Both glucose and glutamine were also used as energy substrates. In contrast, sodium pyruvate does not appear to be as effectively utilized by the ischemic/reperfused rat brain since it did not reduce ischemia-evoked amino acid efflux.
A.J. Sánchez Meador, , ,
Published: 23 February 2009
by Wiley
Journal of Vegetation Science, Volume 20, pp 79-90; doi:10.1046/j.1365-2893.1999.00142.x-i1

The publisher has not yet granted permission to display this abstract.
Published: 17 December 2008
by Wiley
BJU International, Volume 86, pp 218-258; doi:10.1046/j.1464-410x.2000.0860s3218.x

Published: 17 December 2008
by Wiley
BJU International, Volume 86, pp 1-42; doi:10.1046/j.0007-1331.2000.00001.x

K. Foulon, S. Baltora-Rosset, V. Fuentes, F. Mesnard, S. Da Nascimento, E. Bouhassira, J. Rochette
Published: 5 December 2008
by Wiley
Journal of Peptide Research, Volume 63, pp 1-8; doi:10.1046/j.1399-3011.2004.00097.x

The publisher has not yet granted permission to display this abstract.
O. Dawidowska, , , W. Kowalczyk, I. Derdowska, K. Neubert, J. Zabrocki, B. Olejniczak, W. Juzwa, B. Lammek
Published: 5 December 2008
by Wiley
The Journal of Peptide Research, Volume 63, pp 29-35; doi:10.1046/j.1399-3011.2004.00101.x

The publisher has not yet granted permission to display this abstract.
Published: 5 December 2008
by Wiley
Journal of Peptide Research, Volume 63, pp 194-194; doi:10.1046/j.1399-3011.2003.00092.x

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