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  • 1
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of arabinofuranosidase C from Aspergillus niger strain 3M43 (1997)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 222-223 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Crystals of arabinofuranosidase C purified from Aspergillus niger strain 3M43 have been obtained by vapour diffusion. The crystal belongs to the space group P21 with cell parameters a = 44.28, b = 71.99, c = 45.27 Å and β = 105.98° with one molecule in the asymmetric unit. The X-ray diffraction pattern of these crystals extends to at least 2.20 Å resolution with the use of synchrotron radiation. These crystals are stable on exposure to radiation and are suitable for structure determination.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996011936
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  • 2
    Electronic Resource
    Electronic Resource
    Osmotic Regulation of Neuropeptide Y Synthesis in Magnocellular Neurons of the Hypothalamo-Neurohypophysial System (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 689 (1993), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1993.tb55609.x
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  • 3
    Electronic Resource
    Electronic Resource
    Retigabine: Chemical Synthesis to Clinical Application (2005)
    Oxford, UK : Blackwell Publishing Ltd
    CNS drug reviews 11 (2005), S. 0 
    Details
    ISSN: 1527-3458
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Retigabine [D23129; N-(2-amino-4-(4-fluorobenzylamino)-phenyl)carbamic acid ethyl ester] is an antiepileptic drug with a recently described novel mechanism of action that involves opening of neuronal KV7.2–7.5 (formerly KCNQ2-5) voltage-activated K+ channels. These channels (primarily KV7.2/7.3) enable generation of the M-current, a subthreshold K+ current that serves to stabilize the membrane potential and control neuronal excitability. In this regard, retigabine has been shown to have a broad-spectrum of activity in animal models of electrically-induced (amygdala-kindling, maximal electroshock) and chemically-induced (pentylenetetrazole, picrotoxin, NMDA) epileptic seizures. These encouraging results suggest that retigabine may also prove useful in the treatment of other diseases associated with neuronal hyperexcitability. Neuropathic pain conditions are characterized by pathological changes in sensory pathways, which favor action potential generation and enhanced pain transmission. Although sometimes difficult to treat with conventional analgesics, antiepileptics can relieve some symptoms of neuropathic pain. A number of recent studies have reported that retigabine can relieve pain-like behaviors (hyperalgesia and allodynia) in animal models of neuropathic pain. Neuronal activation within several key structures within the CNS can also be observed in various animal models of anxiety. Moreover, amygdala-kindled rats, which have a lowered threshold for neuronal activation, also display enhanced anxiety-like responses. Retigabine dose-dependently reduces unconditioned anxiety-like behaviors when assessed in the mouse marble burying test and zero maze. Early clinical studies have indicated that retigabine is rapidly absorbed and distributed, and is resistant to first pass metabolism. Tolerability is good in humans when titrated up to its therapeutic dose range (600-1200 mg/day). No tolerance, dependence or withdrawal potential has been reported, although adverse effects can include mild dizziness, headache, nausea and somnolence. Thus, retigabine may prove to be useful in the treatment of a diverse range of disease states in which neuronal hyperexcitability is a common underlying factor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1527-3458.2005.tb00033.x
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  • 4
    Electronic Resource
    Electronic Resource
    Antifungal activity of sugar beet chitinase against Cercospora beticola: an autoradiographic study on cell wall degradation (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Plant pathology 43 (1994), S. 0 
    Details
    ISSN: 1365-3059
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Two independent bioassays demonstrated an antifungal effect of a basic sugar beet chitinase on Cercospora beticola, the causal agent of leaf spot disease in sugar beet (Beta vulgaris). In one assay, the growth of submerged spore cultures of C. beticola in microtitre wells was followed by measuring the increase in absorbance at 620 nm. Addition of chitinase to the culture resulted in a delay in germination and a slower initial growth rate. A more detailed picture of the action of the chitinase on the fungal cell wall was provided by an autoradiographic study. An intense labelling was observed at the apex of fungal hyphae grown in medium containing [3H]N-acetylglucosamine, through incorporation of the radioactive chitin monomer into newly synthesized chitin in the cell wall. After fixation of the fungal specimen, the radioactive labelling could be removed by treatment with purified chitinase, i.e. nascent chitin chains were hydrolysed by the enzyme. When the fungal culture was subjected to a chase phase prior to fixation, the radioactive depositions were less accessible to hydrolysis by the chitinase. HPLC analysis of the radioactive hydrolysis products released from the apex of the fungal hyphae showed that the main products were small chito-oligosaccharides, mainly dimers, trimers and tetramers of chitin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3059.1994.tb01647.x
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  • 5
    Electronic Resource
    Electronic Resource
    Chronic Antidepressant Treatments Decrease Pro-Opiomelanocortin mRNA Expression in the Pituitary Gland: Effects of Acute Stress and 5-HT1A Receptor Activation (2001)
    Oxford, UK : Blackwell Science, Ltd
    Journal of neuroendocrinology 13 (2001), S. 0 
    Details
    ISSN: 1365-2826
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Consistent findings in depressed patients are hyperactivity in the hypothalamic-pituitary-adrenal (HPA) axis with high plasma concentrations of adrenocorticotropic hormone and cortisol. Long-term antidepressant treatments seem to normalize this hyperactivity, suggesting a link between the HPA axis and the action of antidepressant treatments. The present study was carried out to study the effects of antidepressant treatments on pro-opiomelanocortin (POMC) mRNA expression, with a focus on interaction with acute stress and 5-HT1A receptor activation. Male rats were treated for 21 days with saline, citalopram, fluoxetine, moclobemide or desipramine, and the expression of POMC mRNA in the anterior pituitary was analysed by semi-quantitative in situ hybridization. All antidepressants, but not saline, cocaine and haloperidol, reduced POMC mRNA expression. The decrease in POMC mRNA was not observed until 9 days of citalopram treatment. Decreased POMC mRNA levels were also observed after 14 days of repeated electroconvulsive stimulation. The decreased POMC mRNA levels did not affect the stress-induced POMC mRNA increase, measured following swim stress and restraint stress. Finally, using Fos as a marker for neural activity, we showed attenuation of 8-OH-DPAT-stimulated activity in the paraventricular nucleus following 21 days of citalopram treatment. In conclusion, antidepressant treatments decrease basal POMC mRNA expression without affecting the acute stress response, and the reduced POMC mRNA may be related to reduced 5-HT1A-stimulated hypothalamic output.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2826.2001.00712.x
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  • 6
    Electronic Resource
    Electronic Resource
    Tissue specificity and induction of class I, II and III chitinases in barley (Hordeum vulgare) (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 89 (1993), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Barley (Hordeum vulgare L.) chitinases (EC 3.2.1.14) were found to be distributed and induced in highly tissue specific patterns. Out of 6 chitinases investigated 3 were present in leaves and only a class II chitinase (molecular mass 24 846 ± 5 Da, pI≥9.8) was markedly induced in leaves heavily infected with powdery mildew (Erysiphe graminis f. sp. hordei). The class II chitinase and a novel class III chitinase (molecular mass 30 kDa, pI≥9.8) were found in intercellular washing fluid of leaves, suggesting extracellular deposition. Neither of these two proteins were induced after infiltration of sodium salicylate (2 mM, pH 6.5) or nickel chloride (2 mM). The class III chitinase showed exochitinase activity in addition to endochitinase activity. No grain specific chitinases were found in leaves after any of the stresses applied. In contrast, 3 grain specific chitinases and one of the leaf chitinases were found in in vitro cultures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1993.tb05203.x
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  • 7
    Electronic Resource
    Electronic Resource
    Characterization of two antifungal endochitinases from barley grain (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 79 (1990), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A basic chitinase (chitinase T, EC 3.2.1.14, molecular mass 33 kDa, pI 9.8) was isolated and compared with a previously described chitinase (chitinase C, molecular mass 28 kDa, pI 9.7). The two chitinases were isolated in homogeneous form from barley (Hordeum vulgare L.) Bomi mutant 1508 grains either by two cation exchange steps or by one affinity step followed by cation exchange. Both chitinases are endochitinases with specific activities of 168 and 54 nkat (mg protein)−1 for chitinase T and chitinase C, respectively. Both inhibit the growth of Trichoderma viride efficiently. The lysozyme activity of both chitinases is 104 times lower than that of hen egg-white lysozyme as measured by lysis of cell walls of Micrococcus lysodeikticus. The amino acid composition and two partial amino acid sequences of chitinase T were determined. A 23 residue sequence of the N-terminal domain of chitinase T, which was not present in chitinase C, showed 73% identity with domain B of wheat germ lectin and 65% identity with the N-terminal domain of an endochitinase from bean leaves (deduced from cDNA). A 9 amino acid sequence of a cyanogen bromide fragment of chitinase T was identical with a cDNA deduced sequence of a barley aleurone endochitinase but differed in one residue from chitinase C. Generally, the two grain chitinases have physico-chemical and enzymatic properties similar to the plant leaf chitinases characterized. Both chitinases are localized in the aleurone layer and starchy endosperm of developing and germinating grain, but not in the embryo. The appearance of chitinases T and C at a late state of grain development suggests a role for these enzymes as a defense against fungi in the quiescent and germinating grain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1990.tb02117.x
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  • 8
    Electronic Resource
    Electronic Resource
    Simultaneous detection of neuropeptides and messenger RNA in the magnocellular hypothalamo-neurohypophysial system by a combination of non-radioactive in situ hybridization histochemistry and immunohistochemistry (1994)
    Springer
    Histochemistry and cell biology 102 (1994), S. 415-423 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A protocol was developed combining non-radioactive in situ hybridization histochemistry with enzyme based immunohistochemistry, detect the expression of mRNA in phenotypically defined neurons. Freefloating brain sections were hybridized with the oligonucleotide probes which have been 3′-end labelled with biotin-11-dUTP. The hybridized probe was visualized by a combined avidin-biotin bridge method, anti-avidin immunohistochemistry, and horseradish peroxidase detection using diaminobenzidine as a substrate. The in situ hybridization step yielded a very stable reaction product enabling subsequent immunohistochemical reactions using horseradish peroxidase and benzidine dihydrochloride as a chromogen. Magnocellular neurons of the hypothalamo-neurophypophysial system synthesize either vasopressin or oxytocin; water deprivation and chronic saline ingestion are potent stimuli for the expression of both of the genes encoding these neuropeptides. A number of other neuropeptides with putative transmitter action are synthesized in magnocellular neurons during such stimulation. Experiments were performed to explore whether neuropeptide Y immunoreactivity is present within magnocellular vasopressin mRNA-expressing neurons of the hypothalamo-neurophypophysial system. The results clearly demonstrated that neuropeptide Y-immunoreactive elements were present within a number of magnocellular vasopressin mRNA-containing cells. In addition, immunohistochemical detection of the neuropeptides ocytocin and cholecystokinin was carried out on sections hybridized non-radioactively for vasopressin; as expected vasopressin mRNA did not co-exist with cholecystokinin, whereas a few oxytocin immunoreactive neurons in osmotically stimulated animals also contained vasopressin mRNA. The developed method makes possible the immunohistochemical detection of intracellular antigens with concomitant detection of intracellular mRNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00269572
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  • 9
    Electronic Resource
    Electronic Resource
    A dual-immunocytochemical method to localize c-fos protein in specific neurons based on their content of neuropeptides and connectivity (1994)
    Springer
    Histochemistry and cell biology 101 (1994), S. 245-251 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Enhanced expression of the immediate early gene c-fos has been used as a marker of cellular activation in many different neuronal pathways. We wished to determine the neurochemical content and the connectivity of neurons, in which expression of c-fos is induced. For this purpose, a dual-immunocytochemical staining technique has been developed with avidin-biotin-peroxidase labelling using diaminobenzidine as the chromogen for c-fos protein located in the nucleus, and benzidine dihydrochloride (BDHC) in the presence of sodium nitroprusside to reveal cytoplasmic antigens (neuropeptide or retrograde tracer) in the same section. The blue granular BDHC reaction product in the cytoplasm combined with the homogeneous brown nuclear DAB staining for c-fos protein provides excellent resolution of dual-labelled cells even in tissue sections of 40 μm in thickness. The high sensitivity of the avidin-biotin-peroxidase immunocytochemistry and the stability of the reaction products provide an excellent tool for quantitative analysis of stimulated cells within a neurochemically defined cell group. The BDHC/DAB protocol was developed to identify activated cells in three experimental situations. Firstly, to investigate the phenotype of light-activated cells in the suprachiasmatic nucleus of the hypothalamus, c-fos protein DAB staining was carried out together with BDHC staining for peptide histidine isoleucine (PHI) and vasoactive intestinal peptide (VIP). Secondly, to identify activated neurons in female Syrian hamsters at the time of the proestrous luteinizing hormone surge, c-fos protein staining with DAB was carried out in combination with BDHC staining for gonadotrophin-releasing hormone (GnRH). In both these studies, cells which co-localized the peptide and c-fos protein in the nucleus could be identified unequivocally. Thirdly, to analyse projections of c-fos-immunoreactive neurons, the retrograde tracer, cholera toxin subunit B (ChB) was pressure-injected into the piriform cortex of rats, which were thereafter fully kindled in the contralateral amygdala. The tract tracer was stained with BDHC as the chromogen. Due to the advantages of the dual-labelling methodology, the combination of retrograde tracing and c-fos protein histochemistry provides an excellent method for identifying projecting and activated neurons in the same section.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00315911
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  • 10
    Electronic Resource
    Electronic Resource
    Innervation of the mink pineal gland with neuropeptide Y (NPY)-containing nerve fibers (1990)
    Springer
    Cell & tissue research 261 (1990), S. 477-483 
    Details
    ISSN: 1432-0878
    Keywords: Pineal gland ; Central innervation ; NPY ; Immunohistochemistry ; Superior cervical ganglionectomy ; Mink (Mustela vison)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary An immunohistochemical investigation of the mink pineal gland was performed by use of antibodies raised in rabbits against neuropeptide Y (NPY) and Cys-NPY (32–36)-amide recognizing neuropeptide Y with an amidation at position 36 (NPYamide). NPY-immunoreactive nerve fibers were located predominantly in the rostral part of the pineal gland and in the pineal stalk. Immunoreactive nerve fibers were found throughout the pineal gland, but the number of fibers in the caudal part of the gland was low. The fibers were present both in the perivascular spaces and between the pinealocytes. Many NPY-immunoreactive fibers were also located in the posterior and habenular commissures; some of these fibers were connected with the fibers in the rostral part of the mink pineal gland, indicating that at least some of the NPY-immunoreactive nerve fibers are of central origin. The nerve fibers immunoreactive to amidated NPY were distributed in a similar manner. However, the number of fibers immunoreactive to NPYamide was lower than the number of fibers immunoreactive to NPY itself. After removal of the superior cervical ganglia bilaterally 22 days or 12 months before sacrifice, NPY-immunoreactive nerve fibers remained in the gland. This immunohistochemical study of the mink pineal gland therefore shows that the NPY/NPYamide-immunoreactive nerve fibers innervating the pineal gland in this spegcies are a component of the central innervation or originnate from extracerebral parasympathetic ganglia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00313526
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