PHARMACOLOGICAL STUDIES ON THE STIMULATION OF THE PHOSPHOLIPASE A2-ACYLATION SYSTEM OF SYNAPTIC MEMBRANES OF BRAIN, BY NEUROTRANSMITTERS AND OTHER AGONISTS

Methacholine, nicotine and succinylcholine stimulated the phospholipase A2-acylation system of synaptic membranes isolated from the cerebral cortex of guinea pig. Stimulation by acetylcholine was partially blocked by atropine and by D-tuberocurarine respectively, indicating both muscarinic and nicotinic stimulation. Muscarinic stimulation by acetylcholine was greater than -isotinic stimulation, and stimulation by acetylcholine was completely blocked by a combip, or;. and n-tuberocurarine. The phospholipase A2-acylat tem was stimulated by phenylcphrine., id. Cqxoterenoi. Stimulation by noradrenaline was J-. tidlr, by phenoxybenzamine and pindalol i:spectively, indicating both 8-adrenergic and P-adrenergic ztimulation. n-Adrenergic stimulation by noradrenaline was greater than P-adrenergic-stimulation. 5 -mlation by noradrenaline was completely blocked by a combination of phenoxybenzamins and pindalol. Stimulation of both acylation and phospholipid hydrolysis, by 5-hydroxytryptamine and histamine were partially blocked by methysergide and diphenhydramine respectively. Stimulation by dopamine was blocked by halopcridol. Stimulation by y-aminobutyric acid was partially blocked by strychnine and by picrotoxin. Dichloroisoproterenol, atropine, methysergidr, diphenhydramine, strychnine, picrotoxin and eserine, at relatively high concentrations (1 mM), stimuhted the phospholipase A2-acylation system. Synergistic stimulations of both acylatior, and hydrolysis of phosphatidylcholine, were observed by adenosine combined with noradrenaline, 5-hydroxytryptamine, histamine, dopamine or yaminobutyric acid, respectively. In the presence of ATP-MgCI, synergistic stimulations of the hydrolysis of phosphatidyicholine were observed after 30 s by noradrenaline combined with 5-hydroxytryptamine, histamine, dopamine, aminobutyric acid or carbamoylcholine respectively. In the presence of GTP-MgC12 synergistic stimulations were obtained by cdrbamoylcholine combined with noradrenaline. 5-hydroxytryptamine. histamine, dopamine or y-aminobutyric acid, respectively. In the presence of ATP-MgC12 plus GTP-MgC12, stimulation by noradrenaline and one other agonist including 5-hydroxytryptamine, histamine, dopamine, y-aminobutyric acid or carbamoylcholine were close to additive.     

植物生长调节物质IP－1号对木薯产量及其生物性状的影响

１９９０和１９９１年在木薯（ＭａｎｉｈｏｔｅｓｃｕｌｅｎｔａＣｒａｎｔｚ）生长期以植物生长调节物质ＩＰ－１号０,２０,３０和４０ｐｐｍ进行叶面喷洒,结果表明：３０ｐｐｍ处理可使木薯块根产量平均增加５４．４４％,块根淀粉含量平均提高２０．８１％。单株最大薯重提高３１．５５％,块根数增加２１．１７％,块根长度增长１７．６２％,地上部鲜重增加３４．３６％,植株高度增加４．３６％,植株收获期保留青叶数增加１９．４２％,主茎直径增加６．２６％,块根直径增加２．５８％,叶片的叶绿素和蛋白质含量分别提高５．５７％和２５．９６％,叶片光合作用强度提高１５．８６％,而对主茎高度、主茎节数没有明显影响。     

Reviews of publications

Book reviewed in this article:
The Voyage of Charles Darwin: His Autobiographical writings, selected and arranged by Christopher Railing.
Penguin Nature Guides: Fungi of Northern Europe, Vols I & II, by S. Nilsson &; O. Persson; illustrated by B. Mossberg
Penguin Nature Guides: Plant Communities, by Anned Biilow-Olsen, illustrated by Susanne Larsen; translated from the Danish by Joan Tate; edited and adapted by Francis Rose.
Penguin Nature Guides: Fishes of the British and Northern European Seas, by J. Moller Christensen; illustrated by Bente Nystrom; translated from the Danish by Gwynne Vevers; edited and adapted by Gwynne Vevers and Philip Orkin.
Birds of Wood, Park and Garden, text and illustrations by Lars Jonsson; translated from the Swedish by Roger Tanner
Birds of Sea and Coast, text and illustrations by Lars Jonsson; translated from the Swedish by Roger Tanner     

Reviews of publications

Principles of Crop Improvement, by N. W. Simmonds
Marine Organisms – Genetics, Ecology & Evolution, edited by B. Battaglia & J. A. Beardrnore
Arthropod Phytogeny, edited by A. P. Gupta. Van Nostrand Reinhold
Field Guide to the Land Snails of Britain and North-west Europe, by M. P. Kernev & R. A. D. Cameron; illustrated by Gordon Riley
Key to the Fishes of Northern Europe, by Alwync Wheeler; illustrated by Peter Stebbing; maps by F. Rodney Fraser
Penguin Nature Guides: The Biology of Flowers, by Eigil Holm; illustrated by Thomas BredsdorfT; translated by Joan Tate; edited & adapted by Ronald Melville
Penguin Nature Guides: Orchids of Northern Europe, by Sven Nilsson; illustrated by Bo Mossberg; edited & adapted by P. Francis Hunt
A New Look at the Dinosaurs, by Alan Charig. Heinemann     

Reviews of Publications

Book reviewed in this article:
Flowers of the Himalaya , by Oleg Polunin and Adam Stainton.
A Guide to the Vegetation of Britain and Europe , by Oleg Polunin and Martin Walters.
The Experimental Biology of Bryophytes, edited by A. F. Dyer & J. G. Duckett.
A Birdwatcher's Miscellany, edited by Rob Hume.
The Moths and Butterjlies of Great Britain and Ireland, Volume 10, Noctuidae (Part II) and Agaristidae, edited by J. Heath.
Atlas of Butterjlies in Britain and Ireland, by J. Heath, E. Pollard & J. A. Thomas.
Colour Identification Guide to Butterjlies of the British Isles, revised edition by T. G. Howarth.
The World of Butterjlies, An Illustrated Encyclopaedia, by V. Sbordoni & S.Forestiero.
Colour Identijcation Guide to Moths of the British Isles, by Bernard Skinner.
The Biology of Buttegies, edited by R. I. Vane-Wright & P. R. Ackery.
Australian Grasses, by Nancy T. Burbidge, revised by Surrey W. L. Jacobs.
Collins Guide to Grasses, Sedges, Rushes and Ferns, by R. Fitter & A. Fitter. Collins.
Grasses of the Soviet Union, by N. N. Tsvelev, edited by A. A. Fedorov.
The European Garden Flora, Volume 2, Monocotyledons (Part ZZ), edited by S. M Walters et al.
Grasses, 3rd edition, by C. E. Hubbard, revised by J. C. E. Hubbard.     

Involvement of transforming growth factor-alpha secreted by macrophages in metallothionein induction by endotoxin

The mechanism of metallothionein (MT) induction of the liver by endotoxin, which is mediated by a factor secreted by endotoxin-stimulated macrophages, was studied in vitro. MT induction of the liver cells by the endotoxin-stimulated macrophage conditioned medium was inhibited by a monoclonal antiepidermal growth factor (EGF) / transforming growth factor-alpha (TGF-alpha) receptor antibody, which acts as an antagonist of EGF and TGF-alpha. MT was induced by the substance, which was adsorbed by polyclonal antibody to TGF-alpha, but not by a monoclonal antibody to EGF, in the conditioned medium of endotoxin-stimulated macrophages. These results suggest that TGF-alpha secreted by macrophages is involved in MT induction by endotoxin.     

Effect of acetaldehyde and cyanamide on the metabolism of formaldehyde by hepatocytes, mitochondria, and soluble supernatant from rat liver

Formaldehyde can be metabolized primarily by two different pathways, one involving oxidation by the low-Km mitochondrial aldehyde dehydrogenase, the other involving a specific, glutathione-dependent, formaldehyde dehydrogenase. To estimate the roles played by each enzyme in formaldehyde metabolism by rat hepatocytes, experiments with acetaldehyde and cyanamide, a potent inhibitor of the low-Km aldehyde dehydrogenase were carried out. The glutathione-dependent oxidation of formaldehyde by 100,000g rat liver supernatant fractions was not affected by either acetaldehyde or by cyanamide. By contrast, the uptake of formaldehyde by intact mitochondria was inhibited 75 to 90% by cyanamide. Acetaldehyde inhibited the uptake of formaldehyde by mitochondria in a competitive fashion. Formaldehyde was a weak inhibitor of the oxidation of acetaldehyde by mitochondria, suggesting that, relative to formaldehyde, acetaldehyde was a preferred substrate. In isolated hepatocytes, cyanamide, which inhibited the oxidation of acetaldehyde by 75 to 90%, produced only 30 to 50% inhibition of formaldehyde uptake by cells as well as of the production of 14CO2 and of formate from [14C]formaldehyde. The extent of inhibition by cyanamide was the same as that produced by acetaldehyde (30-40%). In the presence of cyanamide, acetaldehyde was no longer inhibitory, suggesting that acetaldehyde and cyanamide may act at the same site(s) and inhibit the same formaldehyde-oxidizing enzyme system. These results suggest that, in rat hepatocytes, formaldehyde is oxidized by cyanamide- and acetaldehyde-sensitive (low-Km aldehyde dehydrogenase) and insensitive (formaldehyde dehydrogenase) reactions, and that both enzymes appear to contribute about equally toward the overall metabolism of formaldehyde.     

Relationship between ion requirements for respiration and membrane transport in a marine bacterium.

Intact cells of the marine bacterium Alteromonas haloplanktis 214 oxidized NADH, added to the suspending medium, by a process which was stimulated by Na+ or Li+ but not K+. Toluene-treated cells oxidized NADH at three times the rate of untreated cells by a mechanism activated by Na+ but not by Li+ or K+. In the latter reaction, K+ spared the requirement for Na+. Intact cells of A. haloplanktis oxidized ethanol by a mechanism stimulated by either Na+ or Li+. The uptake of alpha-aminoisobutyric acid by intact cells of A. haloplanktis in the presence of either NADH or ethanol as an oxidizable substrate required Na+, and neither Li+ nor K+ could replace it. The results indicate that exogenous and endogenous NADH and ethanol are oxidized by A. haloplanktis by processes distinguishable from one another by their requirements for alkali metal ions and from the ion requirements for membrane transport. Intact cells of Vibrio natriegens and Photobacterium phosphoreum oxidized NADH, added externally, by an Na+-activated process, and intact cells of Vibrio fischeri oxidized NADH, added externally, by a K+-activated process. Toluene treatment caused the cells of all three organisms to oxidize NADH at much faster rates than untreated cells by mechanisms which were activated by Na+ and spared by K+.     

A prothrombinase complex of mouse peritoneal macrophages

Addition of prothrombin to mouse peritoneal macrophages in vitro resulted in the formation of a thrombin-like enzyme, as demonstrated by use of the luminogenic peptide substrate S-2621. The prothrombinase activity was sedimented by high-speed centrifugation following homogenization of the cells and was abolished by treatment of the cells with the nonionic detergent Triton X-100 at 0.02% concentration. Moreover, the activity was drastically reduced by maintaining cultures in the presence of warfarin and, presumably due to competitive substrate inhibition, by adding S-2222, a chromogenic peptide substrate for Factor Xa. These findings suggest that prothrombin cleavage is catalyzed by Factor Xa at the macrophage surface. The generated thrombin was inhibited by antithrombin, and this reaction was accelerated by heparin with high affinity for antithrombin but not by the corresponding oligosaccharides composed of 8-14 monosaccharide units. Such oligosaccharides which are capable of accelerating the inactivation of Factor Xa by antithrombin, inhibited thrombin formation from prothrombin in the macrophage cultures, presumably by promoting inactivation by antithrombin of Factor Xa in a prothrombinase complex. Activation of the macrophage coagulation system, as proposed to occur in certain inflammatory conditions, thus may be modulated at various levels by heparin, or heparin oligosaccharides, released from mast cells.     

Reviews of publications

Book reviewed in this article:
Taxonomy of Economic Seaweeds: With reference to some Pacific and Caribbean Species, 2 edited by Isabella A. Abbott. La Jolla
Botanic Gardens and the World Conservation Strategy edited by D. Bramwell, O. Hamann, V. Heywood & H. Synge
Introduction to Ecological Biochemistry 3rd ed., by J. B. Harborne
A monographic study of the genus Rosularia (Crassulaceae) by Urs Eggli
The Photographic Guide to Identify Mediterranean Wild Flowers by Roger Phillips assisted by Martin Rix and Nicky Fox
The Photographic Guide to Identify Mediterranean Wild Flowers by Roger Phillips assisted by Martin Rix and Nicky Fox
Conserving the Wild Relatives of Crops by Erich Hoyt.
Somatic Cell Genetics of Woody Plants edited by M. R. Ahuja
Indian Journal of Natural Rubber Research
Dictionary of Weeds of Eastern Europe by G. Williams and K. Hunyadi
Nutrition of the Angiosperm Embryo by David R. Murray.
Plant Pigments edited by T. W. Goodwin.
Panbiogeography edited by R. Craw & G. Sermonti
Saxifrages of Europe: with notes on African, American and some Asiatic species by D. A. Webb & R. J. Gornall     

Metallothionein inhibits peroxynitrite-induced DNA and lipoprotein damage

Previous studies have demonstrated that metallothionein functions as an antioxidant that protects against oxidative DNA, protein, and lipid damage induced by superoxide anion, hydrogen peroxide, hydroxyl radical, and nitric oxide. The present study was undertaken to test the hypothesis that metallothionein also protects from DNA and lipoprotein damage induced by peroxynitrite, an important reactive nitrogen species that causes a diversity of pathological processes. A cell-free system was used. DNA damage was detected by the mobility of plasmid DNA in electrophoresis. Oxidation of low density lipoprotein was measured by a thiobarbituric acid-reactive substance, which was confirmed by lipid hydroperoxide assay. Plasmid DNA damage and low density lipoprotein oxidation were induced by 3-morpholinosydnomine, which produces peroxynitrite through the reaction between nitric oxide and superoxide anion or by synthesized peroxynitrite directly. DNA damage by 3-morpholinosydnomine was prevented by both metallothionein and superoxide dismutase, whereas the damage caused by peroxynitrite was prevented by metallothionein only. The oxidation of low density lipoprotein by 3-morpholinosydnomine and peroxynitrite was also significantly inhibited by metallothionein. This study thus demonstrates that metallothionein may react directly with peroxynitrite to prevent DNA and lipoprotein damage induced by this pathological reactive nitrogen species.     

Regulation of ascorbic acid and of xylulose synthesis in rat-liver extracts. The effect of starvation on the enzymes of the glucuronic acid pathway

1. Control of enzyme formation has been examined in the pathways degrading mandelate and p-hydroxymandelate in Pseudomonas fluorescens. 2. The first three enzymes form a group which is common to both pathways and which is co-ordinately induced or repressed. The genes controlling these enzymes are assumed to form a ;regulon'. This group of enzymes is induced by mandelate or p-hydroxymandelate and repressed by benzoate and by p-hydroxybenzoate (the immediate end products resulting from the action of this group of enzymes). 3. Repression is independently exerted by end products of enzymes controlled by succeeding regulons, i.e. by catechol, by protocatechuate and finally by succinate and acetate. 4. The pattern is repeated further along the pathway, so that benzoate oxidase (controlled by the second regulon) is repressed by its immediate end product, catechol, and again by succinate and acetate. 5. Pyrocatechase, an enzyme controlled by the third regulon, is repressed by succinate and acetate. 6. There is a parallel system of multi-sensitive repression mechanisms controlling production of the enzymes that degrade the hydroxy compounds. Again, the enzymes of each regulon are repressed by the immediate end product of their action and by the end products of each succeeding group of enzymes. 7. Repressor activity appears to be exerted by compounds that are likely to occur as such in the external environment or that occur at points of convergence of the degradative pathways of the cell. 8. The net effect of this control system, involving both induction and end-product repression, appears to be that cells will not form inducible degradative enzymes if the end products are already being supplied from without or are being produced by degradation of some alternative source of carbon and energy.     

Isolation of dicarboxylic acid- and glucose-binding proteins from Pseudomonas aeruginosa.

Inducible binding proteins for C4-dicarboxylic acids (DBP) and glucose (GBP) were isolated from Pseudomonas aeruginosa by extraction of exponential-phase cells with 0.2 M MgC12 (pH 8.5) and by an osmotic shock procedure without affecting cell viability. DBP synthesis was induced by growth on aspartate, alpha-ketoglutarate, succinate, fumarate, malate, and malonate but not by growth on acetate, citrate, pyruvate, or glucose. Binding of succinate by DBP was competitively inhibited by 10-fold concentrations of fumarate and malate but not by a variety of related substances. GBP synthesis and transport of methyl alpha-glucoside by whole cells were induced by growth on glucose or pyruvate plus galactose, 2-deoxyglucose, or methyl alpha-glucoside but not by growth on gluconate, succinate, acetate, or pyruvate. The binding of radioactive glucose by GBP was significantly inhibited by 10-fold concentrations of glucose, galactose, and glucose-1-phosphate but not by the other carbohydrates tested. The binding of glucose by GBP or succinate by DBP did not result in any chemical alteration of the substrates.     

大鼠仙台病毒ELISA、间接免疫荧光和免疫印迹三种检测方法比较

目的比较ELISA（enzyme-linked immunosorbent assay）、IFA（immuno-fluorescence assay）和WB（Western blot）三种方法在大鼠仙台病毒血清学检测中的差异。方法仙台病毒蛋白抗原经凝胶电泳分离转移后用于血清学检测的WB方法;使用IFA、ELISA方法对20份无菌大鼠、227份SPF大鼠以及63份清洁级大鼠送检血清样品进行检测,阳性及可疑样品用WB方法进行了验证。结果 20份无菌大鼠血清样品被3种方法检测为仙台病毒抗体阴性;SPF级大鼠样品被IFA方法判定为阴性,1.32%（3/227）被ELISA方法判定为阳性,其中有2/3被WB确认为阳性;ELISA、IFA和WB在清洁级大鼠样品中检出仙台病毒的阳性率分别为为18.12%、11.34%和15.87%。结论三种检测方法灵敏度从高到低依次为ELISA、WB和IFA。WB方法可作为IFA和ELISA难以确定结果的替代方法。     

Scientific Report on the Belgian Expedition to The Great Barrier Reef in 1967. Nematodes V Observations on Desmoscolex (Nematoda, Desmoscolecida) with description of three new species

Three new species of Desmoscolex , found in samples from Yonge Reef, Lizard Island, Nymphe Island and between One Tree Isles and Wistari Reef are described: D. australiens sp.n., characterized by the head-shape with naked semi-circular anterior part, by the jointed cephalic setae inserted close to the anterior extremity and by the shape of the gubernaculum with less sclerotized proximal part; D. membranosas sp.n. close to D. granulatus Decraemer, 1974, but differing from it by the presence of a partly disconnected circumoral membrane and by the oval amphids not reaching the extreme anterior end; D. yongei sp.n. resembling D. americanus Chitwood, 1936, but differing from it by the longer and more slender spicules, by the presence of fine spines on the secondary rings, by the head-shape without a truncated anterior end and by the almost circular amphids.     

Effect of maleimide derivatives on superoxide-generating system of guinea-pig neutrophils stimulated by different soluble stimuli

The effect of modification of maleimide derivatives on superoxide production by guinea-pig neutrophils induced by a variety of different soluble stimuli was studied. Pretreatment of neutrophils by showdomycin, a very slowly penetrating-SH reagent, did not affect superoxide production by all of the stimuli used, suggesting no exposure of sulfhydryl groups involved in superoxide-generating system on the cell surface. Pretreatment with N-ethylmaleimide (MalNEt), a considerably penetrating-SH reagent, markedly inhibited superoxide production stimulated by formyl-methionyl-leucyl-phenylalanine (HCO-Met-Leu-Phe), cytochalasin E or digitonin, but not superoxide production stimulated by the ionophore A23187 or sodium fluoride. The oxygen consumption stimulated by HCO-Met-Leu-Phe or cytochalasin E was inhibited by MalNEt pretreatment, whereas the oxygen consumption stimulated by A23187 was not inhibited by MalNEt. The inhibition by MalNEt of superoxide production did not appear to be due to the interference with binding of the affected stimuli, since MalNEt pretreatment did not inhibit the release of lysozyme, granule enzyme, induced by HCO-Met-Leu-Phe, cytochalasin E or digitonin. Particulate fractions from MalNEt-pretreated neutrophils before exposure to the stimulus exhibited the inhibition of the enhancement of NADPH-dependent superoxide production induced by HCO-Met-Leu-Phe, cytochalasin E or digitonin, but not A23187, whereas treatment of neutrophils with MalNEt after activation by these stimuli had no effect on the NADPH oxidase activity in particulate fractions. Direct exposure of particulate fractions from A23187-stimulated neutrophils to MalNEt showed no actual susceptibility of NADPH oxidase to MalNEt inhibition. These findings suggest that the inhibitory effect of MalNEt is caused by the modification of the process of the activation by the affected stimuli of the superoxide system, probably NADPH oxidase and that at least two mechanisms exist for activation of superoxide-generating system in guinea-pig neutrophils on the basis of the susceptibility to MalNEt inhibition.     

The regulation of rat liver tryptophan pyrrolase activity by reduced nicotinamide-adenine dinucleotide (phosphate). Experiments with glucose and nicotinamide.

1. Chronic administration of glucose or nicotinamide in drinking water inhibits the activity of rat liver tryptophan pyrrolase, and subsequent withdrawal causes an enhancement. The enzyme activity is also inhibited by administration in drinking water of sucrose, but not fructose, which is capable of preventing the glucose effect. 2. The inhibition by glucose or nictinamide is not due to a defective apoenzyme synthesis nor a decreased cofactor availability. 3. The inhibition by nicotinamide is reversed by regeneration of liver NAD+ and NADP+ in vivo by administration of fructose, pyruvate or phenazine methosulphate. Inhibition by glucose is also reversed by the above agents and by NH4Cl. Reversal of inhibition by glucose or nicotinamide is also achieved in vitro by addition of NAD+ or NADP+. 4. Glucose or nicotinamide increases liver [NADPH]. [NADP+] is also increased by nicotinamide. [NADPH] is also increased by sucrose, but not by fructose, which prevents the glucose effect. Phenazine methosulphate prevents the increase in [NADPH] caused by both glucose and nicotinamide. 5. It is suggested that the inhibition of tryptophan pyrrolase activity by glucose or nicotinamide is mediated by both NADPH and NADH.     

Modern and fossil traces in terrestrial lithic substrates

A number of biogenic processes leads to the formation of distinctive traces in terrestrial lithic substrates. These include: burrowing by vertebrates in moderately lithified rocks; scraping by mammals; smoothing and polishing of limestone surfaces by the locomotion of mammals; excavation by bees, wasps, and ants producing nesting and dwelling tunnels; dissolution of limestone surfaces by terrestrial snails; endolithic activity of fungi, algae, and lichens on subaerial rock surfaces; root corrosion; etc. Processes of biochemical weathering, biophysical erosion, and enlargement of cracks and fissures by the pressure of plant roots do not leave distinctive traces and therefore lie outside the ichnological realm. The fossil preservation of terrestrial bioerosional traces is expected to be uncommon. Nevertheless, various possible means of preservation must be considered, such as by rapid burial by volcanic material, by fluvial sediments, by travertine or tufa, by loess, “conservation”; in caves, case hardening of surfaces of porous rocks, and preservation of subsoil traces below fossil soils.     

Acetaldehyde-mediated hepatic lipid peroxidation: role of superoxide and ferritin

Evidence in alcoholics as well as in experimental models support the role of hepatic lipid peroxidation in the pathogenesis of alcohol-induced liver injury, but the mechanism of this injury is not fully delineated. Previous studies of the metabolism of ethanol by alcohol dehydrogenase revealed iron mobilization from ferritin that was markedly stimulated by superoxide radical generation by xanthine oxidase. Peroxidation of hepatic lipid membranes (assessed as malondialdehyde production) was studied during in vitro alcohol metabolism by alcohol dehydrogenase. Peroxidation was initiated by acetaldehyde-xanthine oxidase, stimulated by ferritin, and inhibited by superoxide dismutase or chelation or iron with desferrioxamine. In conclusion, lipid peroxidation may be initiated during the metabolism of ethanol by alcohol dehydrogenase by an iron-dependent acetaldehyde-xanthine oxidase mechanism.