Comparative biochemistry and physiology. C: Comparative pharmacology最新文献

{"title":"Changes of iron content in eels (Anguilla japonica) infected with atypical Aeromonas salmonicida","authors":"Izuru Kakuta,&nbsp;Shiro Murachi","doi":"10.1016/0742-8413(93)90207-2","DOIUrl":"https://doi.org/10.1016/0742-8413(93)90207-2","url":null,"abstract":"<div><p>1. Hb, MCHC, Na, Ca, Mg and Cu in plasma decreased with atypical <em>Aeromonas salmonicida</em> infection. Whilst plasma K and NPN increased.</p><p>2. Plasma Fe decreased markedly with infection. No statistically significant change in UIBC was found, though moribund eels showed slightly lower values compared to that of the control. The rate of decrease in TIBC is similar to that in most elements in plasma.</p><p>3. Fe content in most tissues decreased with infection. It increased in the gills and head muscle (infection site). No significant change was found in the intestine.</p><p>4. Water content in various tissues increased with infection.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 275-278"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90207-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136597557","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Antitumor and antimicrobial glycoproteins from sea hares","authors":"Masatoshi Yamazaki","doi":"10.1016/0742-8413(93)90185-N","DOIUrl":"10.1016/0742-8413(93)90185-N","url":null,"abstract":"<div><p>1. Novel antitumor and antimicrobial glycoproteins were found in the sea hares. These glycoproteins were purified to apparent homogeneity from <em>Aplysia kurodai, Aplysia Juliana</em> and <em>Dolabella auricularia</em>, and designated as aplysianins, julianins and dolabellanins, respectively.</p><p>2. The nine isolated glycoproteins lysed all the tumor cells tested but did not lyse normal white and red blood cells.</p><p>3. The glycoproteins completely inhibited the synthesis of DNA and RNA by tumor cells within 2 hr and caused tumor lysis within 15hr.</p><p>4. Tumor lysis was inhibited by the presence of <em>N</em>-acetylneuraminic acid, suggesting that the recognition of the sugar moiety is a key step in the cytolysis by antitumor glycoproteins from sea hares.</p><p>5. These antitumor glycoproteins, except dolabellanin P, also showed antimicrobial activities.</p><p>6. The factors were active for Gram-positive and -negative bacteria and some fungi, and their action was not cytocidal but cytostatic.</p><p>7. They exerted the antibacterial action by inhibiting nucleic acid synthesis, as does a DNA-inhibiting chemotherapeutic drug.</p><p>8. The sequence of the <em>N</em>-terminal part of dolabellanin A was similar to other antibacterial peptides from arthropoda, amphibia and mammals, suggesting that dolabellanin-like antibacterial peptides are common throughout the animal kingdom.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 141-146"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90185-N","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19096860","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Neuropeptide-like substances in the retina of intact and tentaculectomized snails","authors":"Sylvie Magdelaine,&nbsp;Claude-Roland Marchand","doi":"10.1016/0742-8413(93)90204-X","DOIUrl":"https://doi.org/10.1016/0742-8413(93)90204-X","url":null,"abstract":"<div><p>1. Immunocytochemical investigations in normal and regenerated eyes of <em>Helix aspersa</em> Müller revealed a positive immunoreactivity toward antibodies directed against four biologically active peptides.</p><p>2. Eighty per cent of tentaculectomized animals regenerated all tentacular structures and the immunoreactivity was found to be identical in normal and regenerated retinas.</p><p>3. Type I photosensory cells are the only αMSH-positive structures, whereas the reactivity to the three other antibodies is localized in one (rarely two) retinal ganglion cell(s).</p><p>4. Using an elution technique, the colocalization of the three substances has been demonstrated in a unique ganglion cell.</p><p>5. These results seem to indicate that the α MSH-like substance(s) play(s) an important role in visual mechanisms, particularly in photoreception.</p><p>6. The colocalization of the three other substances in a unique ganglion cell suggests their probable crucial neuromodulatory and/or neurotransmitter function in rapid conduction of impulses to the brain.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 255-261"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90204-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136597559","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Binding of [3H]batrachotoxinin A-20-α-benzoate and [3h]saxitoxin to receptor sites associated with sodium channels in trout brain synaptoneurosomes","authors":"Jared G. Rubin,&nbsp;David M. Soderlund","doi":"10.1016/0742-8413(93)90200-5","DOIUrl":"10.1016/0742-8413(93)90200-5","url":null,"abstract":"<div><p>1. [³H]Batrachotoxinin A-20-α-benzoate ([³H]BTX-b) and [³H]saxitoxin ([³H]STX), radioligands that bind to distinct sites on the voltage-sensitive sodium channel, were bound specifically to saturable sites in rainbow trout (<em>Oncorhynchus mykiss</em>) brain synaptoneurosomes.</p><p>2. Specific [³H]BTX-B binding was temperature dependent with highest levels of specific [³H]BTX-B binding observed at 7°C. Specific binding was inversely correlated with assay temperature at temperatures above 7°C.</p><p>3. Saturating concentrations of scorpion (<em>Leiurus quinquestriatus</em>) venom (ScV) stimulated specific [³H]BTX-B binding at 27°C, but not at 7°C. The dihydropyrazole insecticide RH 3421 inhibited specific [³H]BTX-B binding at 7°C but had no effect on specific binding at 27°C. The sodium channel activators veratridine and aconitine and the local anesthetic dibucaine inhibited specific [³H]BTX-B binding at both 7°C and 27°C.</p><p>4. Displacement experiments in the presence of ScV at 27°C gave an equilibrium dissociation constant (<em>K</em>_{<span>d</span>}) for [³H]BTX-B of 710 nM and a maximal binding capacity (<em>B</em>_max) of 11.3 pmol/mg protein. Kinetic experiments established the rates of association (1.17 × 10⁵min⁻¹ nM⁻¹) and dissociation (0.0514min⁻¹) of the ligand-receptor complex.</p><p>5. The binding of [³H]STX reached apparent saturation at 7.5 nM. Scatchard analysis of the saturation data indicated a <em>K</em>_{<span>d</span>} of 3.8nM and a <em>B</em>_max of 1.9 pmol/mg protein.</p><p>6. These studies provide evidence for high affinity, saturable binding sites for [³H]BTX-B and [³H]STX in trout brain preparations. Whereas certain neurotoxins modified the specific binding of [³H]BTX-B in trout brain synaptoneurosomes in a predictable fashion, other compounds known to affect specific [³H]BTX-B binding in mammalian brain preparations had no effect on specific [³H]BTX-B binding in the trout.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 231-238"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90200-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19096848","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Hepatic vasopressin receptors (VPRs) exhibit species heterogeneity—absence of VPRs in sheep liver","authors":"John Howl,&nbsp;Mark Wheatley","doi":"10.1016/0742-8413(93)90202-V","DOIUrl":"10.1016/0742-8413(93)90202-V","url":null,"abstract":"<div><p>1. We have studied the binding characteristics of the hepatic VPRs expressed by rat, cow, pig, sheep and human and have demonstrated species heterogeneity.</p><p>2. These species differences are manifested as variation in the VPR capacity (rat &gt; cow &gt; pig &gt; human &gt; sheep), and in the affinity of these receptors for their natural ligand AVP (rat = human &gt; pig = cow).</p><p>3. A single class of VPRs, with high affinity for AVP, is present in rat, cow, human and pig liver. In contrast, ovine hepatocytes do not express a VPR.</p><p>4. The affinity of the V_1a-selective antagonist d(CH₂)₅Tyr(Me)²AVP is highly dependent on the species utilised, such that rat &gt; human &gt; cow.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 247-250"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90202-V","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19096849","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Micronuclei frequency in circulating erythrocytes from rainbow trout (Oncorhynchus mykiss) subjected to radiation, an image analysis and flow cytometric study","authors":"N. Schultz ,&nbsp;L. Norrgren,&nbsp;J. Grawé,&nbsp;A. Johannisson,&nbsp;Ö. Medhage","doi":"10.1016/0742-8413(93)90196-R","DOIUrl":"https://doi.org/10.1016/0742-8413(93)90196-R","url":null,"abstract":"<div><p>1. Rainbow trout (<em>Oncorhynchus mykiss</em>) were exposed to a single X-ray dose of 4Gy.</p><p>2. The frequency of micronuclei in the peripheral erythrocytes was investigated at regular intervals up to 58 days after the exposure.</p><p>3. A flow cytometric method and a semi-automatic image analysis method were used to estimate the micronuclei frequency.</p><p>4. The results show that both methods can detect an increased frequency of micronuclei in peripheral erythrocytes from exposed fish.</p><p>5. However, the semi-automatic image analysis method was the most stable and sensitive.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 207-211"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90196-R","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136597563","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fish electroreception as a model for vincristine-induced neuropathies and a possible preventive role for Org 2766 treatment","authors":"I.S.A. Neuman,&nbsp;P.S. Heijmen,&nbsp;R.C. Peters,&nbsp;G.S.F. Ruigt","doi":"10.1016/0742-8413(93)90189-R","DOIUrl":"https://doi.org/10.1016/0742-8413(93)90189-R","url":null,"abstract":"<div><p>1. Subcutaneous injection of vincristine (more than 3 μg) in the catfish, <em>Ictalurus nebulosus</em>, produces a black spot on the skin with a grey surround. Doses between 1 and 3 μg give a less pronounced discolouration.</p><p>2. Two to three days after injection of 5 μg vincristine, repetitive activity is detected in primary afferents of unstimulated electroreceptor organs close to the site of injection.</p><p>3. Vincristine increases the phase-lag of the modulation of afferent activity in electroreceptor organs during electrical stimulation without a clear effect on the sensitivity of catfish electroreceptor organs.</p><p>4. The amplitude of the action potentials of the primary afferents begins to decrease after 2 days; after</p><p>3 days they gradually disappear in the background noise.</p><p>5. Application of Org 2766, a potentially neurotrophic compound, at 2 days, but not 1 day, before vincristine application prevents vincristine effects on the phase shift.</p><p>6. Preliminary electron-microscopical studies of the synapse shows a severe depletion of glycogen granules in the afferent nerve fibre after vincristine application,</p><p>7. It is concluded that electroreceptor organs can be used to study neuropathies caused by vincristine, and that Org 2766 may be useful for preventive treatment of such neuropathies.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 165-173"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90189-R","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136598189","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"4',6-diamidino 2-phenylindole is a new reversible inhibitor of diamine oxidase and S-adenosyl-l-methionine decarboxylase from mammalian tissues","authors":"C. Cubría ,&nbsp;M. Alvarez-Bujidos ,&nbsp;A. Negro ,&nbsp;R. Balaña-Fouce ,&nbsp;D. Ordóñez","doi":"10.1016/0742-8413(93)90203-W","DOIUrl":"10.1016/0742-8413(93)90203-W","url":null,"abstract":"<div><p>1. 4',6-Diamidino-2-phenylindole is a powerful reversible inhibitor of porcine kidney diamine oxidase and partially purified rabbit liver <span><math><mtext>S-</mtext><mtext>adenosyl-</mtext><mtext>L</mtext><mtext>-methionine</mtext></math></span> decarboxylase.</p><p>2. This diamidine has shown to be a competitive inhibitor of porcine kidney diamine oxidase with a <em>Ki</em> value of 13μM.</p><p>3. A similar inhibitory pattern has been found on rat liver <span><math><mtext>S-</mtext><mtext>adenosyl-</mtext><mtext>L</mtext><mtext>-methionine</mtext></math></span> decarboxylase with an estimated <em>Ki</em> of 21 μM.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 251-254"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90203-W","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19096850","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effects of acute exposure to cadmium (II) chloride and lead (II) chloride on the haematological profile of Oreochromis aureus (Steindachner)","authors":"Paul Allien","doi":"10.1016/0742-8413(93)90197-S","DOIUrl":"https://doi.org/10.1016/0742-8413(93)90197-S","url":null,"abstract":"<div><p>1. <em>Oreochromis aureus</em> (Steindachner) was exposed to two concentrations of lead and cadmium for 24 hr and 1 week to assess the effects of these pollutants on haematological parameters.</p><p>2. Plasma osmolality was found to be the most sensitive blood parameter, affected before other parameters changed.</p><p>3. Cadmium appears to be more toxic to <em>O. aureus</em> than lead, having an adverse effect on blood parameters earlier than lead.</p><p>4. In the earlier stages of toxicity cadmium appears to have a more pronounced effect on haemoglobin concentration than lead.</p><p>5. Cadmium does not depress erythrocyte counts but lead does.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 213-217"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90197-S","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136597562","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The role of biogenic amines in the control of blood glucose level in the decapod crustacean, Carcinus maenas L.","authors":"Walter Lüschen,&nbsp;Axel Willig,&nbsp;Peter P. Jaros","doi":"10.1016/0742-8413(93)90210-C","DOIUrl":"https://doi.org/10.1016/0742-8413(93)90210-C","url":null,"abstract":"<div><p>1. Administration of biogenic amines into intact <em>Carcinus maenas</em> induces dose- and timedependent elevation of hemolymph glucose level.</p><p>2. Removal of the neurosecretory centre containing the crustacean hyperglycemic hormone (CHH) by ablation of the eyestalks did not induce hypoglycemia.</p><p>3. Injection of dopamine (DA) into eyestalkless crabs showed no hyperglycemic effect, while serotonin (5-HT), epinephrine (E), norepinephrine (NE), and octopamine (OA) elevated glucose levels.</p><p>4. The dopaminergic effect was significantly reduced by administration of trifluoperazine (TFP).</p><p>5. 5-HT and OA were found to be strong elevators of glucose levels, while the other biogenic amines had moderate effects only.</p><p>6. The results indicate, that DA exerts its hyperglycemic effect by stimulating the release of CHH from the eyestalk neurosecretory centre. Elevation of hemolymph glucose level by 5-HT, OA, E, and NE, occurs independently of CHH.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 291-296"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90210-C","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136596944","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}