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

{"title":"The physiological action of analogues of philanthotoxin-4.3.3 at insect nicotinic acetylcholine receptors","authors":"J.A. Benson ,&nbsp;L. Kaufmann,&nbsp;B. Hue ,&nbsp;M. Pelhate ,&nbsp;F. Schürmann,&nbsp;L. Gsell,&nbsp;T. Piek","doi":"10.1016/0742-8413(93)90212-4","DOIUrl":"https://doi.org/10.1016/0742-8413(93)90212-4","url":null,"abstract":"<div><p>1. The blocking action of δ-philanthotoxin (PhTX-4.3.3), a polyamine amide wasp toxin, and 33 structural analogues was studied at the nicotinic acetylcholine receptor of isolated neuronal somata from locust thoracic ganglia and at the cockroach cercal nerve-giant interneuron nicotinic cholinergic synapse.</p><p>2. A comparison of the structure-activity relationships reported here for the locust somal and cockroach synaptic nicotinic receptors and for the glutamatergic neuromuscular synapses of housefly larvae reported previously suggests a generally similar pharmacology for the channel-blocking action at ligand-activated ion channels, but with differences that might be due to variation in accessibility between synaptic receptors and those on the neuronal somata or to genuine divergence in ligand-activated ion channel pharmacology.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 303-310"},"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)90212-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136596943","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":"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":"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":"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":"Histamine: Its metabolism and localization in mammary gland","authors":"Czeslaw Maslinski ,&nbsp;Danuta Kierska ,&nbsp;Wieslawa Agnieszka Fogel ,&nbsp;Anu Kinnunen ,&nbsp;Pertti Panula","doi":"10.1016/0742-8413(93)90206-Z","DOIUrl":"10.1016/0742-8413(93)90206-Z","url":null,"abstract":"<div><p>1. Mammary gland of mouse (<em>Mus musculus</em>), rat (<em>Rattus rattus</em>), guinea pig (<em>Cavia porcellus</em>), cow (<em>Bos taurus</em>) and pig (<em>Sus scrofa</em>) contains different but always high concentrations of histamine.</p><p>2. Generally, the tissue histamine is localized in mast cells, although non-mast cell histamine immuno-reactivity is also present in mammary glands of the mouse, cow and pig. No histamine immunoreactive nerves could be detected.</p><p>3. Mammary glands are able to synthesize and inactivate histamine; the activity of specific histidine decarboxylase and at least one of the catabolizing enzyme could be demonstrated.</p><p>4. Histamine fulfils basic criteria for being involved in physiological function of mammary glands.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 269-273"},"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)90206-Z","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19096851","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}