{"title":"A quantitative immunocytochemical approach to the analysis of type I cells in the cat carotid body.","authors":"J Major, B Dinger, L J Stensaas, Z Z Wang","doi":"10.1159/000014611","DOIUrl":"https://doi.org/10.1159/000014611","url":null,"abstract":"<p><p>Digital image analysis of immunostained semithin plastic sections indicates that experimentally induced changes in levels of transmitter-related reaction product in single cells fails to support the concept of clearly defined subsets of type I cells in the carotid body. This objective approach to the quantitation of staining product on a cell-by-cell basis appears to indicate that the observed changes are related to global shifts in the expression of a given neuronal marker throughout a single population of highly labile chemoreceptor elements.</p>","PeriodicalId":79565,"journal":{"name":"Biological signals and receptors","volume":"8 6","pages":"375-81"},"PeriodicalIF":0.0,"publicationDate":"1999-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000014611","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21449446","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":"Cyclic nucleotide-gated channel activation is not required for activity-dependent labeling of zebrafish olfactory receptor neurons by amino acids.","authors":"W C Michel","doi":"10.1159/000014607","DOIUrl":"https://doi.org/10.1159/000014607","url":null,"abstract":"<p><p>The olfactory epithelium of fish is heterogeneous both with respect to the types of receptor cells (ORNs) present and the families of odorant receptors expressed in these cells. As a consequence of this diversity, the transduction cascade(s) activated by odorants has yet to be unambiguously established. In the current study, electrophysiological and activity-dependent labeling techniques were used to assess the role of the cyclic nucleotide-gated channel in zebrafish olfactory transduction. Both amino acid and bile salt odorants elicited robust electrophysiological responses, however, activity-dependent labeling of ORNs could be stimulated only by the amino acid odorants. An adenylate cyclase (AC) activator (forskolin) and a phosphodiesterase inhibitor (3-isobutyl-1-methylxanthine, IBMX) also elicited robust electrophysiological responses; generally larger than the responses elicited by either the amino acid or bile salt odorants. However, neither forskolin alone or a mixture of forskolin and IBMX stimulated activity-dependent labeling. Bathing the olfactory epithelium with forskolin, which presumably increased the intracellular concentration of cAMP, reduced the responses to bile salt odorants to a significantly greater extent than amino acid odorants. Collectively, these findings suggest that the transduction of amino acid input does not rely primarily on cyclic nucleotide-gated (CNG) channel activation and that CNG channel activation may be required for the transduction of bile salt input.</p>","PeriodicalId":79565,"journal":{"name":"Biological signals and receptors","volume":"8 6","pages":"338-47"},"PeriodicalIF":0.0,"publicationDate":"1999-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000014607","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21450256","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":"Calcium signalling in squid olfactory receptor neurons.","authors":"D R Piper, M T Lucero","doi":"10.1159/000014606","DOIUrl":"10.1159/000014606","url":null,"abstract":"<p><p>Isolated squid olfactory receptor neurons respond to dopamine and betaine with hyperpolarizing conductances. We used Ca(2+) imaging techniques to determine if changes in intracellular Ca(2+) were involved in transducing the hyperpolarizing odor responses. We found that dopamine activated release of Ca(2+) from intracellular stores while betaine did not change internal Ca(2+) concentrations. Application of 10 mM caffeine also released Ca(2+) from intracellular stores, suggesting the presence of ryanodine-like receptors. Depletion of intracellular stores with 100 microM thapsigargin revealed the presence of a Ca(2+) store depletion-activated Ca(2+) influx. The influx of Ca(2+) through the store-operated channel was reversibly blocked by 10 mM Cd(2+). Taken together, these data suggest a novel odor transduction system in squid olfactory receptor neurons involving Ca(2+) release from intracellular stores.</p>","PeriodicalId":79565,"journal":{"name":"Biological signals and receptors","volume":"8 6","pages":"329-37"},"PeriodicalIF":0.0,"publicationDate":"1999-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21450305","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}
Z Z Wang, L He, J Chen, B Dinger, L Stensaas, S Fidone
{"title":"Protein phosphorylation signaling mechanisms in carotid body chemoreception.","authors":"Z Z Wang, L He, J Chen, B Dinger, L Stensaas, S Fidone","doi":"10.1159/000014610","DOIUrl":"https://doi.org/10.1159/000014610","url":null,"abstract":"<p><p>Chemotransduction in the carotid body occurs in specialized type I cells and likely involves a complex series of regulated events which culminates in the release of neurotransmitter agents and the excitation of afferent nerve fibers. Previous studies have shown that multiple factors, including the levels of calcium and cyclic nucleotide second messengers, are important regulators of the chemoreceptor transduction cascade in type I cells. In addition, increases in electrical excitability induced in type I cells by chronic exposure to hypoxia are mimicked by agents which elevate intracellular cyclic AMP levels [Stea et al., J Neurosci 1995;15:2192-2202]. These and other findings suggest that protein kinases, and the phosphorylation of specific protein targets are important components of the hypoxic transduction machinery. Moreover, protein kinase-mediated cascades may participate in the well-known physiological adjustments which occur in the carotid body during prolonged stimulation. In the current study, our data demonstrate (1) the presence of specific protein kinases and target phosphoproteins in the carotid body, and also in the morphologically similar small intensely fluorescent cells of the superior cervical sympathetic ganglia. (2) Nitric oxide production and efferent inhibition in the chemosensory tissue is reduced in the presence of the specific tyrosine kinase inhibitor, lavendustin A. (3) Hypoxia-induced catecholamine release from type I cells is inhibited by the protein kinase A antagonist, Rp-cAMPs. And finally (4), exposure to chronic hypoxia up-regulates the expression of the tyrosine kinase, fyn, and an important growth regulatory phosphoprotein, growth associated protein-43 (GAP-43). These findings suggest that second messenger-mediated phosphorylation and dephosphorylation of specific protein targets is a mechanism capable of regulating diverse cellular functions in the carotid body during acute and chronic stimulation.</p>","PeriodicalId":79565,"journal":{"name":"Biological signals and receptors","volume":"8 6","pages":"366-74"},"PeriodicalIF":0.0,"publicationDate":"1999-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000014610","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21449443","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":"Co-localization of epithelial sodium channels and glutamate receptors in single taste cells.","authors":"W Lin, S C Kinnamon","doi":"10.1159/000014609","DOIUrl":"https://doi.org/10.1159/000014609","url":null,"abstract":"<p><p>Umami taste is elicited by monosodium glutamate (MSG), a compound consisting of two potent taste stimuli, Na(+) and glutamate. In rat fungiform taste cells, amiloride-sensitive epithelial sodium channels (ENaCs) mediate Na(+) transduction, while glutamate is transduced by a combination of ionotropic and metabotropic glutamate receptors. We used giga-seal whole-cell recording to determine if responses to glutamate and Na(+) occur in the same taste cells. Approximately 68% of the cells tested responded to amiloride, indicating that they express functional ENaCs. Responses to glutamate occurred in about 58% of the cells tested. Interestingly, responses to glutamate occurred in the subset of cells that also responded to amiloride, indicating that glutamate receptors are located preferentially in the same taste cells that also express ENaCs. Further experiments showed that amiloride did not suppress responses to glutamate under voltage-clamp conditions. Taken together, the data suggest that although ENaCs are not involved directly in glutamate transduction, their co-localization with glutamate receptors provides a substrate for the cellular integration of these independent pathways.</p>","PeriodicalId":79565,"journal":{"name":"Biological signals and receptors","volume":"8 6","pages":"360-5"},"PeriodicalIF":0.0,"publicationDate":"1999-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000014609","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21450258","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":"Chemosensitivity of the rat type I slowly adapting mechanoreceptor.","authors":"L He, R P Tuckett, K B English","doi":"10.1159/000014612","DOIUrl":"https://doi.org/10.1159/000014612","url":null,"abstract":"<p><p>An in vitro lateral thoracic skin preparation of the adult rat was used to test the effect of serotonin (5, 50, 500 microM) and control solutions on the response of the type I slowly adapting mechanoreceptor to a standard mechanical stimulus. Serotonin (5-HT) significantly increased the magnitude of the type I response to mechanical indentation: 50 microM 5-HT infusion enhanced responsiveness more effectively than 5 microM 5-HT. In the absence of mechanical stimulation, little or no change in spontaneous discharge relative to control was observed, and recovery to baseline levels occurred within three stimulus trials. In vitro and in vivo control experiments showed no statistically significant change in responsiveness over a similar number of stimulus cycles. It was concluded that 5-HT modulates, but does not activate the rat type I receptor or alter its ability to encode the depth and/or velocity of mechanical displacement.</p>","PeriodicalId":79565,"journal":{"name":"Biological signals and receptors","volume":"8 6","pages":"382-9"},"PeriodicalIF":0.0,"publicationDate":"1999-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000014612","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21449448","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":"GABA-mediated inhibition of primary olfactory receptor neurons.","authors":"A B Zhainazarov, R E Doolin, R Hoegg, B W Ache","doi":"10.1159/000014608","DOIUrl":"https://doi.org/10.1159/000014608","url":null,"abstract":"<p><p>Applying GABA (1 microM-1 mM) to the soma of cultured lobster olfactory receptor neurons evokes an inward current (V(m) = -60 mV) accompanied by an increase in membrane conductance, with a half-effect of 487 microM GABA. The current-voltage relationship of this current is linear between -100 and 100 mV and reverses polarity at the equilibrium potential for Cl(-). The current is blocked by picrotoxin and bicuculline methiodide, and is evoked by trans-aminocrotonic acid, isoguvacine, muscimol, imidazole-4-acetic acid, and 3-amino-1-propanesulfonic acid, but not by the GABA(C)-receptor agonist cis-4-aminocrotonic acid and the GABA(B)-receptor agonist 3-aminopropylphosphonic. Applying GABA to the soma of the cells in situ reversibly suppresses the spontaneous discharge and substantially decreases the odor-evoked discharge. The effects of GABA on the cell soma in situ are antagonized by both picrotoxin and bicuculline methiodide. Taken together with evidence that GABA directly activates a chloride channel in outside-out patches excised from the soma of these neurons, we conclude that lobster olfactory receptor neurons express an ionotropic GABA receptor that can potentially regulate the output of these cells.</p>","PeriodicalId":79565,"journal":{"name":"Biological signals and receptors","volume":"8 6","pages":"348-59"},"PeriodicalIF":0.0,"publicationDate":"1999-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000014608","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21450257","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":"Protective effects of intermittent hypoxic adaptation on myocardium and its mechanisms.","authors":"J Zhuang, Z Zhou","doi":"10.1159/000014602","DOIUrl":"https://doi.org/10.1159/000014602","url":null,"abstract":"<p><p>Intermittent hypoxic adaptation offers as many beneficial effects in protecting against myocardial injuries as chronic continuous hypoxic adaptation. However, chronic continuous hypoxic adaptation readily causes some adverse effects on the organism, which may be prevented by intermittent hypoxic adaptation. As an approach to potentiate the protective effects, intermittent hypoxic adaptation is also much easier to apply to subjects who are not living at high altitude. The mechanisms underlying the cardioprotective effects of intermittent hypoxic adaptation are less understood, although great similarities exist between chronic continuous and intermittent hypoxic adaptation. The participation of several factors, such as myocardial vascularity, coronary blood flow, and cardiomyoglobin, which comprise the oxygen uptake system is not apparent, while the more efficient energetic metabolism after intermittent hypoxic adaptation may be a mechanism for cardioprotection. The possible roles of several signaling transduction pathways, including adrenoceptors, prostaglandins, and the adenosinergic system, in the beneficial effects of intermittent hypoxia are compared to those of chronic continuous hypoxic adaptation. Antioxidant enzymes and stress proteins may also be part of the mechanisms contributing to the cardioprotection of the intermittent hypoxic adaptation. As the cardioprotective effects of intermittent hypoxic adaptation employ multifold mechanisms, their clear elucidation needs more efforts.</p>","PeriodicalId":79565,"journal":{"name":"Biological signals and receptors","volume":"8 4-5","pages":"316-22"},"PeriodicalIF":0.0,"publicationDate":"1999-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000014602","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21356699","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":"Involvement of K(+) channels in the inhibitory effects of adenosine on anoxia-induced [Ca(2+) ](i) increase in cultured rat hippocampal CA1 neurons.","authors":"Q Wan, H Yao, F Wang","doi":"10.1159/000014601","DOIUrl":"https://doi.org/10.1159/000014601","url":null,"abstract":"<p><p>Changes in intracellular free Ca(2+) concentration ([Ca(2+)](i)) in cultured hippocampal CA1 neurons isolated from newborn rats were measured by a confocal laser scanning microscope, using the Ca(2+) indicator Fluo-3. The results showed that exogenous adenosine (100 microM) significantly attenuated the increase of neuronal [Ca(2+)](i) induced by acute anoxia. This effect of adenosine could be suppressed by the adenosine A1 receptor antagonist 8-cyclopentyltheophylline. Moreover, potassium channel blockers, aminopyridine, and glipizide could also block the inhibitory role of adenosine, but tetraethylammonium had no effect. These results suggest that adenosine may activate 4-AP or ATP-sensitive potassium channels via an A1-receptor-mediated mechanism and consequently inhibit anoxia-induced [Ca(2+)](i) elevation in hippocampal neurons.</p>","PeriodicalId":79565,"journal":{"name":"Biological signals and receptors","volume":"8 4-5","pages":"309-15"},"PeriodicalIF":0.0,"publicationDate":"1999-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000014601","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21356732","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":"Changes of adenosine and its A(1) receptor in hypoxic preconditioning.","authors":"W L Zhang, G W Lu","doi":"10.1159/000014598","DOIUrl":"https://doi.org/10.1159/000014598","url":null,"abstract":"<p><p>Effects of hypoxic preconditioning on adenosine (ADO) and its A(1) receptor were studied in Kunming mice. The ADO content and its metabolites in the brain were measured by a specific enzymatic method; a radioligand binding method was used to study the ADO A(1) receptor. The ADO content of the hippocampus in group C (exposure to 4 runs of hypoxia) was markedly higher than that in group A (control, without exposure to hypoxia and B (exposure to 1 run of hypoxia), showing that the ADO content could be cumulatively increased in the hippocampus, which was more sensitive to ischemia and hypoxia, during acute and repeated exposure to hypoxia. A(1) receptor density in group C was significantly lower than in group A and no difference was seen between groups B and C; A(1) receptor affinity in the hippocampus, pons and medula oblongata in group C was significantly higher than in group A, implying that during hypoxic preconditioning there might be some mechanisms preventing A(1) receptor density from decreasing further and making A(1) receptor affinity increase in some brain regions. These results indicate that cumulatively increased ADO in the hippocampus via A(1) receptor may play a neuroprotective role in the CNS as an inhibitory neuromodulator and thus contribute to the formation and development of acute hypoxic adaptation or tolerance.</p>","PeriodicalId":79565,"journal":{"name":"Biological signals and receptors","volume":"8 4-5","pages":"275-80"},"PeriodicalIF":0.0,"publicationDate":"1999-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000014598","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21356724","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}