Advances in second messenger and phosphoprotein research最新文献

{"title":"Neurotransmitter release mechanisms in autonomic nerve terminals.","authors":"T C Cunnane, T J Searl","doi":"10.1016/s1040-7952(06)80029-7","DOIUrl":"https://doi.org/10.1016/s1040-7952(06)80029-7","url":null,"abstract":"","PeriodicalId":76981,"journal":{"name":"Advances in second messenger and phosphoprotein research","volume":"29 ","pages":"425-59"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18848246","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":"GTP-binding proteins: necessary components of the presynaptic terminal for synaptic transmission and its modulation.","authors":"Y Fang,&nbsp;S Durgerian,&nbsp;T A Basarsky,&nbsp;P G Haydon","doi":"10.1016/s1040-7952(06)80011-x","DOIUrl":"https://doi.org/10.1016/s1040-7952(06)80011-x","url":null,"abstract":"<p><p>Using synapses that form between somata of Helisoma neurons in cell culture, we have studied the presynaptic regulation of synaptic transmission. Guanosine 5'-triphosphate (GTP)-binding proteins play critical roles in regulating synaptic transmission. Injection of guanine nucleotide analogues has demonstrated that one or more GTP-binding protein is necessary for transmitter release. Heterotrimeric G proteins continuously regulate the amount of transmitter released at the synapse by modulating potassium and calcium channels, and by controlling the secretory response to calcium. Perturbations of the synapse using guanosine 5'-diphosphate (GDP) beta S, GTP gamma S, and rab effector domain peptides suggest that small GTP-binding proteins also play critical roles in the synapse. We discuss the possibility that rab3, or related proteins, are required for exocytosis, and by cooperating with other proteins maintain vesicles in a docked state in the synapse.</p>","PeriodicalId":76981,"journal":{"name":"Advances in second messenger and phosphoprotein research","volume":"29 ","pages":"121-32"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18848283","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":"Molecular pathways for presynaptic calcium signaling.","authors":"G J Augustine,&nbsp;H Betz,&nbsp;K Bommert,&nbsp;M P Charlton,&nbsp;W M DeBello,&nbsp;M Hans,&nbsp;D Swandulla","doi":"10.1016/s1040-7952(06)80013-3","DOIUrl":"https://doi.org/10.1016/s1040-7952(06)80013-3","url":null,"abstract":"<p><p>The results presented in this article describe two distinct, Ca-regulated molecular pathways in presynaptic terminals and implicate these two pathways in differentially mediating neurotransmitter secretion and PTP. Our current view of the Ca-dependent triggering of secretion and PTP is shown in Fig. 9. According to this scheme, differential activation of these two pathways is achieved by a combination of diffusion-based dilution of Ca that enters the terminal through voltage-gated Ca channels and by coupling these pathways to Ca receptors with different affinities for Ca ions. A simple way to achieve these conditions is to position these two receptors at different distances from the Ca channels, as shown in Fig. 2. Given that Ca ions are involved in activating many different presynaptic processes (Fig. 1), we propose that closer scrutiny of the molecular physiology of nerve terminals will reveal a wide variety of Ca-activated pathways responsible for producing these diverse processes.</p>","PeriodicalId":76981,"journal":{"name":"Advances in second messenger and phosphoprotein research","volume":"29 ","pages":"139-54"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18848285","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":"Central glutamatergic transmission. A view from the presynaptic axon.","authors":"L Brodin,&nbsp;O Shupliakov,&nbsp;S E Grillner","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":76981,"journal":{"name":"Advances in second messenger and phosphoprotein research","volume":"29 ","pages":"205-21"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18848289","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":"Nonuniformity and plasticity of quantal release at crustacean motor nerve terminals.","authors":"H L Atwood,&nbsp;R L Cooper,&nbsp;J M Wojtowicz","doi":"10.1016/s1040-7952(06)80026-1","DOIUrl":"https://doi.org/10.1016/s1040-7952(06)80026-1","url":null,"abstract":"","PeriodicalId":76981,"journal":{"name":"Advances in second messenger and phosphoprotein research","volume":"29 ","pages":"363-82"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18848299","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":"Regulation of transmitter release by muscle length in frog motor nerve terminals. Dynamics of the effect and the role of integrin-ECM interactions.","authors":"B M Chen,&nbsp;A D Grinnell","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Changes in muscle length cause large changes in the probability of transmitter release from frog motor nerve terminals. A 5% to 10% stretch from rest length can increase EPP amplitude or mEPP frequency by more than 100%. The phenomenon is fully reversible and extremely rapid. Within 7-10 milliseconds of the stretch, the enhancement is complete, and it is maintained essentially constant at the new level for as long as the stretch is sustained. Given these properties, the length modulation of release is unquestionably of functional importance, strongly amplifying the spinal stretch reflex. The stretch-induced enhancement of transmitter release persists at a reduced level in a 0 Ca++, 2 mM Mg++ Ringer. This finding indicates a lack of dependence on Ca++ influx from outside the terminal. Release of Ca++ from intracellular stores close to release sites cannot be ruled out as a contributing factor. Our results, however, suggest a mechanism involving physical connections between the extracellular matrix and the nerve terminal that can alter release probability directly. Morphological evidence for connections that might be responsible can be demonstrated in micrographs of deep-etched freeze fractures through neuromuscular junctions. Hypothesizing that the ECM-nerve terminal connections responsible for the stretch effect involve proteins from the integrin family and knowing that many of the integrin-ECM binding interactions occur at sites on the ECM proteins containing the amino acid sequence RGD, we treated preparations with 0 Ca++, 2 mM Mg++ Ringer to reduce integrin binding and then returned the muscle to normal Ringer containing 0.1-0.2 mM of a six-amino-acid peptide containing the RGD sequence. This peptide strongly suppressed the stretch effect, while a control peptide (RGE) had no effect. A 50 microM Ca++/50 microM Mg++ Ringer had little effect on stretch enhancement but permitted a strong inhibition of enhancement when RGD was present. The identity of the ECM molecule(s), the integrin(s), and the mechanism of enhancement of release are unknown. However, our findings imply that much or all of the length-dependent modulation of release probability is mediated by an RGD-sensitive integrin-ECM interaction that depends more on external Ca++ than on Mg++.</p>","PeriodicalId":76981,"journal":{"name":"Advances in second messenger and phosphoprotein research","volume":"29 ","pages":"383-98"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18848300","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":"Activity-dependent modulation of developing neuromuscular synapses.","authors":"M M Poo","doi":"10.1016/s1040-7952(06)80033-9","DOIUrl":"https://doi.org/10.1016/s1040-7952(06)80033-9","url":null,"abstract":"<p><p>Spontaneous and impulse-evoked synaptic currents were observed immediately following nerve-muscle contact in Xenopus cell cultures. The functional significance of this early synaptic activity was examined. Stimulation of pre- and/or post-synaptic cells was found to exert immediate and persistent effects on the efficacy of synaptic transmission. Exogenous application of calcitonin gene-related peptide (CGRP) and neurotrophins, factors that may be coreleased with ACh in activity-dependent manner at the developing neuromuscular junctions, also modulate either the postsynaptic ACh response or presynaptic ACh release. These results underscore the plasticity of developing neuromuscular synapses and suggest a complex interplay between electrical activity and chemical factors during the formation and maturation of neuronal connections.</p>","PeriodicalId":76981,"journal":{"name":"Advances in second messenger and phosphoprotein research","volume":"29 ","pages":"521-7"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18848251","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":"Low synaptic convergence of CA3 collaterals on CA1 pyramidal cells suggests few release sites.","authors":"P Andersen,&nbsp;M Trommald,&nbsp;V Jensen","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":76981,"journal":{"name":"Advances in second messenger and phosphoprotein research","volume":"29 ","pages":"340-51"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18848297","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":"Low synaptic convergence of CA3 collaterals on CA1 pyramidal cells suggests few release sites.","authors":"P. Andersen, M. Trommald, V. Jensen","doi":"10.1016/s1040-7952(06)80024-8","DOIUrl":"https://doi.org/10.1016/s1040-7952(06)80024-8","url":null,"abstract":"","PeriodicalId":76981,"journal":{"name":"Advances in second messenger and phosphoprotein research","volume":"29 1","pages":"340-51"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56384845","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":"Tetanus and botulinal neurotoxins. Tools to understand exocytosis in neurons.","authors":"E Link,&nbsp;J Blasi,&nbsp;E R Chapman,&nbsp;L Edelmann,&nbsp;A Baumeister,&nbsp;T Binz,&nbsp;S Yamasaki,&nbsp;H Niemann,&nbsp;R Jahn","doi":"10.1016/s1040-7952(06)80006-6","DOIUrl":"https://doi.org/10.1016/s1040-7952(06)80006-6","url":null,"abstract":"","PeriodicalId":76981,"journal":{"name":"Advances in second messenger and phosphoprotein research","volume":"29 ","pages":"47-58"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18848248","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}