Receptors & channels最新文献_第7页

The urea transporter (UT) family: bioinformatic analyses leading to structural, functional, and evolutionary predictions. 尿素转运体（UT）家族：结构、功能和进化预测的生物信息学分析。

Receptors & channels Pub Date : 2003-01-01 DOI: 10.3109/714041015

Ranjeet Minocha, Keith Studley, Milton H Saier

引用次数: 32

Pharmacological analysis of the contractile role of M2 and M3 muscarinic receptors in smooth muscle. 平滑肌中M2和M3毒蕈碱受体收缩作用的药理学分析。

Receptors & channels Pub Date : 2003-01-01

Frederick J Ehlert

{"title":"Pharmacological analysis of the contractile role of M2 and M3 muscarinic receptors in smooth muscle.","authors":"Frederick J Ehlert","doi":"","DOIUrl":"","url":null,"abstract":"Muscarinic receptors expressed on smooth muscle cells are primarily of the M(2) and M(3) subtypes. The M(3) subtype triggers contraction through an interaction with G(q) proteins to stimulate phosphoinositide hydrolysis and mobilize Ca(2+). In contrast, activation of M(2) receptors modulates contraction by preventing relaxation or by potentiating M(3) receptor-mediated contractions, which enhances heterologous desensitization. These effects can be explained by the coupling of M(2) receptors to G(i) proteins that mediate an inhibition of adenylyl cyclase and calcium-activated potassium channels. The pharmacological antagonism of a response mediated through an interaction between M(2) and M(3) receptors has been shown to resemble the profile of the directly acting receptor (M(3)), primarily, and not that of the conditional receptor (M(2)). Evidence for a contractile role of the M(2) receptor has been obtained by inactivating its signaling pathway with pertussis toxin or by measuring contractile effects of muscarinic agonists after M(3) receptors have been covalently inactivated. Under these conditions, M(2) receptors have been shown to mediate an inhibition of the relaxant effects of agents, like isoproterenol, on the contractile effects of nonmuscarinic spasmogens. Muscarinic M(2) and M(3) receptor knockout mice are useful tools for exploring interactions between these receptors in smooth muscle.","PeriodicalId":20928,"journal":{"name":"Receptors & channels","volume":"9 4","pages":"261-77"},"PeriodicalIF":0.0,"publicationDate":"2003-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22510910","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}

引用次数: 0

Activity, regulation, and intracellular localization of RGS proteins. RGS蛋白的活性、调控和细胞内定位。

Receptors & channels Pub Date : 2003-01-01 DOI: 10.3109/10606820308244

P. Chidiac, A. A. Roy

引用次数: 54

Protein complexes involved in heptahelical receptor-mediated signal transduction. 参与七螺旋受体介导的信号转导的蛋白质复合物。

Receptors & channels Pub Date : 2003-01-01

R Victor Rebois, Terence E Hébert

引用次数: 0

Introduction: an evolution of electrophysiology. 导言:电生理学的进化。

Receptors & channels Pub Date : 2003-01-01

Jennings Worley

引用次数: 0

Application of the Cytosensor microphysiometer to drug discovery. 细胞传感器微生理仪在药物发现中的应用。

Receptors & channels Pub Date : 2003-01-01

Kirsten Wille, Lisa A Paige, Alan J Higgins

引用次数: 0

Accessory proteins for G protein-signaling systems: activators of G protein signaling and other nonreceptor proteins influencing the activation state of G proteins. G蛋白信号系统的辅助蛋白:G蛋白信号的激活因子和其他影响G蛋白激活状态的非受体蛋白。

Receptors & channels Pub Date : 2003-01-01 DOI: 10.1080/10606820308240

J. Blumer, S. Lanier

引用次数: 39

Upscaling and automation of electrophysiology: toward high throughput screening in ion channel drug discovery. 电生理学的升级和自动化:迈向离子通道药物发现的高通量筛选。

Receptors & channels Pub Date : 2003-01-01 DOI: 10.3109/10606820308258

M. Asmild, Nicholas Oswald, K. Krzywkowski, S. Friis, R. B. Jacobsen, Dirk Reuter, R. Taboryski, Jonathan Kutchinsky, R. Vestergaard, R. L. Schrøder, C. Sørensen, M. Bech, Mads P. G. Korsgaard, N. Willumsen

引用次数: 28

Characterization of adenosine A1 receptors in human proximal tubule epithelial (HK-2) cells. 人近端小管上皮细胞(HK-2)中腺苷A1受体的表征。

Receptors & channels Pub Date : 2003-01-01

Yuting Tang, Lubing Zhou

{"title":"Characterization of adenosine A1 receptors in human proximal tubule epithelial (HK-2) cells.","authors":"Yuting Tang, Lubing Zhou","doi":"","DOIUrl":"","url":null,"abstract":"Background: Adenosine A1 receptors (A1ARs) modulate various aspects of renal functions, such as hormone release, hemodynamics and tubular absorption. Here we set up to demonstrate the expression of A1ARs in an immortalized cell line (HK-2) derived from normal adult human proximal tubule. We also examined the mechanism whereby A1ARs signal in HK-2 cells and their potential role in renal physiology such as sodium-dependent phosphate transport.Methods: Ligand binding assay of A1ARs was performed using plasma membranes of HK-2 cells and a selective high-affinity A1AR radioligand [3H]DPCPX. HK-2 cells in 96-well plates were treated with various agents (forskolin, adenosine receptor agonists, and antagonists) to activate or inhibit adenylate cyclase. Intracellular cyclic AMP accumulation was measured using cAMP flashplates. mRNA levels of adenosine receptors in HK-2 cells was determined by real-time PCR technique. Sodium-dependent phosphate transport across cell membrane was measured after 15-minute incubation of phosphorus-33 in transport buffer with HK-2 cells at room temperature.Results: In HK-2 cells, A1ARs were expressed at a density of 211 +/- 74 fmol/mg membrane proteins. [3H]DPCPX bound to A1ARs on HK-2 cell membranes with Kd of 8.3 +/- 2.2 nM. Activation of A1ARs inhibited isoproterenol-stimulated adenylate cyclase activity through pertussis toxin-sensitive Gi protein in HK-2 cells. Coexpression of adenosine A2a receptors at a seemingly lower level than A1ARs was revealed by synergistically activating adenylate cyclase with forskolin. Real-time RT-PCR further demonstrated the expression of both A1AR and A2aAR in HK-2 cells. Sodium-dependent phosphate transport was augmented by activation of A1ARs in HK-2 cells.Conclusion: A1ARs are expressed in human proximal tubule epithelial (HK-2) cells and modulate sodium-dependent phosphate transport.","PeriodicalId":20928,"journal":{"name":"Receptors & channels","volume":"9 2","pages":"67-75"},"PeriodicalIF":0.0,"publicationDate":"2003-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22529263","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}

引用次数: 0

Putative dynamics of vasopressin in its V1a receptor binding site. 抗利尿激素在其V1a受体结合位点的推测动力学。

Receptors & channels Pub Date : 2003-01-01

Astrid Kaltenböck, Marcel Hibert, Thierry Langer

{"title":"Putative dynamics of vasopressin in its V1a receptor binding site.","authors":"Astrid Kaltenböck, Marcel Hibert, Thierry Langer","doi":"","DOIUrl":"","url":null,"abstract":"The molecular architecture of the GPCRs, including the dynamic set of interactions between the receptor and the ligand, is one of the key structural questions of biophysical approaches. In the present study, molecular dynamics (MD) simulations were performed on the well-validated molecular model of the vasopressin V1a receptor applying different parameters (i.e., force fields, time variation, use of constraints) in order to sample the conformational space of the endogenous ligand arginine vasopressin (AVP), to explore different putative binding modes, and to analyze the simulation results with respect to experimental data. Noteworthy, it is to mention that for the first time a model of the vasopressin receptor remained stable in a 500 ps MD simulation run under vacuo boundary conditions using the Kollman all-atom FF even though no constraints were imposed. Conclusively, we determined an optimized experimental procedure for studying the dynamics and structure-functionship of this highly important family of GPCRs: the use of MD simulations with the Kollman all-atom force-field parameters on a constrained receptor. Our simplified model may be used as a basis for structure based design of new GPCR ligands and for in silico screening of virtual combinatorial chemistry libraries.","PeriodicalId":20928,"journal":{"name":"Receptors & channels","volume":"9 2","pages":"93-106"},"PeriodicalIF":0.0,"publicationDate":"2003-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22529266","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}

引用次数: 0