发布求助
文献互助 智能选刊 最新文献

Second messengers and phosphoproteins最新文献

筛选
英文 中文
The old and the new in transformed cell signalling: glycolysis, diacylglycerol and protein kinase C. 转化细胞信号传导的新旧:糖酵解、二酰基甘油和蛋白激酶C。
Second messengers and phosphoproteins Pub Date : 1990-01-01
V Chiarugi, G Basi, A Quattrone, R Micheletti, M Ruggiero
{"title":"The old and the new in transformed cell signalling: glycolysis, diacylglycerol and protein kinase C.","authors":"V Chiarugi, G Basi, A Quattrone, R Micheletti, M Ruggiero","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77384,"journal":{"name":"Second messengers and phosphoproteins","volume":"13 1","pages":"69-85"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13438280","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
Cellular distribution and pharmacological sensitivity of low Km cyclic nucleotide phosphodiesterase isozymes in human cardiac muscle from normal and cardiomyopathic subjects. 正常人和心肌病患者心肌低Km环核苷酸磷酸二酯酶同工酶的细胞分布和药理学敏感性。
Second messengers and phosphoproteins Pub Date : 1990-01-01
P J Silver, P Allen, J H Etzler, L T Hamel, R G Bentley, E D Pagani
{"title":"Cellular distribution and pharmacological sensitivity of low Km cyclic nucleotide phosphodiesterase isozymes in human cardiac muscle from normal and cardiomyopathic subjects.","authors":"P J Silver,&nbsp;P Allen,&nbsp;J H Etzler,&nbsp;L T Hamel,&nbsp;R G Bentley,&nbsp;E D Pagani","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Cyclic nucleotide phosphodiesterase (PDE) isozymes isolated by DEAE-Sephacel or Mono-Q High Performance Liquid Chromatography from cardiac left ventricular tissue of normal subjects and patients with end-stage heart failure have been compared. With both separation techniques, four major peaks of PDE activity were evident in the soluble fractions; only one peak of activity was present in particulate fractions. The specific activity of the particulate PDE from myopathics was approximately 30-50% of that of normals while the specific activity of a soluble form of this PDE (peak IIIa) was reduced by 30% in myopathics. No differences in comparison of the other peaks of PDE activity were evident. The particulate PDE isozyme has a low Km for cAMP (0.27-0.29 microM), is inhibited by cGMP (60-80% at 1 microM), is sensitive to inhibition by submicromolar concentrations of CI-930 but not rolipram, and is competitively inhibited by milrinone (Kj = 0.3 microM). The first soluble peak of PDE activity hydrolyzes both cAMP and cGMP and is stimulated by calmodulin while cyclic AMP hydrolysis by peak II PDE is stimulated by cGMP. The other soluble peak III fractions (IIIa and IIIb) hydrolyze cAMP; peak IIIa is inhibited by cGMP or by CI-930 and milrinone, whereas peak IIIb is also inhibited by rolipram when the cardiotonic sensitive PDE is inhibited by CI-930. Thus, cardiotonic-sensitive, cGMP-inhibitable, low Km cAMP PDE is present in both the soluble and particulate fractions of human cardiac left ventricular muscle of hearts from normal and cardiomyopathic subjects while the rolipram-sensitive PDE is present in the soluble fraction. The major differences in PDE activity of myopathic relative to normal left ventricular tissue are a reduced specific activity and Vmax of particulate PDE and one of the soluble peak III PDEs.</p>","PeriodicalId":77384,"journal":{"name":"Second messengers and phosphoproteins","volume":"13 1","pages":"13-25"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13438278","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
Albumin and GTP modulate the affinity of prostaglandin E2 receptors in rat epididymal adipocyte membranes. 白蛋白和GTP调节大鼠附睾脂肪细胞膜上前列腺素E2受体的亲和力。
Second messengers and phosphoproteins Pub Date : 1988-01-01
R Cohen-Luria, G Rimon
{"title":"Albumin and GTP modulate the affinity of prostaglandin E2 receptors in rat epididymal adipocyte membranes.","authors":"R Cohen-Luria,&nbsp;G Rimon","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Detailed studies of PGE2 binding to isolated rat adipocyte membranes revealed two different classes of binding sites, namely high affinity-low capacity binding sites and low affinity-high capacity binding sites. Addition of albumin or GTP to the incubation medium enhanced the specific binding of PGE2 by decreasing the dissociation constant of the low affinity-high capacity binding sites. Albumin also increased the affinity of PGE2 binding to native canine renal medullary membranes and enhanced the binding of PGE2 to prostaglandin receptors solubilized from these membranes. Pretreatment of the adipocyte membranes with the alkylating agent NEM completely abolished the enhancement of PGE2 binding by GTP, while the enhancement of PGE2 binding by albumin was only partially inhibited. The enhancement of PGE2 binding by GTP was shown to be dependent on the presence of Mg+2, while the albumin effect was independent of Mg+2. These results suggest that the affinity of the prostaglandin receptors is modulated by more than one mechanism.</p>","PeriodicalId":77384,"journal":{"name":"Second messengers and phosphoproteins","volume":"12 5-6","pages":"225-34"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14210118","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
Stimulatory and inhibitory effects of sodium salts on adenylate cyclase of rat liver. Implications for salt modulation of guanine nucleotide-binding regulatory component function. 钠盐对大鼠肝脏腺苷酸环化酶的刺激和抑制作用。盐对鸟嘌呤核苷酸结合调控组分功能的影响。
Second messengers and phosphoproteins Pub Date : 1988-01-01
L R Joshi, M S Katz
{"title":"Stimulatory and inhibitory effects of sodium salts on adenylate cyclase of rat liver. Implications for salt modulation of guanine nucleotide-binding regulatory component function.","authors":"L R Joshi,&nbsp;M S Katz","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>We have examined the effects of sodium (Na+) salts on rat liver adenylate cyclase. Increasing concentrations of Na+ salts produced biphasic stimulation and inhibition of adenylate cyclase and potentiated enzyme activation by GTP and its hydrolysis resistant analog 5'-guanylyl imidodiphosphate. Salt effects were temperature dependent, of rapid onset, and specific for the Na+ cation though also partly dependent on the accompanying anion. Sodium salt stimulation of adenylate cyclase and enhancement of GTP activation were attenuated by agents (pertussis toxin and N-ethylmaleimide) which inactivate the inhibitory guanine nucleotide-binding regulatory component (Gi) of adenylate cyclase. Cholera toxin, which activates the stimulatory guanine nucleotide-binding regulatory component (Gs) of adenylate cyclase and thereby increases enzyme activity, augmented the inhibitory phase of Na+ salt action. These results suggest that the stimulatory and inhibitory effects of Na+ salts may be due, respectively, to inhibition of Gi and Gs modulation of adenylate cyclase.</p>","PeriodicalId":77384,"journal":{"name":"Second messengers and phosphoproteins","volume":"12 2-3","pages":"105-21"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14279884","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
Characterization of two casein kinase activities in the fungus Mucor rouxii. 鲁氏毛霉两种酪蛋白激酶活性的研究。
Second messengers and phosphoproteins Pub Date : 1988-01-01
P Pardo, S Moreno
{"title":"Characterization of two casein kinase activities in the fungus Mucor rouxii.","authors":"P Pardo,&nbsp;S Moreno","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Two cyclic-nucleotide independent soluble casein kinase activities (CK I and CK II) from the fungus Mucor rouxii have been isolated, characterized and found to fit in the general classification of type 1 (CK I) and 2 (CK II) casein kinases, according to their enzymatic and structural properties. Both enzymes phosphorylate acidic substrates, require Mg2+ and have a chromatographic behaviour on DEAE-Sepharose and phosphocellulose similar to their mammalian counterparts. CK I has a sedimentation coefficient of 3.5 S, uses ATP as a phosphate donor (Km = 40 microM), phosphorylates casein mainly on serine residues, its activity is strongly inhibited by KCl and polyamines. CK II has a sedimentation coefficient of 7.4 S, uses ATP and GTP as phosphate donors (Km ATP = 10 microM; Km GTP = 40 microM), phosphorylates casein in serine and threonine, its activity is stimulated by KCl and by polyamines and is inhibited by heparin (I50 = 0.5 micrograms/ml). Casein kinase activity associated to particulate fraction (40% of total) has been partially characterized and shown to be similar to the soluble CK I activity.</p>","PeriodicalId":77384,"journal":{"name":"Second messengers and phosphoproteins","volume":"12 4","pages":"183-96"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14375169","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
Attomole sensitive radioimmunoassay for cyclic GMP. 环GMP的雾化敏感放射免疫测定。
Second messengers and phosphoproteins Pub Date : 1988-01-01
K L Axelsson, K E Bornefeldt, B Norlander, J E Wikberg
{"title":"Attomole sensitive radioimmunoassay for cyclic GMP.","authors":"K L Axelsson,&nbsp;K E Bornefeldt,&nbsp;B Norlander,&nbsp;J E Wikberg","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The sensitivity of the radioimmunoassay for cyclic GMP has been improved to readily detect attomole (200-300) amounts of the nucleotide in tissue extracts. The improved sensitivity has been achieved by using a high specific radioactivity [125I] cyclic GMP 2'O-succinyl tyrosine methyl ester (2200 Ci/mmole) as labeled antigen in conjunction with acetylation of the cyclic GMP in the samples as well as by using a selected cyclic GMP antibody. The high specific [125I] cyclic GMP 2'O-succinyl tyrosine methyl ester was prepared radiochemically pure by radioiodination of cyclic GMP 2'O-succinyl tyrosine methyl ester and purification using HPLC. The new attomole sensitive cyclic GMP radioimmunoassay is simple to perform and fast and has been applied with success to determine attomole quantities of cyclic GMP in cultured smooth muscle cells and AG 1523 fibroblasts.</p>","PeriodicalId":77384,"journal":{"name":"Second messengers and phosphoproteins","volume":"12 4","pages":"145-54"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13991628","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
Phosphorylation of ribosomal protein S6 is dependent on cyclic AMP in Dictyostelium discoideum. 核糖体蛋白S6的磷酸化依赖于环状AMP。
Second messengers and phosphoproteins Pub Date : 1988-01-01
A M Silva, S L Gomes, J C Maia, M H Juliani
{"title":"Phosphorylation of ribosomal protein S6 is dependent on cyclic AMP in Dictyostelium discoideum.","authors":"A M Silva,&nbsp;S L Gomes,&nbsp;J C Maia,&nbsp;M H Juliani","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Extracts of aggregation-competent cells of Dictyostelium discoideum have an S6 protein kinase activity which is inhibited in the presence of the inhibitor of the cAMP-dependent protein kinase. The phosphorylation of S6 is rapid, and decays rapidly. The S6 kinase activity is detectable in the 150,000g supernatant only in the presence of phosphatase inhibitors known for preserving the S6 kinase in other systems, indicating that the activated form of the enzyme is phosphorylated by the cAMP-dependent protein kinase. S6 kinase elutes as a peak from DEAE-Sephacel at 100 mM NaC1, with an activity that is cAMP-dependent.</p>","PeriodicalId":77384,"journal":{"name":"Second messengers and phosphoproteins","volume":"12 5-6","pages":"271-80"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13994048","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
Cyclic AMP opposes IP3-induced calcium release from permeabilized human platelets. 环AMP对抗ip3诱导的钙从渗透性人血小板释放。
Second messengers and phosphoproteins Pub Date : 1988-01-01
M Moos, N D Goldberg
{"title":"Cyclic AMP opposes IP3-induced calcium release from permeabilized human platelets.","authors":"M Moos,&nbsp;N D Goldberg","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Platelets permeabilized by means of a high voltage electric field demonstrated time- and ATP-dependent uptake of 45Ca++. Submicromolar concentrations of inositol-1,4,5-trisphosphate (IP3) caused a rapid release of 45Ca++ which was followed by a slower reuptake. Adenosine 3':5'-cyclic monophosphate (cAMP) did not affect 45Ca++ uptake but did reduce IP3-mediated calcium release in a concentration-dependent manner over the range of 1-100 microM. Because cAMP concentrations in this range occur following exposure of platelets to prostacyclin and other agents which interfere with platelet function, it is proposed that cAMP-mediated inhibition of the action of IP3 may play a role in the antithrombotic activity of compounds believed to elevate levels of this cyclic nucleotide.</p>","PeriodicalId":77384,"journal":{"name":"Second messengers and phosphoproteins","volume":"12 4","pages":"163-70"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13991629","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
Measurement of 3':5'cyclic AMP in biological samples using a specific monoclonal antibody. 使用特异性单克隆抗体测定生物样品中的3':5'环AMP。
Second messengers and phosphoproteins Pub Date : 1988-01-01
C Colling, R Gilles, M Cramer, N Nass, R Moka, L Jaenicke
{"title":"Measurement of 3':5'cyclic AMP in biological samples using a specific monoclonal antibody.","authors":"C Colling,&nbsp;R Gilles,&nbsp;M Cramer,&nbsp;N Nass,&nbsp;R Moka,&nbsp;L Jaenicke","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A fast and sensitive radioimmunoassay for 3':5'cyclic AMP based on a monoclonal antibody has been worked out. Mice were immunized with protein-conjugated 2'-O-succinyl-3':5'-cyclic AMP. The monoclonal antibody detects 0.1 and 1 pmole cAMP with succinyl cAMP (125I)iodotyrosine methyl ester and (3H) cAMP, respectively, as tracers. It shows no cross-reactivity to other adenosine nucleotides up to the millimolar range; cGMP interferes only if present at a 500 fold excess. Plant and animal tissue samples as well as adenylate cyclase activity were analysed directly or after appropriate purification in case of interfering substances. Cyclic AMP levels measured in various tissues by the antibody binding assay correspond to those obtained by HPLC determination using fluorescent etheno-cAMP.</p>","PeriodicalId":77384,"journal":{"name":"Second messengers and phosphoproteins","volume":"12 2-3","pages":"123-33"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13992713","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
Type II cAMP-dependent protein kinase is associated with the rabbit kidney brush border membranes. II型camp依赖性蛋白激酶与兔肾刷状缘膜相关。
Second messengers and phosphoproteins Pub Date : 1988-01-01
S Shenolikar, K Fischer, L Chang, E J Weinman
{"title":"Type II cAMP-dependent protein kinase is associated with the rabbit kidney brush border membranes.","authors":"S Shenolikar,&nbsp;K Fischer,&nbsp;L Chang,&nbsp;E J Weinman","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Photolabelling with 32P-8-azido-cAMP identified a major cAMP-binding protein (54 kDa) in isolated rabbit renal apical membranes, whose labelling was competitively inhibited by cAMP. Membrane associated cAMP-binding polypeptides were extensively purified by affinity chromatography on cAMP-Sepharose. The 54 kDa polypeptide represented 70-80% of the total protein eluted with cAMP. This protein was rapidly phosphorylated by the catalytic subunit of cAMP-dependent protein kinase, with a shift in its apparent mobility on SDS-PAGE to Mr 56/58,000. The phosphopeptide maps of autophosphorylated rat skeletal muscle RII and rabbit kidney 56/58 kDa proteins were essentially identical. Western immuno-blot analysis, using antibodies generated against purified rat RI and RII, indicated preferential cross-reactivity of rabbit kidney 54 kDa protein with anti-RII antibodies. The data demonstrates the specific association of the regulatory subunit of type II cAMP dependent protein kinase with rabbit renal brush border membranes.</p>","PeriodicalId":77384,"journal":{"name":"Second messengers and phosphoproteins","volume":"12 2-3","pages":"95-104"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13992715","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
首页 上一页 下一页 尾页
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整，为了账户安全，请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
请完成安全验证×
相关产品
×
本文献相关产品
联系我们：info@booksci.cn Book学术提供免费学术资源搜索服务，方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号：604180095
Book学术官方微信