Journal of biochemistry and molecular biology最新文献_第10页

Clenbuterol inhibits SREBP-1c expression by activating CREB1. 盐酸克仑特罗通过激活CREB1抑制SREBP-1c的表达。

Journal of biochemistry and molecular biology Pub Date : 2007-07-31 DOI: 10.5483/bmbrep.2007.40.4.525

Lei Zhou, Yixing Li, Tao Nie, Shengqiu Feng, Jihong Yuan, Huaping Chen, Zaiqing Yang

{"title":"Clenbuterol inhibits SREBP-1c expression by activating CREB1.","authors":"Lei Zhou, Yixing Li, Tao Nie, Shengqiu Feng, Jihong Yuan, Huaping Chen, Zaiqing Yang","doi":"10.5483/bmbrep.2007.40.4.525","DOIUrl":"https://doi.org/10.5483/bmbrep.2007.40.4.525","url":null,"abstract":"As a beta(2)-adrenergic agonist, clenbuterol decreases body fat, but the molecular mechanism underlying this process is unclear. In the present study, we treated 293T and L-02 cells with clenbuterol and found that clenbuterol downregulates SREBP-1c expression and upregulates CREB1 expression. Considering SREBP-1c has the function of regulating the transcription of several lipogenic enzymes, we considered that the downregulation of SREBP-1c is responsible for body fat reduction by clenbuterol. Many previous studies have found that clenbuterol markedly increases intracellular cAMP levels, therefore, we also investigated whether CREB1 is involved in this process. The data from our experiments indicate that CREB1 overexpression inhibits SREBP-1c transcription, and that this action is antagonized by CREB2, a competitive inhibitor of CREB1. Furthermore, since PPARs are able to repress SREBP-1c transcription, we investigated whether clenbuterol and CREB1 function via a pathway involving PPAR activation. However, our results showed that clenbuterol or CREB1 overexpression suppressed PPARs transcription in 293T and L-02 cells, which suggested that they impair SREBP-1c expression in other ways.","PeriodicalId":15113,"journal":{"name":"Journal of biochemistry and molecular biology","volume":"40 4","pages":"525-31"},"PeriodicalIF":0.0,"publicationDate":"2007-07-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26863028","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: 22

Some motifs were important for myostatin transcriptional regulation in sheep (Ovis aries). 一些基序在绵羊(Ovis aries)的肌肉生长抑制素转录调控中很重要。

Journal of biochemistry and molecular biology Pub Date : 2007-07-31 DOI: 10.5483/bmbrep.2007.40.4.547

Rong Du, Xiao-Rong An, Yong-Fu Chen, Jian Qin

引用次数: 40

Rat liver 10-formyltetrahydrofolate dehydrogenase, carbamoyl phosphate synthetase 1 and betaine homocysteine S-methytransferase were co-purified on Kunitz-type soybean trypsin inhibitor-coupled sepharose CL-4B. 大鼠肝脏10-甲酰基四氢叶酸脱氢酶、氨甲酰磷酸合成酶1和甜菜碱同型半胱氨酸s -甲基转移酶在kuniz型大豆胰蛋白酶抑制剂偶联的蔗糖CL-4B上共纯化。

Journal of biochemistry and molecular biology Pub Date : 2007-07-31 DOI: 10.5483/bmbrep.2007.40.4.604

Hyun-Sic Kim, Ji-Man Kim, Kyung-Baeg Roh, Hyeon-Hwa Lee, Su-Jin Kim, Young Hee Shin, Bok Luel Lee

{"title":"Rat liver 10-formyltetrahydrofolate dehydrogenase, carbamoyl phosphate synthetase 1 and betaine homocysteine S-methytransferase were co-purified on Kunitz-type soybean trypsin inhibitor-coupled sepharose CL-4B.","authors":"Hyun-Sic Kim, Ji-Man Kim, Kyung-Baeg Roh, Hyeon-Hwa Lee, Su-Jin Kim, Young Hee Shin, Bok Luel Lee","doi":"10.5483/bmbrep.2007.40.4.604","DOIUrl":"https://doi.org/10.5483/bmbrep.2007.40.4.604","url":null,"abstract":"An Asp/His catalytic site of 10-formyltetrahydrofolate dehydrogenase (FDH) was suggested to have a similar catalytic topology with the Asp/His catalytic site of serine proteases. Many studies supported the hypothesis that serine protease inhibitors can bind and modulate the activity of serine proteases by binding to the catalytic site of serine proteases. To explore the possibility that soybean trypsin inhibitor (SBTI) can recognize catalytic sites of FDH and can make a stable complex, we carried out an SBTI-affinity column by using rat liver homogenate. Surprisingly, the Rat FDH molecule with two typical liver proteins, carbamoyl-phosphate synthetase 1 (CPS1) and betaine homocysteine S-methyltransferase (BHMT) were co-purified to homogeneity on SBTI-coupled Sepharose and Sephacryl S-200 followed by Superdex 200 FPLC columns. These three liver-specific proteins make a protein complex with 300 kDa molecular mass on the gel-filtration column chromatography in vitro. Immuno-precipitation experiments by using anti-FDH and anti-SBTI antibodies also supported the fact that FDH binds to SBTI in vitro and in vivo. These results demonstrate that the catalytic site of rat FDH has a similar structure with those of serine proteases. Also, the SBTI-affinity column will be useful for the purification of rat liver proteins such as FDH, CPS1 and BHMT.","PeriodicalId":15113,"journal":{"name":"Journal of biochemistry and molecular biology","volume":"40 4","pages":"604-9"},"PeriodicalIF":0.0,"publicationDate":"2007-07-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26862872","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: 3

Overexpressed Drosophila DNA methyltransferase 2 isoform C interacts with Hsp70 in vivo. 果蝇DNA甲基转移酶2异构体C在体内与Hsp70相互作用。

Journal of biochemistry and molecular biology Pub Date : 2007-07-31 DOI: 10.5483/bmbrep.2007.40.4.554

Karim Roder

{"title":"Overexpressed Drosophila DNA methyltransferase 2 isoform C interacts with Hsp70 in vivo.","authors":"Karim Roder","doi":"10.5483/bmbrep.2007.40.4.554","DOIUrl":"https://doi.org/10.5483/bmbrep.2007.40.4.554","url":null,"abstract":"Shen and colleagues (Lin et al., 2004) have recently shown that overexpression of the Drosophila DNA methyltransferase 2 isoform C, dDnmt2c, extended life span of fruit flies, probably due to increased expression of small heat shock proteins such as Hsp22 or Hsp26. Here, I demonstrate with immunoprecipitations that overexpressed dDnmt2c interacts with endogenous Hsp70 protein in vivo in S2 cells. However, its C-terminal half, dDnmt2c(178-345) forms approximately 10-fold more Hsp70-containing protein complexe than wild-type dDnmt2c. Overexpressed dDnmt2c(178-345) but not the full length dDnmt2c is able to increase endogenous mRNA levels of the small heat shock proteins, Hsp26 and Hsp22. I provide evidence that dDnmt2c(178-345) increases Hsp26 promoter activity via two heat shock elements, HSE6 and HSE7. Simultaneously overexpressed Hsp40 or a dominant negative form of heat shock factor abrogates the dDnmt2c(178-345)-dependent increase in Hsp26 transcription. The data support a model in which the activation of heat shock factor normally found as an inactive monomer bound to chaperones is linked to the overexpressed C-terminus of dDnmt2c. Despite the differences observed in flies and S2 cells, these findings provide a possible explanation for the extended lifespan in dDnmt2c-overexpressing flies with increased levels of small heat shock proteins.","PeriodicalId":15113,"journal":{"name":"Journal of biochemistry and molecular biology","volume":"40 4","pages":"554-61"},"PeriodicalIF":0.0,"publicationDate":"2007-07-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26864169","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: 1

Determination and characterization of thermostable esterolytic activity from a novel thermophilic bacterium Anoxybacillus gonensis A4. 新型嗜热细菌gonoxybacillus A4的热稳定酯水解活性测定与表征。

Journal of biochemistry and molecular biology Pub Date : 2007-07-31 DOI: 10.5483/bmbrep.2007.40.4.588

Ozlem Faiz, Ahmet Colak, Nagihan Saglam, Sabriye Canakçi, Ali Osman Beldüz

{"title":"Determination and characterization of thermostable esterolytic activity from a novel thermophilic bacterium Anoxybacillus gonensis A4.","authors":"Ozlem Faiz, Ahmet Colak, Nagihan Saglam, Sabriye Canakçi, Ali Osman Beldüz","doi":"10.5483/bmbrep.2007.40.4.588","DOIUrl":"https://doi.org/10.5483/bmbrep.2007.40.4.588","url":null,"abstract":"A novel hot spring thermophile, Anoxybacillus gonensis A4 (A. gonensis A4) was investigated in terms of capability of tributyrin degradation and characterization of its thermostable esterase activity by the hydrolysis of p-nitrophenyl butyrate (PNPB). It was observed that A. gonensis A4 has an esterase with a molecular weight of 62 kDa. The extracellular crude preparation was characterized in terms of substrate specificity, pH and temperature optima and stability, kinetic parameters and inhibition/activation behaviour towards some chemicals and metal ions. Tributyrin agar assay showed that A. gonensis A4 secreted an esterase and V(max) and K(m) values of its activity were found to be 800 U/L and 176.5 microM, respectively in the presence of PNPB substrate. The optimum temperature and pH, for A. gonensis A4 esterase was 60-80 degrees C and 5.5, respectively. Although the enzyme activity was not significantly changed by incubating crude extract solution at 30-70 degrees C for 1 h, the enzyme activity was fully lost at 80 degrees C for same incubation period. The pH-stability profile showed that original crude esterase activity increased nearly 2-fold at pH 6.0. The effect of some chemicals on crude esterase activity indicated that A. gonensis A4 produce an esterase having serine residue in active site and -SH groups were essential for its activity.","PeriodicalId":15113,"journal":{"name":"Journal of biochemistry and molecular biology","volume":"40 4","pages":"588-94"},"PeriodicalIF":0.0,"publicationDate":"2007-07-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26864173","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: 43

DNA-dependent protein kinase mediates V(D)J recombination via RAG2 phosphorylation. dna依赖性蛋白激酶通过RAG2磷酸化介导V(D)J重组。

Journal of biochemistry and molecular biology Pub Date : 2007-05-31 DOI: 10.5483/bmbrep.2007.40.3.432

Young-Sool Hah, Jung Hwa Lee, Deok Ryong Kim

引用次数: 15

STP-C, an oncoprotein of herpesvirus saimiri augments the activation of NF-kappaB through ubiquitination of TRAF6. 猴疱疹病毒的一种癌蛋白STP-C通过TRAF6的泛素化增强NF-kappaB的激活。

Journal of biochemistry and molecular biology Pub Date : 2007-05-31 DOI: 10.5483/bmbrep.2007.40.3.341

Young-Hwa Chung, Byung Hak Jhun, Su-Chak Ryu, Heui-Soo Kim, Cheol-Min Kim, Bong-Seok Kim, Young-Ok Kim, Sang Jun Lee

{"title":"STP-C, an oncoprotein of herpesvirus saimiri augments the activation of NF-kappaB through ubiquitination of TRAF6.","authors":"Young-Hwa Chung, Byung Hak Jhun, Su-Chak Ryu, Heui-Soo Kim, Cheol-Min Kim, Bong-Seok Kim, Young-Ok Kim, Sang Jun Lee","doi":"10.5483/bmbrep.2007.40.3.341","DOIUrl":"https://doi.org/10.5483/bmbrep.2007.40.3.341","url":null,"abstract":"Herpesvirus saimiri (HVS), a member of the gamma-herpesvirus family, encodes an oncoprotein called Saimiri Transforming Protein (STP) which is required for lymphoma induction in non-human primates. Previous study has shown that STP-C, an oncoprotein of HVS, activates NF-kappaB signaling pathway. However, the detailed mechanism of STP-C-mediated NF-kappaB activation has not been reported yet. We first report that STP-C interacts with TRAF6 protein in vivo and in vitro and further investigation shows that Glu(12) residue of STP-C is critical for binding to TRAF6. Introduction of ubiquitin together with STP-C augments NF-kappaB activity compared to that of STP-C expression alone. STP-C expression further induces ubiquitination of endogenous TRAF6. In addition, either a deubiquitination enzyme, CYLD or a dominant negative E2-conjugation enzyme reduced NF-kappaB activity in spite of the presence of STP-C, supporting that the interaction between STP-C and TRAF6 induces ubiquitination of TRAF6. NF-kappaB activation by STP-C through the ubiquitinated TRAF6 causes the increased production of IL-8, an inflammatory chemokine and the enhanced expression of costimulatory molecule ICAM, which might ultimately contribute cellular transformation by the exposure of HVS-infected cells with inflammatory microenvironment and chronic activation.","PeriodicalId":15113,"journal":{"name":"Journal of biochemistry and molecular biology","volume":"40 3","pages":"341-8"},"PeriodicalIF":0.0,"publicationDate":"2007-05-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26771677","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: 10

The effect of benzene on the activity of adenosine deaminase in tissues of rats. 苯对大鼠组织中腺苷脱氨酶活性的影响。

Journal of biochemistry and molecular biology Pub Date : 2007-05-31 DOI: 10.5483/bmbrep.2007.40.3.295

Ali Turhan, Egemen Dere

{"title":"The effect of benzene on the activity of adenosine deaminase in tissues of rats.","authors":"Ali Turhan, Egemen Dere","doi":"10.5483/bmbrep.2007.40.3.295","DOIUrl":"https://doi.org/10.5483/bmbrep.2007.40.3.295","url":null,"abstract":"Swiss Albino (Rat rattus norvegicus) rats were intraperitoneally injected with a 100 mg kg(-1) dosage of benzene, a toxic and carcinogenic agent widely used for industrial purposes. Changes in the adenosine deaminase (ADA) activity in the liver, kidney and serum of rats were investigated at 0, 2, 4, 8, 16, 32 and 64 h following injection. Serum physiological was administered to each control group. Enzyme activities were measured spectrophotometrically. Our purpose was to further investigations of some diseases caused by benzene, and present evidence of variations in the activity of ADA enzyme effected by benzene. While benzene caused significant inhibitions in ADA activity in the liver at 16 and 32 h and at 0.05 probability level, no significant inhibition or activation occurred at other test periods (hours). ADA activity did not present any significant variation in the kidneys. It was observed that ADA activity displayed similar patterns in the control groups. Comparisons of ADA activities in the two groups showed a statistically significant decrease between 4(th) and 64(th) hours (p< 0.05), demonstrating a direct correlation between benzene and its effects on ADA enzymes.","PeriodicalId":15113,"journal":{"name":"Journal of biochemistry and molecular biology","volume":"40 3","pages":"295-301"},"PeriodicalIF":0.0,"publicationDate":"2007-05-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26770226","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: 9

Cloning and expression of cyclodextrin glycosyltransferase gene from Paenibacillus sp. T16 isolated from hot spring soil in northern Thailand. 泰国北部温泉土壤Paenibacillus sp. T16环糊精糖基转移酶基因的克隆与表达

Journal of biochemistry and molecular biology Pub Date : 2007-05-31 DOI: 10.5483/bmbrep.2007.40.3.333

Ratiya Charoensakdi, Shuichiro Murakami, Kenji Aoki, Vichien Rimphanitchayakit, Tipaporn Limpaseni

{"title":"Cloning and expression of cyclodextrin glycosyltransferase gene from Paenibacillus sp. T16 isolated from hot spring soil in northern Thailand.","authors":"Ratiya Charoensakdi, Shuichiro Murakami, Kenji Aoki, Vichien Rimphanitchayakit, Tipaporn Limpaseni","doi":"10.5483/bmbrep.2007.40.3.333","DOIUrl":"https://doi.org/10.5483/bmbrep.2007.40.3.333","url":null,"abstract":"Gene encoding cyclodextrin glycosyltransferase (CGTase), from thermotolerant Paenibacillus sp. T16 isolated from hot spring area in northern Thailand, was cloned and expressed in E. coli (JM109). The nucleotide sequences of both wild type and transformed CGTases consisted of 2139 bp open reading frame, 713 deduced amino acids residues with difference of 4 amino acid residues. The recombinant cells required 24 h culture time and a neutral pH for culture medium to produce compatible amount of CGTase compared to 72 h culture time and pH 10 for wild type. The recombinant and wild-type CGTases were purified by starch adsorption and phenyl sepharose column chromatography and characterized in parallel. Both enzymes showed molecular weight of 77 kDa and similar optimum pHs and temperatures with recombinant enzyme showing broader range. There were some significant difference in pH, temperature stability and kinetic parameters. The presence of high starch concentration resulted in higher thermostability in recombinant enzyme than the wild type. The recombinant enzyme was more stable at higher temperature and lower pH, with lower K(m) for coupling reaction using cellobiose and cyclodextrins as substrates.","PeriodicalId":15113,"journal":{"name":"Journal of biochemistry and molecular biology","volume":"40 3","pages":"333-40"},"PeriodicalIF":0.0,"publicationDate":"2007-05-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26770230","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: 20

A 43 kD protein isolated from the herb Cajanus indicus L attenuates sodium fluoride-induced hepatic and renal disorders in vivo. 从野菜Cajanus indicus L中分离的43 kD蛋白在体内可减轻氟化钠诱导的肝脏和肾脏疾病。

Journal of biochemistry and molecular biology Pub Date : 2007-05-31 DOI: 10.5483/bmbrep.2007.40.3.382

Prasenjit Manna, Mahua Sinha, Parames C Sil

{"title":"A 43 kD protein isolated from the herb Cajanus indicus L attenuates sodium fluoride-induced hepatic and renal disorders in vivo.","authors":"Prasenjit Manna, Mahua Sinha, Parames C Sil","doi":"10.5483/bmbrep.2007.40.3.382","DOIUrl":"https://doi.org/10.5483/bmbrep.2007.40.3.382","url":null,"abstract":"The herb, Cajanus indicus L, is well known for its hepatoprotective action. A 43 kD protein has been isolated, purified and partially sequenced from the leaves of this herb. A number of in vivo and in vitro studies carried out in our laboratory suggest that this protein might be a major component responsible for the hepatoprotective action of the herb. Our successive studies have been designed to evaluate the potential efficacy of this protein in protecting the hepatic as well as renal tissues from the sodium fluoride (NaF) induced oxidative stress. The experimental groups of mice were exposed to NaF at a dose of 600 ppm through drinking water for one week. This exposure significantly altered the activities of the antioxidant enzymes like superoxide dismutase (SOD), catalase (CAT), glutathione-S-transferase (GST), glutathione reductase (GR) and the cellular metabolites such as reduced glutathione (GSH), oxidized glutathione (GSSG), total thiols, lipid peroxidation end products in liver and kidney compared to the normal mice. Intraperitoneal administration of the protein at a dose of 2 mg/kg body weight for seven days followed by NaF treatment (600 ppm for next seven days) normalized the activities of the hepato-renal antioxidant enzymes, the level of cellular metabolites and lipid peroxidation end products. Post treatment with the protein for four days showed that it could help recovering the damages after NaF administration. Time-course study suggests that the protein could stimulate the recovery of both the organs faster than natural process. Effects of a known antioxidant, vitamin E, and a non-relevant protein, bovine serum albumin (BSA) have been included in the study to validate the experimental data. Combining all, result suggests that NaF could induce severe oxidative stress both in the liver and kidney tissues in mice and the protein possessed the ability to attenuate that hepato-renal toxic effect of NaF probably via its antioxidant activity.","PeriodicalId":15113,"journal":{"name":"Journal of biochemistry and molecular biology","volume":"40 3","pages":"382-95"},"PeriodicalIF":0.0,"publicationDate":"2007-05-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26771682","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: 39