The Journal of Biochemistry最新文献_第2页

NEU1 sialidase controls gene expression and secretion of IL-6 and MCP-1 through NF-&kgr;B pathway in 3T3-L1 adipocytes NEU1唾液酸酶通过NF-&kgr;B途径控制3T3-L1脂肪细胞中IL-6和MCP-1的基因表达和分泌

The Journal of Biochemistry Pub Date : 2017-08-01 DOI: 10.1093/jb/mvx006

Y. Natori, M. Nasui, K. Edo, Shogo Sato, T. Sakurai, T. Kizaki, F. Kihara-Negishi

引用次数: 15

Phosphorylation of clustered serine residues in the N-terminus of BPS domain negatively regulates formation of the complex between human Grb14 and insulin receptor BPS结构域n端丝氨酸簇残基的磷酸化负向调控人Grb14与胰岛素受体复合物的形成

The Journal of Biochemistry Pub Date : 2017-08-01 DOI: 10.1093/jb/mvx007

J. Taira, Yutaka Kida, Kohei Inatomi, H. Komatsu, Y. Higashimoto, H. Sakamoto

{"title":"Phosphorylation of clustered serine residues in the N-terminus of BPS domain negatively regulates formation of the complex between human Grb14 and insulin receptor","authors":"J. Taira, Yutaka Kida, Kohei Inatomi, H. Komatsu, Y. Higashimoto, H. Sakamoto","doi":"10.1093/jb/mvx007","DOIUrl":"https://doi.org/10.1093/jb/mvx007","url":null,"abstract":"Growth factor receptor-bound protein 14 (Grb14) is a negative regulator of insulin receptor (IR) and is involved in a negative feedback mechanism of insulin signaling. Grb14 associates with IR and inhibits its tyrosine kinase activity through the between pleckstrin homology and Src homology-2 (BPS) domain. We previously reported that the pharmacological inhibition and knockdown of glycogen synthase kinase-3 (GSK-3) facilitates the insulin-induced complex formation of human Grb14 (hGrb14) and IR, suggesting that GSK-3 suppresses hGrb14 recruitment to IR. This study further investigated a functional phosphorylation of the serine residues in hGrb14 BPS domain, identified as putative GSK-3 targets to verify an effect of GSK-3 on the hGrb14-IR complex formation. In vitro kinase assay using the motif-derived peptides showed that the serine residues located in N-terminal (Ser358, Ser362 and Ser366) and C-terminal (Ser419 and Ser423) regions of the BPS domain were phosphorylated by GSK-3. Co-immunoprecipitation and yeast two-hybrid (Y2H) experiments suggested that the negative charges genetically introduced on the Ser358, Ser362 and Ser366 suppressed the association of hGrb14 to IR. Surface plasmon resonance experiment gave Kd values of 8 nM for recombinant hGrb14 with respect to the interaction with IR β-subunit, and this affinity was lost after the replacements of the Ser358, Ser362 and Ser366 with glutamic acid residues. Y2H experiment with the BPS domain alone; however, did not show any difference owing to the same mutations. It is therefore evident that the N-terminus of the BPS domain plays an important role in the regulation of hGrb14-IR complex formation through phosphorylation, in addition to other domains.","PeriodicalId":22605,"journal":{"name":"The Journal of Biochemistry","volume":"12 1","pages":"113–122"},"PeriodicalIF":0.0,"publicationDate":"2017-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91355782","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: 4

Papain cleavage of the 38,000-dalton fragment inhibits the binding of 4, 4′-diisothiocyanostilbene-2, 2′-disulfonate to lys-539 on the 60,000-dalton fragment in human band 3 木瓜蛋白酶对38,000道尔顿片段的切割抑制了4,4 ' -二异硫氰基二苯乙烯- 2,2 ' -二磺酸盐与人带3中60,000道尔顿片段上的赖氨酸-539的结合

The Journal of Biochemistry Pub Date : 2017-08-01 DOI: 10.1093/jb/mvx005

Takeo Yamaguchi, Hideaki Kojima, Shiori Kawaguchi, M. Shimada, Haruka Aso

{"title":"Papain cleavage of the 38,000-dalton fragment inhibits the binding of 4, 4′-diisothiocyanostilbene-2, 2′-disulfonate to lys-539 on the 60,000-dalton fragment in human band 3","authors":"Takeo Yamaguchi, Hideaki Kojima, Shiori Kawaguchi, M. Shimada, Haruka Aso","doi":"10.1093/jb/mvx005","DOIUrl":"https://doi.org/10.1093/jb/mvx005","url":null,"abstract":"Human band 3 is a 98-kDa transmembrane (TM) protein comprising 14 TM segments. Papain cleavages band 3 into 38- and 60-kDa fragments. Under vigorous conditions, the cleavage of the loop region between the TM 7 of gate domain and the TM 8 of core domain in the 38-kDa fragment produces 7- and 31-kDa fragments. Conformational changes of the TM 5 segment containing Lys-539 by cleavage of the 38-kDa fragment remain unclear. Pressure-induced haemolysis of erythrocytes was suppressed by binding of 4, 4'-diisothiocyanostilbene-2, 2'-disulfonate (DIDS) to Lys-539. Such effect of DIDS was not observed upon cleavage of the 38-kDa fragment, because of inhibition of DIDS binding to Lys-539. Using fluorescence of DIDS labelled to Lys-539, conformational changes of band 3 were examined. Fluorescence spectra demonstrated that the molecular motion of DIDS is more restricted upon digestion of the 38-kDa fragment. Interestingly, the quenching of DIDS fluorescence showed that Hg2+ is less accessible to DIDS upon digestion of the 38-kDa fragment. Taken together, we propose that the conformational changes of the TM 5 segment characterized by the sequestration and restricted motion of Lys-539 are induced by the cleavage of the loop region between the TM 7 and the TM 8.","PeriodicalId":22605,"journal":{"name":"The Journal of Biochemistry","volume":"117 1","pages":"103–111"},"PeriodicalIF":0.0,"publicationDate":"2017-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84159787","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

PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X PRMT2与剪接因子相互作用，调控BCL-X的选择性剪接

The Journal of Biochemistry Pub Date : 2017-07-01 DOI: 10.1093/jb/mvw102

M. Vhuiyan, Magnolia L. Pak, Margaret A. Park, Dylan Thomas, Ted M. Lakowski, C. Chalfant, A. Frankel

引用次数: 24

Plakoglobin maintains the integrity of vascular endothelial cell junctions and regulates VEGF-induced phosphorylation of VE-cadherin 血小板红蛋白维持血管内皮细胞连接的完整性并调节vegf诱导的ve -钙粘蛋白磷酸化

The Journal of Biochemistry Pub Date : 2017-07-01 DOI: 10.1093/jb/mvx001

F. Muramatsu, H. Kidoya, Hisamichi Naito, Yumiko Hayashi, Tomohiro Iba, N. Takakura

{"title":"Plakoglobin maintains the integrity of vascular endothelial cell junctions and regulates VEGF-induced phosphorylation of VE-cadherin","authors":"F. Muramatsu, H. Kidoya, Hisamichi Naito, Yumiko Hayashi, Tomohiro Iba, N. Takakura","doi":"10.1093/jb/mvx001","DOIUrl":"https://doi.org/10.1093/jb/mvx001","url":null,"abstract":"Plakoglobin, also known as γ-catenin, is a close homolog of β-catenin and interacts with shared protein partners. Functions of β-catenin in cell adhesion are well-documented in terms of maintaining endothelial barrier function by interacting with vascular endothelial (VE)-cadherin. Plakoglobin also interacts with VE-cadherin, but its function in cell adhesion is not well understood. Here, we investigated plakoglobin function in vascular endothelial cell (ECs)-cell junction integrity. Knock-down of plakoglobin expression in ECs did not prevent cell proliferation or cell migration, but induced destabilization of the membrane distribution of VE-cadherin and resulted in increased permeability. Plakoglobin contributes to VE-cadherin-dependent adhesion in the steady state, but on stimulation with vascular endothelial growth factor (VEGF), it is essential for inducing sufficient VE-cadherin phosphorylation on VEGF signaling, thereby destabilizing cell-cell junctions. Furthermore, knock-down of plakoglobin expression increased vascular endothelial protein tyrosine phosphatase activity, an endothelial-specific membrane protein associating with VE-cadherin. These results indicate that plakoglobin plays multiple roles in regulation of cell-cell adhesion in a context dependent manner.","PeriodicalId":22605,"journal":{"name":"The Journal of Biochemistry","volume":"49 1","pages":"55–62"},"PeriodicalIF":0.0,"publicationDate":"2017-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77088491","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: 13

High dose of antibiotic colistin induces oligomerization of molecular chaperone HSP90 高剂量粘菌素诱导分子伴侣HSP90寡聚

The Journal of Biochemistry Pub Date : 2017-07-01 DOI: 10.1093/jb/mvw104

Shuntaro Togashi, Kyosuke Takahashi, Arisa Tamura, I. Toyota, S. Hatakeyama, A. Komatsuda, Ikuru Kudo, Erina Sasaki Kudoh, Tomoya Okamoto, Asami Haga, Asuka Miyamoto, Ewa Grave, T. Sugawara, Hiroaki Shimizu, H. Itoh

{"title":"High dose of antibiotic colistin induces oligomerization of molecular chaperone HSP90","authors":"Shuntaro Togashi, Kyosuke Takahashi, Arisa Tamura, I. Toyota, S. Hatakeyama, A. Komatsuda, Ikuru Kudo, Erina Sasaki Kudoh, Tomoya Okamoto, Asami Haga, Asuka Miyamoto, Ewa Grave, T. Sugawara, Hiroaki Shimizu, H. Itoh","doi":"10.1093/jb/mvw104","DOIUrl":"https://doi.org/10.1093/jb/mvw104","url":null,"abstract":"Colistin is an antimicrobial cationic peptide that belongs to the polymyxin family. Colistin was clinically used for the treatment of gram-negative infections but fell out of favour because of its significant side effects including neurotoxicity and nephrotoxicity. More recently, colistin has been regarded as one of the important options for nosocomial infections caused by multidrug resistant bacteria. Mechanisms of both the side effect onset of the drug and the side effect reduction are yet to be elucidated. In this study, we identified the specific binding protein of colistin using an affinity column chromatography. Colistin binds to the molecular chaperone HSP90. Although colistin slightly suppressed the chaperone activity of HSP90, there are no effects on the ATPase activity for a low concentration of colistin. Interestingly, colistin-induced aggregation of HSP90 via the N-domain. As for the cell viability of the SHSY5Y cell, the cell viability decreased to approximately 80% by the colistin 300 μM. However, the cell viability recovered to approximately 100% by adding ATP dosage. The same result was obtained by dot blot assay using anti-HSP90 antibody. Our results may help to understand the side effect mechanism of colistin.","PeriodicalId":22605,"journal":{"name":"The Journal of Biochemistry","volume":"34 1","pages":"27–36"},"PeriodicalIF":0.0,"publicationDate":"2017-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88011595","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

Characterization of two ferredoxin-dependent sulfite reductases having different substrate specificity in the red alga Cyanidioschyzon merolae 红藻中具有不同底物特异性的两种依赖铁氧化还原蛋白的亚硫酸盐还原酶的表征

The Journal of Biochemistry Pub Date : 2017-07-01 DOI: 10.1093/jb/mvw103

Kohsuke Sekine, Takashi Moriyama, JuYaen Kim, T. Hase, N. Sato

{"title":"Characterization of two ferredoxin-dependent sulfite reductases having different substrate specificity in the red alga Cyanidioschyzon merolae","authors":"Kohsuke Sekine, Takashi Moriyama, JuYaen Kim, T. Hase, N. Sato","doi":"10.1093/jb/mvw103","DOIUrl":"https://doi.org/10.1093/jb/mvw103","url":null,"abstract":"Assimilatory sulfite reductase (SiR) and nitrite reductase (NiR), which are important determinants in biomass productivity, are homologous enzymes that catalyze the reduction of sulfite to sulfide and nitrite to ammonium, respectively. They have a siroheme and a [4Fe-4S] cluster as prosthetic groups in common. The red alga Cyanidioschyzon merolae encodes two SiR-like enzymes, CmSiRA and CmSiRB, which are likely products of recent gene duplication, but no homologues of NiR. The growth in a medium containing nitrate, however, must be supported by a nitrite reducing activity. CmSiRB was not detected in the ammonium medium, but, in the nitrate medium, it was present at a level 1/6 of that of constitutively expressed CmSiRA. Kinetic analysis of the two enzymes showed that CmSiRA has high kcat values with both sulfite and nitrite, but CmSiRB has virtually only the activity of nitrite reduction, although the Km value against nitrite was fairly high in both enzymes. The six amino acid residues that are specific to CmSiRB among various SiR-like enzymes in the active site were mutagenized to mimic partially CmSiRA. Among them, the mutation S217C in CmSiRB partially recovered sulfite reduction activity, suggesting that this residue is a major determinant of substrate specificity.","PeriodicalId":22605,"journal":{"name":"The Journal of Biochemistry","volume":"28 1","pages":"37–43"},"PeriodicalIF":0.0,"publicationDate":"2017-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74012657","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: 2

The FOXP2 forkhead domain binds to a variety of DNA sequences with different rates and affinities FOXP2叉头结构域以不同的速率和亲和力与多种DNA序列结合

The Journal of Biochemistry Pub Date : 2017-07-01 DOI: 10.1093/jb/mvx003

Helen Webb, Olga Steeb, Ashleigh A Blane, L. Rotherham, S. Aron, P. Machanick, H. Dirr, S. Fanucchi

{"title":"The FOXP2 forkhead domain binds to a variety of DNA sequences with different rates and affinities","authors":"Helen Webb, Olga Steeb, Ashleigh A Blane, L. Rotherham, S. Aron, P. Machanick, H. Dirr, S. Fanucchi","doi":"10.1093/jb/mvx003","DOIUrl":"https://doi.org/10.1093/jb/mvx003","url":null,"abstract":"FOXP2 is a member of the P subfamily of FOX transcription factors, the DNA-binding domain of which is the winged helix forkhead domain (FHD). In this work we show that the FOXP2 FHD is able to bind to various DNA sequences, including a novel sequence identified in this work, with different affinities and rates as detected using surface plasmon resonance. Combining the experimental work with molecular docking, we show that high-affinity sequences remain bound to the protein for longer, form a greater number of interactions with the protein and induce a greater structural change in the protein than low-affinity sequences. We propose a binding model for the FOXP2 FHD that involves three types of binding sequence: low affinity sites which allow for rapid scanning of the genome by the protein in a partially unstructured state; moderate affinity sites which serve to locate the protein near target sites and high-affinity sites which secure the protein to the DNA and induce a conformational change necessary for functional binding and the possible initiation of downstream transcriptional events.","PeriodicalId":22605,"journal":{"name":"The Journal of Biochemistry","volume":"63 1","pages":"45–54"},"PeriodicalIF":0.0,"publicationDate":"2017-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87572832","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: 7

Mitochondrial function is required for extracellular ATP-induced NLRP3 inflammasome activation 细胞外atp诱导的NLRP3炎性体激活需要线粒体功能

The Journal of Biochemistry Pub Date : 2017-06-01 DOI: 10.1093/jb/mvw098

Daichi Sadatomi, Kazutaka Nakashioya, Sayaka Mamiya, Shino Honda, Yuka Kameyama, Y. Yamamura, S. Tanimura, K. Takeda

{"title":"Mitochondrial function is required for extracellular ATP-induced NLRP3 inflammasome activation","authors":"Daichi Sadatomi, Kazutaka Nakashioya, Sayaka Mamiya, Shino Honda, Yuka Kameyama, Y. Yamamura, S. Tanimura, K. Takeda","doi":"10.1093/jb/mvw098","DOIUrl":"https://doi.org/10.1093/jb/mvw098","url":null,"abstract":"The NLRP3 inflammasome plays a critical role in the processing and release of inflammatory cytokines, such as interleukin-1β (IL-1β) and IL-18. Accumulating evidence suggests that mitochondria are common mediators of NLRP3 inflammasome activation induced by a wide range of inflammatory stimuli; however, the precise role of mitochondria is still not fully understood. Here, we show that mitochondrial function is required for extracellular ATP-induced NLRP3 inflammasome activation. Extracellular ATP induced the loss of mitochondrial membrane potential and mitochondrial fragmentation in a different manner than other stimuli in primary mouse macrophages. CCCP, an uncoupler and antimycin A, an inhibitor of the mitochondrial electron transport chain, inhibited IL-1β release induced by ATP but not by other stimuli. CCCP did not inhibit the ATP-induced generation of reactive oxygen species and cell death, both of which are known to promote IL-1β release, but did inhibit the ATP-induced activation of caspase-1, a component of the NLRP3 inflammasome. These results suggest that mitochondrial function is required somewhat specifically for ATP-induced NLRP3 inflammasome activation. In contrast to many previous reports that dysfunctional mitochondria promote NLRP3 inflammasome activation, the function of intact mitochondria appears to be required for NLRP3 inflammasome activation, depending on the stimulus.","PeriodicalId":22605,"journal":{"name":"The Journal of Biochemistry","volume":"7 1","pages":"503–512"},"PeriodicalIF":0.0,"publicationDate":"2017-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75524698","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: 41

Simultaneous ablation of prmt-1 and prmt-5 abolishes asymmetric and symmetric arginine dimethylations in Caenorhabditis elegans 同时消融prmt-1和prmt-5可消除秀丽隐杆线虫中不对称和对称精氨酸二甲基化

The Journal of Biochemistry Pub Date : 2017-06-01 DOI: 10.1093/jb/mvw101

K. Hirota, Chihiro Shigekawa, Sho Araoi, L. Sha, Takayuki Inagawa, Akihiko Kanou, K. Kako, H. Daitoku, A. Fukamizu

{"title":"Simultaneous ablation of prmt-1 and prmt-5 abolishes asymmetric and symmetric arginine dimethylations in Caenorhabditis elegans","authors":"K. Hirota, Chihiro Shigekawa, Sho Araoi, L. Sha, Takayuki Inagawa, Akihiko Kanou, K. Kako, H. Daitoku, A. Fukamizu","doi":"10.1093/jb/mvw101","DOIUrl":"https://doi.org/10.1093/jb/mvw101","url":null,"abstract":"Protein arginine methyltransferases (PRMTs) catalyze the transfer of a methyl group from S-adenosylmethionine to arginine residues and are classified into two types: type I producing asymmetric dimethylarginine (ADMA) and type II producing symmetric dimethylarginine (SDMA). PRMTs have been shown to regulate many cellular processes, including signal transduction, transcriptional regulation and RNA processing. Since the loss-of-function mutation of PRMT1 and PRMT5, each of which is the predominant type I and II, respectively, causes embryonic lethality in mice, their physiological significance at the whole-body level remains largely unknown. Here, we show the morphological and functional phenotypes of single or double null alleles of prmt-1 and prmt-5 in Caenorhabditis elegans. The prmt-1;prmt-5 double mutants are viable, and exhibit short body length and small brood size compared to N2 and each of the single mutants. The liquid chromatography-tandem mass spectrometry analysis demonstrated that the levels of ADMA and SDMA were abolished in the prmt-1;prmt-5 double mutants. Both prmt-1 and prmt-5 were required for resistance to heat and oxidative stresses, whereas prmt-5 is not involved in lifespan regulation even when prmt-1 is ablated. This mutant strain would be a useful model animal for investigating the role of asymmetric and symmetric arginine dimethylation in vivo.","PeriodicalId":22605,"journal":{"name":"The Journal of Biochemistry","volume":"27 1","pages":"521–527"},"PeriodicalIF":0.0,"publicationDate":"2017-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73481849","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