Journal of Biological Chemistry (J BIOL CHEM )

Publisher: American Society of Biological Chemists; Rockefeller Institute for Medical Research; American Society for Biochemistry and Molecular Biology, American Society for Biochemistry and Molecular Biology

Description

Complete content of the Journal of Biological Chemistry as of April 1995.

Impact factor 4.60

  • Hide impact factor history
     
    Impact factor
  • 5-year impact
    5.02
  • Cited half-life
    10.00
  • Immediacy index
    0.94
  • Eigenfactor
    0.68
  • Article influence
    1.95
  • Website
    Journal of Biological Chemistry website
  • Other titles
    The Journal of biological chemistry, JBC
  • ISSN
    0021-9258
  • OCLC
    1782222
  • Material type
    Periodical, Internet resource
  • Document type
    Journal / Magazine / Newspaper, Internet Resource

Publisher details

American Society for Biochemistry and Molecular Biology

  • Pre-print
    • Author cannot archive a pre-print version
  • Post-print
    • Author cannot archive a post-print version
  • Restrictions
    • 12 months embargo
  • Conditions
    • Authors accepted peer-reviewed manuscript may be posted on an institutional repository
    • Publisher copyright and source must be acknowledged with set phrase: "This research was originally published in Journal Name. Author(s). Title. Journal Name. Year. Vol:pp-pp. © the American Society for Biochemistry and Molecular Biology"
    • On a non-profit server
    • Publisher's version/PDF cannot be used
  • Classification
    ​ white

Publications in this journal

  • Journal of Biological Chemistry 01/2015;
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    ABSTRACT: Due to the significant tumor suppressive role of microRNA-22 (miR-22), the current study was designed to understand the regulation of miR-22 and to identify additional downstream miR-22 targets in liver and colon cells. The data showed miR-22 was transcriptionally regulated by bile acid receptor farnesoid X receptor (FXR) through direct binding to an invert repeat-1 (IR-1) motif located at -1012 to -1025 bp upstream from miR-22. Among the studied primary and secondary bile acids, chenodeoxycholic acid (CDCA), which has the highest binding affinity to FXR, induced miR-22 level in both Huh7 liver and HCT116 colon cells in a dose-dependent manner. In addition, cyclin A2 (CCNA2) was identified as a miR-22 novel target in liver and colon cancer cells. The sequence of miR-22, which is conserved in mice, rats, humans, and other mammalians, aligns with the sequence of 3' UTR of CCNA2. CDCA treatment and miR-22 mimics reduced CCNA2 protein and increased the number of G0/G1 Huh7 and HCT116 cells. In FXR knockout (KO) mice, reduction of miR-22 was accompanied by elevated hepatic and ileal CCNA2 protein as well as increased number of hepatic and colonic Ki-67-positive cells. In humans, the expression levels of miR-22 and CCNA2 are inversely correlated in liver and colon cancers. Taken together, our data showed that bile acid-activated FXR stimulates miR-22-silenced CCNA2, a novel pathway for FXR to exert its protective effect in the gastrointestinal tract.
    Journal of Biological Chemistry 01/2015;
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    ABSTRACT: The ATP synthase of many archaea has the conserved sodium ion binding motif in its rotor subunit, implying that these A1AO ATP synthases use Na(+) as coupling ion. However, this has never been experimentally verified with a purified system. To experimentally address the nature of the coupling ion, we have purified the A1AO ATP synthase from T. onnurineus. It contains nine subunits that are functionally coupled. The enzyme hydrolyzed ATP, CTP, GTP, UTP and ITP with nearly identical activities of around 40 U/mg protein and was active over a wide pH range with maximal activity at pH 7. Noteworthy was the temperature profile. ATP hydrolysis was maximal at 80°C and still retained an activity of 2.5 U/mg protein at 45°C. The high activity of the enzyme at 45°C opened, for the first time, a way to directly measure ion transport in an A1AO ATP synthase. Therefore, the enzyme was reconstituted into liposomes generated from Escherichia coli lipids. These proteoliposomes were still active at 45°C and coupled ATP hydrolysis to primary and electrogenic Na(+) transport. This is the first proof of Na(+) transport by an A1AO ATP synthase and these findings are discussed in light of the distribution of the sodium ion binding motif in archaea and the role of Na(+) in the bioenergetics of archaea. Copyright © 2015, The American Society for Biochemistry and Molecular Biology.
    Journal of Biological Chemistry 01/2015;
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    ABSTRACT: Non-thermal atmospheric pressure plasma provides a novel therapeutic opportunity to control redox-based processes, e.g. wound healing, cancer, or inflammatory diseases. By spatial and time resolved delivery of reactive oxygen- and nitrogen species, it allows to stimulate or inhibit cellular processes in biological systems. Our data show that both, gene and protein expression, are highly affected by non-thermal plasma. The nuclear erythroid-related factor 2 (Nrf2) and phase II enzyme-pathway components were found to act as key controllers orchestrating the cellular response in keratinocytes. Additionally, the glutathione metabolism was affected which is a marker for Nrf2-related signaling events. Among the most robustly increased genes and proteins heme oxygenase 1, NADPH quinone oxidoreductase 1, and growth factors were found. The roles of Nrf2-targets, investigated by siRNA silencing, revealed that Nrf2 acts as an important switch for sensing oxidative stress events. Moreover, the influence of non-thermal plasma on the Nrf2 pathway prepares cells against exogenic noxae and increases their resilience against oxidative species. Via paracrine mechanisms distant cells benefit from cell-cell communication. The finding that non-thermal plasma triggers hormesis-like processes in keratinocytes facilitates the understanding of plasma-tissue interaction and its clinical application.
    Journal of Biological Chemistry 01/2015;
  • [Show abstract] [Hide abstract]
    ABSTRACT: Non-thermal atmospheric pressure plasma provides a novel therapeutic opportunity to control redox-based processes, e.g. wound healing, cancer, or inflammatory diseases. By spatial and time resolved delivery of reactive oxygen- and nitrogen species, it allows to stimulate or inhibit cellular processes in biological systems. Our data show that both, gene and protein expression, are highly affected by non-thermal plasma. The nuclear erythroid-related factor 2 (Nrf2) and phase II enzyme-pathway components were found to act as key controllers orchestrating the cellular response in keratinocytes. Additionally, the glutathione metabolism was affected which is a marker for Nrf2-related signaling events. Among the most robustly increased genes and proteins heme oxygenase 1, NADPH quinone oxidoreductase 1, and growth factors were found. The roles of Nrf2-targets, investigated by siRNA silencing, revealed that Nrf2 acts as an important switch for sensing oxidative stress events. Moreover, the influence of non-thermal plasma on the Nrf2 pathway prepares cells against exogenic noxae and increases their resilience against oxidative species. Via paracrine mechanisms distant cells benefit from cell-cell communication. The finding that non-thermal plasma triggers hormesis-like processes in keratinocytes facilitates the understanding of plasma-tissue interaction and its clinical application.
    Journal of Biological Chemistry 01/2015;
  • [Show abstract] [Hide abstract]
    ABSTRACT: Proton-coupled monocarboxylate transporters (MCTs) mediate the exchange of high-energy metabolites like lactate between different cells and tissues. We have reported previously that carbonic anhydrase II augments transport activity of MCT1 and MCT4 by a non-catalytic mechanism, while leaving transport activity of MCT2 unaltered. In the present study we combined electrophysiological measurements in Xenopus oocytes and pull-down experiments to analyze the direct interaction between CAII and MCT1, MCT2 and MCT4, respectively. Transport activity of MCT2-WT, which lacks a putative CAII-binding site, is not augmented by CAII. However, introduction of a CAII-binding site into the C-terminus of MCT2 resulted in CAII-mediated facilitation of MCT2 transport activity. Interestingly, introduction of three glutamic acid residues alone was not sufficient to establish a direct interaction between MCT2 and CAII, but the cluster had to be arranged in a fashion that allowed access to the binding moiety in CAII. We further demonstrate that functional interaction between MCT4 and CAII requires direct binging of the enzyme to the acidic cluster E431EE in the C-terminus of MCT4 in a similar fashion as previously shown for binding of CAII to the cluster E489EE in the C-terminus of MCT1. In CAII, binding to MCT1 and MCT4 is mediated by a histidine residue at position 64. Taken together, our results suggest that facilitation of MCT transport activity by CAII requires direct binding between histidine 64 in CAII and a cluster of glutamic acid residues in the transporter's C-terminus that has to be positioned in a surrounding that allows access to CAII.
    Journal of Biological Chemistry 01/2015;
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    ABSTRACT: Mixed Lineage Leukemia protein-1 (MLL1) is a member of the SET1 family of histone H3 lysine 4 (H3K4) methyltransferases that are required for metazoan development. MLL1 is the best-characterized human SET1 family member, which includes MLL1-4 and Setd1A/B. MLL1 assembles with WRAD (WDR5, RbBP5, Ash2L, DPY-30) to form the MLL1 core complex, which is required for H3K4 dimethylation and transcriptional activation. Since all SET1 family proteins interact with WRAD in vivo, it is hypothesized they are regulated by similar mechanisms. However, recent evidence suggests differences among family members that may reflect unique regulatory inputs in the cell. Missing is an understanding of the intrinsic enzymatic activities of different SET1 family complexes under standard conditions. In this investigation, we reconstituted each human SET1 family core complex and compared subunit assembly and enzymatic activities. We found that in the absence of WRAD, all but one SET domain catalyzes at least weak H3K4 monomethylation. In the presence of WRAD, all SET1 family members showed stimulated monomethtranferase activity, but differed in their di- and trimethylation activities. We found that these differences are correlated with evolutionary lineage, suggesting these enzyme complexes have evolved to accomplish unique tasks within metazoan genomes. To understand the structural basis for these differences, we employed a ″phylogenetic scanning mutagenesis″ assay and identified a cluster of amino acid substitutions that confer a WRAD-dependent gain-of-function dimethylation activity on complexes assembled with the MLL3 or Drosophila Trithorax proteins. These results form the basis for understanding how WRAD differentially regulates SET1 family complexes in vivo.
    Journal of Biological Chemistry 01/2015;
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    ABSTRACT: CCL28 is a human chemokine constitutively expressed by epithelial cells in diverse mucosal tissues and is known to attract a variety of immune cell types including T-cell subsets and eosinophils. Elevated levels of CCL28 have been found in the airways of individuals with asthma, and previous studies have indicated that CCL28 plays a vital role in the acute development of post-viral asthma. Our study builds on this demonstrating that CCL28 is also important in the chronic post-viral asthma phenotype. In the absence of a viral infection, we also demonstrate that CCL28 is both necessary and sufficient for induction of asthma pathology. Additionally, we present the first effort aimed at elucidating the structural features of CCL28. Chemokines are defined by a conserved tertiary structure comprised of a three-stranded β-sheet and a C-terminal α-helix constrained by two disulfide bonds. In addition to the four disulfide bond-forming cysteine residues that define the traditional chemokine fold, CCL28 possesses two additional cysteine residues that form a third disulfide bond. If all disulfide bonds are disrupted, recombinant human CCL28 is no longer able to drive mouse CD4+ T-cell chemotaxis or in vivo airway hyper-reactivity indicating that the conserved chemokine fold is necessary for its biologic activity. Due to the intimate relationship between CCL28 and asthma pathology, it is clear that CCL28 presents a novel target for the development of alternative asthma therapeutics. Copyright © 2015, The American Society for Biochemistry and Molecular Biology.
    Journal of Biological Chemistry 01/2015;
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    ABSTRACT: The global prevalence of weight loss is increasing, especially in young women. However, the extent and mechanisms by which maternal weight loss affects the offspring is still poorly understood. Here using an enriched environment (EE)-induced weight loss model, we show that maternal weight loss improves the general health and reprograms metabolic gene expression in mouse offspring, and the epigenetic alterations can be inherited for at least two generations. EE in mothers induced weight loss and its associated physiological and metabolic changes such as decreased adiposity and improved glucose tolerance and insulin sensitivity. Relative to controls, their offspring exhibited improved general health such as reduced fat accumulation, decreased plasmic and hepatic lipid levels, as well as improved glucose tolerance and insulin sensitivity. Maternal weight loss altered gene expression patterns in the liver of offspring, with coherent downregulation of genes involved in lipid and cholesterol biosynthesis. Epigenomic profiling of offspring livers revealed numerous changes in cytosine methylation depending on maternal weight loss, including reproducible changes in promoter methylation over several key lipid biosynthesis genes, correlated with their expression patterns. Embryo transfer studies indicated that oocyte alteration responding to maternal metabolic conditions is a strong factor in determining metabolic and epigenetic changes in offspring. Several important lipid metabolism-related genes have been identified to partially inherit methylated alleles from oocytes. Our study reveals a molecular and mechanistic basis of how maternal lifestyle modification affects metabolic changes in the offspring. Copyright © 2015, The American Society for Biochemistry and Molecular Biology.
    Journal of Biological Chemistry 01/2015;
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    ABSTRACT: Synapse-associated protein 102 (SAP102) is a scaffolding protein abundantly expressed early in development that mediates glutamate receptor trafficking during synaptogenesis. Mutations in human SAP102 have been reported to cause intellectual disability, which is consistent with its important role during early postnatal development. SAP102 contains PDZ, SH3 and guanylate kinase (GK)-like domains, which mediate specific protein-protein interactions. SAP102 binds directly to N-methyl-D-aspartate receptors (NMDARs), anchors receptors at synapses and facilitates transduction of NMDAR signals. Proper localization of SAP102 at the postsynaptic density (PSD) is essential to these functions. However, how SAP102 is targeted to synapses is unclear. In the current study, we find that synaptic localization of SAP102 is regulated by alternative splicing. The SAP102 splice variant that possesses a C-terminal insert (I2) between the SH3 and GK domains is highly enriched at dendritic spines. We also show that there is an intramolecular interaction between the SH3 and GK domains in SAP102 but that the I2 splicing does not influence SH3-GK interaction. Previously, we have shown that SAP102 expression promotes spine lengthening. We now find that the spine lengthening effect is independent of the C-terminal alternative splicing of SAP102. In addition, expression of I2-containing SAP102 isoforms is regulated developmentally. Knockdown of endogenous I2-containing SAP102 isoforms differentially affect NMDAR surface expression in a subunit-specific manner. These data shed new light on the role of SAP102 in the regulation of NMDAR trafficking. Copyright © 2015, The American Society for Biochemistry and Molecular Biology.
    Journal of Biological Chemistry 01/2015;