Pseudopeptidic ligands: exploring the self-assembly of isopthaloylbisglycine (H2IBG) and divalent metal ions

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The Influence of Chemical and Mineral Compositions on the Parameterization of Immersion Freezing by Volcanic Ash Particles

Volcanic ash (VA) from explosive eruptions contributes to aerosol loadings in the atmosphere. Aside from the negative impact of VA on air quality and aviation, these particles can alter the optical and microphysical properties of clouds by triggering ice formation, thereby influencing precipitation and climate. Depending on the volcano and eruption style, VA displays a wide range of different physical, chemical, and mineralogical properties. Here, we present a unique data set on the ice nucleation activity of 15 VA samples obtained from different volcanoes worldwide. The ice nucleation activities of these samples were studied in the Aerosol Interaction and Dynamics in the Atmosphere (AIDA) cloud simulation chamber as well as with the Ice Nucleation Spectrometer of the Karlsruhe Institute of Technology (INSEKT). All VA particles nucleated ice in the immersion freezing mode from 263 to 238K with ice nucleation active site (INAS) densities ranging from ∼10$^{5}$ to 10$^{11}$ m$^{-2}$, respectively. The variabilities observed among the VA samples, at any given temperature, range over 3.5 orders of magnitude. The ice-nucleating abilities of VA samples correlate to varying degrees with their bulk pyroxene and plagioclase contents as a function of temperature. We combined our new data set with existing literature data to develop an improved ice nucleation parameterization for natural VA in the immersion freezing mode. This should be useful for modeling the impact of VA on clouds

The Influence of Chemical and Mineral Compositions on the Parameterization of Immersion Freezing by Volcanic Ash Particles

Funder: Helmholtz Association of German Research CentresAbstract: Volcanic ash (VA) from explosive eruptions contributes to aerosol loadings in the atmosphere. Aside from the negative impact of VA on air quality and aviation, these particles can alter the optical and microphysical properties of clouds by triggering ice formation, thereby influencing precipitation and climate. Depending on the volcano and eruption style, VA displays a wide range of different physical, chemical, and mineralogical properties. Here, we present a unique data set on the ice nucleation activity of 15 VA samples obtained from different volcanoes worldwide. The ice nucleation activities of these samples were studied in the Aerosol Interaction and Dynamics in the Atmosphere (AIDA) cloud simulation chamber as well as with the Ice Nucleation Spectrometer of the Karlsruhe Institute of Technology (INSEKT). All VA particles nucleated ice in the immersion freezing mode from 263 to 238K with ice nucleation active site (INAS) densities ranging from ∼105 to 1011 m−2, respectively. The variabilities observed among the VA samples, at any given temperature, range over 3.5 orders of magnitude. The ice‐nucleating abilities of VA samples correlate to varying degrees with their bulk pyroxene and plagioclase contents as a function of temperature. We combined our new data set with existing literature data to develop an improved ice nucleation parameterization for natural VA in the immersion freezing mode. This should be useful for modeling the impact of VA on clouds

Galiellalactone Inhibits Stem Cell-Like ALDH-Positive Prostate Cancer Cells

Galiellalactone is a potent and specific inhibitor of STAT3 signaling which has been shown to possess growth inhibitory effects on prostate cancer cells expressing active STAT3. In this study we aimed to investigate the effect of galiellalactone on prostate cancer stem cell-like cells. We explored the expression of aldehyde dehydrogenase (ALDH) as a marker for cancer stem cell-like cells in different human prostate cancer cell lines and the effects of galiellalactone on ALDH expressing (ALDH+) prostate cancer cells. ALDH+ subpopulations were detected and isolated from the human prostate cancer cell lines DU145 and long-term IL-6 stimulated LNCaP cells using ALDEFLUOR® assay and flow cytometry. In contrast to ALDH− cells, ALDH+ prostate cancer cells showed cancer stem cell-like characteristics such as increased self-renewing and colony forming capacity and tumorigenicity. In addition, ALDH+ cells showed an increased expression of putative prostate cancer stem cell markers (CD44 and integrin α2β1). Furthermore, ALDH+ cells expressed phosphorylated STAT3. Galiellalactone treatment decreased the proportion of ALDH+ prostate cancer cells and induced apoptosis of ALDH+ cells. The gene expression of ALDH1A1 was downregulated in vivo in galiellalactone treated DU145 xenografts. These findings emphasize that targeting the STAT3 pathway in prostate cancer cells, including prostate cancer stem cell-like cells, is a promising therapeutic approach and that galiellalactone is an interesting compound for the development of future prostate cancer drugs

Pathogen and Circadian Controlled 1 (PCC1) Protein Is Anchored to the Plasma Membrane and Interacts with Subunit 5 of COP9 Signalosome in Arabidopsis

The Pathogen and Circadian Controlled 1 (PCC1) gene, previously identified and further characterized as involved in defense to pathogens and stress-induced flowering, codes for an 81-amino acid protein with a cysteine-rich C-terminal domain. This domain is essential for homodimerization and anchoring to the plasma membrane. Transgenic plants with the ß- glucuronidase (GUS) reporter gene under the control of 1.1 kb promoter sequence of PCC1 gene display a dual pattern of expression. At early post-germination, PCC1 is expressed only in the root vasculature and in the stomata guard cells of cotyledons. During the transition from vegetative to reproductive development, PCC1 is strongly expressed in the vascular tissue of petioles and basal part of the leaf, and it further spreads to the whole limb in fully expanded leaves. This developmental pattern of expression together with the late flowering phenotype of long-day grown RNA interference (iPCC1) plants with reduced PCC1 expression pointed to a regulatory role of PCC1 in the photoperiod-dependent flowering pathway. iPCC1 plants are defective in light perception and signaling but are not impaired in the function of the core CO-FT module of the photoperiod-dependent pathway. The regulatory effect exerted by PCC1 on the transition to flowering as well as on other reported phenotypes might be explained by a mechanism involving the interaction with the subunit 5 of the COP9 signalosome (CSN).This work was funded by grants BIO2008-00839, BIO2011-27526 and CSD2007-0057 from Ministerio de Ciencia e Innovacion of Spain to J.L. A fellowship/contract of the FPU program of the Ministerio de Educacion y Ciencia (Spain) funded R.M. work. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Mir Moreno, R.; Leon Ramos, J. (2014). Pathogen and Circadian Controlled 1 (PCC1) Protein Is Anchored to the Plasma Membrane and Interacts with Subunit 5 of COP9 Signalosome in Arabidopsis. PLoS ONE. 1(9):1-14. https://doi.org/10.1371/journal.pone.0087216S11419Sauerbrunn, N., & Schlaich, N. L. (2004). PCC1 : a merging point for pathogen defence and circadian signalling in Arabidopsis. Planta, 218(4), 552-561. doi:10.1007/s00425-003-1143-zSEGARRA, S., MIR, R., MARTÍNEZ, C., & LEÓN, J. (2009). Genome-wide analyses of the transcriptomes of salicylic acid-deficient versus wild-type plants uncover Pathogen and Circadian Controlled 1 (PCC1) as a regulator of flowering time in Arabidopsis. Plant, Cell & Environment, 33(1), 11-22. doi:10.1111/j.1365-3040.2009.02045.xVenancio, T. M., & Aravind, L. (2009). CYSTM, a novel cysteine-rich transmembrane module with a role in stress tolerance across eukaryotes. Bioinformatics, 26(2), 149-152. doi:10.1093/bioinformatics/btp647Lau, O. S., & Deng, X. W. (2010). Plant hormone signaling lightens up: integrators of light and hormones. Current Opinion in Plant Biology, 13(5), 571-577. doi:10.1016/j.pbi.2010.07.001Seo, M., Nambara, E., Choi, G., & Yamaguchi, S. (2008). Interaction of light and hormone signals in germinating seeds. Plant Molecular Biology, 69(4), 463-472. doi:10.1007/s11103-008-9429-yDe Lucas, M., Davière, J.-M., Rodríguez-Falcón, M., Pontin, M., Iglesias-Pedraz, J. M., Lorrain, S., … Prat, S. (2008). A molecular framework for light and gibberellin control of cell elongation. Nature, 451(7177), 480-484. doi:10.1038/nature06520Feng, S., Martinez, C., Gusmaroli, G., Wang, Y., Zhou, J., Wang, F., … Deng, X. W. (2008). Coordinated regulation of Arabidopsis thaliana development by light and gibberellins. Nature, 451(7177), 475-479. doi:10.1038/nature06448Mutasa-Gottgens, E., & Hedden, P. (2009). Gibberellin as a factor in floral regulatory networks. Journal of Experimental Botany, 60(7), 1979-1989. doi:10.1093/jxb/erp040Bastian, R., Dawe, A., Meier, S., Ludidi, N., Bajic, V. B., & Gehring, C. (2010). Gibberellic acid and cGMP-dependent transcriptional regulation inArabidopsis thaliana. Plant Signaling & Behavior, 5(3), 224-232. doi:10.4161/psb.5.3.10718Yu, S., Galvão, V. C., Zhang, Y.-C., Horrer, D., Zhang, T.-Q., Hao, Y.-H., … Wang, J.-W. (2012). Gibberellin Regulates the Arabidopsis Floral Transition through miR156-Targeted SQUAMOSA PROMOTER BINDING–LIKE Transcription Factors. The Plant Cell, 24(8), 3320-3332. doi:10.1105/tpc.112.101014Arc, E., Galland, M., Cueff, G., Godin, B., Lounifi, I., Job, D., & Rajjou, L. (2011). Reboot the system thanks to protein post-translational modifications and proteome diversity: How quiescent seeds restart their metabolism to prepare seedling establishment. PROTEOMICS, 11(9), 1606-1618. doi:10.1002/pmic.201000641Dill, A., Thomas, S. G., Hu, J., Steber, C. M., & Sun, T. (2004). The Arabidopsis F-Box Protein SLEEPY1 Targets Gibberellin Signaling Repressors for Gibberellin-Induced Degradation. The Plant Cell, 16(6), 1392-1405. doi:10.1105/tpc.020958Wang, F., & Deng, X. W. (2011). Plant ubiquitin-proteasome pathway and its role in gibberellin signaling. Cell Research, 21(9), 1286-1294. doi:10.1038/cr.2011.118Hotton, S. K., & Callis, J. (2008). Regulation of Cullin RING Ligases. Annual Review of Plant Biology, 59(1), 467-489. doi:10.1146/annurev.arplant.58.032806.104011Cope, G. A. (2002). Role of Predicted Metalloprotease Motif of Jab1/Csn5 in Cleavage of Nedd8 from Cul1. Science, 298(5593), 608-611. doi:10.1126/science.1075901Gusmaroli, G., Figueroa, P., Serino, G., & Deng, X. W. (2007). Role of the MPN Subunits in COP9 Signalosome Assembly and Activity, and Their Regulatory Interaction with Arabidopsis Cullin3-Based E3 Ligases. The Plant Cell, 19(2), 564-581. doi:10.1105/tpc.106.047571Serino, G., & Deng, X.-W. (2003). THECOP9 SIGNALOSOME: Regulating Plant Development Through the Control of Proteolysis. Annual Review of Plant Biology, 54(1), 165-182. doi:10.1146/annurev.arplant.54.031902.134847Stratmann, J. W., & Gusmaroli, G. (2012). Many jobs for one good cop – The COP9 signalosome guards development and defense. Plant Science, 185-186, 50-64. doi:10.1016/j.plantsci.2011.10.004Lozano-Juste, J., & León, J. (2011). Nitric Oxide Regulates DELLA Content and PIF Expression to Promote Photomorphogenesis in Arabidopsis. Plant Physiology, 156(3), 1410-1423. doi:10.1104/pp.111.177741Nakagawa, T., Kurose, T., Hino, T., Tanaka, K., Kawamukai, M., Niwa, Y., … Kimura, T. (2007). Development of series of gateway binary vectors, pGWBs, for realizing efficient construction of fusion genes for plant transformation. Journal of Bioscience and Bioengineering, 104(1), 34-41. doi:10.1263/jbb.104.34Fromont-Racine, M., Rain, J.-C., & Legrain, P. (1997). Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens. Nature Genetics, 16(3), 277-282. doi:10.1038/ng0797-277Belda-Palazón B, Ruiz L, Martí E, Tárraga S, Tiburcio AF, et al.. (2012) Aminopropyltransferases involved in polyamine biosynthesis localize preferentially in the nucleus of plant cells. PLoS One 7(10), e46907.Simon, R., Igeño, M. I., & Coupland, G. (1996). Activation of floral meristem identity genes in Arabidopsis. Nature, 384(6604), 59-62. doi:10.1038/384059a0Martínez, C., Pons, E., Prats, G., & León, J. (2003). Salicylic acid regulates flowering time and links defence responses and reproductive development. The Plant Journal, 37(2), 209-217. doi:10.1046/j.1365-313x.2003.01954.xKyte, J., & Doolittle, R. F. (1982). A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology, 157(1), 105-132. doi:10.1016/0022-2836(82)90515-0Marmagne, A., Rouet, M.-A., Ferro, M., Rolland, N., Alcon, C., Joyard, J., … Ephritikhine, G. (2004). Identification of New Intrinsic Proteins inArabidopsisPlasma Membrane Proteome. Molecular & Cellular Proteomics, 3(7), 675-691. doi:10.1074/mcp.m400001-mcp200Nühse, T. S., Stensballe, A., Jensen, O. N., & Peck, S. C. (2004). Phosphoproteomics of the Arabidopsis Plasma Membrane and a New Phosphorylation Site Database. The Plant Cell, 16(9), 2394-2405. doi:10.1105/tpc.104.023150Kobayashi, Y., & Weigel, D. (2007). Move on up, it’s time for change mobile signals controlling photoperiod-dependent flowering. Genes & Development, 21(19), 2371-2384. doi:10.1101/gad.1589007Jaeger, K. E., & Wigge, P. A. (2007). FT Protein Acts as a Long-Range Signal in Arabidopsis. Current Biology, 17(12), 1050-1054. doi:10.1016/j.cub.2007.05.008Mathieu, J., Warthmann, N., Küttner, F., & Schmid, M. (2007). Export of FT Protein from Phloem Companion Cells Is Sufficient for Floral Induction in Arabidopsis. Current Biology, 17(12), 1055-1060. doi:10.1016/j.cub.2007.05.009Mir, R., Hernández, M. L., Abou-Mansour, E., Martínez-Rivas, J. M., Mauch, F., Métraux, J.-P., & León, J. (2013). Pathogen and Circadian Controlled 1 (PCC1) regulates polar lipid content, ABA-related responses, and pathogen defence in Arabidopsis thaliana. Journal of Experimental Botany, 64(11), 3385-3395. doi:10.1093/jxb/ert177Nordgård, O., Dahle, Ø., Andersen, T. Ø., & Gabrielsen, O. S. (2001). JAB1/CSN5 interacts with the GAL4 DNA binding domain: A note of caution about two-hybrid interactions. Biochimie, 83(10), 969-971. doi:10.1016/s0300-9084(01)01329-3Kwok, S. F., Staub, J. M., & Deng, X.-W. (1999). Characterization of two subunits of Arabidopsis 19S proteasome regulatory complex and its possible interaction with the COP9 complex 1 1Edited by J. Karn. Journal of Molecular Biology, 285(1), 85-95. doi:10.1006/jmbi.1998.2315Nezames, C. D., & Deng, X. W. (2012). The COP9 Signalosome: Its Regulation of Cullin-Based E3 Ubiquitin Ligases and Role in Photomorphogenesis. Plant Physiology, 160(1), 38-46. doi:10.1104/pp.112.198879Moon, J., Parry, G., & Estelle, M. (2004). The Ubiquitin-Proteasome Pathway and Plant Development. The Plant Cell, 16(12), 3181-3195. doi:10.1105/tpc.104.161220Dreher, K., & Callis, J. (2007). Ubiquitin, Hormones and Biotic Stress in Plants. Annals of Botany, 99(5), 787-822. doi:10.1093/aob/mcl255Parry, G., & Estelle, M. (2004). Regulation of cullin-based ubiquitin ligases by the Nedd8/RUB ubiquitin-like proteins. Seminars in Cell & Developmental Biology, 15(2), 221-229. doi:10.1016/j.semcdb.2003.12.003Wee, S., Geyer, R. K., Toda, T., & Wolf, D. A. (2005). CSN facilitates Cullin–RING ubiquitin ligase function by counteracting autocatalytic adapter instability. Nature Cell Biology, 7(4), 387-391. doi:10.1038/ncb1241Kuramata, M., Masuya, S., Takahashi, Y., Kitagawa, E., Inoue, C., Ishikawa, S., … Kusano, T. (2008). Novel Cysteine-Rich Peptides from Digitaria ciliaris and Oryza sativa Enhance Tolerance to Cadmium by Limiting its Cellular Accumulation. Plant and Cell Physiology, 50(1), 106-117. doi:10.1093/pcp/pcn175Zeng, W., Melotto, M., & He, S. Y. (2010). Plant stomata: a checkpoint of host immunity and pathogen virulence. Current Opinion in Biotechnology, 21(5), 599-603. doi:10.1016/j.copbio.2010.05.006Wigge, P. A. (2011). FT, A Mobile Developmental Signal in Plants. Current Biology, 21(9), R374-R378. doi:10.1016/j.cub.2011.03.038Kardailsky, I. (1999). Activation Tagging of the Floral Inducer FT. Science, 286(5446), 1962-1965. doi:10.1126/science.286.5446.1962Srikanth, A., & Schmid, M. (2011). Regulation of flowering time: all roads lead to Rome. Cellular and Molecular Life Sciences, 68(12), 2013-2037. doi:10.1007/s00018-011-0673-yGalvao, V. C., Horrer, D., Kuttner, F., & Schmid, M. (2012). Spatial control of flowering by DELLA proteins in Arabidopsis thaliana. Development, 139(21), 4072-4082. doi:10.1242/dev.080879Cerdán, P. D., & Chory, J. (2003). Regulation of flowering time by light quality. Nature, 423(6942), 881-885. doi:10.1038/nature01636Guo, H. (1998). Regulation of Flowering Time by Arabidopsis Photoreceptors. Science, 279(5355), 1360-1363. doi:10.1126/science.279.5355.1360Liu, B., Zuo, Z., Liu, H., Liu, X., & Lin, C. (2011). Arabidopsis cryptochrome 1 interacts with SPA1 to suppress COP1 activity in response to blue light. Genes & Development, 25(10), 1029-1034. doi:10.1101/gad.2025011Weidler, G., zur Oven-Krockhaus, S., Heunemann, M., Orth, C., Schleifenbaum, F., Harter, K., … Batschauer, A. (2012). Degradation of Arabidopsis CRY2 Is Regulated by SPA Proteins and Phytochrome A. The Plant Cell, 24(6), 2610-2623. doi:10.1105/tpc.112.09821