Journal articles: 'PSPC1'

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Moreno, Adriana T., Maria Leonor S. Oliveira, Paulo L. Ho, Cintia F. M. Vadesilho, Giovana M. P. Palma, Jorge M. C. Ferreira, Daniela M. Ferreira, Silvia R. Santos, Marina B. Martinez, and Eliane N. Miyaji. "Cross-Reactivity of Antipneumococcal Surface Protein C (PspC) Antibodies with Different Strains and Evaluation of Inhibition of Human Complement Factor H and Secretory IgA Binding via PspC." Clinical and Vaccine Immunology 19, no. 4 (February 15, 2012): 499–507. http://dx.doi.org/10.1128/cvi.05706-11.

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ABSTRACTPneumococcal surface protein C (PspC) is an important candidate for a cost-effective vaccine with broad coverage against pneumococcal diseases. Previous studies have shown thatStreptococcus pneumoniaeis able to bind to both human factor H (FH), an inhibitor of complement alternative pathway, and human secretory IgA (sIgA) via PspC. PspC was classified into 11 groups based on variations of the gene. In this work, we used three PspC fragments from different groups (PspC3, PspC5, and PspC8) to immunize mice for the production of antibodies. Immunization with PspC3 induced antibodies that recognized the majority of the clinical isolates as analyzed by Western blotting of whole-cell extracts and flow cytometry of intact bacteria, while anti-PspC5 antibodies showed cross-reactivity with the paralogue pneumococcal surface protein A (PspA), and anti-PspC8 antibodies reacted only with the PspC8-expressing strain. Most of the isolates tested showed strong binding to FH and weaker interaction with sIgA. Preincubation with anti-PspC3 and anti-PspC5 IgG led to some inhibition of binding of FH, and preincubation with anti-PspC3 partially inhibited sIgA binding in Western blotting. The analysis of intact bacteria through flow cytometry showed only a small decrease in FH binding after incubation of strain D39 with anti-PspC3 IgG, and one clinical isolate showed inhibition of sIgA binding by anti-PspC3 IgG. We conclude that although anti-PspC3 antibodies were able to recognize PspC variants from the majority of the strains tested, partial inhibition of FH and sIgA binding through anti-PspC3 antibodiesin vitrocould be observed for only a restricted number of isolates.

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Jen, Hsin-Wei, De-Leung Gu, Yaw-Dong Lang, and Yuh-Shan Jou. "PSPC1 Potentiates IGF1R Expression to Augment Cell Adhesion and Motility." Cells 9, no. 6 (June 18, 2020): 1490. http://dx.doi.org/10.3390/cells9061490.

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Paraspeckle protein 1 (PSPC1) overexpression in cancers is known to be the pro-metastatic switch of tumor progression associated with poor prognosis of cancer patients. However, the detail molecular mechanisms to facilitate cancer cell migration remain elusive. Here, we conducted integrated analysis of human phospho-kinase antibody array, transcriptome analysis with RNA-seq, and proteomic analysis of protein pulldown to study the molecular detail of PSPC1-potentiated phenotypical transformation, adhesion, and motility in human hepatocellular carcinoma (HCC) cells. We found that PSPC1 overexpression re-assembles and augments stress fiber formations to promote recruitment of focal adhesion contacts at the protruding edge to facilitate cell migration. PSPC1 activated focal adhesion-associated kinases especially FAK/Src signaling to enhance cell adhesion and motility toward extracellular matrix (ECM). Integrated transcriptome and gene set enrichment analysis indicated that PSPC1 modulated receptor tyrosine kinase IGF1R involved in the focal adhesion pathway and induction of diverse integrins expression. Knockdown IGF1R expression and treatment of IGF1R inhibitor suppressed PSPC1-induced cell motility. Interestingly, knockdown PSPC1-interacted paraspeckle components including NONO, FUS, and the lncRNA Neat1 abolished PSPC1-activated IGF1R expression. Together, PSPC1 overexpression induced focal adhesion formation and facilitated cell motility via activation of IGF1R signaling. PSPC1 overexpression in tumors could be a potential biomarker of target therapy with IGF1R inhibitor for improvement of HCC therapy.

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Major, Andrew T., Cathryn A. Hogarth, Yoichi Miyamoto, Mai A. Sarraj, Catherine L. Smith, Peter Koopman, Yasuyuki Kurihara, David A. Jans, and Kate L. Loveland. "Specific interaction with the nuclear transporter importin α2 can modulate paraspeckle protein 1 delivery to nuclear paraspeckles." Molecular Biology of the Cell 26, no. 8 (April 15, 2015): 1543–58. http://dx.doi.org/10.1091/mbc.e14-01-0678.

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Importin (IMP) superfamily members mediate regulated nucleocytoplasmic transport, which is central to key cellular processes. Although individual IMPα proteins exhibit dynamic synthesis and subcellular localization during cellular differentiation, including during spermatogenesis, little is known of how this affects cell fate. To investigate how IMPαs control cellular development, we conducted a yeast two-hybrid screen for IMPα2 cargoes in embryonic day 12.5 mouse testis, a site of peak IMPα2 expression coincident with germ-line masculization. We identified paraspeckle protein 1 (PSPC1), the original defining component of nuclear paraspeckles, as an IMPα2-binding partner. PSPC1-IMPα2 binding in testis was confirmed in immunoprecipitations and pull downs, and an enzyme-linked immunosorbent assay–based assay demonstrated direct, high-affinity PSPC1 binding to either IMPα2/IMPβ1 or IMPα6/IMPβ1. Coexpression of full-length PSPC1 and IMPα2 in HeLa cells yielded increased PSPC1 localization in nuclear paraspeckles. High-throughput image analysis of >3500 cells indicated IMPα2 levels can directly determine PSPC1-positive nuclear speckle numbers and size; a transport-deficient IMPα2 isoform or small interfering RNA knockdown of IMPα2 each reduced endogenous PSPC1 accumulation in speckles. This first validation of an IMPα2 nuclear import cargo in fetal testis provides novel evidence that PSPC1 delivery to paraspeckles, and consequently paraspeckle function, may be controlled by modulated synthesis of specific IMPs.

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Díaz-García, Elena, Sara García-Tovar, Raquel Casitas, Ana Jaureguizar, Ester Zamarrón, Begoña Sánchez-Sánchez, Ana Sastre-Perona, Eduardo López-Collazo, Francisco Garcia-Rio, and Carolina Cubillos-Zapata. "Intermittent Hypoxia Mediates Paraspeckle Protein-1 Upregulation in Sleep Apnea." Cancers 13, no. 15 (August 2, 2021): 3888. http://dx.doi.org/10.3390/cancers13153888.

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As some evidence suggests that hypoxia might be an inducer of nuclear paraspeckle formation, we explore whether intermittent hypoxia (IH)-mediated paraspeckle protein-1 (PSPC1) overexpression might contribute to the activation of tumor growth factor (TGF)β-SMAD pathway in patients with obstructive sleep apnea (OSA). This activation would promote changes in intracellular signaling that would explain the increased cancer aggressiveness reported in these patients. Here, we show that patients with OSA exhibit elevated PSPC1 levels both in plasma and in monocytes. Our data suggest that PSPC1 is ultimately delivered to the plasma through its cleavage from OSA monocytes by matrix metalloproteinase-2 (MMP2). In addition, IH promotes PSPC1, TGFβ, and MMP2 expression in monocytes through the hypoxia-inducible factor. Lastly, both PSPC1 and TGFβ induce increased expression of genes that drive the epithelial-to-mesenchymal transition. Our study details the mechanism by which hypoxemia upmodulates the extracellular release of PSPC1 by means of MMP2, such that plasma PSPC1 together with TGFβ activation signaling further promotes tumor metastasis and supports cancer aggressiveness in patients with OSA.

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Li, Shuyi, Zhentian Li, Feng-Jue Shu, Hairong Xiong, Andrew C. Phillips, and William S. Dynan. "Double-strand break repair deficiency in NONO knockout murine embryonic fibroblasts and compensation by spontaneous upregulation of the PSPC1 paralog." Nucleic Acids Research 42, no. 15 (August 6, 2014): 9771–80. http://dx.doi.org/10.1093/nar/gku650.

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Abstract NONO, SFPQ and PSPC1 make up a family of proteins with diverse roles in transcription, RNA processing and DNA double-strand break (DSB) repair. To understand long-term effects of loss of NONO, we characterized murine embryonic fibroblasts (MEFs) from knockout mice. In the absence of genotoxic stress, wild-type and mutant MEFs showed similar growth rates and cell cycle distributions, and the mutants were only mildly radiosensitive. Further investigation showed that NONO deficiency led to upregulation of PSPC1, which replaced NONO in a stable complex with SFPQ. Knockdown of PSPC1 in a NONO-deficient background led to severe radiosensitivity and delayed resolution of DSB repair foci. The DNA-dependent protein kinase (DNA-PK) inhibitor, NU7741, sensitized wild-type and singly deficient MEFs, but had no additional effect on doubly deficient cells, suggesting that NONO/PSPC1 and DNA-PK function in the same pathway. We tested whether NONO and PSPC1 might also affect repair indirectly by influencing mRNA levels for other DSB repair genes. Of 12 genes tested, none were downregulated, and several were upregulated. Thus, NONO or related proteins are critical for DSB repair, NONO and PSPC1 are functional homologs with partially interchangeable functions and a compensatory response involving PSPC1 blunts the effect of NONO deficiency.

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Major, Andrew T., Cathryn A. Hogarth, Julia C. Young, Yasuyuki Kurihara, David A. Jans, and Kate L. Loveland. "Dynamic paraspeckle component localisation during spermatogenesis." Reproduction 158, no. 3 (September 2019): 267–80. http://dx.doi.org/10.1530/rep-19-0139.

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Expression profiles and subcellular localisations of core Drosophila behaviour/human splicing (DBHS) proteins (PSPC1, SFPQ and NONO) and NEAT1, a long noncoding RNA (lncRNA), are investigated in developing and adult mouse testes. Core DBHS proteins are markers for the distinct subnuclear domain termed paraspeckles, while a long NEAT1 isoform scaffold facilitates paraspeckle nucleation. Paraspeckles contain many proteins (>40) and are broadly involved in RNA metabolism, including transcriptional regulation by protein sequestration, nuclear retention of A-to-I edited RNA transcripts to regulate translation and promoting survival during cellular stress. Immunohistochemistry reveals cell-specific profiles for core DBHS paraspeckle protein expression, indicating their functional diversity. PSPC1 is an androgen receptor co-activator, and it is detected in differentiating Sertoli cell nuclei from day 15 onwards, as they develop androgen responsiveness. PSPC1 is nuclear in the most mature male germ cell type present at each age, from foetal to adult life. In adult mouse testes, PSPC1 and SFPQ are present in Sertoli cells, spermatocytes and round spermatids, while the NEAT1 lncRNA appears in the punctate nuclear foci delineating paraspeckles only within Leydig cells. Identification of NEAT1 in the cytoplasm of spermatogonia and spermatocytes must reflect non-paraspeckle-related functions. NONO was absent from germ cells but nuclear in Sertoli cells. Reciprocal nuclear profiles of PSPC1 and γ-H2AX in spermatogenic cells suggest that each performs developmentally regulated roles in stress responses. These findings demonstrate paraspeckles and paraspeckle-related proteins contribute to diverse functions during testis development and spermatogenesis.

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Yeh, Hsi-Wen, and Yuh-Shan Jou. "PSPC1 potentiates TGF-β-dependent metastatic dissemination." Molecular & Cellular Oncology 5, no. 4 (July 4, 2018): e1472058. http://dx.doi.org/10.1080/23723556.2018.1472058.

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Lang, Yaw-Dong, and Yuh-Shan Jou. "PSPC1: a contextual determinant of tumor progression." Molecular & Cellular Oncology 7, no. 2 (February 3, 2020): 1721253. http://dx.doi.org/10.1080/23723556.2020.1721253.

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9

Passon, Daniel M., Mihwa Lee, Archa H. Fox, and Charles S. Bond. "Crystallization of a paraspeckle protein PSPC1–NONO heterodimer." Acta Crystallographica Section F Structural Biology and Crystallization Communications 67, no. 10 (September 29, 2011): 1231–34. http://dx.doi.org/10.1107/s1744309111026212.

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Knott, Gavin J., Yee Seng Chong, Daniel M. Passon, Xue-hai Liang, Evelyne Deplazes, Maria R. Conte, Andrew C. Marshall, Mihwa Lee, Archa H. Fox, and Charles S. Bond. "Structural basis of dimerization and nucleic acid binding of human DBHS proteins NONO and PSPC1." Nucleic Acids Research 50, no. 1 (December 14, 2021): 522–35. http://dx.doi.org/10.1093/nar/gkab1216.

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Abstract The Drosophila behaviour/human splicing (DBHS) proteins are a family of RNA/DNA binding cofactors liable for a range of cellular processes. DBHS proteins include the non-POU domain-containing octamer-binding protein (NONO) and paraspeckle protein component 1 (PSPC1), proteins capable of forming combinatorial dimers. Here, we describe the crystal structures of the human NONO and PSPC1 homodimers, representing uncharacterized DBHS dimerization states. The structures reveal a set of conserved contacts and structural plasticity within the dimerization interface that provide a rationale for dimer selectivity between DBHS paralogues. In addition, solution X-ray scattering and accompanying biochemical experiments describe a mechanism of cooperative RNA recognition by the NONO homodimer. Nucleic acid binding is reliant on RRM1, and appears to be affected by the orientation of RRM1, influenced by a newly identified ‘β-clasp’ structure. Our structures shed light on the molecular determinants for DBHS homo- and heterodimerization and provide a basis for understanding how DBHS proteins cooperatively recognize a broad spectrum of RNA targets.

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He, Huocong, Lurong Zhang, Keyu Lin, Zhengrong Huang, Yan Zhou, Shaojun Lin, Ying Su, and Jianru Pan. "The Prognosis Value of PSPC1 Expression in Nasopharyngeal Cancer." Cancer Management and Research Volume 13 (April 2021): 3281–91. http://dx.doi.org/10.2147/cmar.s300567.

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Kleene, Ralf, Gabriele Loers, and Melitta Schachner. "The KDET Motif in the Intracellular Domain of the Cell Adhesion Molecule L1 Interacts with Several Nuclear, Cytoplasmic, and Mitochondrial Proteins Essential for Neuronal Functions." International Journal of Molecular Sciences 24, no. 2 (January 4, 2023): 932. http://dx.doi.org/10.3390/ijms24020932.

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Abnormal functions of the cell adhesion molecule L1 are linked to several neural diseases. Proteolytic L1 fragments were reported to interact with nuclear and mitochondrial proteins to regulate events in the developing and the adult nervous system. Recently, we identified a 55 kDa L1 fragment (L1-55) that interacts with methyl CpG binding protein 2 (MeCP2) and heterochromatin protein 1 (HP1) via the KDET motif. We now show that L1-55 also interacts with histone H1.4 (HistH1e) via this motif. Moreover, we show that this motif binds to NADH dehydrogenase ubiquinone flavoprotein 2 (NDUFV2), splicing factor proline/glutamine-rich (SFPQ), the non-POU domain containing octamer-binding protein (NonO), paraspeckle component 1 (PSPC1), WD-repeat protein 5 (WDR5), heat shock cognate protein 71 kDa (Hsc70), and synaptotagmin 1 (SYT1). Furthermore, applications of HistH1e, NDUFV2, SFPQ, NonO, PSPC1, WDR5, Hsc70, or SYT1 siRNAs or a cell-penetrating KDET-carrying peptide decrease L1-dependent neurite outgrowth and the survival of cultured neurons. These findings indicate that L1’s KDET motif binds to an unexpectedly large number of molecules that are essential for nervous system-related functions, such as neurite outgrowth and neuronal survival. In summary, L1 interacts with cytoplasmic, nuclear and mitochondrial proteins to regulate development and, in adults, the formation, maintenance, and flexibility of neural functions.

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Knott, Gavin J., Charles S. Bond, and Archa H. Fox. "The DBHS proteins SFPQ, NONO and PSPC1: a multipurpose molecular scaffold." Nucleic Acids Research 44, no. 9 (April 15, 2016): 3989–4004. http://dx.doi.org/10.1093/nar/gkw271.

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Hoekstra, Elisa J., Simone Mesman, Willem A. de Munnik, and Marten P. Smidt. "LMX1B Is Part of a Transcriptional Complex with PSPC1 and PSF." PLoS ONE 8, no. 1 (January 4, 2013): e53122. http://dx.doi.org/10.1371/journal.pone.0053122.

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Passon, D. M., M. Lee, A. H. Fox, and C. S. Bond. "A novel structure: PSPC1/NONO heterodimer, members of the DBHS protein family." Acta Crystallographica Section A Foundations of Crystallography 67, a1 (August 22, 2011): C632. http://dx.doi.org/10.1107/s0108767311084029.

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Mohankumar, Kumaravel, Rupesh Shrestha, and Stephen Safe. "Nuclear receptor 4A1 (NR4A1) antagonists target paraspeckle component 1 (PSPC1) in cancer cells." Molecular Carcinogenesis 61, no. 1 (October 26, 2021): 73–84. http://dx.doi.org/10.1002/mc.23362.

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Wang, Jiexin, Prashant Rajbhandari, Andrey Damianov, Areum Han, Tamer Sallam, Hironori Waki, Claudio J. Villanueva, et al. "RNA-binding protein PSPC1 promotes the differentiation-dependent nuclear export of adipocyte RNAs." Journal of Clinical Investigation 127, no. 3 (February 13, 2017): 987–1004. http://dx.doi.org/10.1172/jci89484.

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Knott, Gavin, Mihwa Lee, Daniel Passon, Agata Sadowska, Archa Fox, Maria Conte, and Charles Bond. "Structure and dynamics of the DBHS protein family members SFPQ, NONO and PSPC1." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C1655. http://dx.doi.org/10.1107/s2053273314083442.

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The Drosophila behaviour/human splicing (DBHS) proteins are a family of obligatory dimeric proteins found in higher order mammals down to the simplest invertebrates. `Multifunctional protein family' essentially captures what is understood regarding DBHS protein function where they are cited to regulate transcriptional initiation, the processing and export of RNA, maintenance of genomic DNA, nuclear pH homeostasis and carcinogenesis [1]. Furthermore, with roles in binding a diverse range of RNAs and both single and double stranded DNA, it is difficult to establish a coherent picture for their nuclear activities. In humans, the family consists of three highly conserved members, namely Non-POU domain-containing octamer-binding protein (NONO/p54nrb), splicing factor proline/glutamine rich (SFPQ/PSF) and paraspeckle protein component 1 (PSPC1). The conserved DBHS region of these proteins comprises tandem RNA recognition motifs (RRMs), a NOPS domain and a C-terminal coiled-coil domain. The unique structural arrangement of these domains facilitates an intimate dimerisation interface that gives rise to a novel arrangement of RRMs [2]. Given this interface, it is not surprising that DBHS proteins likely exist as either homo- or heterodimers in vivo. Here we report the first structure of the ancestral C. elegans DBHS protein, NONO-1, refined to 2.8 Å. The structure clearly illustrates the consistent obligatory nature of DBHS dimerisation and through isothermal titration calorimetry we have demonstrated that human DBHS proteins prefer a heterodimeric state in vitro. There is a growing appreciation for the fundamental significance of DBHS proteins in human health and disease and this work highlights the critical need for a more robust assessment of in vivo DBHS function.

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Bond, Charles S., and Archa H. Fox. "Paraspeckles: nuclear bodies built on long noncoding RNA." Journal of Cell Biology 186, no. 5 (August 31, 2009): 637–44. http://dx.doi.org/10.1083/jcb.200906113.

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Paraspeckles are ribonucleoprotein bodies found in the interchromatin space of mammalian cell nuclei. These structures play a role in regulating the expression of certain genes in differentiated cells by nuclear retention of RNA. The core paraspeckle proteins (PSF/SFPQ, P54NRB/NONO, and PSPC1 [paraspeckle protein 1]) are members of the DBHS (Drosophila melanogaster behavior, human splicing) family. These proteins, together with the long nonprotein-coding RNA NEAT1 (MEN-ε/β), associate to form paraspeckles and maintain their integrity. Given the large numbers of long noncoding transcripts currently being discovered through whole transcriptome analysis, paraspeckles may be a paradigm for a class of subnuclear bodies formed around long noncoding RNA.

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Huang, Xin, Nazym Bashkenova, Yantao Hong, Cong Lyu, Diana Guallar, Zhe Hu, Vikas Malik, et al. "A TET1-PSPC1-Neat1 molecular axis modulates PRC2 functions in controlling stem cell bivalency." Cell Reports 39, no. 10 (June 2022): 110928. http://dx.doi.org/10.1016/j.celrep.2022.110928.

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Rothzerg, Emel, Wenyu Feng, Dezhi Song, Hengyuan Li, Qingjun Wei, Archa Fox, David Wood, Jiake Xu, and Yun Liu. "Single-Cell Transcriptome Analysis Reveals Paraspeckles Expression in Osteosarcoma Tissues." Cancer Informatics 21 (January 2022): 117693512211401. http://dx.doi.org/10.1177/11769351221140101.

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Nuclear paraspeckles are subnuclear bodies contracted by nuclear-enriched abundant transcript 1 (NEAT1) long non-coding RNA, localised in the interchromatin space of mammalian cell nuclei. Paraspeckles have been critically involved in tumour progression, metastasis and chemoresistance. To this date, there are limited findings to suggest that paraspeckles, NEAT1 and heterogeneous nuclear ribonucleoproteins (hnRNPs) directly or indirectly play roles in osteosarcoma progression. Herein, we analysed NEAT1, paraspeckle proteins (SFPQ, PSPC1 and NONO) and hnRNP members (HNRNPK, HNRNPM, HNRNPR and HNRNPD) gene expression in 6 osteosarcoma tumour tissues using the single-cell RNA-sequencing method. The normalised data highlighted that the paraspeckles transcripts were highly abundant in osteoblastic OS cells, except NEAT1, which was highly expressed in myeloid cell 1 and 2 subpopulations.

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Tyzack, Giulia E., Giulia Manferrari, Jia Newcombe, Nicholas M. Luscombe, Raphaelle Luisier, and Rickie Patani. "Paraspeckle components NONO and PSPC1 are not mislocalized from motor neuron nuclei in sporadic ALS." Brain 143, no. 8 (August 1, 2020): e66-e66. http://dx.doi.org/10.1093/brain/awaa205.

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Dong, Bing-wei, Xiao-hang Jin, Chang-you Yan, Tian Yang, Guo-qing Cai, and Jian Lu. "Synergistic upregulation of NONO and PSPC1 regulates Sertoli cell response to MEHPviamodulation of ALDH1A1 signaling." FEBS Letters 591, no. 6 (March 2017): 914–23. http://dx.doi.org/10.1002/1873-3468.12568.

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Lee, Mihwa, Daniel M. Passon, Sven Hennig, Archa H. Fox, and Charles S. Bond. "Construct optimization for studying protein complexes: obtaining diffraction-quality crystals of the pseudosymmetric PSPC1–NONO heterodimer." Acta Crystallographica Section D Biological Crystallography 67, no. 11 (October 19, 2011): 981–87. http://dx.doi.org/10.1107/s0907444911039606.

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Huang, Jie, G. Patricia Casas Garcia, Matthew A. Perugini, Archa H. Fox, Charles S. Bond, and Mihwa Lee. "Crystal structure of a SFPQ/PSPC1 heterodimer provides insights into preferential heterodimerization of human DBHS family proteins." Journal of Biological Chemistry 293, no. 17 (March 12, 2018): 6593–602. http://dx.doi.org/10.1074/jbc.ra117.001451.

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Yeh, Hsi-Wen, En-Chi Hsu, Szu-Shuo Lee, Yaw-Dong Lang, Yuh-Charn Lin, Chieh-Yu Chang, Suz-Yi Lee, et al. "PSPC1 mediates TGF-β1 autocrine signalling and Smad2/3 target switching to promote EMT, stemness and metastasis." Nature Cell Biology 20, no. 4 (March 28, 2018): 479–91. http://dx.doi.org/10.1038/s41556-018-0062-y.

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Gao, Xiangjing, Liya Kong, Xianghong Lu, Guanglin Zhang, Linfeng Chi, Ying Jiang, Yihua Wu, et al. "Paraspeckle Protein 1 (PSPC1) Is Involved in the Cisplatin Induced DNA Damage Response—Role in G1/S Checkpoint." PLoS ONE 9, no. 5 (May 12, 2014): e97174. http://dx.doi.org/10.1371/journal.pone.0097174.

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Souquere, Sylvie, Guillaume Beauclair, Francis Harper, Archa Fox, and Gérard Pierron. "Highly Ordered Spatial Organization of the Structural Long Noncoding NEAT1 RNAs within Paraspeckle Nuclear Bodies." Molecular Biology of the Cell 21, no. 22 (November 15, 2010): 4020–27. http://dx.doi.org/10.1091/mbc.e10-08-0690.

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Paraspeckles (PSPs) are nuclear bodies associated with the retention in the nucleus of specific mRNAs. Two isoforms of a long noncoding RNA (NEAT1_v1/Menε and NEAT1_v2/Menβ) are required for the integrity of PSPs. Here, we analyzed the molecular organization of PSPs by immuno- and in situ hybridization electron microscopy. Detection of the paraspeckle markers PSPC1 and P54NRB/NONO confirm the identity between PSPs and the previously described interchromatin granule-associated zones (IGAZs). High-resolution in situ hybridization of NEAT1 transcripts revealed a highly ordered organization of IGAZ/PSPs. Although the 3.7-kb NEAT1_v1 and the identical 5′ end of the 22.7-kb NEAT1_v2 transcripts are confined to the periphery, central sequences of NEAT1_v2 are found within the electron-dense core of the bodies. Moreover, the 3′ end of NEAT1_v2 also localize to the periphery, indicating possible architectures for IGAZ/PSPs. These results further suggest that the organization of NEAT1 transcripts constrains the geometry of these bodies. Accordingly, we observed in HeLa and NIH 3T3 cells that IGAZ/PSPs are elongated structures with a well-defined diameter. Our results provide new insight on the ability of noncoding RNAs to form subcellular structures.

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Kuwahara, Sho, Asako Ikei, Yusuke Taguchi, Yoshiaki Tabuchi, Nariaki Fujimoto, Masuo Obinata, Seiichi Uesugi, and Yasuyuki Kurihara. "PSPC1, NONO, and SFPQ Are Expressed in Mouse Sertoli Cells and May Function as Coregulators of Androgen Receptor-Mediated Transcription1." Biology of Reproduction 75, no. 3 (September 1, 2006): 352–59. http://dx.doi.org/10.1095/biolreprod.106.051136.

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Zhang, Pengpeng, Wenyan Wu, Chaofeng Ma, Chunyu Du, Yueru Huang, Haixia Xu, Cencen Li, Xiaofang Cheng, Ruijie Hao, and Yongjie Xu. "RNA-Binding Proteins in the Regulation of Adipogenesis and Adipose Function." Cells 11, no. 15 (July 31, 2022): 2357. http://dx.doi.org/10.3390/cells11152357.

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The obesity epidemic represents a critical public health issue worldwide, as it is a vital risk factor for many diseases, including type 2 diabetes (T2D) and cardiovascular disease. Obesity is a complex disease involving excessive fat accumulation. Proper adipose tissue accumulation and function are highly transcriptional and regulated by many genes. Recent studies have discovered that post-transcriptional regulation, mainly mediated by RNA-binding proteins (RBPs), also plays a crucial role. In the lifetime of RNA, it is bound by various RBPs that determine every step of RNA metabolism, from RNA processing to alternative splicing, nucleus export, rate of translation, and finally decay. In humans, it is predicted that RBPs account for more than 10% of proteins based on the presence of RNA-binding domains. However, only very few RBPs have been studied in adipose tissue. The primary aim of this paper is to provide an overview of RBPs in adipogenesis and adipose function. Specifically, the following best-characterized RBPs will be discussed, including HuR, PSPC1, Sam68, RBM4, Ybx1, Ybx2, IGF2BP2, and KSRP. Characterization of these proteins will increase our understanding of the regulatory mechanisms of RBPs in adipogenesis and provide clues for the etiology and pathology of adipose-tissue-related diseases.

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Kondoh, Kuniyo, Hiromichi Akahori, Yoshinori Muto, and Tomoyoshi Terada. "Identification of Key Genes and Pathways Associated with Preeclampsia by a WGCNA and an Evolutionary Approach." Genes 13, no. 11 (November 17, 2022): 2134. http://dx.doi.org/10.3390/genes13112134.

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Preeclampsia (PE) is the serious obstetric-related disease characterized by newly onset hypertension and causes damage to the kidneys, brain, liver, and more. To investigate genes with key roles in PE’s pathogenesis and their contributions, we used a microarray dataset of normotensive and PE patients and conducted a weighted gene co-expression network analysis (WGCNA). Cyan and magenta modules that are highly enriched with differentially expressed genes (DEGs) were revealed. By using the molecular complex detection (MCODE) algorithm, we identified five significant clusters in the cyan module protein–protein interaction (PPI) network and nine significant clusters in the magenta module PPI network. Our analyses indicated that (i) human accelerated region (HAR) genes are enriched in the magenta-associated C6 cluster, and (ii) positive selection (PS) genes are enriched in the cyan-associated C3 and C5 clusters. We propose these enriched HAR and PS genes, i.e., EIF4E, EIF5, EIF3M, DDX17, SRSF11, PSPC1, SUMO1, CAPZA1, PSMD14, and MNAT1, including highly connected hub genes, HNRNPA1, RBMX, PRKDC, and RANBP2, as candidate key genes for PE’s pathogenesis. A further clarification of the functions of these PPI clusters and key enriched genes will contribute to the discovery of diagnostic biomarkers for PE and therapeutic intervention targets.

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Zhang, Chen, Wu Zhong, Ying Cao, Bohao Liu, Xiaojun Tao, and Zhuan Li. "Sorafenib/2800Z Co-Loaded into Cholesterol and PEG Grafted Polylysine NPs for Liver Cancer Treatment." Pharmaceuticals 16, no. 1 (January 13, 2023): 119. http://dx.doi.org/10.3390/ph16010119.

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The treatment of liver cancer remains challenging due to the low responsiveness of advanced cancer to therapeutic options. Sorafenib is the first line chemotherapeutic drug for advanced liver cancer but is frequently associated with severe side effects lead to discontinuation of chemotherapy. We previously developed a specific SIRT7 inhibitor 2800Z, which suppressed tumor growth and enhanced the chemosensitivity of sorafenib. In this study, we constructed polylysine polymer nanoparticles modified with cholesterol and GSH-sensitive PEG (mPssPC) to load sorafenib (SOR) and the SIRT7 inhibitor 2800Z to form dual-loaded NPs (S2@PsPCs) to reduce the toxicity and increase efficacy of sorafenib in liver cancer. The average size of S2@PsPC NPs was approximately 370 nm and the zeta potential was approximately 50–53 mV. We found that the release of the drugs exhibited pH sensitivity and was significantly accelerated in an acid release medium simulating the tumor environment. In addition, S2@PsPC NPs inhibited the proliferation and induced apoptosis of liver cancer cells in vitro. An in vivo study further revealed that S2@PsPCs showed high specificity to the liver cancer but low affinity and toxicity to the main organs including the heart, kidneys, lungs, and liver. Our data thus further approved the combination of a SIRT7 inhibitor and sorafenib for the treatment of liver cancer and provided new drug delivery system for targeted therapy.

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Kusano, A., M. Iwama, A. Sanda, K. Suwa, E. Nakaizumi, Y. Nakatani, H. Ohkawa, K. Ohgi, and M. Irie. "Primary structure of porcine spleen ribonuclease: sequence homology." Acta Biochimica Polonica 44, no. 4 (December 31, 1997): 689–99. http://dx.doi.org/10.18388/abp.1997_4371.

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The primary structure of porcine spleen RNase (RNase Psp1) was investigated as a mean of assessing the structure-function relationship of base non-specific ribonucleases of animal origin. N-terminal analysis of RNase Psp1 yielded three N-terminal sequences. These peptides were separated by gel-filtration on Superdex 75HR, after reduction and S-carboxymethylation of RNase Psp1. Determination of the amino-acid sequence of these peptides indicated that the RNase Psp1 preparation consisted of three peptides having 20 (RCM RNase Psp1 pep1), 15 (RCM RNase Psp1 pep2), and 164 (RCM RNase Psp1 pro) amino-acid residues, respectively. It possessed two unique segments containing most of the active site amino-acid residues of the RNases of the RNase T2 family. The alignment of these three peptides in RNase Psp1 was determined by comparison with the other enzymes in the RNase T2 family. The overall results showed that RCM RNase Psp1 pep1 and RCM RNase Psp1 pep2 are derived from the N-terminal and C-terminal regions of RNase Psp1, respectively, probably by processing by some protease. The molecular mass of the protein moiety of RNase Psp1 was 23235 Da.

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Yu, Yang, Bo Liu, and Zhen Chen. "Improving the Performance of Pseudo-Random Single-Photon Counting Ranging Lidar." Sensors 19, no. 16 (August 20, 2019): 3620. http://dx.doi.org/10.3390/s19163620.

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A new encoding method is proposed to improve the performance of pseudo-random single-photon counting ranging (PSPCR) Lidar. The encoding principle and methodology are presented. In addition, the influence of detector’s dead time on the detection probability is analyzed with theoretical derivation and Monte Carlo simulation. Meanwhile, we propose using macro code as the analysis unit to quantitatively analyze the detection probability and single-photon detection efficiency of the traditional PSPCR Lidar and the modulated PSPCR Lidar. The Monte Carlo simulation and experiment prove that the proposed method exhibited better ranging performance than the traditional PSPCR Lidar system.

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Wang, Xin, Zi-Feng Zhang, Gui-Hong Zheng, Ai-Min Wang, Chun-Hui Sun, Su-Ping Qin, Juan Zhuang, Jun Lu, Dai-Fu Ma, and Yuan-Lin Zheng. "Attenuation of hepatic steatosis by purple sweet potato colour is associated with blocking Src/ERK/C/EBPβ signalling in high-fat-diet–treated mice." Applied Physiology, Nutrition, and Metabolism 42, no. 10 (October 2017): 1082–91. http://dx.doi.org/10.1139/apnm-2016-0635.

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Our previous work showed that purple sweet potato colour (PSPC), a class of naturally occurring anthocyanins, effectively improved hepatic glucose metabolic dysfunction in high-fat-diet (HFD)–treated mice. This study investigated the effects of PSPC on HFD-induced hepatic steatosis and the signalling events associated with these effects. Mice were divided into 4 groups: control group, HFD group, HFD+PSPC group, and PSPC group. PSPC was administered daily for 20 weeks at oral doses of 700 mg/(kg·day)−1). Our results showed that PSPC significantly improved obesity and related metabolic parameters, as well as liver injury in HFD-treated mice. Moreover, PSPC dramatically attenuated hepatic steatosis in HFD-treated mice. PSPC markedly prevented oxidative stress-mediated Src activation in HFD-treated mouse livers. Furthermore, PSPC feeding remarkably suppressed mitogen-activated protein kinase kinase/extracellular-signal-regulated kinase (MEK/ERK) signalling and consequent CCAAT/enhancer binding protein β (C/EBPβ) activation and restored AMPK activation in HFD-treated mouse livers, which was confirmed by U0126 treatment. Ultimately, PSPC feeding dramatically reduced protein expression of FAS and CD36 and the activation of ACC, and increased the protein expression of CPT1A in the livers of HFD-treated mice, indicating decreased lipogenesis and fatty acid uptake and enhanced fatty acid oxidation. In conclusion, PSPC exhibited beneficial effects on hepatic steatosis, which were associated with blocking Src and C/EBPβ activation.

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Keller, Maria, Claudia Gebhardt, Sandra Huth, Dorit Schleinitz, Henrike Heyne, Markus Scholz, Michael Stumvoll, Yvonne Böttcher, Anke Tönjes, and Peter Kovacs. "Genetically programmed changes in transcription of the novel progranulin regulator." Journal of Molecular Medicine 98, no. 8 (July 3, 2020): 1139–48. http://dx.doi.org/10.1007/s00109-020-01942-7.

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Abstract Progranulin is a glycoprotein marking chronic inflammation in obesity and type 2 diabetes. Previous studies suggested PSRC1 (proline and serine rich coiled-coil 1) to be a target of genetic variants associated with serum progranulin levels. We aimed to identify potentially functional variants and characterize their role in regulation of PSRC1. Phylogenetic module complexity analysis (PMCA) prioritized four polymorphisms (rs12740374, rs629301, rs660240, rs7528419) altering transcription factor binding sites with an overall score for potential regulatory function of Sall > 7.0. The effects of these variants on transcriptional activity and binding of transcription factors were tested by luciferase reporter and electrophoretic mobility shift assays (EMSA). In parallel, blood DNA promoter methylation of two regions was tested in subjects with a very high (N = 100) or a very low (N = 100) serum progranulin. Luciferase assays revealed lower activities in vectors carrying the rs629301-A compared with the C allele. Moreover, EMSA indicated a different binding pattern for the two rs629301 alleles, with an additional prominent band for the A allele, which was finally confirmed with the supershift for the Yin Yang 1 transcription factor (YY1). Subjects with high progranulin levels manifested a significantly higher mean DNA methylation (P < 1 × 10−7) in one promoter region, which was in line with a significantly lower PSRC1 mRNA expression levels in blood (P = 1 × 10−3). Consistently, rs629301-A allele was associated with lower PSRC1 mRNA expression (P < 1 × 10−7). Our data suggest that the progranulin-associated variant rs629301 modifies the transcription of PSRC1 through alteration of YY1 binding capacity. DNA methylation studies further support the role of PSRC1 in regulation of progranulin serum levels. Key messages PSRC1 (proline and serine rich coiled-coil 1) SNPs are associated with serum progranulin levels. rs629301 regulates PSRC1 expression by affecting Yin Yang 1 transcription factor (YY1) binding. PSRC1 is also epigenetically regulated in subjects with high progranulin levels.

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Balachandran, Priya, Alexis Brooks-Walter, Anni Virolainen-Julkunen, Susan K. Hollingshead, and David E. Briles. "Role of Pneumococcal Surface Protein C in Nasopharyngeal Carriage and Pneumonia and Its Ability To Elicit Protection against Carriage of Streptococcus pneumoniae." Infection and Immunity 70, no. 5 (May 2002): 2526–34. http://dx.doi.org/10.1128/iai.70.5.2526-2534.2002.

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ABSTRACT Previous studies suggested that PspC is important in adherence and colonization within the nasopharynx. In this study, we conducted mutational studies to further identify the role PspC plays in the pathogenesis of pneumococci. pspC and/or pspA was insertionally inactivated in a serotype 2 Streptococcus pneumoniae strain and in a serotype 19 S. pneumoniae strain. In the mouse colonization model, pneumococcal strains with mutations in pspC were significantly attenuated in their abilities to colonize. In a mouse pneumonia model, strains with mutations in pspC were unable to infect or multiply within the lung. Using reverse transcriptase PCR we were able to demonstrate that pspC is actively transcribed in vivo, when the bacteria are growing in the nasal cavity and in the lungs. In the bacteremia model, a strain mutated for pspC alone behaved like the wild type, but the absence of both pspC and pspA caused accelerated clearance of the bacteria. Intranasal immunization with PspC with cholera toxin subunit B as an adjuvant protected against intranasal challenge. Evidence was also obtained that revertants that spontaneously acquired PspC expression could multiply and colonize the nasal tissue. This latter finding strongly indicates that pneumococci are actively metabolizing and growing while in the nasopharynx.

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Yuste, Jose, Suneeta Khandavilli, Naadir Ansari, Kairya Muttardi, Laura Ismail, C. Hyams, Jeffrey Weiser, Timothy Mitchell, and Jeremy S. Brown. "The Effects of PspC on Complement-Mediated Immunity to Streptococcus pneumoniae Vary with Strain Background and Capsular Serotype." Infection and Immunity 78, no. 1 (November 2, 2009): 283–92. http://dx.doi.org/10.1128/iai.00541-09.

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ABSTRACT Streptococcus pneumoniae may evade complement activity by binding of factor H (FH), a negative regulator of the alternative pathway, to the surface protein PspC. However, existing data on the effects of FH binding to PspC on complement activity are conflicting, and there is also considerable allelic variation in PspC structure between S. pneumoniae strains that may influence PspC-dependent effects on complement. We have investigated interactions with complement for several S. pneumoniae strains in which the gene encoding PspC has been deleted. The degree of FH binding varied between strains and was entirely dependent on PspC for seven strains. Data obtained with TIGR4 strains expressing different capsular serotypes suggest that FH binding is affected by capsular serotype. Results of immunoblot analysis for C3 degradation products and iC3b deposition assays suggested that FH bound to PspC retained functional activity, but loss of PspC had strikingly varied effects on C3b/iC3b deposition on S. pneumoniae, with large increases on serotype 4, 6A, 6B, and 9V strains but only small increases or even decreases on serotype 2, 3, 17, and 23F strains. Repeating C3b/iC3b assays with TIGR4 strains expressing different capsular serotypes suggested that differences in the effect of PspC on C3b/iC3b deposition were largely independent of capsular serotype and depend on strain background. However, data obtained from infection in complement-deficient mice demonstrated that differences between strains in the effects of PspC on complement surprisingly did not influence the development of septicemia.

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Dave, Sandhya, Alexis Brooks-Walter, Michael K. Pangburn, and Larry S. McDaniel. "PspC, a Pneumococcal Surface Protein, Binds Human Factor H." Infection and Immunity 69, no. 5 (May 1, 2001): 3435–37. http://dx.doi.org/10.1128/iai.69.5.3435-3437.2001.

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ABSTRACT PspC was found to bind human complement factor H (FH) by Western blot analysis of D39 (pspC +) and an isogenic mutant TRE108 (pspC). We confirmed that PspA does not bind FH, while purified PspC binds FH very strongly. The binding of FH to exponentially growing pneumococci varied among different isolates when analyzed by fluorescence activated cell sorting analysis.

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Quin, Lisa R., Quincy C. Moore, and Larry S. McDaniel. "Pneumolysin, PspA, and PspC Contribute to Pneumococcal Evasion of Early Innate Immune Responses during Bacteremia in Mice." Infection and Immunity 75, no. 4 (January 12, 2007): 2067–70. http://dx.doi.org/10.1128/iai.01727-06.

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ABSTRACTThe pneumococcal virulence factors include capsule, PspA, PspC, and Ply. Cytometric analysis demonstrated that the greatest levels of C3 deposition were on a ΔplyPspA−PspC−mutant. Also, Ply, PspA, and PspC expression resulted in C3 degradation in vitro and in vivo. Finally, blood clearance assays demonstrated that there was enhanced clearance of ΔplyPspA−PspC−pneumococci compared to the clearance of nonencapsulated pneumococci.

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Wang, Yue, Xue-Hao Chen, Xin-Yi Wu, Guo-He Cai, and Shao-Wei Zhai. "Effects of Dietary Supplementation of Peanut Skin Proanthocyanidins on Growth Performance and Lipid Metabolism of the Juvenile American Eel (Anguilla rostrata)." Animals 12, no. 18 (September 12, 2022): 2375. http://dx.doi.org/10.3390/ani12182375.

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As a functional feed additive, grape seed proanthocyanidin extract has received a lot of attention due to its biological activity in the health of aquatic animals, but its high cost limits the application of this feed additive in the diet of many fish species. It is thus urgent to develop a new resource of proanthocyanidin extract. We aimed to investigate the effects of dietary supplementation with peanut skin proanthocyanidins (PSPc) on growth parameters and lipid metabolism of juvenile American eel (Anguilla rostrata). Four hundred and fifty juvenile eels were randomly divided into five groups fed diets with five PSPc supplementation levels. The trial lasted for 8 weeks. Dietary PSPc supplementation significantly improved weight gain and feed utilization, and the best growth performance was found in the group fed with 900 mg/kg PSPc. PSPc supplementation significantly affected the crude protein level of whole fish and serum lipid parameters, and the best lipid-lowering effect was found in the fish fed with 900 mg/kg PSPc. Dietary PSPc supplementation increased lipolytic enzyme activities and decrease lipid synthase levels in the liver. The lipid metabolites affected by 900 mg/kg PSPc in the liver were mainly upregulated phosphatidylethanolamine in autophagy, downregulated ceramides in sphingolipid metabolism, upregulated phosphatidylcholine and phosphatidylethanolamine, downregulated 2-lysophosphatidylcholine in glycerophospholipid metabolism, and upregulated phosphatidylcholine in linoleic acid metabolism. In conclusion, an appropriate level of PSPc might effectively improve growth performance and regulate the lipid metabolism of the juvenile American eel, and 900 mg/kg PSPc is recommended in the diet of this fish species.

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Quin, Lisa R., Quincy C. Moore, Justin A. Thornton, and Larry S. McDaniel. "Peritoneal Challenge Modulates Expression of Pneumococcal Surface Protein C during Bacteremia in Mice." Infection and Immunity 76, no. 3 (December 26, 2007): 1122–27. http://dx.doi.org/10.1128/iai.01066-07.

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ABSTRACT Differential expression of pneumococcal virulence proteins has been demonstrated. We previously demonstrated challenge route-dependent differences in pneumococcal surface protein C (PspC) expression during bacteremia. In this study, we investigated differences in PspC expression during the transition of pneumococci from the peritoneum to the blood. Time course analysis of PspC expression using flow cytometry demonstrated that Streptococcus pneumoniae D39 collected from blood expressed significantly more PspC than did D39 collected from the peritoneum of intraperitoneally (i.p.)-infected mice. Various challenge models were then used to determine whether host responses originating from the peritoneum can influence PspC expressed by pneumococci in the blood. Using heat-inactivated D39 (HI-D39) and sterile peritoneal dialysis fluid (PDF), we investigated whether stimulation of peritoneal responses can influence PspC expression. Injection of mice i.p. with HI-D39 or PDF immediately prior to intravenous (i.v.) infection with D39 caused a significant increase in PspC expressed by D39 in the blood. Finally, we used cytokine array analysis to investigate specific inflammatory mediators that may result in differential PspC expression. Of the 96 inflammatory cytokines assayed, D39 i.p. challenge led to increased expression of 33 cytokines in serum; whereas D39 i.v. challenge led to increased expression of 15 and decreased expression of 11 cytokines relative to serum of the uninfected control. These results indicate that PspC is differentially regulated during growth in vivo and that the level of expression varies depending on the host environment.

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Flores-Kim, Josué, and Andrew J. Darwin. "Phage Shock Protein C (PspC) of Yersinia enterocolitica Is a Polytopic Membrane Protein with Implications for Regulation of the Psp Stress Response." Journal of Bacteriology 194, no. 23 (September 28, 2012): 6548–59. http://dx.doi.org/10.1128/jb.01250-12.

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ABSTRACTPhage shock proteins B (PspB) and C (PspC) are integral cytoplasmic membrane proteins involved in inducing theYersinia enterocoliticaPsp stress response. A fundamental aspect of these proteins that has not been studied in depth is their membrane topologies. Variousin silicoanalyses universally predict that PspB is a bitopic membrane protein with the C terminus inside. However, similar analyses yield conflicting predictions for PspC: a bitopic membrane protein with the C terminus inside, a bitopic membrane protein with the C terminus outside, or a polytopic protein with both termini inside. Previous studies ofEscherichia coliPspB-LacZ and PspC-PhoA fusion proteins supported bitopic topologies, with the PspB C terminus inside and the PspC C terminus outside. Here we have used a series of independent approaches to determine the membrane topologies of PspB and PspC inY. enterocolitica. Our data support the predicted arrangement of PspB, with its C terminus in the cytoplasm. In contrast, data from multiple independent approaches revealed that both termini of PspC are located in the cytoplasm. Additional experiments suggested that the C terminus of PspC might be the recognition site for the FtsH protease and an interaction interface with PspA, both of which would be compatible with its newly proposed cytoplasmic location. This unexpected arrangement of PspC allows a new model for events underlying activation of the Psp response, which is an excellent fit with observations from various previous studies.

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Li, Jinwei, Lianfu Zhang, and Yuanfa Liu. "Optimization of Extraction of Natural Pigment from Purple Sweet Potato by Response Surface Methodology and Its Stability." Journal of Chemistry 2013 (2013): 1–5. http://dx.doi.org/10.1155/2013/590512.

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Purple sweet potato colour (PSPC) was a kind of natural pigment that attracted the general concern in recent years. In this paper, the response surface methodology was employed to optimize the extraction conditions of PSPC. The results showed that the extraction yield of purple colour was 11.6355 mg/g at the optimum extraction conditions of extraction temperature 60°C, extraction time 1 h, the ratio of solid to liquid ratio of 1 : 30, and acidified ethanol solution concentration 80%. Stability experiment showed that Fe3+and Al3+could increase the stability of PSPC, but Cu2+, Zn2+, and Pb2+would decrease the stability of PSPC. Ascorbic acidified could significantly increase the stability of PSPC, and Na2SO3would reduce the PSPC’s stability.

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Souza, Liliana, Shuyi Li, Erica Silva, Zhentian Li, Shu Feng-jue, Hairong Xiong, William S. Dynan, and Morgan L. McLemore. "Deletion of Nono, a Novel Double-Strand Break Repair Factor, Leads to Hematopoietic Stem Cell Defects." Blood 124, no. 21 (December 6, 2014): 478. http://dx.doi.org/10.1182/blood.v124.21.478.478.

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Abstract Three genes, SFPQ, NONO, and PSPC1 encode for a small family of tandem RRM domain-containing proteins with diverse functions in RNA processing, transcription, and DNA repair. Our previous work has shown that an SFPQ•NONO complex promotes a distinct sub-pathway of non-homologous end joining (NHEJ) in vitro, implicating it as a novel double-strand break (DSB) repair factor. Consistently, attenuation of NONO function in human fibroblasts leads to partial radiosensitivity, delayed resolution of DNA repair foci, and an increase in radiation-dependent chromosome aberrations. To investigate the in vivo function of this complex, we knocked out Nono, the mouse homolog of the human NONO gene. We hypothesized that a DSB repair deficiency would lead to stem cell exhaustion, sensitivity to DNA damaging agents, or both. First, we investigated hematopoietic stem cells (HSCs), which are known to be sensitive to impairment of DNA repair. Nono-deficient (gt/0) mice showed reduced bone marrow and spleen cellularity, potentially due to reduced body size. The proportion of HSCs (LSK-SLAM) in relation to total bone marrow cells was similar in Nono-deficient and wild type (WT) mice, and bone marrow cell cultures yielded similar numbers and types of colonies. However, HSCs from Nono-deficient mice showed severe impairment in competitive repopulation assays in primary and secondary recipients. HSCs from gt/0 mice also displayed significantly higher levels of ROS and proliferation (accessed via BrdU incorporation), as well as higher percentage of Ki-67 positivity when compared to HSCs from WT mice. Together, these results indicate that Nono-deficient HSCs exhibit impaired capacity for self-renewal that may be caused by excessive HSC proliferation, a primary defect in response to genotoxic stress or a combination of both. To further elucidate this phenomenon, we investigated potential differences in sensitivity to the DNA crosslinking agent mitomycin C (MMC) and radiation. As previously observed in other genomic instability models (e.g., Fanconi anemia), colony-forming-cells from Nono-deficient mice were highly sensitive to MMC and X-rays (2 Gγ). Utilizing FACS-sorted HSCs, we determined that NONO protein levels are induced after X-ray treatment, and that Nono-deficient HSCs show delayed resolution of γ-H2AX foci and increased apoptosis. We also evaluated changes in the testis, another organ frequently affected by DNA repair gene mutations. Accordingly, testes of Nono-deficient mice showed growth retardation that became apparent between 18 and 26 days of postnatal development. The co-occurrence of hematopoietic and germ cell defects is reminiscent of other DNA repair gene defects, including those seen in Fanconi anemia. Collectively, our data identify NONO as a novel and important regulator of both HSC maintenance and germ cell function. Its potential effect in other organ systems and mechanism of action are under investigation. Disclosures No relevant conflicts of interest to declare.

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Li, Jie, David T. Glover, Alexander J. Szalai, Susan K. Hollingshead, and David E. Briles. "PspA and PspC Minimize Immune Adherence and Transfer of Pneumococci from Erythrocytes to Macrophages through Their Effects on Complement Activation." Infection and Immunity 75, no. 12 (October 8, 2007): 5877–85. http://dx.doi.org/10.1128/iai.00839-07.

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ABSTRACT Pneumococcal surface protein A (PspA) and PspC are important virulence factors. Their absence has been shown to allow improved clearance of pneumococci from the blood of mice and to decrease pneumococcal virulence. In the presence of antibody and complement, pneumococci attach to erythrocytes in a process called immune adherence (IA), which facilitates their delivery to, and eventual phagocytosis by, macrophages. It is not known, however, if PspA and PspC affect IA. Using PspA and/or PspC isogenic mutants and complement-deficient mouse sera, we demonstrated that absence of PspA allows greater deposition of C1q and thus increased classical-pathway-mediated C3 deposition. In the absence of both PspA and PspC, there is also a major increase in C1q-independent C3 deposition through the alternative pathway. The latter was observed even though absence of PspC alone did not have a major effect on alternative-pathway-dependent complement deposition. The enhanced complement C3 deposition realized in the absence of PspA alone and in the absence of PspA and PspC resulted in both greatly increased IA to human erythrocytes and improved transfer of pneumococci from erythrocytes to phagocytes. These data provide new insight into how PspA and PspC act in synergy to protect pneumococci from complement-dependent clearance during invasive infection.

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Shan, Qun, Jun Lu, Yuanlin Zheng, Jing Li, Zhong Zhou, Bin Hu, Zifeng Zhang, et al. "Purple Sweet Potato Color Ameliorates Cognition Deficits and Attenuates Oxidative Damage and Inflammation in Aging Mouse Brain Induced by D-Galactose." Journal of Biomedicine and Biotechnology 2009 (2009): 1–9. http://dx.doi.org/10.1155/2009/564737.

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Purple sweet potato color (PSPC), a naturally occurring anthocyanin, has a powerful antioxidant activity in vitro and in vivo. This study explores whether PSPC has the neuroprotective effect on the aging mouse brain induced by D-galactose (D-gal). The mice administrated with PSPC (100 mg/kg.day, 4 weeks, from 9th week) via oral gavage showed significantly improved behavior performance in the open field and passive avoidance test compared with D-gal-treated mice (500 mg/kg.day, 8 weeks). We further investigate the mechanism involved in neuroprotective effects of PSPC on mouse brain. Interestingly, we found, PSPC decreased the expression level of glial fibrillary acidic protein (GFAP), inducible nitric oxide synthase (iNOS), and cyclooxygenase-2 (COX-2), inhibited nuclear translocation of nuclear factor-kappaB (NF-κB), increased the activity of copper/zinc superoxide dismutase (Cu/Zn-SOD) and catalase (CAT), and reduced the content of malondialdehyde (MDA), respectively. Our data suggested that PSPC attenuated D-gal-induced cognitive impairment partly via enhancing the antioxidant and anti-inflammatory capacity.

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Wang, Na, Weixuan Chen, Chenxu Cui, Yuru Zheng, Qiuying Yu, Hongtao Ren, Zhigang Liu, Chao Xu, and Gaiping Zhang. "The Peanut Skin Procyanidins Attenuate DSS-Induced Ulcerative Colitis in C57BL/6 Mice." Antioxidants 11, no. 11 (October 25, 2022): 2098. http://dx.doi.org/10.3390/antiox11112098.

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Polyphenols from peanut skin have been reported to possess many beneficial functions for human health, including anti-oxidative, antibacterial, anticancer, and other activities. To date, however, its anti-inflammatory effect and the underlying mechanism remain unclear. In this study, the anti-inflammatory effect of peanut skin procyanidins extract (PSPE) and peanut skin procyanidins (PSPc) were investigated by a dextran sodium sulfate (DSS)-induced colitis mouse model. The results showed that both PSPE and PSPc supplementation reversed the DSS-induced body weight loss and reduced disease activity index (DAI) values, accompanied by enhanced goblet cell numbers and tight junction protein claudin-1 expression in the colon. PSPE and PSPc treatment also suppressed the inflammatory responses and oxidative stress in the colon by down-regulating IL-1β, TNF-α, and MDA expressions. Meanwhile, PSPE and PSPc significantly altered the gut microbiota composition by increasing the relative abundance of Clostridium XlVb and Anaerotruncus, and inhibiting the relative abundance of Alistipes at the genus level. PSPE and PSPc also significantly elevated the production of short-chain fatty acids (SCFAs) in mice with colitis. The correlation analysis suggested that the protective effects of PSPE and PSPc on colitis might be related to the alteration of gut microbiota composition and the formation of SCFAs. In conclusion, the current research indicates that supplementation of PSPE and PSPc could be a promising nutritional strategy for colitis prevention and treatment.

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Meroni, Marica, Miriam Longo, Erika Paolini, Anna Alisi, Luca Miele, Emilia Rita De Caro, Giuseppina Pisano, et al. "The rs599839 A>G Variant Disentangles Cardiovascular Risk and Hepatocellular Carcinoma in NAFLD Patients." Cancers 13, no. 8 (April 8, 2021): 1783. http://dx.doi.org/10.3390/cancers13081783.

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Background and Aims: Dyslipidemia and cardiovascular diseases (CVD) are comorbidities of nonalcoholic fatty liver disease (NAFLD), which ranges from steatosis to hepatocellular carcinoma (HCC). The rs599839 A>G variant, in the CELSR2-PSRC1-SORT1 gene cluster, has been associated CVD, but its impact on metabolic traits and on the severity liver damage in NAFLD has not been investigated yet. Methods: We evaluated the effect of the rs599839 variant in 1426 NAFLD patients (Overall cohort) of whom 131 had HCC (NAFLD-HCC), in 500,000 individuals from the UK Biobank Cohort (UKBBC), and in 366 HCC samples from The Cancer Genome Atlas (TCGA). Hepatic PSRC1, SORT1 and CELSR2 expressions were evaluated by RNAseq (n = 125). Results: The rs599839 variant was associated with reduced circulating LDL, carotid intima-media thickness, carotid plaques and hypertension (p < 0.05) in NAFLD patients and with protection against dyslipidemia in UKBBC. The minor G allele was associated with higher risk of HCC, independently of fibrosis severity (odds ratio (OR): 5.62; 95% c.i. 1.77–17.84, p = 0.003), poor prognosis and advanced tumor stage (p < 0.05) in the overall cohort. Hepatic PSRC1, SORT1 and CELSR2 expressions were increased in NAFLD patients carrying the rs599839 variant (p < 0.0001). SORT1 mRNA levels negatively correlated with circulating lipids and with those of genes involved in lipoprotein turnover (p < 0.0001). Conversely, PSRC1 expression was positively related to that of genes implicated in cell proliferation (p < 0.0001). In TCGA, PSRC1 over-expression promoted more aggressive HCC development (p < 0.05). Conclusions: In sum, the rs599839 A>G variant is associated with protection against dyslipidemia and CVD in NAFLD patients, but as one it might promote HCC development by modulating SORT1 and PSRC1 expressions which impact on lipid metabolism and cell proliferation, respectively.

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Duthy, Thomas G., Rebecca J. Ormsby, Eleni Giannakis, A. David Ogunniyi, Uwe H. Stroeher, James C. Paton, and David L. Gordon. "The Human Complement Regulator Factor H Binds Pneumococcal Surface Protein PspC via Short Consensus Repeats 13 to 15." Infection and Immunity 70, no. 10 (October 2002): 5604–11. http://dx.doi.org/10.1128/iai.70.10.5604-5611.2002.

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Abstract:

ABSTRACT The innate ability of Streptococcus pneumoniae to resist complement activation and complement-mediated phagocytosis may be a direct consequence of the ability of the bacteria to bind components of the complement regulatory system. One such component, factor H (fH), is a crucial fluid-phase negative regulator of the alternative pathway of complement and is utilized by a number of pathogenic organisms to resist complement attack. The pneumococcal surface protein C (PspC [also known as CbpA] and SpsA) has been shown to bind fH, although the exact binding site within one or more of the 20 short consensus repeats (SCRs) of the molecule is not known. The purpose of the current study was to map specific SCRs on fH responsible for this binding. Initial experiments utilizing type 2 pneumococcal strain D39 and its isogenic PspC-negative derivative (D39/pspC mutant) showed that fH binding was PspC dependent. A purified recombinant protein derivative of PspC that lacked the proline-rich region (PspCΔPro) had a reduced binding efficiency for fH, thereby directly showing the importance of this region for the fH interaction. We have specifically shown by inhibition experiments that SCRs responsible for heparin and C3b binding of fH are not involved in binding PspC and the interaction between fH and PspC is largely hydrophobic, since no inhibition was observed in the presence of high concentrations of NaCl. Construction of SCR proteins encompassing the whole fH molecule showed that SCRs 8 to 15 (SCR 8-15) mediated binding to PspC. Further localization experiments revealed that SCR 13 and SCR 15 were required for full binding, although partial binding was retained when either SCR was removed.

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