The International Journal of Biochemistry & Cell Biology (INT J BIOCHEM CELL B)

Publications in this journal

• Article: Viroporin Activity and Membrane Topology of Classic Swine Fever Virus p7 Protein.

  Guo HC, Sun SQ, Sun DH, Wei YQ, Xu J, Huang M, Liu XT, Liu ZX, Luo JX, Yin H, Liu DX
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  ABSTRACT: Viroporins are a group of viral proteins that participate in viral replication cycles, including modification of membrane permeability and promotion of viral release. Although biological data have been accumulated on viroporion-like proteins of other viruses belonging to family Flaviviridae, the viroporin activity and membrane topology of p7 protein from classical swine fever virus (CSFV), a member of the genus Pestivirus of the family Flaviviridae, are largely unknown. In this study, sequence analysis of the primary structure of p7 polypeptide demonstrates that p7 contains two putative transmembrane regions connected by a short hydrophilic segment. Expression of p7 protein in Escherichia coli leads to the permeabilization of bacterial cells to small molecules. The p7 protein also enhances the permeability of mammalian cells, increasing the intracellular Ca2+ concentration and the permeability of cells to the translation inhibitor hygromycin B. This protein is an integral membrane protein and can form homo-oligomers. It mainly localizes to the ER at the early stage of the expression and can be transferred to the plasma membrane at the late stage of the expression. Detergent permeabilization assays confirmed that the p7 protein is a 2-pass transmembrane protein and its N and C termini are exposed to the ER lumen. Deletion analysis showed that amino acid residues 41-63 may be essential for the viroporin activity of the protein. Our studies demonstrate that CSFV p7 possesses properties commonly associated with viroporins, which could be a potential target for the development of a therapeutic intervention for classic swine fever virus infection.
  The International Journal of Biochemistry & Cell Biology 03/2013;
• Article: Angiotensin II- induced pro-fibrotic effects require p38MAPK activity and Transforming Growth Factor beta 1 expression in skeletal muscle cells

  María Gabriela Morales, Yaneisi Vazquez, María José Acuña, Juan Carlos Rivera, Felipe Simon, José Diego Salas, Joel Alvarez Ruf, Enrique Brandan, Claudio Cabello-Verrugio
  The International Journal of Biochemistry & Cell Biology 01/2012; 44:1993-2002.
• Article: Angiotensin II- induced pro-fibrotic effects require p38MAPK activity and Transforming Growth Factor beta 1 expression in skeletal muscle cells

  Morales MG, Vazquez Y, Acuña MJ, Rivera JC, Simon F, Salas JD, Alvarez-Ruf J, Brandan E, Cabello-Verrugio C
  The International Journal of Biochemistry & Cell Biology 01/2012; 44:1993-2002.
• Article: Crosstalk between Nrf2 and the proteasome: therapeutic potential of Nrf2 inducers in vascular disease and aging Sarah Chapple, Richard CM Siow, Giovanni E. Mann Intern. J. Biochem. Cell Biol. (in press)

  Sarah Chapple, Richard CM Siow, Giovanni E. Mann
  The International Journal of Biochemistry & Cell Biology 01/2012;
• Article: Effect of divalent cations on the porcine kidney cortex membrane-bound form of dipeptidyl peptidase IV

  Pascual I, Gómez H, Pons T, Chappé M, Vargas MA, Valdés G, Lopéz A, Saroyán A, Charli JL, de los Angeles Chávez M
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  ABSTRACT: Dipeptidyl peptidase IV is an ectopeptidase with multiple physiological roles including the degradation of incretins, and a target of therapies for type 2 diabetes mellitus. Divalent cations can inhibit its activity, but there has been little effort to understand how they act. The intact membrane-bound form of porcine kidney dipeptidyl peptidase IV was purified by a simple and fast procedure. The purified enzyme hydrolyzed Gly-Pro-p-nitroanilide with an average V(max) of 1.397±0.003 μmol min(-1) mL(-1), k(cat) of 145.0±1.2 s(-1), K(M) of 0.138±0.005 mM and k(cat)/K(M) of 1050 mM(-1) s(-1). The enzyme was inhibited by bacitracin, tosyl-L-lysine chloromethyl ketone, and by the dipeptidyl peptidase IV family inhibitor L-threo-Ile-thiazolidide (K(i) 70 nM). The enzyme was inhibited by the divalent ions Ca(2+), Co(2+), Cd(2+), Hg(2+) and Zn(2+), following kinetic mechanisms of mixed inhibition, with K(i) values of 2.04×10(-1), 2.28×10(-2), 4.21×10(-4), 8.00×10(-5) and 2.95×10(-5) M, respectively. According to bioinformatic tools, Ca(2+) ions preferentially bound to the β-propeller domain of the porcine enzyme, while Zn(2+) ions to the α-β hydrolase domain; the binding sites were strikingly conserved in the human enzyme and other homologues. The functional characterization indicates that porcine and human homologues have very similar functional properties. Knowledge about the mechanisms of action of divalent cations may facilitate the design of new inhibitors.
  The International Journal of Biochemistry & Cell Biology 03/2011; 43(3):363-71.
• Article: Integrated genomics of chemotherapy resistant ovarian cancer: a role for extracellular matrix, TGFbeta and regulating microRNAs.

  J. Helleman, M. P.H.M. Jansen, C. Burger, M.E.L. van der Burg, E.M.J.J. Berns
  The International Journal of Biochemistry & Cell Biology 01/2010; 42(1):25.
• Article: MicroRNAs in ovarian cancer biology and therapy resistance.

  M.T.M. van Jaarsveld, J. Helleman, E.M.J.J. Berns, E.A.C. Wiemer
  The International Journal of Biochemistry & Cell Biology 01/2010; 42(8):1282.
• Article: Rhodopsin: structure, signal transduction and oligomerisation.

  Morris MB, Dastmalchi S, Church WB
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  ABSTRACT: Rhodopsin was the first G protein-coupled receptor (GPCR) for which a high-resolution crystal structure was obtained. Several crystal structures have now been solved representing different activation states of the receptor. These structures, together with those from lower resolution techniques (e.g. electron microscopy), shed light on the stepwise process by which energy from an extracellular photon is transduced across the membrane to the intracellular compartment thereby activating signalling mechanisms responsible for very low-level light detection. Controversy remains in several areas including: (i) transmembrane helix movements responsible for the transduction process, (ii) the stoichiometry of coupling to G proteins and their mode of activation, (iii) the role, if any, of receptor oligomerisation and (iv) the suitability of using structures of this GPCR as templates for modelling the structures of other GPCRs, and their mechanisms of activation.
  The International Journal of Biochemistry & Cell Biology 04/2009; 41(4):721-4.
• Article: Darwin's legacy in modern bioscience.

  Joanna Kargul, Geoffrey J Laurent
  The International Journal of Biochemistry & Cell Biology 11/2008;
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  Article: Evolution and self-assembly of protocells.

  Ricard V Solé
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  ABSTRACT: Cells define the minimal building blocks of life. How cellular life emerged and evolved implies to cross the boundary between living and nonliving matter. Here we explore this problem by presenting several relevant components of the whole picture involving chemistry, physics and natural selection. Available evidence suggests that the basic logic of life can be understood and eventually translated into synthetic forms of cellular life. A simple, physically sound model of information-free protocell replication suggests that the basic logic of how to couple metabolism and container can be more relevant than the specific set of parameters used, thus indicating that the emergence of cells might have been easier than we would expect.
  The International Journal of Biochemistry & Cell Biology 11/2008; 41(2):274-84.
• Article: Epigenetics and human disease.

  Joanna Kargul, Geoffrey J Laurent
  The International Journal of Biochemistry & Cell Biology 11/2008; 41(1):1.
• Article: Predation and eukaryote cell origins: a coevolutionary perspective.

  T Cavalier-Smith
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  ABSTRACT: Cells are of only two kinds: bacteria, with DNA segregated by surface membrane motors, dating back approximately 3.5Gy; and eukaryotes, which evolved from bacteria, possibly as recently as 800-850My ago. The last common ancestor of eukaryotes was a sexual phagotrophic protozoan with mitochondria, one or two centrioles and cilia. Conversion of bacteria (=prokaryotes) into a eukaryote involved approximately 60 major innovations. Numerous contradictory ideas about eukaryogenesis fail to explain fundamental features of eukaryotic cell biology or conflict with phylogeny. Data are best explained by the intracellular coevolutionary theory, with three basic tenets: (1) the eukaryotic cytoskeleton and endomembrane system originated through cooperatively enabling the evolution of phagotrophy; (2) phagocytosis internalised DNA-membrane attachments, unavoidably disrupting bacterial division; recovery entailed the evolution of the nucleus and mitotic cycle; (3) the symbiogenetic origin of mitochondria immediately followed the perfection of phagotrophy and intracellular digestion, contributing greater energy efficiency and group II introns as precursors of spliceosomal introns. Eukaryotes plus their archaebacterial sisters form the clade neomura, which evolved from a radically modified derivative of an actinobacterial posibacterium that had replaced the ancestral eubacterial murein peptidoglycan by N-linked glycoproteins, radically modified its DNA-handling enzymes, and evolved cotranslational protein secretion, but not the isoprenoid-ether lipids of archaebacteria. I focus on this phylogenetic background and on explaining how in response to novel phagotrophic selective pressures and ensuing genome internalisation this prekaryote evolved efficient digestion of prey proteins by retrotranslocation and 26S proteasomes, then internal digestion by phagocytosis, lysosomes, and peroxisomes, and eukaryotic vesicle trafficking and intracellular compartmentation.
  The International Journal of Biochemistry & Cell Biology 11/2008; 41(2):307-22.
• Article: Molecular evolution of the cadherin superfamily.

  Paco Hulpiau, Frans van Roy
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  ABSTRACT: This review deals with the large and pleiotropic superfamily of cadherins and its molecular evolution. We compiled literature data and an in-depth phylogenetic analysis of more than 350 members of this superfamily from about 30 species, covering several but not all representative branches within metazoan evolution. We analyzed the sequence homology between either ectodomains or cytoplasmic domains, and we reviewed protein structural data and genomic architecture. Cadherins and cadherin-related molecules are defined by having an ectodomain in which at least two consecutive calcium-binding cadherin repeats are present. There are usually 5 or 6 domains, but in some cases as many as 34. Additional protein modules in the ectodomains point at adaptive evolution. Despite the occurrence of several conserved motifs in subsets of cytoplasmic domains, these domains are even more diverse than ectodomains and most likely have evolved separately from the ectodomains. By fine tuning molecular classifications, we reduced the number of solitary superfamily members. We propose a cadherin major branch, subdivided in two families and 8 subfamilies, and a cadherin-related major branch, subdivided in four families and 11 subfamilies. Accordingly, we propose a more appropriate nomenclature. Although still fragmentary, our insight into the molecular evolution of these remarkable proteins is steadily growing. Consequently, we can start to propose testable hypotheses for structure-function relationships with impact on our models of molecular evolution. An emerging concept is that the ever evolving diversity of cadherin structures is serving dual and important functions: specific cell adhesion and intricate cell signaling.
  The International Journal of Biochemistry & Cell Biology 11/2008; 41(2):349-69.
• Article: Epigenetic therapy of leukemia: An update.

  Nitin Jain, Adriana Rossi, Guillermo Garcia-Manero
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  ABSTRACT: Carcinogenesis is classically thought to result from genetic alterations in DNA sequence such as deletions, mutations, or chromosomal translocations. These in turn may lead to the activation of oncogenes, inactivation of tumor suppressor genes or formation of chimeric oncoproteins. Epigenetics, in contrast, refers to a number of biochemical modifications of chromatin, either to DNA directly or to its associated protein complexes that affect gene expression without altering the primary sequence of DNA [Robertson KD, Wolffe AP. DNA methylation in health and disease. Nat Rev Genet 2000;1:11-9; Jones PA, Baylin SB. The epigenomics of cancer. Cell. 2007;128:683-92]. A fundamental difference between genetic and epigenetic alterations is the irreversible nature of genetic lesions whereas epigenetic ones are potentially reversible, allowing for therapeutic intervention. In the last decade, it has become apparent that epigenetic changes play an important role in cancer, particularly in leukemia. Significant advances have been made in the elucidation of these processes as well as in translating this knowledge to the clinic, as in the development of new prognostic biomarkers or targeted therapies. In this review, we will focus on recent advances in epigenetic therapy in leukemia.
  The International Journal of Biochemistry & Cell Biology 11/2008; 41(1):72-80.