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आयतन 4, मुद्दा 2 (2018)

संपादकीय नोट

Editorial Note : Journal of Molecular and Cellular Biochemistry

Deepthi R

All published articles of this journal are included in the indexing and abstracting coverage of CAS Source Index (CASSI), Index Copernicus, Google Scholar, Sherpa Romeo, Academic Journals Database, GenamicsJournalSeek, JournalTOCs, CiteFactor, Electronic Journals Library, RefSeek, Hamdard University, EBSCO A-Z, Directory of Abstract Indexing for Journals, World Catalogue of Scientific Journals, OCLC- WorldCat, Scholarsteer, SWB online catalog, Virtual Library of Biology (vifabio), Publons, Dtufindit, Geneva Foundation for Medical Education and Research.

लघु संचार

Glycobiology 2020: Hyaluronan Metabolism is Associated with DNA Repair Genes in Breast and Colorectal Cancer. Screening of Potential Progression Markers Using qPCR- Ina Sevic, Center for Basic and Applied Research (CIBA), CIT NOBA

Ina Sevic 1, Fiorella Mercedes Spinelli 1, Daiana Lujan Vitale 1, Antonella Icardi 1, Lucia Romano 2, Alejandra Brandone 3, Paula Giannoni 4, Carolina Cristina 2, Marcela Fabiana Bolontrade 5 and Laura Alaniz 1

In this work, we compared mRNA levels of Hyaluronan (HA) metabolism members and BRCA genes, known to be involved in the tumoral process, between tumor and non-tumor adjacent tissue and its correlation with previously proposed biomarkers (ER, PR, HER2 and KI67) in order to assess their value as a progression biomarkers. We show alteration in HA metabolism in colorectal but not breast cancer. However, we found a decrease in Hyaluronidase 1 HYAL1 levels in the breast but not colorectal cancer. We also show lower HA levels in tumor compared with normal tissue that could indicate a possible influence of tumor on its surrounding “normal” tissue. In both breast and colorectal cancer, CD44 and BRCA2 showed a strong positive correlation. Besides, our results show first indicators that qPCR of the analyzed genes could be used as an easy and low-cost procedure for the evaluation of molecular markers we propose here

लघु संचार

Glycobiology 2020: The heparan sulfate proteoglycan Syndecan-1 and heparanase are novel regulators of cancer stem cell function and therapeutic resistance - Martin Gotte- Munster University Hospital

Martin Gotte 1, Sampath Kumar Katakam 1, Valeria Tria 2, Paride Pelucchi 2, Cinzia Cocola 2, Israel Vlodavsky 3, George W Yip 4, Ileana Zucchi 2, Rolland Reinbold 2, Burkhard Greve 5

The heparan sulfate proteoglycan Syndecan-1 binds cytokines, morphogens and extracellular matrix components, regulating cancer stem cell properties and invasiveness. Syndecan-1 is modulated by the heparan sulfate-degrading enzyme heparanase, but the underlying regulatory mechanisms are only poorly understood (1). In colon cancer pathogenesis, complex changes occur in the expression pattern of Syndecan-1 and heparanase during progression from well-differentiated to undifferentiated tumors. Loss of Syndecan-1 and increased expression of heparanase are associated with a change in phenotypic plasticity and an increase in invasiveness, metastasis and dedifferentiation. Here we investigated the regulatory and functional interplay of Syndecan-1 and heparanase employing siRNA-mediated silencing and plasmid-based overexpression approaches in human colon cancer cell lines and in a xenograft model . Sdc-1 small-interfering RNA knockdown in the human colon cancer cell lines Caco2 and HT-29 resulted in an increased side population (SP), enhanced aldehyde dehydrogenase 1 activity, and higher expression of CD133, LGR5, EPCAM, NANOG, SRY (sex-determining region Y)-box 2, KLF2, and TCF4/TCF7L2. Notably, heparanase expression and activity were upregulated in Syndecan-1 depleted cells. This increase was linked to an upregulation of the transcription factor Egr1, which regulates heparanase at the promoter level. Sdc-1 knockdown enhanced sphere formation, cell viability, Matrigel invasiveness, and epithelial-to-mesenchymal transition-related gene expression. Likewise, upregulation of heparanase increased the colon cancer stem cell phenotype based on sphere formation assays and phenotypic marker analysis (Side-population, NANOG, KLF4, NOTCH, Wnt, and TCF4 expression). Sdc-1-depleted HT-29 xenograft growth was increased compared to controls. Decreased Sdc-1 expression was associated with an increased activation of β1-integrins, focal adhesion kinase (FAK), and wingless-type (Wnt) signaling. Pharmacological FAK, Wnt and heparanase inhibition blocked the enhanced stem cell phenotype and invasive growth. Sequential flow cytometric SP enrichment substantially enhanced the stem cell phenotype of Sdc-1-depleted cells, which showed increased resistance to doxorubicin chemotherapy and irradiation. In addition, upregulated expression of heparanase resulted in increased resistance to radiotherapy, whereas high expression of enzymatically inactive heparanase promoted chemoresistance to paclitaxel and cisplatin. In conclusion, Sdc-1 depletion cooperatively enhances expression of heparanase and activation of integrins and FAK, which then generates signals for increased invasiveness and cancer stem cell properties. Our findings provide a new avenue to target a stemness-associated signaling axis as a therapeutic strategy to reduce metastatic spread and cancer recurrence.

लघु संचार

Structural Biology 2019: Nrf2, the key transcription factor that regulates the cellular response to oxidative stress, is intrinsically disordered- Nadun Chanaka Karunatilleke- The University of Western Ontario

Nadun Chanaka Karunatilleke1, Courtney Fast2, Vy Ngo3, Anne Brickenden1, Martin Duennwald3, Lars Konermann1,2, Wing-Yiu Choy1

Receptive oxygen and nitrogen species (ROS, RNS) are continually produced in the body from interior digestion and outside introduction. In ordinary cells, responsive oxidants are created in a controlled way and some fill helpful needs. Oxidants shaped in light of physiological prompts go about as significant flagging particles to direct such procedures as cell division, aggravation, insusceptible capacity, autophagy, and stress reaction. Uncontrolled creation of oxidants brings about oxidative pressure that impedes cell capacities and adds to the improvement of malignancy, incessant illness, and poisonousness (2–5). From prokaryotes to people, responsive oxidants apparently work as significant controllers of both physiological and pathophysiological results.

लघु संचार

Structural Biology 2019: NMR Exploration of The Phage Protein Structure Compendium- Andrei T. Alexandrescu, University of Connecticut

Andrei T. Alexandrescu University of Connecticut, USA

Viruses enclose their genomes in protein shells called capsids, assembled from multiple copies of one or more types of coat proteins. (i) Phage P22 has an icosahedral capsid comprised of 420 copies of a coat protein based on the HK97-fold, which additionally contains a genetically inserted domain (I-domain). The NMR structure of the P22 I-domain has a 6-stranded β-barrel fold, flanked by two long disordered loops called the S and D-loops. The dynamic loops form functionally important interactions within and between the coat proteins. We recently extended NMR studies of the P22 I-domain to the distantly related phages CUS-3 and Sf6, to examine the extent to which the structure and disorder of the I-domain is conserved in these three representatives of divergent phage groups.  While the 6-stranded -barrel fold is conserved, there are considerable differences in secondary structure at the periphery of the conserved fold and in loop dynamics, that relate to variations in surface morphologies between the phages. (ii) To further understand capsid surface properties we studied the phage L encoded decoration protein (Dec). Dec trimers non-covalently bind both phages L and P22, preferentially at icosahedral quasi-three-fold sites. Dec binding stabilizes the capsids against the internal pressure that results from dsDNA genome packaging. The NMR structure of the Dec monomer has a globular segment comprised of an OB-fold structure, followed by a 40-residue disordered tail that folds into a trimeric -helix spike when Dec binds capsids. (iii) P22 phage capsids do not assemble spontaneously but through a nucleated process governed by scaffolding protein (Scaff). The Scaff amino acid sequence encodes an intrinsically disordered protein (IDP), with a C-terminal helix-turn-helix domain that binds coat protein to nucleate capsid assembly. When Scaff is incorporated into P22 procapsids to form a 23 MDa complex, NMR signals from N-terminal portion of the protein persist, indicating this segment retains its flexibility when bound to procapsids. The unstructured character of the N-terminus is likely important for the dissociation and release of Scaff during the genome packaging step, accompanying phage maturation.

संपादकीय नोट

Molecular and Cellular Biochemistry Editorial Note

Deepthi R

I am pleased to introduce Journal of Molecular and Cellular Biochemistry which is an open access Biochemistry journal aiming to provide an online compendium for variations in cellular, Molecular, biochemistry, Molecular cloning, and case reports in Biomolecules, and Metabolism. We have been started in year 2017 Journal of Molecular and Cellular Biochemistry is growing continuously. It is our pleasure to announce that during year 2019, all issues of volume 12 were published online on time and the print issues were also brought out and dispatched within 30 days of publishing the issue online.

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