Littérature scientifique sur le sujet « Ζ-crystallin »

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Articles de revues sur le sujet "Ζ-crystallin"

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Malik, Ajamaluddin, Hajar Ahmed Almaharfi, Javed Masood Khan, Malik Hisamuddin, Salman Freeh Alamery, Samina Hyder Haq et Mohammad Z. Ahmed. « Protection of ζ-crystallin by α-crystallin under thermal stress ». International Journal of Biological Macromolecules 167 (janvier 2021) : 289–98. http://dx.doi.org/10.1016/j.ijbiomac.2020.11.183.

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Curthoys, Norman P. « ζ-Crystallin : a tale of two cells ». Kidney International 76, no 7 (octobre 2009) : 691–93. http://dx.doi.org/10.1038/ki.2009.227.

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Duhaiman, Ali S. « Kinetic properties of camel lens ζ-crystallin ». International Journal of Biochemistry & ; Cell Biology 28, no 10 (octobre 1996) : 1163–68. http://dx.doi.org/10.1016/1357-2725(96)00048-9.

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Duhaiman, Ali S. « Characterization of ζ-Crystallin Inhibition by Juglone ». Biochemical and Biophysical Research Communications 218, no 3 (janvier 1996) : 648–52. http://dx.doi.org/10.1006/bbrc.1996.0116.

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Schroeder, Jill M., Wenlin Liu et Norman P. Curthoys. « pH-responsive stabilization of glutamate dehydrogenase mRNA in LLC-PK1-F+cells ». American Journal of Physiology-Renal Physiology 285, no 2 (août 2003) : F258—F265. http://dx.doi.org/10.1152/ajprenal.00422.2002.

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During chronic metabolic acidosis, the adaptive increase in rat renal ammoniagenesis is sustained, in part, by increased expression of mitochondrial glutaminase (GA) and glutamate dehydrogenase (GDH) enzymes. The increase in GA activity results from the pH-responsive stabilization of GA mRNA. The 3′-untranslated region (3′-UTR) of GA mRNA contains a direct repeat of an eight-base AU-rich element (ARE) that binds ζ-crystallin/NADPH:quinone reductase (ζ-crystallin) with high affinity and functions as a pH-response element. RNA EMSAs established that ζ-crystallin also binds to the full-length 3′-UTR of GDH mRNA. This region contains four eight-base sequences that are 88% identical to one of the two GA AREs. Direct binding assays and competition studies indicate that the two individual eight-base AREs from GA mRNA and the four individual GDH sequences bind ζ-crystallin with different affinities. Insertion of the 3′-UTR of GDH cDNA into a β-globin expression vector (pβG) produced a chimeric mRNA that was stabilized when LLC-PK1-F+cells were transferred to acidic medium. A pH-responsive stabilization was also observed using a βG construct that contained only the single GDH4 ARE and a destabilizing element from phospho enolpyruvate carboxykinase mRNA. Therefore, during acidosis, the pH-responsive stabilization of GDH mRNA may be accomplished by the same mechanism that affects an increase in GA mRNA.
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Dominova, Irina N., et Valery V. Zhukov. « Mollusc Crystallins : Physical and Chemical Properties and Phylogenetic Analysis ». Diversity 14, no 10 (1 octobre 2022) : 827. http://dx.doi.org/10.3390/d14100827.

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The purpose of the present study was to perform bioinformatic analysis of crystallin diversity in aquatic molluscs based on the sequences in the NCBI Protein database. The objectives were as follows: (1) analysis of some physical and chemical properties of mollusc crystallins, (2) comparison of mollusc crystallins with zebrafish and cubomedusa Tripedalia cystophora crystallins, and (3) determination of the most probable candidates for the role of gastropod eye crystallins. The calculated average GRAVY values revealed that the majority of the seven crystallin groups, except for μ- and ζ-crystallins, were hydrophilic proteins. The predominant predicted secondary structures of the crystallins in most cases were α-helices and coils. The highest values of refractive index increment (dn/dc) were typical for crystallins of aquatic organisms with known lens protein composition (zebrafish, cubomedusa, and octopuses) and for S-crystallin of Pomacea canaliculata. The evolutionary relationships between the studied crystallins, obtained from multiple sequence alignments using Clustal Omega and MUSCLE, and the normalized conservation index, calculated by Mirny, showed that the most conservative proteins were Ω-crystallins but the most diverse were S-crystallins. The phylogenetic analysis of crystallin was generally consistent with modern mollusc taxonomy. Thus, α- and S-, and, possibly, J1A-crystallins, can be assumed to be the most likely candidates for the role of gastropod lens crystallins.
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Bazzi, Mohammad D., Nayyar Rabbani et Ali S. Duhaiman. « Sequential inactivation of ζ-crystallin by o-phthalaldehyde ». Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1597, no 1 (mai 2002) : 67–73. http://dx.doi.org/10.1016/s0167-4838(02)00272-8.

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Sharon-Friling, Ronit, Jill Richardson, Sally Sperbeck, Douglas Lee, Michael Rauchman, Richard Maas, Anand Swaroop et Graeme Wistow. « Lens-Specific Gene Recruitment of ζ-Crystallin through Pax6, Nrl-Maf, and Brain Suppressor Sites ». Molecular and Cellular Biology 18, no 4 (1 avril 1998) : 2067–76. http://dx.doi.org/10.1128/mcb.18.4.2067.

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ABSTRACT ζ-Crystallin is a taxon-specific crystallin, an enzyme which has undergone direct gene recruitment as a structural component of the guinea pig lens through a Pax6-dependent mechanism. Tissue specificity arises through a combination of effects involving three sites in the lens promoter. The Pax6 site (ZPE) itself shows specificity for an isoform of Pax6 preferentially expressed in lens cells. High-level expression of the promoter requires a second site, identical to an αCE2 site or half Maf response element (MARE), adjacent to the Pax6 site. A promoter fragment containing Pax6 and MARE sites gives lens-preferred induction of a heterologous promoter. Complexes binding the MARE in lens nuclear extracts are antigenically related to Nrl, and cotransfection with Nrl elevates ζ-crystallin promoter activity in lens cells. A truncated ζ promoter containing Nrl-MARE and Pax6 sites has a high level of expression in lens cells in transgenic mice but is also active in the brain. Suppression of the promoter in the brain requires sequences between −498 and −385, and a site in this region forms specific complexes in brain extract. A three-level model for lens-specific Pax6-dependent expression and gene recruitment is suggested: (i) binding of a specific isoform of Pax6; (ii) augmentation of expression through binding of Nrl or a related factor; and (iii) suppression of promoter activity in the central nervous system by an upstream negative element in the brain but not in the lens.
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Bazzi, Mohammad D. « ζ-Crystallin displays strong selectivity for salicylic acid over aspirin ». Biochemical and Biophysical Research Communications 293, no 1 (avril 2002) : 440–45. http://dx.doi.org/10.1016/s0006-291x(02)00248-6.

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Simpanya, Mukoma F., Victor R. Leverenz et Frank J. Giblin. « Expression and purification of his-tagged recombinant mouse ζ-crystallin ». Protein Expression and Purification 69, no 2 (février 2010) : 147–52. http://dx.doi.org/10.1016/j.pep.2009.08.001.

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Thèses sur le sujet "Ζ-crystallin"

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LOFFREDO, ROSA. « Impact of acidosis on ζ-crystallin-mediated bcl-2 expression in leukemic cells ». Doctoral thesis, 2014. http://hdl.handle.net/2158/849907.

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The human antiapoptotic bcl-2 gene is over-expressed in various malignancies, including leukemias/lymphomas. Its post-transcriptional regulation is orchestrated by an adenine-uracil rich element (AU-Rich Element, ARE) lying in the 3’-UTR of bcl-2 mRNA which interacts with numerous ARE-binding proteins (AUBPs) in modulating mRNA stability or translation. In 2010, we identified a new bcl-2 mRNA stabilizing AUBP, namely ζ-crystallin, and demonstrated that it contributed to the over-expression of bcl-2 in acute lymphatic leukemia (ALL) cells as a result of its increased binding to the bcl-2 ARE in T cells of ALL patients compared to normal T lymphocytes. Moreover, ζ-crystallin has been previously demonstrated to bind to specific AU-Rich RNA sequences, called pH-response element (pH-RE), lying in the 3’-UTR of some mRNAs whose genes code for proteins involved in the physiological maintenance of acid-base balance in renal cells. Acidosis, mainly consequent to the “Warburg effect”, is a biochemical hallmark of the tumour microenvironment. Associating the above evidences with the recent report that acidosis increased the level of some antiapoptotic proteins, included Bcl-2, by a mechanism involving the acid-sensing G protein-coupled receptor (TDGA8), prompted us to hypothesize that the direct actor of bcl-2 overexpression in acidosis is ζ-crystallin. Here, we report by which mechanisms acute acidosis impacts on ζ-crystallin-mediated bcl-2 over-expression and on cellular resistance to apoptotic stimuli in Jurkat cells. We demonstrated that ζ-crystallin elevated bcl-2 mRNA stability through a mechanisms involving acidosis, which increased its cellular levels. In the effort to unravel the mechanisms involved in the acidosis mediated ζ-crystallin up-regulation, we revealed that acidosis activated the p38 MAPK pathway which in turn could contribute to increase ζ-crystallin expression.
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