Relevant bibliographies by topics / T2/S-ribonuclease

Academic literature on the topic 'T2/S-ribonuclease'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "T2/S-ribonuclease"

1

Diaz-Baena, Mercedes, Elena Delgado-García, Manuel Pineda, Gregorio Galvez-Valdivieso, and Pedro Piedras. "S-Like Ribonuclease T2 Genes Are Induced during Mobilisation of Nutrients in Cotyledons from Common Bean." Agronomy 11, no. 3 (March 6, 2021): 490. http://dx.doi.org/10.3390/agronomy11030490.

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Germination and seedling development are crucial phases in a plant’s life cycle with economical and agronomical implications. The RNA quality in seeds is linked to seed viability, being an important agronomic trait since this leads to a loss in germination efficiency. In addition, RNA can be an important phosphorous reservoir in seeds, affecting the efficiency of the mobilisation of nutrients towards the seedlings. However, knowledge about the physiological function of ribonucleases during germination and seedling development is scarce. We analysed the ribonuclease activities of cotyledons during these processes and the expression of S-like ribonucleases T2. Ribonuclease activity was detected in cotyledons at 1 day after imbibition and the specific activity increased during germination and seedling development, reaching a maximal value at 10 days after imbibition. At this stage, the levels of proteins and RNA in cotyledons were very low. Using in-gel assays, three ribonucleases were detected with apparent molecular masses of 16, 17 and 19 kDa along cotyledon ontogeny. The S-like ribonucleases T2 family consists of four genes in common bean (PvRNS1 to PvRNS4). The expression of PvRNS1, PvRNS2 and PvRNS4 increased in the phase of nutrient mobilisation in cotyledons. The expression of PvRNS1 increased 1000 fold in cotyledons, from 1 to 6 days after imbibition. The suppression of the induction of ribonuclease activity and gene expression in decapitated seedlings suggests that the regulatory signal comes from the developing axes. These results clearly state that S-like ribonucleases T2 are involved in RNA turnover in cotyledons during seedling development.
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2

Jankovic, Dragana, Svenja Steinfelder, John F. Andersen, and Alan Sher. "Helminth secretory product Ribonuclease T2 is a Th2-inducing agent (43.8)." Journal of Immunology 178, no. 1_Supplement (April 1, 2007): S37. http://dx.doi.org/10.4049/jimmunol.178.supp.43.8.

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Abstract Helminth-induced Th2 polarization is associated with down-regulated dendritic cell (DC) function but the underlying molecular mechanism remains elusive due to the poor characterization of helminth molecules with Th2-inducing activity. During Schistosoma mansoni infection egg, but not worm, Ag are a target of a strong Th2 response. Moreover, when injected in naïve mice schistosome eggs or water-soluble egg extract (SEA) have an intrinsic ability to promote development of Th2 cells. Using as a read-out an in vitro model of CD4+ T cell priming with CD11c+ splenic DC we demonstrated that SEA fractions containing molecule(s) with an approximate MW of 30 kD selectively promote Th2 polarization and down-regulate DC functions. Moreover, similar positive fractions were isolated from preparations containing egg excretory/secretory molecules. The N-terminal sequence of the latter identified the S. mansoni enzyme Ribonuclease T2 as the active component and this was further confirmed with the recombinant protein. S. mansoni ribonuclease is the first chemically defined protein with Th2-promoting activity known to act on dendritic cells.
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3

Sassa, H., T. Koba, H. Ikehashi, T. Nishio, Y. Kowyama, and H. Hirano. "Self-incompatibility (S) alleles of the rosaceae encode members of a distinct class of the T2/S ribonuclease superfamily." Molecular and General Genetics MGG 252, no. 1-2 (August 1996): 222. http://dx.doi.org/10.1007/bf02173225.

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4

Sassa, Hidenori, Takeshi Nishio, Yasuo Kowyama, Hisashi Hirano, Takato Koba, and Hiroshi Ikehashi. "Self-incompatibility (S) alleles of the rosaceae encode members of a distinct class of the T2/S ribonuclease superfamily." Molecular and General Genetics MGG 250, no. 5 (March 1996): 547–57. http://dx.doi.org/10.1007/bf02174443.

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5

Steinfelder, Svenja, John F. Andersen, Jennifer L. Cannons, Carl G. Feng, Manju Joshi, Dennis Dwyer, Pat Caspar, Pamela L. Schwartzberg, Alan Sher, and Dragana Jankovic. "The major component in schistosome eggs responsible for conditioning dendritic cells for Th2 polarization is a T2 ribonuclease (omega-1)." Journal of Experimental Medicine 206, no. 8 (July 27, 2009): 1681–90. http://dx.doi.org/10.1084/jem.20082462.

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Schistosoma mansoni eggs contain factors that trigger potent Th2 responses in vivo and condition mouse dendritic cells (DCs) to promote Th2 lymphocyte differentiation. Using an in vitro bystander polarization assay as the readout, we purified and identified the major Th2-inducing component from soluble egg extract (SEA) as the secreted T2 ribonuclease, omega-1. The Th2-promoting activity of omega-1 was found to be sensitive to ribonuclease inhibition and did not require MyD88/TRIF signaling in DCs. In common with unfractioned SEA, the purified native protein suppresses lipopolysaccharide-induced DC activation, but unlike SEA, it fails to trigger interleukin 4 production from basophils. Importantly, omega-1–exposed DCs displayed pronounced cytoskeletal changes and exhibited decreased antigen-dependent conjugate formation with CD4+ T cells. Based on this evidence, we hypothesize that S. mansoni omega-1 acts by limiting the interaction of DCs with CD4+ T lymphocytes, thereby lowering the strength of the activation signal delivered.
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6

Diaz-Baena, Mercedes, Gregorio Galvez-Valdivieso, Elena Delgado-Garcia, Manuel Pineda, and Pedro Piedras. "Nuclease and ribonuclease activities in response to salt stress: Identification of PvRNS3, a T2/S-like ribonuclease induced in common bean radicles by salt stress." Plant Physiology and Biochemistry 147 (February 2020): 235–41. http://dx.doi.org/10.1016/j.plaphy.2019.12.016.

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7

Jankovic, Dragana, John Andersen, Svenja Steinfelder, Jennifer L. Cannons, Pamela L. Schwartzberg, and Alan Sher. "The major Th2 polarizing component in schistosome eggs is a T2 ribonuclease (omega-1) that inhibits dendritic-T cell interaction (133.23)." Journal of Immunology 182, no. 1_Supplement (April 1, 2009): 133.23. http://dx.doi.org/10.4049/jimmunol.182.supp.133.23.

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Abstract Although helminth parasites are the most potent infectious stimuli for the induction of Th2 cells, the identity of their Th2-inducing components has remained elusive. Schistosoma mansoni eggs contain factors that trigger potent Th2 responses in vivo and condition murine dendritic cells (DC) to promote Th2 lymphocyte differentiation. We have performed a classical biochemical purification of the DC-dependent Th2-polarizing molecule(s) in both secreted egg products and in a water-soluble egg extract (SEA) and identified the active Th2-inducing component as a 31 kDa molecule identical to the previously described S. mansoni ribonuclease T2, omega-1. The Th2-promoting activity of this glycoprotein is sensitive to ribonuclease inhibition and does not require MyD88 or TRIF signaling in DC. In common with unfractioned SEA the purified native protein suppresses LPS-induced DC activation, but unlike SEA fails to trigger IL-4 production from basophils. We further demonstrate that SEA as well as purified omega-1 directly affect both DC morphology and the ability of these APC to interact physically with CD4 T lymphocytes. Based on this evidence, we propose that SEA and its omega-1 bioactive component promote Th2 polarization by lowering the strength of the activation signal delivered by DC. This work was supported by the Intramural Research Program of the NIAID.
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8

Hime, Gary, Leanne Prior, and Robert Saint. "The Drosophila melanogaster genome contains a member of the Rh/T2/S-glycoprotein family of ribonuclease-encoding genes." Gene 158, no. 2 (June 1995): 203–7. http://dx.doi.org/10.1016/0378-1119(94)00896-z.

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9

Trubia, M., L. Sessa, and R. Taramelli. "Mammalian Rh/T2/S-Glycoprotein Ribonuclease Family Genes: Cloning of a Human Member Located in a Region of Chromosome 6 (6q27) Frequently Deleted in Human Malignancies." Genomics 42, no. 2 (June 1997): 342–44. http://dx.doi.org/10.1006/geno.1997.4679.

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10

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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