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Immune RNA and Tumor Immunity*
Published in Edward P. Cohen, A. Arthur Gottlieb, Immune RNA, 2020
In our previous animal experiments, it appeared desirable to administer I-RNA in a medium containing a strong ribonuclease inhibitor (the poly-anion sodium dextran sulfate). However, as the safety of administration of dextran sulfate in man has not been determined as yet, we have not incorporated this ribonuclease inhibitor into our RNA preparations. Perhaps by so doing we might significantly increase the efficacy of I-RNA therapy.
Wei Chang An pill regulates gastrointestinal motility in a bidirectional manner
Published in Pharmaceutical Biology, 2021
Sitong Jia, Lijuan Chai, Jing Zhang, Min Zhang, Lin Li, Yaxin Qi, Yafen Pang, Xi Chen, Nana Fan, Lin Wang, Yujing Wang, Jixiang Song, Yingjie Sun, Yi Wang, Lin Miao, Han Zhang
Total RNA was isolated from rat antrum and duodenum using TRIzol reagent (CWBIO, Beijing, China) following the manufacturer’s protocol. The estimated RNA concentration was obtained by absorbance the value of A260 (ng/mL). The reverse transcription was then performed at 37 °C for 2 h, as described previously (Miao et al. 2019). The 20 μL reaction solution included 1–2 g of RNA, 0.5 mM of deoxy-NTPs, 5 M of random hexamers, 10 mM of dithiothreitol, 200 U Moloney murine leukaemia virus reverse transcriptase and 20 U ribonuclease inhibitor (all from Promega, Madison, WI). Real-time PCR was performed to determine the levels of mRNA for ROCK-1 by Go Tap-qPCR-Master-Mix (Promega, Beijing, China) according to the instructions. The relative gene expression was determined using the comparative CT method and normalized to a housekeeping gene GAPDH. The primers used are listed in Table 3 and were synthesized by Sangon (Shanghai, China).
Combination of podophyllotoxin and rutin modulate radiation-induced alterations of jejunal proteome in mice
Published in International Journal of Radiation Biology, 2020
Sania Bajaj, Syed Imteyaz Alam, Basir Ahmad, Humaira Farooqi, Manju Lata Gupta
Exposure to 9 Gy radiation resulted in upregulation of bimolecular transportation and metabolic pathway related proteins such as alcohol dehydrogenase 6 A (class V), ribonuclease inhibitor, and UMP-CMP kinase in mice jejunum. Retinol-binding protein 2 of the same category upregulated immediately after radiation exposure but decreased significantly at 216 h. It was found upregulated at initial time-points even with G-003M pretreatment but its expression gradually returned to normal at 840 h post-experimentation. Cytoskeleton proteins like tropomyosin alpha-4 chain, tropomyosin alpha-3 chain, gamma-actin, and cofilin-1 were also observed to downregulate after 9 gray IR exposures. Cofilin-1 drastically decreased post 1 h radiation exposure, but tropomyosin alpha chain 3 and 4 showed a gradual decrease till death of the animal. Myosin regulatory light polypeptide 9 (MYL9) increased initially (24 h) but a gradual decrease was observed thereafter to 0.66 ± 0.3-fold post-IR. Radiation mediated decrease in expression of these proteins not just affects the rearrangement of cellular cytoskeleton but also destabilizes their dynamics which severely disbalances cellular homeostasis. The pre-administration of G-003M expressed a positive modulation over these proteins. The tropomyosin proteins and MYL9 revealed a non-significant change in expression even post-IR but cofilin-1 declined initially to 0.57 ± 0.13-fold till 120 h but later enhanced to control level by 840 h.
Eosinophil accumulation predicts response to melanoma treatment with immune checkpoint inhibitors
Published in OncoImmunology, 2020
Sonja C. S. Simon, Xiaoying Hu, Jasper Panten, Mareike Grees, Simon Renders, Daniel Thomas, Rebekka Weber, Torsten J. Schulze, Jochen Utikal, Viktor Umansky
Eosinophils were isolated from the peripheral blood using an Eosinophil Isolation Kit (130-092-010, Miltenyi Biotec) after density gradient centrifugation and red blood cell lysis as previously described. The purity of isolated eosinophils was evaluated by flow cytometry and was around 98%. Isolation of total eosinophil RNA from isolated eosinophils was conducted with Trizol (15596018, Thermo Fisher Scientific), followed by quantification using a NanoDrop Spectrophotometer (ND-2000, Thermo Fisher Scientific). DNase digestion for RNA purification was performed using RQ1 RNase-Free DNase (M6101) and RNasin® Ribonuclease Inhibitor (N2611, both Promega Corporation) in accordance with the manufacturer’s instructions and subsequent precipitation. Quality control of RNA was performed using Agilent RNA 6000 Pico Kit with the Agilent 2100 Bioanalyzer (Agilent Technologies).