An amino acid-based oral rehydration solution (AA-ORS) enhanced intestinal epithelial proliferation in mice exposed to radiation

Scientific Reports

Volumn 6, Issue , 2016, Pages

  Yin, Liangjie ^a   Gupta, Reshu ^a   Vaught, Lauren ^a   Grosche, Astrid ^a   Okunieff, Paul ^a   Vidyasagar, Sadasivan ^a  

^a UNIVERSITY OF FLORIDA HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ORAL REHYDRATION SOLUTION; SLC5A1 PROTEIN, MOUSE; SLC9A3 PROTEIN, MOUSE; SODIUM GLUCOSE COTRANSPORTER 1; SODIUM PROTON EXCHANGE PROTEIN 3;

ANIMAL; BIOSYNTHESIS; CELL PROLIFERATION; CHEMISTRY; DRUG EFFECT; EXPERIMENTAL RADIATION INJURY; GAMMA RADIATION; GENE EXPRESSION REGULATION; INTESTINE MUCOSA; MALE; METABOLISM; MOUSE; PATHOLOGY; RADIATION RESPONSE;

AMINO ACIDS; ANIMALS; CELL PROLIFERATION; GAMMA RAYS; GENE EXPRESSION REGULATION; INTESTINAL MUCOSA; MALE; MICE; RADIATION INJURIES, EXPERIMENTAL; REHYDRATION SOLUTIONS; SODIUM-GLUCOSE TRANSPORTER 1; SODIUM-HYDROGEN EXCHANGER 3;

EID: 84996587639     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep37220     Document Type: Article

References (62)

1. Booth, C., Tudor, G., Tudor, J., Katz, B. P. & MacVittie, T. J. Acute gastrointestinal syndrome in high-dose irradiated mice. Health Phys 103, 383-399 (2012).
2. Mettler, F. A. Jr. & Voelz, G. L. Major radiation exposure-what to expect and how to respond. N Engl J Med 346, 1554-1561, doi: 10.1056/NEJMra000365 (2002).
3. Dorr, H. & Meineke, V. Acute radiation syndrome caused by accidental radiation exposure-therapeutic principles. BMC Med 9, 126, doi: 10.1186/1741-7015-9-126 (2011).
4. Williams, J. P. et al. Animal models for medical countermeasures to radiation exposure. Radiat Res 173, 557-578, doi: 10.1667/ RR1880.1 (2010).
5. Macia, I. G. M., Lucas Calduch, A. & Lopez, E. C. Radiobiology of the acute radiation syndrome. Rep Pract Oncol Radiother 16, 123-130, doi: 10.1016/j.rpor.2011.06.001 (2011).
6. Dainiak, N. et al. Literature review and global consensus on management of acute radiation syndrome affecting nonhematopoietic organ systems. Disaster Med Public Health Prep 5, 183-201, doi: 10.1001/dmp.2011.73 (2011).
7. Citrin, D. et al. Radioprotectors and mitigators of radiation-induced normal tissue injury. Oncologist 15, 360-371, doi: 10.1634/ theoncologist.2009-S104 (2010).
8. Greenberger, J. S. Radioprotection. In Vivo 23, 323-336 (2009).
9. Yu, J. Intestinal stem cell injury and protection during cancer therapy. Transl Cancer Res 2, 384-396 (2013).
10. Crosnier, C., Stamataki, D. & Lewis, J. Organizing cell renewal in the intestine: stem cells, signals and combinatorial control. Nat Rev Genet 7, 349-359, doi: 10.1038/nrg1840 (2006).
11. Houghton, J. et al. Gastric cancer originating from bone marrow-derived cells. Science 306, 1568-1571, doi: 10.1126/science.1099513 (2004).
12. Li, X. M., Hu, Z., Jorgenson, M. L., Wingard, J. R. & Slayton, W. B. Bone marrow sinusoidal endothelial cells undergo nonapoptotic cell death and are replaced by proliferating sinusoidal cells in situ to maintain the vascular niche following lethal irradiation. Exp Hematol 36, 1143-1156, doi: 10.1016/j.exphem.2008.06.009 (2008).
13. Niu, Y. et al. Intraesophageal MnSOD-plasmid liposome enhances engraftment and self-renewal of bone marrow derived progenitors of esophageal squamous epithelium. Gene Ther 15, 347-356, doi: 10.1038/sj.gt.3303089 (2008).
14. Leibowitz, B. J. et al. Ionizing irradiation induces acute haematopoietic syndrome and gastrointestinal syndrome independently in mice. Nat Commun 5, 3494, doi: 10.1038/ncomms4494 (2014).
15. Barker, N., van Oudenaarden, A. & Clevers, H. Identifying the stem cell of the intestinal crypt: strategies and pitfalls. Cell Stem Cell 11, 452-460, doi: 10.1016/j.stem.2012.09.009 (2012).
16. Cheng, H. & Leblond, C. P. Origin, differentiation and renewal of the four main epithelial cell types in the mouse small intestine. V. Unitarian Theory of the origin of the four epithelial cell types. Am J Anat 141, 537-561 (1974).
17. Potten, C. S., Booth, C. & Pritchard, D. M. The intestinal epithelial stem cell: the mucosal governor. Int J Exp Pathol 78, 219-243 (1997).
18. Karam, S. M. Lineage commitment and maturation of epithelial cells in the gut. Front Biosci 4, D286-D298 (1999).
19. Zhang, K. et al. Radiation decreases murine small intestinal HCO3-secretion. Int J Radiat Biol 87, 878-888, doi: 10.3109/ 09553002.2011.583314 (2011).
20. Yin, L. et al. An amino acid mixture mitigates radiation-induced gastrointestinal toxicity. Health Phys 106, 734-744, doi: 10.1097/ HP.0000000000000117 (2014).
21. Zhang, H., Ameen, N., Melvin, J. E. & Vidyasagar, S. Acute inflammation alters bicarbonate transport in mouse ileum. J Physiol 581, 1221-1233, doi: 10.1113/jphysiol.2007.129262 (2007).
22. Pageot, L. P. et al. Human cell models to study small intestinal functions: recapitulation of the crypt-villus axis. Microsc Res Tech 49, 394-406, doi: 10.1002/(SICI)1097-0029(20000515)49:4< 394::AID-JEMT8> 3.0.CO;2-K (2000).
23. LaPointe, M. S., Sodhi, C., Sahai, A. & Batlle, D. Na+ /H+ exchange activity and NHE-3 expression in renal tubules from the spontaneously hypertensive rat. Kidney Int 62, 157-165, doi: 10.1046/j.1523-1755.2002.00406.x (2002).
24. Thiaville, M. M. et al. MEK signaling is required for phosphorylation of eIF2alpha following amino acid limitation of HepG2 human hepatoma cells. J Biol Chem 283, 10848-10857, doi: 10.1074/jbc.M708320200 (2008).
25. Youle, R. J. & Strasser, A. The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 9, 47-59, doi: 10.1038/nrm2308 (2008).
26. Yamamoto, K. et al. Contribution of Bcl-2, but not Bcl-xL and Bax, to antiapoptotic actions of hepatocyte growth factor in hypoxiaconditioned human endothelial cells. Hypertension 37, 1341-1348 (2001).
27. Potten, C. S. A comprehensive study of the radiobiological response of the murine (BDF1) small intestine. Int J Radiat Biol 58, 925-973, doi: 7AQN1HHQNK5ERATM [pii] (1990).
28. Pritchard, D. M., Potten, C. S., Korsmeyer, S. J., Roberts, S. & Hickman, J. A. Damage-induced apoptosis in intestinal epithelia from bcl-2-null and bax-null mice: investigations of the mechanistic determinants of epithelial apoptosis in vivo. Oncogene 18, 7287-7293, doi: 10.1038/sj.onc.1203150 (1999).
29. Stacey, R. & Green, J. T. Radiation-induced small bowel disease: latest developments and clinical guidance. Ther Adv Chronic Dis 5, 15-29, doi: 10.1177/2040622313510730 (2014).
30. Yin, L. et al. Glucose stimulates calcium-activated chloride secretion in small intestinal cells. Am J Physiol Cell Physiol 306, C687-C696, doi: 10.1152/ajpcell.00174.2013 (2014).
31. Shivdasani, R. A. Radiation redux: reserve intestinal stem cells miss the call to duty. Cell Stem Cell 14, 135-136, doi: 10.1016/j. stem.2014.01.015 (2014).
32. Li, L. & Clevers, H. Coexistence of quiescent and active adult stem cells in mammals. Science 327, 542-545, doi: 10.1126/ science.1180794 (2010).
33. Takeda, N. et al. Interconversion between intestinal stem cell populations in distinct niches. Science 334, 1420-1424, doi: 10.1126/ science.1213214 (2011).
34. Yan, K. S. et al. The intestinal stem cell markers Bmi1 and Lgr5 identify two functionally distinct populations. Proc Natl Acad Sci USA 109, 466-471, doi: 10.1073/pnas.1118857109 (2012).
35. Metcalfe, C., Kljavin, N. M., Ybarra, R. & de Sauvage, F. J. Lgr5+ stem cells are indispensable for radiation-induced intestinal regeneration. Cell Stem Cell 14, 149-159, doi: 10.1016/j.stem.2013.11.008 (2014).
36. Meloche, S. Cell cycle reentry of mammalian fibroblasts is accompanied by the sustained activation of p44mapk and p42mapk isoforms in the G1 phase and their inactivation at the G1/S transition. J Cell Physiol 163, 577-588, doi: 10.1002/jcp.1041630319 (1995).
37. Lu, Z. & Xu, S. ERK1/2 MAP kinases in cell survival and apoptosis. IUBMB Life 58, 621-631, doi: 10.1080/15216540600957438 (2006).
38. Fukuda, M., Gotoh, Y. & Nishida, E. Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase. EMBO J 16, 1901-1908, doi: 10.1093/emboj/16.8.1901 (1997).
39. Reszka, A. A., Seger, R., Diltz, C. D., Krebs, E. G. & Fischer, E. H. Association of mitogen-activated protein kinase with the microtubule cytoskeleton. Proc Natl Acad Sci USA 92, 8881-8885 (1995).
40. Kahan, C., Seuwen, K., Meloche, S. & Pouyssegur, J. Coordinate, biphasic activation of p44 mitogen-activated protein kinase and S6 kinase by growth factors in hamster fibroblasts. Evidence for thrombin-induced signals different from phosphoinositide turnover and adenylylcyclase inhibition. J Biol Chem 267, 13369-13375 (1992).
41. Yamamoto, T. et al. Continuous ERK activation downregulates antiproliferative genes throughout G1 phase to allow cell-cycle progression. Curr Biol 16, 1171-1182, doi: 10.1016/j.cub.2006.04.044 (2006).
42. Sarbassov, D. D., Guertin, D. A., Ali, S. M. & Sabatini, D. M. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307, 1098-1101, doi: 10.1126/science.1106148 (2005).
43. Stephens, L. et al. Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B. Science 279, 710-714 (1998).
44. Adams, P. D. et al. Identification of a cyclin-cdk2 recognition motif present in substrates and p21-like cyclin-dependent kinase inhibitors. Mol Cell Biol 16, 6623-6633 (1996).
45. Ramaswamy, S. et al. Regulation of G1 progression by the PTEN tumor suppressor protein is linked to inhibition of the phosphatidylinositol 3-kinase/Akt pathway. Proc Natl Acad Sci USA 96, 2110-2115 (1999).
46. Kandel, E. S. et al. Activation of Akt/protein kinase B overcomes a G(2)/m cell cycle checkpoint induced by DNA damage. Mol Cell Biol 22, 7831-7841 (2002).
47. Datta, S. R., Brunet, A. & Greenberg, M. E. Cellular survival: a play in three Akts. Genes Dev 13, 2905-2927 (1999).
48. Danial, N. N. & Korsmeyer, S. J. Cell death: critical control points. Cell 116, 205-219 (2004).
49. Cryns, V. & Yuan, J. Proteases to die for. Genes Dev 12, 1551-1570 (1998).
50. Thornberry, N. A. & Lazebnik, Y. Caspases: enemies within. Science 281, 1312-1316 (1998).
51. Ezekwudo, D. et al. Inhibition of expression of anti-apoptotic protein Bcl-2 and induction of cell death in radioresistant human prostate adenocarcinoma cell line (PC-3) by methyl jasmonate. Cancer Lett 270, 277-285, doi: 10.1016/j.canlet.2008.05.022 (2008).
52. Davis, N. M. et al. Deregulation of the EGFR/PI3K/PTEN/Akt/mTORC1 pathway in breast cancer: possibilities for therapeutic intervention. Oncotarget 5, 4603-4650, doi: 10.18632/oncotarget.2209 (2014).
53. Hall, P. A. & Lane, D. P. Tumor suppressors: a developing role for p53? Curr Biol 7, R144-R147 (1997).
54. Donehower, L. A. et al. Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours. Nature 356, 215-221, doi: 10.1038/356215a0 (1992).
55. Fei, P. & El-Deiry, W. S. P53 and radiation responses. Oncogene 22, 5774-5783, doi: 10.1038/sj.onc.1206677 (2003).
56. Komarova, E. A. et al. Dual effect of p53 on radiation sensitivity in vivo: p53 promotes hematopoietic injury, but protects from gastro-intestinal syndrome in mice. Oncogene 23, 3265-3271, doi: 10.1038/sj.onc.1207494 (2004).
57. Leibowitz, B. J. et al. Uncoupling p53 functions in radiation-induced intestinal damage via PUMA and p21. Mol Cancer Res 9, 616-625, doi: 10.1158/1541-7786.MCR-11-0052 (2011).
58. Qiu, W. et al. PUMA regulates intestinal progenitor cell radiosensitivity and gastrointestinal syndrome. Cell Stem Cell 2, 576-583, doi: 10.1016/j.stem.2008.03.009 (2008).
59. Sanzari, J. K., Wambi, C., Lewis-Wambi, J. S. & Kennedy, A. R. Antioxidant dietary supplementation in mice exposed to proton radiation attenuates expression of programmed cell death-associated genes. Radiat Res 175, 650-656, doi: 10.1667/RR2330.1 (2011).
60. Mitchell, M. A. & Levin, R. J. Amino acid absorption in jejunum and ileum in vivo - a kinetic comparison of function on surface area and regional bases. Experientia 37, 265-266 (1981).
61. Tucker, S. L., Withers, H. R., Mason, K. A. & Thames, H. D. Jr. A dose-surviving fraction curve for mouse colonic mucosa. Eur J Cancer Clin Oncol 19, 433-437 (1983).
62. Vidyasagar, S., Barmeyer, C., Geibel, J., Binder, H. J. & Rajendran, V. M. Role of short-chain fatty acids in colonic HCO3-secretion. Am J Physiol Gastrointest Liver Physiol 288, G1217-G1226 (2005).