Stimulation by glutamine and proline of HGF production in hepatic stellate cells

Biochemical and Biophysical Research Communications

Volumn 363, Issue 4, 2007, Pages 978-982

  Nishikawa, Takako ^a   Tomiya, Tomoaki ^a   Ohtomo, Natsuko ^a   Inoue, Yukiko ^a   Ikeda, Hitoshi ^b   Tejima, Kazuaki ^b   Watanabe, Naoko ^a   Tanoue, Yasushi ^a   Omata, Masao ^a   Fujiwara, Kenji ^c  

^a UNIVERSITY OF TOKYO   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c YOKOHAMA ROSAI HOSPITAL   (Japan)

Author keywords

Eukaryotic initiation factor 4E binding protein 1; Glutamine; Hepatic stellate cells; Hepatocyte growth factor; Mammalian target of rapamycin; p70 S6 kinase; Proline

Indexed keywords

GLUTAMINE; INITIATION FACTOR 4E BINDING PROTEIN 1; LEUCINE; MAMMALIAN TARGET OF RAPAMYCIN; PROLINE; S6 KINASE; SCATTER FACTOR;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CONTROLLED STUDY; LIVER CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; RAT; STELLATE CELL; WESTERN BLOTTING;

ANIMALS; CARRIER PROTEINS; CELL LINE; CELL SEPARATION; CULTURE MEDIA; GLUTAMINE; HEPATOCYTE GROWTH FACTOR; HEPATOCYTES; MALE; PHOSPHOPROTEINS; PHOSPHORYLATION; PROLINE; RATS; RATS, SPRAGUE-DAWLEY; RIBOSOMAL PROTEIN S6 KINASES, 70-KDA;

EUKARYOTA; MAMMALIA; RATTUS;

EID: 35148821126     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.09.082     Document Type: Article

References (46)

1. Ichihara A. BCA, HGF, and proteasomes. Biochem. Biophys. Res. Commun. 266 (1999) 647-651
2. Zarnegar R., and Michalopoulos G.K. The many faces of hepatocyte growth factor: from hepatopoiesis to hematopoiesis. J. Cell. Biol. 129 (1995) 1177-1180
3. Matsumoto K., and Nakamura T. Hepatocyte growth factor (HGF) as a tissue organizer for organogenesis and regeneration. Biochem. Biophys. Res. Commun. 239 (1997) 639-644
4. Michalopoulos G.K., and DeFrances M.C. Liver regeneration. Science 276 (1997) 60-66
5. Tsubouchi H. Hepatocyte growth factor for liver disease. Hepatology 30 (1999) 333-334
6. Funakoshi H., and Nakamura T. Hepatocyte growth factor: from diagnosis to clinical applications. Clin. Chim. Acta 327 (2003) 1-23
7. Ware L.B., and Matthay M.A. Keratinocyte and hepatocyte growth factors in the lung: roles in lung development, inflammation, and repair. Am. J. Physiol. 282 (2002) L924-L940
8. Ishiki Y., Ohnishi H., Muto Y., Matsumoto K., and Nakamura T. Direct evidence that hepatocyte growth factor is a hepatotrophic factor for liver regeneration and has a potent antihepatitis effect in vivo. Hepatology 16 (1992) 1227-1235
9. Fujiwara K., Nagoshi S., Ohno A., Hirata K., Ohta Y., Mochida S., Tomiya T., Higashio K., and Kurokawa K. Stimulation of liver growth by exogenous human hepatocyte growth factor in normal and partially hepatectomized rats. Hepatology 18 (1993) 1443-1449
10. Yamaoka M., Hirata K., Ogata I., Tomiya T., Nagoshi S., Mochida S., and Fujiwara K. Enhancement of albumin production by hepatocyte growth factor in rat hepatocytes: distinction in mode of action from stimulation of DNA synthesis. Liver 18 (1998) 52-59
11. Reeds P.J., and Biolo G. Non-protein roles of amino acids: an emerging aspect of nutrient requirements. Curr. Opin. Clin. Nutr. Metab. Care 5 (2002) 43-45
12. Nelsen C.J., Rickheim D.G., Tucker M.M., McKenzie T.J., Hansen L.K., Pestell R.G., and Albrecht J.H. Amino acids regulate hepatocyte proliferation through modulation of cyclin D1 expression. J. Biol. Chem. 278 (2003) 25853-25858
13. Hutson S.M., and Harris R.A. Symposium: Leucine as a nutritional signal: introduction. J. Nutr. 131 (2001) 839-840
14. Gautsch T.A., Anthony J.C., Kimball S.R., Paul G.L., Layman D.K., and Jefferson L.S. Availability of eIF4E regulates skeletal muscle protein synthesis during recovery from exercise. Am. J. Physiol. 274 (1998) C406-C414
15. Harris R.A., Kobayashi R., Murakami T., and Shimomura Y. Regulation of branched-chain α-keto acid dehydrogenase kinase expression in rat liver. J. Nutr. 131 (2001) 841S-845S.19
16. May M.E., and Buse M.G. Effects of branched-chain amino acids on protein turnover. Diabetes Metab. Rev. 5 (1989) 227-245
17. Louard R.J., Barrett E.J., and Gelfand R.A. Overnight branched-chain amino acid infusion causes sustained suppression of muscle proteolysis. Metabolism 44 (1995) 424-429
18. Peyrollier K., Hajduch E., Blair A.S., Hyde R., and Hundal H.S. l-Leucine availability regulates phosphatidylinositol 3-kinase, p70 S6 kinase and glycogen synthase kinase-3 activity in L6 muscle cells: evidence for the involvement of the mammalian target of rapamycin (mTOR) pathway in the l-leucine-induced up-regulation of System A amino acid transport. Biochem. J. 350 (2000) 361-368
19. Shigemitsu K., Tsujishita Y., Miyake H., Hidayat S., Tanaka N., Hara K., and Yonezawa K. Structural requirement of leucine for activation of p70 S6 kinase. FEBS Lett. 447 (1999) 303-306
20. Xu G., Kwon G., Marshall C.A., Lin T.A., Lawrence Jr. J.C., and McDaniel M.L. Branched-chain amino acids are essential in the regulation of PHAS-I and p70 S6 kinase by pancreatic beta-cells. A possible role in protein translation and mitogenic signaling. J. Biol. Chem. 273 (1998) 28178-28184
21. Kimball S.R., and Jefferson L.S. Regulation of global and specific mRNA translation by oral administration of branched-chain amino acids. Biochem. Biophys. Res. Commun. 313 (2004) 423-427
22. Proud C.G. mTOR-mediated regulation of translation factors by amino acids. Biochem. Biophys. Res. Commun. 313 (2004) 429-436
23. Ijichi C., Matsumura T., Tsuji T., and Eto Y. Branched-chain amino acids promote albumin synthesis in rat primary hepatocytes through the mTOR signal transduction system. Biochem. Biophys. Res. Commun. 303 (2003) 59-64
24. Roh C., Han J., Tzatsos A., and Kandror K.V. Nutrient-sensing mTOR-mediated pathway regulates leptin production in isolated rat adipocytes. Am. J. Physiol. Endocrinol. Metab. 284 (2003) E322-E330
25. Anthony J.C., Anthony T.G., Kimball S.R., and Jefferson L.S. Signaling pathways involved in translational control of protein synthesis in skeletal muscle by leucine. J. Nutr. 131 (2001) 856S-860S
26. Reiter A.K., Anthony T.G., Anthony J.C., Jefferson L.S., and Kimball S.R. The mTOR signaling pathway mediates control of ribosomal protein mRNA translation in rat liver. Int. J. Biochem. Cell. Biol. 36 (2004) 2169-2179
27. Lynch C.J., Patson B.J., Anthony J., Vaval A., Jefferson L.S., and Vary T.C. Leucine is a direct-acting nutrient signal that regulates protein synthesis in adipose tissue. Am. J. Physiol. Endocrinol. Metab. 283 (2002) E503-E513
28. Tomiya T., Inoue Y., Yanase M., Arai M., Ikeda H., Tejima K., Nagashima K., Nishikawa T., and Fujiwara K. Leucine stimulates the secretion of hepatocyte growth factor by hepatic stellate cells. Biochem. Biophys. Res. Commun. 297 (2002) 1108-1111
29. Tomiya T., Nishikawa T., Inoue Y., Ohtomo N., Ikeda H., Tejima K., Watanabe N., Tanoue Y., Omata M., and Fujiwara K. Leucine stimulates HGF production by hepatic stellate cells through mTOR pathway. Biochem. Biophys. Res. Commun. 358 (2007) 176-180
30. Tomiya T., Inoue Y., Yanase M., Arai M., Ikeda H., Tejima K., Nagashima K., Nishikawa T., Watanabe N., Omata M., and Fujiwara K. Treatment with leucine stimulates the production of hepatocyte growth factor in vivo. Biochem. Biophys. Res. Commun. 322 (2004) 772-777
31. Greenwel P., Schwartz M., Rosas M., Peyrol S., Grimaud J.A., and Rojkind M. Characterization of fat-storing cell lines derived from normal and CCl4-cirrhotic livers. Differences in the production of interleukin-6. Lab. Invest. 65 (1991) 644-653
32. Greenwel P., Rubin J., Schwartz M., Hertzberg E.L., and Rojkind M. Liver fat-storing cell clones obtained from a CCl4-cirrhotic rat are heterogeneous with regard to proliferation, expression of extracellular matrix components, interleukin-6, and connexin 43. Lab. Invest. 69 (1993) 210-216
33. Yamada A., Matsumoto K., Iwanari H., Sekiguchi K., Kawata S., Matsuzawa Y., and Nakamura T. Rapid and sensitive enzyme-linked immunosorbent assay for measurement of HGF in rat and human tissues. Biomed. Res. 16 (1995) 105-114
34. Tomiya T., Ogata I., and Fujiwara K. Transforming growth factor alpha levels in liver and blood correlate better than hepatocyte growth factor with hepatocyte proliferation during liver regeneration. Am. J. Pathol. 153 (1998) 955-961
35. Matsumura T., Morinaga Y., Fujitani S., Takehana K., Nishitani S., and Sonaka I. Oral administration of branched-chain amino acids activates the mTOR signal in cirrhotic rat liver. Hepatol. Res. 33 (2005) 27-32
36. Proud C.G. Regulation of mammalian translation factors by nutrients. Eur. J. Biochem. 269 (2002) 5338-5349
37. Fingar D.C., and Blenis J. Target of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression. Oncogene 23 (2004) 3151-3171
38. Rowinsky E.K. Targeting the molecular target of rapamycin (mTOR). Curr. Opin. Oncol. 16 (2004) 564-575
39. Gleason C.E., Lu D., Witters L.A., Newgard C.B., and Birnbaum M.J. The role of AMPK and mTOR in nutrient sensing in pancreatic beta-cells. J. Biol. Chem. 282 (2007) 10341-10351
40. Watatani Y., Kimura N., Shimizu Y.I., Akiyama I., Tonaki D., Hirose H., Takahashi S., and Takahashi Y. Amino acid limitation induces expression of ATF5 mRNA at the post-transcriptional level. Life Sci. 80 (2007) 879-885
41. Fumarola C., La Monica S., and Guidotti G.G. Amino acid signaling through the mammalian target of rapamycin (mTOR) pathway: role of glutamine and of cell shrinkage. J. Cell. Physiol. 204 (2005) 155-165
42. Nakajo T., Yamatsuji T., Ban H., Shigemitsu K., Haisa M., Motoki T., Noma K., Nobuhisa T., Matsuoka J., Gunduz M., Yonezawa K., Tanaka N., and Naomoto Y. Glutamine is a key regulator for amino acid-controlled cell growth through the mTOR signaling pathway in rat intestinal epithelial cells. Biochem. Biophys. Res. Commun. 326 (2005) 174-180
43. Xia Y., Wen H.Y., Young M.E., Guthrie P.H., Taegtmeyer H., and Kellems R.E. Mammalian target of rapamycin and protein kinase A signaling mediate the cardiac transcriptional response to glutamine. J. Biol. Chem. 278 (2003) 13143-13150
44. Kadowaki M., and Kanazawa T. Amino acids as regulators of proteolysis. J. Nutr. 133 (2003) 2052S-2056S
45. Hanauske-Abel H.M. Fibrosis: representative molecular elements, a basic concept, and a emerging targets for suppressive treatment. In: Zakim D., and Boyer T.D. (Eds). Hepatology, a Text Book of Liver Disease (1996), W.B. Saunders, Philadelphia 465-505
46. Nishitani S., Matsumura T., Fujitani S., Sonaka I., Miura Y., and Yagasaki K. Leucine promotes glucose uptake in skeletal muscles of rats. Biochem. Biophys. Res. Commun. 299 (2002) 693-696