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. 1995 Oct 1;311(Pt 1):293–297. doi: 10.1042/bj3110293

Molecular cloning of mouse intestinal trefoil factor and its expression during goblet cell changes.

M Tomita 1, H Itoh 1, N Ishikawa 1, A Higa 1, H Ide 1, Y Murakumo 1, H Maruyama 1, Y Koga 1, Y Nawa 1
PMCID: PMC1136151  PMID: 7575467

Abstract

A cDNA encoding mouse intestinal trefoil factor (mITF) was successfully cloned and sequenced from the small intestine of C57BL/6 mouse by using the combination of reverse transcription-PCR and rapid amplification of cDNA ends methods. The gene was, similar to rat and human ITFs, mainly expressed in the small and large intestine. The mITF expression was up-regulated during the recovery phase after depletion of goblet cells in acetic acid-induced colitis. On the other hand, the expression in the jejunum was not altered, while goblet cell hyperplasia was induced by Nippostrongylus brasiliensis infection. These results suggest that the mITF expression did not simply correlate with the number of goblet cells. The mITF may play an important role in the maintenance and repair of mucosal function of the rectum. Additionally, the mITF in the jejunum may play a role in alteration of the physicochemical nature of goblet cell mucins, thereby affecting the establishment of intestinal helminths.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Chinery R., Poulsom R., Rogers L. A., Jeffery R. E., Longcroft J. M., Hanby A. M., Wright N. A. Localization of intestinal trefoil-factor mRNA in rat stomach and intestine by hybridization in situ. Biochem J. 1992 Jul 1;285(Pt 1):5–8. doi: 10.1042/bj2850005. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Dignass A., Lynch-Devaney K., Kindon H., Thim L., Podolsky D. K. Trefoil peptides promote epithelial migration through a transforming growth factor beta-independent pathway. J Clin Invest. 1994 Jul;94(1):376–383. doi: 10.1172/JCI117332. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Fretland D. J., Widomski D. L., Anglin C. P., Walsh R. E., Levin S., Gasiecki A. F., Collins P. W. Mucosal protective activity of prostaglandin analogs in rodent colonic inflammation. Inflammation. 1992 Dec;16(6):623–629. doi: 10.1007/BF00919345. [DOI] [PubMed] [Google Scholar]
  4. Frohman M. A. Rapid amplification of complementary DNA ends for generation of full-length complementary DNAs: thermal RACE. Methods Enzymol. 1993;218:340–356. doi: 10.1016/0076-6879(93)18026-9. [DOI] [PubMed] [Google Scholar]
  5. Gum J. R., Jr, Hicks J. W., Lagace R. E., Byrd J. C., Toribara N. W., Siddiki B., Fearney F. J., Lamport D. T., Kim Y. S. Molecular cloning of rat intestinal mucin. Lack of conservation between mammalian species. J Biol Chem. 1991 Nov 25;266(33):22733–22738. [PubMed] [Google Scholar]
  6. Hauser F., Poulsom R., Chinery R., Rogers L. A., Hanby A. M., Wright N. A., Hoffmann W. hP1.B, a human P-domain peptide homologous with rat intestinal trefoil factor, is expressed also in the ulcer-associated cell lineage and the uterus. Proc Natl Acad Sci U S A. 1993 Aug 1;90(15):6961–6965. doi: 10.1073/pnas.90.15.6961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hoffmann W., Hauser F. The P-domain or trefoil motif: a role in renewal and pathology of mucous epithelia? Trends Biochem Sci. 1993 Jul;18(7):239–243. doi: 10.1016/0968-0004(93)90170-r. [DOI] [PubMed] [Google Scholar]
  8. Ide H., Itoh H., Nawa Y. Sequencing of cDNAs encoding alpha 1-microglobulin/bikunin of Mongolian gerbil and Syrian golden hamster in comparison with man and other species. Biochim Biophys Acta. 1994 Dec 14;1209(2):286–292. doi: 10.1016/0167-4838(94)90198-8. [DOI] [PubMed] [Google Scholar]
  9. Ishikawa N. Histochemical characteristics of the goblet cell mucins and their role in defence mechanisms against Nippostrongylus brasiliensis infection in the small intestine of mice. Parasite Immunol. 1994 Dec;16(12):649–654. doi: 10.1111/j.1365-3024.1994.tb00321.x. [DOI] [PubMed] [Google Scholar]
  10. Ishikawa N., Horii Y., Nawa Y. Immune-mediated alteration of the terminal sugars of goblet cell mucins in the small intestine of Nippostrongylus brasiliensis-infected rats. Immunology. 1993 Feb;78(2):303–307. [PMC free article] [PubMed] [Google Scholar]
  11. Ishikawa N., Horii Y., Nawa Y. Inhibitory effects of concurrently present 'normal' Nippostrongylus brasiliensis worms on expulsion of 'damaged' worms and associated goblet cell changes in rats. Parasite Immunol. 1994 Jun;16(6):329–332. doi: 10.1111/j.1365-3024.1994.tb00357.x. [DOI] [PubMed] [Google Scholar]
  12. Ishikawa N., Horii Y., Nawa Y. Reconstitution by bone marrow grafting of the defective protective capacity at the migratory phase but not at the intestinal phase of Nippostrongylus brasiliensis infection in W/Wv mice. Parasite Immunol. 1994 Apr;16(4):181–186. doi: 10.1111/j.1365-3024.1994.tb00338.x. [DOI] [PubMed] [Google Scholar]
  13. Ishikawa N., Horii Y., Oinuma T., Suganuma T., Nawa Y. Goblet cell mucins as the selective barrier for the intestinal helminths: T-cell-independent alteration of goblet cell mucins by immunologically 'damaged' Nippostrongylus brasiliensis worms and its significance on the challenge infection with homologous and heterologous parasites. Immunology. 1994 Mar;81(3):480–486. [PMC free article] [PubMed] [Google Scholar]
  14. Itoh H., Hattori Y., Sakamoto H., Ishii H., Kishi T., Sasaki H., Yoshida T., Koono M., Sugimura T., Terada M. Preferential alternative splicing in cancer generates a K-sam messenger RNA with higher transforming activity. Cancer Res. 1994 Jun 15;54(12):3237–3241. [PubMed] [Google Scholar]
  15. Itoh H., Ide H., Ishikawa N., Nawa Y. Mast cell protease inhibitor, trypstatin, is a fragment of inter-alpha-trypsin inhibitor light chain. J Biol Chem. 1994 Feb 4;269(5):3818–3822. [PubMed] [Google Scholar]
  16. Itoh H., Ide H., Kataoka H., Tomita M., Yoshihara H., Nawa Y. cDNA sequencing of mouse alpha 1-microglobulin/inter-alpha-trypsin inhibitor light chain and its expression in acute inflammation. J Biochem. 1994 Oct;116(4):767–772. doi: 10.1093/oxfordjournals.jbchem.a124594. [DOI] [PubMed] [Google Scholar]
  17. Lefebvre O., Wolf C., Kédinger M., Chenard M. P., Tomasetto C., Chambon P., Rio M. C. The mouse one P-domain (pS2) and two P-domain (mSP) genes exhibit distinct patterns of expression. J Cell Biol. 1993 Jul;122(1):191–198. doi: 10.1083/jcb.122.1.191. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. McCafferty D. M., Zeitlin I. J. Short chain fatty acid-induced colitis in mice. Int J Tissue React. 1989;11(4):165–168. [PubMed] [Google Scholar]
  19. McLeod A. D., Fedorak R. N., Friend D. R., Tozer T. N., Cui N. A glucocorticoid prodrug facilitates normal mucosal function in rat colitis without adrenal suppression. Gastroenterology. 1994 Feb;106(2):405–413. doi: 10.1016/0016-5085(94)90599-1. [DOI] [PubMed] [Google Scholar]
  20. Miller H. R., Nawa Y. Nippostrongylus brasiliensis: intestinal goblet-cell response in adoptively immunized rats. Exp Parasitol. 1979 Feb;47(1):81–90. doi: 10.1016/0014-4894(79)90010-9. [DOI] [PubMed] [Google Scholar]
  21. Nawa Y., Ishikawa N., Tsuchiya K., Horii Y., Abe T., Khan A. I., Bing-Shi, Itoh H., Ide H., Uchiyama F. Selective effector mechanisms for the expulsion of intestinal helminths. Parasite Immunol. 1994 Jul;16(7):333–338. doi: 10.1111/j.1365-3024.1994.tb00358.x. [DOI] [PubMed] [Google Scholar]
  22. Podolsky D. K., Lynch-Devaney K., Stow J. L., Oates P., Murgue B., DeBeaumont M., Sands B. E., Mahida Y. R. Identification of human intestinal trefoil factor. Goblet cell-specific expression of a peptide targeted for apical secretion. J Biol Chem. 1993 Mar 25;268(9):6694–6702. [PubMed] [Google Scholar]
  23. Poulsom R., Chinery R., Sarraf C., Van Noorden S., Stamp G. W., Lalani E. N., Elia G., Wright N. A. Trefoil peptide gene expression in small intestinal Crohn's disease and dietary adaptation. J Clin Gastroenterol. 1993;17 (Suppl 1):S78–S91. doi: 10.1097/00004836-199312001-00016. [DOI] [PubMed] [Google Scholar]
  24. Poulsom R., Wright N. A. Trefoil peptides: a newly recognized family of epithelial mucin-associated molecules. Am J Physiol. 1993 Aug;265(2 Pt 1):G205–G213. doi: 10.1152/ajpgi.1993.265.2.G205. [DOI] [PubMed] [Google Scholar]
  25. Suemori S., Lynch-Devaney K., Podolsky D. K. Identification and characterization of rat intestinal trefoil factor: tissue- and cell-specific member of the trefoil protein family. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11017–11021. doi: 10.1073/pnas.88.24.11017. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Tomasetto C., Rio M. C., Gautier C., Wolf C., Hareuveni M., Chambon P., Lathe R. hSP, the domain-duplicated homolog of pS2 protein, is co-expressed with pS2 in stomach but not in breast carcinoma. EMBO J. 1990 Feb;9(2):407–414. doi: 10.1002/j.1460-2075.1990.tb08125.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Wright N. A., Poulsom R., Stamp G., Van Noorden S., Sarraf C., Elia G., Ahnen D., Jeffery R., Longcroft J., Pike C. Trefoil peptide gene expression in gastrointestinal epithelial cells in inflammatory bowel disease. Gastroenterology. 1993 Jan;104(1):12–20. doi: 10.1016/0016-5085(93)90830-6. [DOI] [PubMed] [Google Scholar]
  28. Wright N. A. Trefoil peptides and the gut. Gut. 1993 May;34(5):577–579. doi: 10.1136/gut.34.5.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. von Heijne G. How signal sequences maintain cleavage specificity. J Mol Biol. 1984 Feb 25;173(2):243–251. doi: 10.1016/0022-2836(84)90192-x. [DOI] [PubMed] [Google Scholar]

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