Asian-Australasian Journal of Animal Sciences

Asian Australasian Association of Animal Production Societies (아세아태평양축산학회)
권호 표지
DOI QR코드

DOI QR Code

Expression of Cdc25B mRNA in Duodenal Mucosa of Chicken

  • Qin, Junhui (College of Veterinary Medicine, Nanjing Agricultural University) ;
  • Zhang, Hui (College of Veterinary Medicine, Nanjing Agricultural University) ;
  • Bao, Huijun (College of Veterinary Medicine, Nanjing Agricultural University) ;
  • Zhou, Qiang (College of Veterinary Medicine, Nanjing Agricultural University) ;
  • Liu, Yi (College of Veterinary Medicine, Nanjing Agricultural University) ;
  • Xu, Chunsheng (College of Veterinary Medicine, Nanjing Agricultural University) ;
  • Chu, Xiaohong (College of Veterinary Medicine, Nanjing Agricultural University) ;
  • Chen, Qiusheng (College of Veterinary Medicine, Nanjing Agricultural University)
  • Received : 2009.07.16
  • Accepted : 2009.10.08
  • Published : 2010.04.01
Download PDF
⟨ Previous Next ⟩

Abstract

Cdc25B is a mitotic regulator that might act as a starter phosphatase to initiate the positive feedback loop at the entry into mitotic (M) phase. In the present study, distribution of Cdc25B mRNA in duodenal mucosa of the chicken was demonstrated by means of in situ hybridization histochemistry (ISHH) using sense and antisense digoxigenin (DIG)-labeled RNA probes. The results showed that there were many labeled cells distributing in the duodenal mucosa of the adult chicken. Of these labeled cells, 81.60${\pm}$9.63% of Cdc25B mRNA positive cells was distributed in the basilar part and mid-portion of the intestinal gland and 36.21${\pm}$8.81% in the middle and basilar portion of villi of the small intestine of the chicken, respectively. Most of these labeled cells were positive in the regions of the stem cell and proliferation. The signals of ISHH decreased from basilar to upper part in the crypt of Lieberkuhn and weakened in the inferior villi of the duodenum. Moreover, the positive signals were both in the cytoplasm and cell nucleus. However, the labeled cells were negative in both the lamina muscularis mucosae and muscular layer. The results of ISHH suggested the existence of Cdc25B mRNA and vigorous proliferation activities in the duodenal mucosa of adult chicken, replenishing the cells which had sloughed off from the superior part of the villus. Our results provide some molecular evidence for a regular pattern of avian intestinal epitheliosis and functional partition and provide an approach to further study of the locations of Cdc25B in the chicken.

Keywords

References

  1. Bertrand, B., Q. S. Chen, E. Peco and P. Fabienne. 2006. Identification of an unexpected link between the Shh pathway and a G2/M regulator. the phosphatase CDC25B. Dev. Biol. 294:133-147 https://doi.org/10.1016/j.ydbio.2006.02.035
  2. Boudolf, V., D. Inze and L. De Veylder. 2006. What it higher Plants lack a CDC25 phosphatase? Trends Plant Sci. 11:474-479 https://doi.org/10.1016/j.tplants.2006.08.009
  3. Boutros, R., C. Dozier and B. Ducommun. 2006. The when and where of Cdc25 phosphatases. Curr. Opin. Cell Biol. 18:1-7 https://doi.org/10.1016/j.ceb.2005.12.010
  4. Boutros, R., V. Lobjois and B. Ducommun. 2007. CDC25 phosphatases in cancer cells: key players? Good targets? Cancer 7:495-507 https://doi.org/10.1038/nrc2169
  5. Bulavind, V., Y. Higashimoto and J. Popoffi. 2001. Initiation of a G2/M checkpoint after ultraviolet radiation requires P38 kinase. Nature 411- 6833:102-107 https://doi.org/10.1038/35075107
  6. Cheng, L. Z., C. P. Zhong and W. Q. Cai. 2003. Modern histology. Publishing company of Shanghai science technology literature. Shanghai
  7. Claudio, D. 2005. The chick: A great model system commentary becomes even greater. Dev. Cell 8:9-17 https://doi.org/10.1016/j.devcel.2004.11.018
  8. Dunphy, W. G. and A. Kumagai. 1991. The cdc25 protein contains an intrinsic phosphatase activity. Cell 67:189-196 https://doi.org/10.1016/0092-8674(91)90582-J
  9. Lammer, C. and S. Wagerer. 1998. The cdc25B phosphatase is essential for the G2/M phase transition in human cells. J. Cell Sci. 111:2445-2453
  10. Feng, Y. M., J. X. Liu and Q. S. Chen. 2008. Preparation of chicken SP-mRNA probe and its detection in INR by in situ hybridizati on histochem istry. Acta Veterinaria et Zootechnica Sinica 39(1):117-122
  11. Gaberielli, B., C. Desouza and K. Ellem. 1996. Cytoplasmic accumulation of cdc25B phosphatase in mitosis triggers centrosomal microtubule nucleation in HeLa cells. J. Cell Sci. 109:1081-1093
  12. Galaktionov, K. and D. Beach. 1991. Specific activation of CDC25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins. Cell 67:1181-1194 https://doi.org/10.1016/0092-8674(91)90294-9
  13. Gasparotto, D., R. Maestro and S. Piccinin. 1997. Overexpression of CDC25A and CDC25B in head and neck cancers. Cancer Res. 57-12:2366-2368
  14. Gautier, J., M. J. Solomon, R. N. Booher, J. F. Bazan and M. W. Kirschner. 1991. Cdc25 is a specific tyrosine phosphatase that directly activates p34cdc2. Cell 67:197-211 https://doi.org/10.1016/0092-8674(91)90583-K
  15. Gould, K. L. and P. Nurse. 1989. Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis. Nature 342:39-45 https://doi.org/10.1038/342039a0
  16. Hamburger, V. and H. L. Hamilton. 1951. A series of normal stages in thedevelopment of the chick embryo. Dev. Dyn. 195: 23-272
  17. Hortwell, L. H. and M. B. Kastan. 1994. Cell cycle control and cancer. Science 266:1821-1828 https://doi.org/10.1126/science.7997877
  18. Izumi, T. and J. Maller. 1993. Elimination of cdc2 phosphorylation sites in the CDC25 phosphatase blocks initiation of M-phase. Mol. Cell. Biol. 4:1337-1350
  19. Lee, M. S., S. Ogg, M. Xu, L. L. Parker, D. J. Donaghue, J. M. Maller and H. Piwnica-Worms. 1992. Cdc25+ encodes a protein phosphatase that dephosphorylates $\text p34^{cdc2}$. Mol. Biol. Cell 3:73-84
  20. Lindqvist, A., H. Kallstrom and C. Rosenthalk. 2004. Characterisation of Cdc25B localisation and nuclear export during the cell cycle and in response to stress. J. Cell Sci. 117: 4979-4990 https://doi.org/10.1242/jcs.01395
  21. Lindqvist, A., H. Kallstrom and A. Lundgren. 2005. CDC25B cooperates with CDC25A to induce mitosis but has a unique role in activating cyclin B1/Cdk1 at the cent rosome. J. Cell Biol. 171-1: 35-45 https://doi.org/10.1083/jcb.200503066
  22. Ma, Y. T. and H. Qi. 2006. Functions and regulation mechanisms of CDC25 in cell cycle progression and response to cell cycle checkpoint. Journal of Xi'an University of Art s & Science (Nat. Sci. Ed). 9-4
  23. Millar, J. B. A., C. H. McGowan, G. Lenaers, R. Jones and P. Russell. 1991. $\text p80^{cdc25}$ mitotic inducer is the tyrosine phosphatase that activates $\text p34^{cdc2}$ kinase in fission yeast. EMBO J. 10:4301-4309
  24. Mozdziak, P. E., D. Hodgson and J. N. Petitte. 2008. Avian somatic cell chimeras using surrogate eggshell technology. Asian-Aust. J. Anim. Sci. 21:801-806
  25. Nagata, A., M. Igarashi and S. Jinno. 1991. An additional homolog of the fissonyeast CDC25 gene occurs in humans and is highly expressed in some cancer cells. New Biol. 3:959-968
  26. Nisson, I. and I. Hoffmann. 2000. Cell cycle regulation by the Cdc25 phosphatase family. Prog. Cell Cycle Res. 4:107-114
  27. Okazaki, K. 1996. Isolation of a cDNA encoding the xenopus homologue of mammalian CDC25A that can induce meiotic maturation of oocytes. Gene 178:111-114 https://doi.org/10.1016/0378-1119(96)00344-7
  28. Russell, P. and P. Nurse. 1986. Cdc25 function as an inducer of the mitotic control of fission yeast. Cell 45:145-153 https://doi.org/10.1016/0092-8674(86)90546-5
  29. Sadhu, K., S. Reed and H. Richardson. 1990. Human homolog of fission yeast CDC25 mitotic inducer is predominantly expressed in G2. Proc. Natl. Acad. Sci. USA. 87:5139-5143 https://doi.org/10.1073/pnas.87.13.5139
  30. Strausfield, U., J. C. Labbe, D. Fesquet, J. C. Caradore, A. Picard, K. Sadhu, P. Russell and M. Doree. 1991. Dephosphorylation and activation of a $\text p34^{cdc2}$/cyclin B complex in vitro by human CDC25 protein. Nature 351:242-245 https://doi.org/10.1038/351242a0
  31. Su, B. Y., W. Q. Cai and C. G. Zhang. 1998. Expression of nov in spinal cord of vertebrates. Chin. J. Neurosci. 14-3:237-241
  32. Uchidas, Ohtsubom and Shimuram. 2004. Nuclear export signal in CDC25B. Biochem. Biophys. Res. Commun. 316:226-232 https://doi.org/10.1016/j.bbrc.2004.02.039
  33. Wickramasinghe, D., S. Becker and P. Donovan. 1995. Two CDC25 homologues are differentially expressed during mouse. Dev. 121:2047-2056
  34. Young, W., T. Bonner and M. Brann. 1986. Mesencephalic dopamine neurons regulate the expression of neuropeptide mRNAs in the rat forebrain. Proc. Natl. Acad. Sci. USA. 83:9827-9831 https://doi.org/10.1073/pnas.83.24.9827
  35. Zai, D. Z. and Q. Huang. 2006. Study of cdc2 and tumorigenesis in malignant tumor. Cancer 26-5