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2012 | 30 | 3 |
Tytuł artykułu

cDNA cloning of porcine CDH1 and its expression profile in porcine early parthenotes*

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Języki publikacji
EN
Abstrakty
EN
The study aimed at cloning the complete cDNA sequence of porcine CDH1 gene and detecting its expression in different developmental stages of early parthenotes. After cloning the CDH1 gene from porcine oviduct using rapid amplification of cDNA ends (RACE) method, the sequence analysis revealed that porcine CDH1 gene complete cDNA nucleotide sequence amounted to 4283 bp including 2652 bp of open reading frame (ORF), 105 bp of 5’ untranslated region (UTR) and 1526 bp of 3’ UTR. The ORF encoded a deduced protein precursor of 97 kD with 883 amino acid residues. The precursor protein including signal peptide, extracellular region, membrane-spanning region and cytoplasmic region had a single transmembrane structure, and its extracellular region had HAV motif and some Ca2+ binding regions. The porcine CDH1 protein showed high homology with cattle (89%), horse (87%), dog (86%), human (84%), chimpanzee (83%) and mouse (83%) CDH1. The results from RT-PCR and real-time PCR indicated that CDH1 gene could be Expressem in both immature and mature oocytes, as well as early parthenotes (2-, 4-, 8-cell embryos, morula, blastocysts). The data of real-time PCR showed that the expression of CDH1 was the highest at 2-cell parthenogenetic embryos stage, and then it decreased significantly till 8-cell embryos stage; the second increased expression level occurred at morulas stage, and then also showed a diminishing trend in the following developmental stage. This is the first report of cloning and analysing the porcine CDH1 cDNA that provides critical information for further research of its functions in pig embryo development.
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-
Rocznik
Tom
30
Numer
3
Opis fizyczny
p.249-259,fig.,ref.
Twórcy
autor
  • Animal Reproduction Institute, Guangxi University, Nanning, Guangxi 530004, China
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Bibliografia
  • Ao.A., Erickson R.P., 1992 – Injection of Antisense RNA specific for E-cadherin demonstrates that E-cadherin facilitates compaction, the first differentiative step of the mammalian embryo.Antisense Research & Development 2, 153-163.
  • Barcroft L.C., Hay -Schmidt A.., Caveney A.., Gilfoyle E., Overstrom E.W.,Hyttel P., Watson A.J., 1998 – Trophectoderm differentiation in the bovine embryo:characterization of a polarized epithelium. Journal of Reproduction and Fertility 114, 327-339.
  • Dickgiesser N., Bennett P.M., Richmond M.H., 1982 – Penicillinase-producing Neisseria gonorrhoeae: a molecular comparison of 5.3-kb and 7.4-kb beta-lactamase plasmids. The Journal of Bacteriology 151, 1171-1175.
  • Frohman M.A., 1994 – On beyond classic RACE (rapid amplification of cDNA ends). PCR Methods Appl 4: S40-58.
  • Huang X., Madan A.., 1999 – CAP3: A DNA sequence assembly program. Genome Research 9, 868-877.
  • HWANG, K.C., Lee, H.Y., CUI, X.S., KIM, J.H., KIM, N.H. 2005 – Identification of Materna mRNAs in porcine parthenotes at the 2-cell stage: a comparison with the blastocyst stage. Molecular Reproduction and Development 70, 314-323.
  • Hyafil F., Babinet C., Jacob F., 1981 – Cell-cell interactions in early embryogenesis: a molecular approach to the role of calcium. Cell 26, 447-454.
  • Jiang Z., Rothschild M.F., 2007 – Swine genome science comes of age. International Journal of Biological Sciences 3, 129-131.
  • Kawai Y., Yamaguchi T., Yoden T., Hanada M., Miyake M., 2002 – Effect of protein phosphatase inhibitors on the development of mouse embryos: protein phosphorylation is involved in the E-cadherin distribution in mouse two-cell embryos. Biological & Pharmaceutical Bulletin 25: 179-183.
  • Larue L., Ohsugi M., Hirchenhain J., Kemler R., 1994 – E-cadherin null mutant embryos fail to form a trophectoderm epithelium. Proceedings of the National Academy of Sciences of the USA 91, 8263-8267.
  • Livak K.J., Schmittgen T.D., 2001 – Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25, 402-408.
  • Lunney J.K., 2007 – Advances in swine biomedical model genomics. International Journal of Biological Sciences 3: 179-184.
  • Modina S., Leoni G.G., Lodde V., Naitana S., Pirani S., Succu S., Berlinguer F., Luciano , A.M., 2010 – Involvement of E-cadherin in early in vitro development of adult and juvenile sheep embryos. Reproduction, Fertility and Development 22, 468-477.
  • Nagar B., Overduin M., Ikura M., Rini J.M., 1996 – Structural basis of calcium-induced E-cadherin rigidification and dimerization. Nature 380, 360-364.
  • Nganvongpanit K., Muller H., Rings F., Gilles M., Jennen D., Holker M.,Tholen E., Schellander , K., Tesfaye D. 2006 – Targeted suppression of E-cadherin gene expression in bovine preimplantation embryo by RNA interference technology using double-stranded RNA. Molecular Reproduction and Development 73: 153-163.
  • Nose A., Tsuji K., Takeichi M., 1990 – Localization of specificity determining sites in cadherin cell adhesion molecules. Cell 61, 147-155.
  • Nygard A.B., Jorgensen C.B., Cirera S., Fredholm M., 2007 – Selection of reference genes for gene expression studies in pig tissues using SYBR green qPCR. BMC Molecular Biology 8, 67.
  • Overduin M., Tong K.I., Kay C.M., Ikura M., 1996 – 1H, 15N and 13C resonance assignments and monomeric structure of the amino-terminal extracellular domain of epithelial cadherin. Journal of Biomolecular NMR 7, 173-189.
  • Overduin M., Harvey T.S., Bagby S., Tong K.I., Yau P., Takeichi M., Ikura M., 1995 – Solution structure of the epithelial cadherin domain responsible for selective cell adhesion. Science 267, 386-389.
  • Pertz O., Bozic D., Koch A.W., Fauser C., Brancaccio A.., Engel J., 1999 – A New crystal structure, Ca2+ dependence and mutational analysis reveal molecular details of E-cadherin homoassociation. The EMBO Journal 18, 1738-1747.
  • Peyrieras N., Hyafil F., Louvard D., Ploegh H.L., Jacob F., 1983 – Uvomorulin: a nonintegral membrane protein of early mouse embryo. Proceedings of the National Academy of Sciences of the USA 80, 6274-6277.
  • Ringwald M., Schuh R., Vestweber D., Eistetter H., Lottspeich F., Engel J.,Dolz R., Jahnig F., Epplen J., Maye R S., Müller c., Kemler R., 1987 – The structure of cell adhesion molecule uvomorulin. Insights into the molecular mechanism of Ca2+-dependent cell adhesion. The EMBO Journal 6, 3647-3653.
  • Shapiro L., Fannon A.M., Kwong P.D., Thompson A., Lehmann M.S., Grubel G.,Legrand J. F., Als -Nielsen J., Colman D.R., Hendrickson W.A.., 1995 – Structural basis of cell-cell adhesion by cadherins. Nature 374, 327-337.
  • VAN THUAN, N., HARAYAMA, H., MIYAKE, M. 2002 – Characteristics of preimplantational development of porcine parthenogenetic diploids relative to the existence of amino acids in vitro.Biology of Reproduction 67, 1688-1698.
  • Wianny F., Zernicka -Goetz M., 2000 – Specific interference with gene function by doublestranded RNA in early mouse development. Nature Cell Biology 2, 70-75.
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