caa a22 4500 39755852X CHVBK 20180308164810.0 cr unu---uuuuu 161202e199611 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021513 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021513 Molecular Cloning of the Xenopus c-met/Hepatocyte Growth Factor Receptor and Its Regional Expression during Early Development [Elektronische Daten] [Shunsuke Aoki, Kuniaki Takahashi, Kunio Matsumoto, Toshikazu Nakamura] Hepatocyte growth factor (HGF), a ligand for c-Met receptor tyrosine kinase, regulates the cell growth, migration and morphogenesis of a wide variety of cells, and plays important roles in organogenesis in embryos as well as regeneration of organs. HGF is structurally conserved in Xenopus laevis, and the Xenopus HGF gene is expressed in neurula and tailbud embryos. In the present work, we cloned complementary DNA for the Xenopus Met/HGF receptor and analyzed its expression during embryogenesis. The open reading frame of Xenopus c-met is 4,125 base pairs long and encodes a putative polypeptide of 1,375 amino acids. The deduced amino acid sequences of the Xenopus and human Met proteins are 63% identical, the tyrosine kinase domains in the intracellular regions showing particular homology, over 90% identity in the amino acid sequences between Xenopus and human. During Xenopus embryogenesis, c-met mRNA was expressed at a high level from the gastrula to the neurula stage, while HGF mRNA expression was seen from the early neurula stage. Whole mount in situ hybridization showed that c-met mRNA was specifically localized in the foregut region, mesenchymal tissue of the tailbud, and neural tissues in neurula embryos. Thus, c-Met is a highly conserved molecule in a wide range of species, as is its ligand, HGF. The HGF-Met system may be involved in early multiple organogenesis in Xenopus embryos. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence c-met nationallicence embryogenesis nationallicence epithelial-mesenchymal interaction nationallicence hepatocyte growth factor nationallicence Xenopus laevis nationallicence Aoki Shunsuke Division of Biochemistry, Department of Oncology, Biomedical Research Center, Osaka University Medical School, Suita, Osaka 565 aut Takahashi Kuniaki Division of Biochemistry, Department of Oncology, Biomedical Research Center, Osaka University Medical School, Suita, Osaka 565 aut Matsumoto Kunio Division of Biochemistry, Department of Oncology, Biomedical Research Center, Osaka University Medical School, Suita, Osaka 565 aut Nakamura Toshikazu Division of Biochemistry, Department of Oncology, Biomedical Research Center, Osaka University Medical School, Suita, Osaka 565 aut The Journal of Biochemistry Oxford University Press 120/5(1996-11), 961-968 0021-924X 120:5<961 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021513 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021513 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Aoki Shunsuke Division of Biochemistry, Department of Oncology, Biomedical Research Center, Osaka University Medical School, Suita, Osaka 565 aut NATIONALLICENCE 700 1- Takahashi Kuniaki Division of Biochemistry, Department of Oncology, Biomedical Research Center, Osaka University Medical School, Suita, Osaka 565 aut NATIONALLICENCE 700 1- Matsumoto Kunio Division of Biochemistry, Department of Oncology, Biomedical Research Center, Osaka University Medical School, Suita, Osaka 565 aut NATIONALLICENCE 700 1- Nakamura Toshikazu Division of Biochemistry, Department of Oncology, Biomedical Research Center, Osaka University Medical School, Suita, Osaka 565 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/5(1996-11), 961-968 0021-924X 120:5<961 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford