메뉴 건너뛰기




Volumn 289, Issue 8, 2014, Pages 4989-4999

Transglutaminase 2-dependent deamidation of glyceraldehyde-3-phosphate dehydrogenase promotes trophoblastic cell fusion

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CHEMICAL REACTIONS;

EID: 84894494824     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.525568     Document Type: Article
Times cited : (17)

References (39)
  • 1
    • 0025057052 scopus 로고
    • Modulators of cyclic AMP metabolism induce syncytiotrophoblast formation in vitro
    • Wice, B., Menton, D., Geuze, H., and Schwartz, A. L. (1990) Modulators of cyclic AMP metabolism induce syncytiotrophoblast formation in vitro. Exp. Cell Res. 186, 306-316
    • (1990) Exp. Cell Res. , vol.186 , pp. 306-316
    • Wice, B.1    Menton, D.2    Geuze, H.3    Schwartz, A.L.4
  • 3
    • 0033935126 scopus 로고    scopus 로고
    • The glial cells missing-1 protein is essential for branching morphogenesis in the chorioallantoic placenta
    • Anson-Cartwright, L., Dawson, K., Holmyard, D., Fisher, S. J., Lazzarini, R. A., and Cross, J. C. (2000) The glial cells missing-1 protein is essential for branching morphogenesis in the chorioallantoic placenta. Nat. Genet. 25, 311-314
    • (2000) Nat. Genet. , vol.25 , pp. 311-314
    • Anson-Cartwright, L.1    Dawson, K.2    Holmyard, D.3    Fisher, S.J.4    Lazzarini, R.A.5    Cross, J.C.6
  • 4
    • 21844455753 scopus 로고    scopus 로고
    • Stimulation ofGCMaand syncytin via cAMP mediated PKA signaling in human trophoblastic cells under normoxic and hypoxic conditions
    • Knerr, I., Schubert, S. W., Wich, C., Amann, K., Aigner, T., Vogler, T., Jung, R., Dötsch, J., Rascher, W., and Hashemolhosseini, S. (2005) Stimulation ofGCMaand syncytin via cAMP mediated PKA signaling in human trophoblastic cells under normoxic and hypoxic conditions. FEBS Lett. 579, 3991-3998
    • (2005) FEBS Lett. , vol.579 , pp. 3991-3998
    • Knerr, I.1    Schubert, S.W.2    Wich, C.3    Amann, K.4    Aigner, T.5    Vogler, T.6    Jung, R.7    Dötsch, J.8    Rascher, W.9    Hashemolhosseini, S.10
  • 5
    • 0347928824 scopus 로고    scopus 로고
    • GCMa regulates the syncytin-mediated trophoblastic fusion
    • Yu, C., Shen, K., Lin, M., Chen, P., Lin, C., Chang, G. D., and Chen, H. (2002) GCMa regulates the syncytin-mediated trophoblastic fusion. J. Biol. Chem. 277, 50062-50068
    • (2002) J. Biol. Chem. , vol.277 , pp. 50062-50068
    • Yu, C.1    Shen, K.2    Lin, M.3    Chen, P.4    Lin, C.5    Chang, G.D.6    Chen, H.7
  • 6
    • 77956126689 scopus 로고    scopus 로고
    • GCM1 regulation of the expression of syncytin 2 and its cognate receptor MFSD2A in human placenta
    • Liang, C. Y., Wang, L. J., Chen, C. P., Chen, L. F., Chen, Y. H., and Chen, H. (2010) GCM1 regulation of the expression of syncytin 2 and its cognate receptor MFSD2A in human placenta. Biol. Reprod. 83, 387-395
    • (2010) Biol. Reprod. , vol.83 , pp. 387-395
    • Liang, C.Y.1    Wang, L.J.2    Chen, C.P.3    Chen, L.F.4    Chen, Y.H.5    Chen, H.6
  • 8
    • 67749122582 scopus 로고    scopus 로고
    • Syncytin-A knockout mice demonstrate the critical role in placentation of a fusogenic, endogenous retrovirus-derived, envelope gene
    • Dupressoir, A., Vernochet, C., Bawa, O., Harper, F., Pierron, G., Opolon, P., and Heidmann, T. (2009) Syncytin-A knockout mice demonstrate the critical role in placentation of a fusogenic, endogenous retrovirus-derived, envelope gene. Proc. Natl. Acad. Sci. U.S.A. 106, 12127-12132
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 12127-12132
    • Dupressoir, A.1    Vernochet, C.2    Bawa, O.3    Harper, F.4    Pierron, G.5    Opolon, P.6    Heidmann, T.7
  • 14
    • 0021112527 scopus 로고
    • Coating cells with colloidal silica for high yield isolation of plasma membrane sheets and identification of transmembrane proteins
    • Chaney, L. K., and Jacobson, B. S. (1983) Coating cells with colloidal silica for high yield isolation of plasma membrane sheets and identification of transmembrane proteins. J. Biol. Chem. 258, 10062-10072
    • (1983) J. Biol. Chem. , vol.258 , pp. 10062-10072
    • Chaney, L.K.1    Jacobson, B.S.2
  • 15
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J. V., and Mann, M. (2006) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1, 2856-2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 19
    • 34848907698 scopus 로고    scopus 로고
    • A role for tissue transglutaminase in stabilization of membrane-cytoskeletal particles shed from the human placenta
    • Robinson, N. J., Baker, P. N., Jones, C. J., and Aplin, J. D. (2007) A role for tissue transglutaminase in stabilization of membrane-cytoskeletal particles shed from the human placenta. Biol. Reprod. 77, 648-657
    • (2007) Biol. Reprod. , vol.77 , pp. 648-657
    • Robinson, N.J.1    Baker, P.N.2    Jones, C.J.3    Aplin, J.D.4
  • 20
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases. Nature's biological glues
    • Griffin, M., Casadio, R., and Bergamini, C. M. (2002) Transglutaminases. Nature's biological glues. Biochem. J. 368, 377-396
    • (2002) Biochem. J. , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 21
    • 84861065569 scopus 로고    scopus 로고
    • Subcellular dynamics of multifunctional protein regulation. Mechanisms of GAPDH intracellular translocation
    • Sirover, M. A. (2012) Subcellular dynamics of multifunctional protein regulation. Mechanisms of GAPDH intracellular translocation. J. Cell Biochem. 113, 2193-2200
    • (2012) J. Cell Biochem. , vol.113 , pp. 2193-2200
    • Sirover, M.A.1
  • 22
    • 39149092676 scopus 로고    scopus 로고
    • Tissue transglutaminase catalyzes the deamidation of glutamines in lens B(2)-and B(3)-crystallins
    • Boros, S., Wilmarth, P. A., Kamps, B., de Jong, W. W., Bloemendal, H., Lampi, K., and Boelens, W. C. (2008) Tissue transglutaminase catalyzes the deamidation of glutamines in lens B(2)-and B(3)-crystallins. Exp. Eye Res. 86, 383-393
    • (2008) Exp. Eye Res. , vol.86 , pp. 383-393
    • Boros, S.1    Wilmarth, P.A.2    Kamps, B.3    De Jong, W.W.4    Bloemendal, H.5    Lampi, K.6    Boelens, W.C.7
  • 23
    • 79953317964 scopus 로고    scopus 로고
    • Tissue transglutaminase-mediated glutamine deamidation of amyloid peptide increases peptide solubility, whereas enzymatic cross-linking and peptide fragmentation may serve as molecular triggers for rapid peptide aggregation
    • Schmid, A. W., Condemi, E., Tuchscherer, G., Chiappe, D., Mutter, M., Vogel, H., Moniatte, M., and Tsybin, Y. O. (2011) Tissue transglutaminase- mediated glutamine deamidation of amyloid peptide increases peptide solubility, whereas enzymatic cross-linking and peptide fragmentation may serve as molecular triggers for rapid peptide aggregation. J. Biol. Chem. 286, 12172-12188
    • (2011) J. Biol. Chem. , vol.286 , pp. 12172-12188
    • Schmid, A.W.1    Condemi, E.2    Tuchscherer, G.3    Chiappe, D.4    Mutter, M.5    Vogel, H.6    Moniatte, M.7    Tsybin, Y.O.8
  • 24
    • 78651227733 scopus 로고    scopus 로고
    • Deamidation and transamidation of substance P by tissue transglutaminase revealed by electron-capture dissociation Fourier transform mass spectrometry
    • Fornelli, L., Schmid, A. W., Grasso, L., Vogel, H., and Tsybin, Y. O. (2011) Deamidation and transamidation of substance P by tissue transglutaminase revealed by electron-capture dissociation Fourier transform mass spectrometry. Chemistry 17, 486-497
    • (2011) Chemistry , vol.17 , pp. 486-497
    • Fornelli, L.1    Schmid, A.W.2    Grasso, L.3    Vogel, H.4    Tsybin, Y.O.5
  • 25
    • 84860410754 scopus 로고    scopus 로고
    • Ionic strength dependence of F-actin and glycolytic enzyme associations. A Brownian dynamics simulations approach
    • Forlemu, N. Y., Njabon, E. N., Carlson, K. L., Schmidt, E. S., Waingeh, V. F., and Thomasson, K. A. (2011) Ionic strength dependence of F-actin and glycolytic enzyme associations. A Brownian dynamics simulations approach. Proteins 79, 2813-2827
    • (2011) Proteins , vol.79 , pp. 2813-2827
    • Forlemu, N.Y.1    Njabon, E.N.2    Carlson, K.L.3    Schmidt, E.S.4    Waingeh, V.F.5    Thomasson, K.A.6
  • 26
    • 0020758755 scopus 로고
    • A porcine brain protein (35 K protein) which bundles microtubules and its identification as glyceraldehyde 3-phosphate dehydrogenase
    • Kumagai, H., and Sakai, H. (1983) A porcine brain protein (35 K protein) which bundles microtubules and its identification as glyceraldehyde 3-phosphate dehydrogenase. J. Biochem. 93, 1259-1269
    • (1983) J. Biochem. , vol.93 , pp. 1259-1269
    • Kumagai, H.1    Sakai, H.2
  • 27
    • 0030449503 scopus 로고    scopus 로고
    • Phosphatidylserine directs differential phosphorylation of actin and glyceraldehyde-3-phosphate dehydrogenase by protein kinase C. Possible implications for regulation of actin polymerization
    • Reiss, N., Oplatka, A., Hermon, J., and Naor, Z. (1996) Phosphatidylserine directs differential phosphorylation of actin and glyceraldehyde-3-phosphate dehydrogenase by protein kinase C. Possible implications for regulation of actin polymerization. Biochem. Mol. Biol. Int. 40, 1191-1200
    • (1996) Biochem. Mol. Biol. Int. , vol.40 , pp. 1191-1200
    • Reiss, N.1    Oplatka, A.2    Hermon, J.3    Naor, Z.4
  • 28
    • 10644272564 scopus 로고    scopus 로고
    • Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and microtubules
    • Andrade, J., Pearce, S. T., Zhao, H., and Barroso, M. (2004) Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and microtubules. Biochem. J. 384, 327-336
    • (2004) Biochem. J. , vol.384 , pp. 327-336
    • Andrade, J.1    Pearce, S.T.2    Zhao, H.3    Barroso, M.4
  • 30
    • 0031053704 scopus 로고    scopus 로고
    • Developmental regulation of tissue transglutaminase during human placentation and expression in neoplastic trophoblast
    • Hager, H., Gliemann, J., Hamilton-Dutoit, S., Ebbesen, P., Koppelhus, U., and Jensen, P. H. (1997) Developmental regulation of tissue transglutaminase during human placentation and expression in neoplastic trophoblast. J. Pathol. 181, 106-110
    • (1997) J. Pathol. , vol.181 , pp. 106-110
    • Hager, H.1    Gliemann, J.2    Hamilton-Dutoit, S.3    Ebbesen, P.4    Koppelhus, U.5    Jensen, P.H.6
  • 32
    • 82755161784 scopus 로고    scopus 로고
    • Protein transamidation by transglutaminase 2 in cells. A disputed Ca2dependent action of a multifunctional protein
    • Király, R., Demény, M., and Fésüs, L. (2011) Protein transamidation by transglutaminase 2 in cells. A disputed Ca2dependent action of a multifunctional protein. FEBS J. 278, 4717-4739
    • (2011) FEBS J. , vol.278 , pp. 4717-4739
    • Király, R.1    Demény, M.2    Fésüs, L.3
  • 34
    • 33751241720 scopus 로고    scopus 로고
    • Epac proteins. Multi-purpose cAMP targets
    • Bos, J. L. (2006) Epac proteins. Multi-purpose cAMP targets. Trends Biochem. Sci. 31, 680-686
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 680-686
    • Bos, J.L.1
  • 35
    • 80052569744 scopus 로고    scopus 로고
    • A novel cyclic AMP/ Epac1/CaMKI signaling cascade promotesGCM1desumoylation and placental cell fusion
    • Chang, C. W., Chang, G. D., and Chen, H. (2011) A novel cyclic AMP/ Epac1/CaMKI signaling cascade promotesGCM1desumoylation and placental cell fusion. Mol. Cell Biol. 31, 3820-3831
    • (2011) Mol. Cell Biol. , vol.31 , pp. 3820-3831
    • Chang, C.W.1    Chang, G.D.2    Chen, H.3
  • 38
    • 62149083814 scopus 로고    scopus 로고
    • Maternal celiac disease autoantibodies bind directly to syncytiotrophoblast and inhibit placental tissue transglutaminase activity
    • Anjum, N., Baker, P. N., Robinson, N. J., and Aplin, J. D. (2009) Maternal celiac disease autoantibodies bind directly to syncytiotrophoblast and inhibit placental tissue transglutaminase activity. Reprod. Biol. Endocrinol. 7, 16
    • (2009) Reprod. Biol. Endocrinol. , vol.7 , pp. 16
    • Anjum, N.1    Baker, P.N.2    Robinson, N.J.3    Aplin, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.