메뉴 건너뛰기




Volumn 13, Issue 3, 2006, Pages 323-331

Lipoprotein p37 from Mycoplasma hyorhinis inhibiting mammalian cell adhesion

Author keywords

Cell adhesion; Golgi apparatus; Mycoplasma hyorhinis; p37 protein

Indexed keywords

BETA ACTIN; BETA1 INTEGRIN; INTERCELLULAR ADHESION MOLECULE 1; LIPOPROTEIN; PROTEIN P37;

EID: 33646549928     PISSN: 10217770     EISSN: 14230127     Source Type: Journal    
DOI: 10.1007/s11373-005-9045-7     Document Type: Article
Times cited : (12)

References (31)
  • 1
    • 4644299038 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae and Legionella pneumophila in community-acquired lower respiratory tract infections among hospitalized children: Diagnosis by real time PCR
    • Maltezou H.C., La-Scola B., Astra H., Constantopoulou I., Vlahou V., Kafetzis D.A., Constantopoulos A.G. and Raoult D., Mycoplasma pneumoniae and Legionella pneumophila in community-acquired lower respiratory tract infections among hospitalized children: diagnosis by real time PCR. Scand. J. Infect. Dis. 36: 639-642, 2004.
    • (2004) Scand. J. Infect. Dis. , vol.36 , pp. 639-642
    • Maltezou, H.C.1    La-Scola, B.2    Astra, H.3    Constantopoulou, I.4    Vlahou, V.5    Kafetzis, D.A.6    Constantopoulos, A.G.7    Raoult, D.8
  • 2
    • 3242734841 scopus 로고    scopus 로고
    • Unusual manifestations of infections due to Mycoplasma pneumoniae in children
    • Timitilli A., Di Rocco M., Nattero G., Tacchella A. and Giacchino R., Unusual manifestations of infections due to Mycoplasma pneumoniae in children. Infez. Med. 12: 113-117, 2004.
    • (2004) Infez. Med. , vol.12 , pp. 113-117
    • Timitilli, A.1    Di Rocco, M.2    Nattero, G.3    Tacchella, A.4    Giacchino, R.5
  • 3
    • 12744259897 scopus 로고    scopus 로고
    • Detection of Mycoplasma genitalium in urogenital specimens by real-time PCR and by conventional PCR assay
    • Jurstrand M., Jensen J.S., Fredlund H., Falk L. and Molling P., Detection of Mycoplasma genitalium in urogenital specimens by real-time PCR and by conventional PCR assay. J. Med. Microbiol. 54: 23-29, 2005.
    • (2005) J. Med. Microbiol. , vol.54 , pp. 23-29
    • Jurstrand, M.1    Jensen, J.S.2    Fredlund, H.3    Falk, L.4    Molling, P.5
  • 4
    • 0024198510 scopus 로고
    • A Mycoplasma high-affinity transport system and the in vitro invasiveness of mouse sarcoma cells
    • Dudler R., Schmidhauser C., Parish R.W., Wettenhall R.E. and Schmidt T., A Mycoplasma high-affinity transport system and the in vitro invasiveness of mouse sarcoma cells. The EMBO J. 7: 3963-3970, 1988.
    • (1988) The EMBO J. , vol.7 , pp. 3963-3970
    • Dudler, R.1    Schmidhauser, C.2    Parish, R.W.3    Wettenhall, R.E.4    Schmidt, T.5
  • 5
    • 0033508049 scopus 로고    scopus 로고
    • Mycoplasma1 infections prevent apoptosis and induce malignant trans-formation of interleukin-3-dependent 32D hematopoietic cells
    • Feng S.H., Tsai S., Rodriguez J. and Lo S.C., Mycoplasma1 infections prevent apoptosis and induce malignant trans-formation of interleukin-3- dependent 32D hematopoietic cells. Mol. Cell. Biol. 19: 7995-8002, 1999.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7995-8002
    • Feng, S.H.1    Tsai, S.2    Rodriguez, J.3    Lo, S.C.4
  • 7
    • 0025240119 scopus 로고
    • A mycoplasma1 protein influences tumor cell invasiveness and contact inhibition in vitro
    • Schmidhauser C., Dudler R., Schmidt T. and Parish R.W., A mycoplasma1 protein influences tumor cell invasiveness and contact inhibition in vitro. J. Cell Sci. 95: 499-506, 1990.
    • (1990) J. Cell Sci. , vol.95 , pp. 499-506
    • Schmidhauser, C.1    Dudler, R.2    Schmidt, T.3    Parish, R.W.4
  • 8
    • 0028786848 scopus 로고
    • Mycoplasmas and oncogenesis: Persistent infection and multistage malignant transformation
    • USA
    • Tsai S., Wear D.J., Shih J.W. and Lo S.C., Mycoplasmas and oncogenesis: persistent infection and multistage malignant transformation. Proc. Natl. Acad. Sci. USA 92: 10197-10201, 1995.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 10197-10201
    • Tsai, S.1    Wear, D.J.2    Shih, J.W.3    Lo, S.C.4
  • 9
    • 4344704061 scopus 로고    scopus 로고
    • Is gastric cancer preventable?
    • Correa P., Is gastric cancer preventable?. Gut 53: 1217-1219, 2004.
    • (2004) Gut , vol.53 , pp. 1217-1219
    • Correa, P.1
  • 10
    • 4344578188 scopus 로고    scopus 로고
    • Helicobacter pylori and gastric diseases: A dangerous association
    • De Luca A. and Iaquinto G., Helicobacter pylori and gastric diseases: a dangerous association. Cancer Lett. 213: 1-10, 2004.
    • (2004) Cancer Lett. , vol.213 , pp. 1-10
    • De Luca, A.1    Iaquinto, G.2
  • 13
    • 0025254311 scopus 로고
    • Bovine beta 1, 4-galactosyltransferase: Two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains. In vitro translation experiments demonstrate that both the short and the long forms of the enzyme are type II membrane-bound glycoproteins
    • Russo R.N., Shaper N.L. and Shaper J.H., Bovine beta 1, 4-galactosyltransferase: two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains. In vitro translation experiments demonstrate that both the short and the long forms of the enzyme are type II membrane-bound glycoproteins. J. Biol. Chem. 265: 3324-3331, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3324-3331
    • Russo, R.N.1    Shaper, N.L.2    Shaper, J.H.3
  • 16
    • 0032517780 scopus 로고    scopus 로고
    • Role of xklp3, a subunit of the Xenopus kinesin II heterotrimeric complex, in membrane transport between the endoplasmic reticulum and the Golgi apparatus
    • Le Bot N., Antony C., White J., Karsenti E. and Vernos I., Role of xklp3, a subunit of the Xenopus kinesin II heterotrimeric complex, in membrane transport between the endoplasmic reticulum and the Golgi apparatus. J. Cell Biol. 143: 1559-1573, 1998.
    • (1998) J. Cell Biol. , vol.143 , pp. 1559-1573
    • Le Bot, N.1    Antony, C.2    White, J.3    Karsenti, E.4    Vernos, I.5
  • 17
  • 18
    • 4344687315 scopus 로고    scopus 로고
    • ICAM-1 supports adhesion of human small-cell lung carcinoma to endothelial cells
    • Finzel A.H., Reininger A.J., Bode P.A. and Wurzinger L.J., ICAM-1 supports adhesion of human small-cell lung carcinoma to endothelial cells. Clin. Exp. Metastasis. 21: 185-189, 2004.
    • (2004) Clin. Exp. Metastasis , vol.21 , pp. 185-189
    • Finzel, A.H.1    Reininger, A.J.2    Bode, P.A.3    Wurzinger, L.J.4
  • 20
    • 1842530955 scopus 로고    scopus 로고
    • Butyrate inhibits cytokine-induced VCAM-1 and ICAM-1 expression in cultured endothelial cells: The role of NF-kappa B and PPAR alpha
    • Zapolska-Downar D., Siennicka A., Kaczmarczyk M., Kolodziej B. and Naruszewicz M., Butyrate inhibits cytokine-induced VCAM-1 and ICAM-1 expression in cultured endothelial cells: the role of NF-kappa B and PPAR alpha. J. Nutr. Biochem. 15: 220-228, 2004.
    • (2004) J. Nutr. Biochem. , vol.15 , pp. 220-228
    • Zapolska-Downar, D.1    Siennicka, A.2    Kaczmarczyk, M.3    Kolodziej, B.4    Naruszewicz, M.5
  • 21
    • 2942704035 scopus 로고    scopus 로고
    • Intercellular adhesion molecule 1 deficiency leads to impaired recruitment of T lymphocytes and enhanced host susceptibility to infection with Trypanosoma cruzi
    • Michailowsky V., Celes M.R., Marino A.P., Silva A.A., Vieira L.Q., Rossi M.A., Gazzinelli R.T., Lannes-Vieira J. and Silva J.S., Intercellular adhesion molecule 1 deficiency leads to impaired recruitment of T lymphocytes and enhanced host susceptibility to infection with Trypanosoma cruzi. J. Immunol. 173: 463-470, 2004.
    • (2004) J. Immunol. , vol.173 , pp. 463-470
    • Michailowsky, V.1    Celes, M.R.2    Marino, A.P.3    Silva, A.A.4    Vieira, L.Q.5    Rossi, M.A.6    Gazzinelli, R.T.7    Lannes-Vieira, J.8    Silva, J.S.9
  • 23
    • 12344285901 scopus 로고    scopus 로고
    • Negative regulation of EGFR signaling through integrin-alpha 1 beta 1-mediated activation of protein tyrosine phosphatase TCPTP
    • Mattila E., Pellinen T., Nevo J., Vuoriluoto K., Arjonen A. and Ivaska J., Negative regulation of EGFR signaling through integrin-alpha 1 beta 1-mediated activation of protein tyrosine phosphatase TCPTP. Nat. Cell Biol. 7: 78-85, 2005.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 78-85
    • Mattila, E.1    Pellinen, T.2    Nevo, J.3    Vuoriluoto, K.4    Arjonen, A.5    Ivaska, J.6
  • 24
    • 4644354738 scopus 로고    scopus 로고
    • Inhibition of integrin-mediated adhesion and signaling disrupts retinal development
    • Li M. and Sakaguchi D.S., Inhibition of integrin-mediated adhesion and signaling disrupts retinal development. Dev. Biol. 275: 202-214, 2004.
    • (2004) Dev. Biol. , vol.275 , pp. 202-214
    • Li, M.1    Sakaguchi, D.S.2
  • 26
    • 7944224785 scopus 로고    scopus 로고
    • Actin's many actions start at the genes
    • Franke W.W., Actin's many actions start at the genes. Nat. Cell Biol. 6: 1013-1014, 2004.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1013-1014
    • Franke, W.W.1
  • 27
    • 0034085789 scopus 로고    scopus 로고
    • Nuclear distribution of RNA polymerase II in human oocytes from antral follicles: Dynamics relative to the transcriptional state and association with splicing factors
    • Parfenov V.N., Davis D.S., Pochukalina G.N., Kostyuchek D. and Murti K.G., Nuclear distribution of RNA polymerase II in human oocytes from antral follicles: dynamics relative to the transcriptional state and association with splicing factors. J. Cell Biochem. 77: 654-665, 2000.
    • (2000) J. Cell Biochem. , vol.77 , pp. 654-665
    • Parfenov, V.N.1    Davis, D.S.2    Pochukalina, G.N.3    Kostyuchek, D.4    Murti, K.G.5
  • 28
    • 4344708309 scopus 로고    scopus 로고
    • Actin is closely associated with RNA polymerase II and involved in activation of gene transcription
    • Zhu X., Zeng X., Huang B. and Hao S., Actin is closely associated with RNA polymerase II and involved in activation of gene transcription. Biochem. Biophys. Res. Commun. 321: 623-630, 2004.
    • (2004) Biochem. Biophys. Res. Commun. , vol.321 , pp. 623-630
    • Zhu, X.1    Zeng, X.2    Huang, B.3    Hao, S.4
  • 29
    • 10044278254 scopus 로고    scopus 로고
    • Isolation and identification of a protein interacting with p37 protein of Mycoplasma hyorhinis
    • Chinese
    • Sun Y.N., Jin G.L., Zhang J.Z., Wu J. and Shou C.C., Isolation and identification of a protein interacting with p37 protein of Mycoplasma hyorhinis. Prog. Biochem. Biophys. 31: 902-905, 2004(Chinese).
    • (2004) Prog. Biochem. Biophys. , vol.31 , pp. 902-905
    • Sun, Y.N.1    Jin, G.L.2    Zhang, J.Z.3    Wu, J.4    Shou, C.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.