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NUP37  -  nucleoporin 37kDa

Homo sapiens

Synonyms: FLJ22618, MGC5585, Nucleoporin Nup37, Nup107-160 subcomplex subunit Nup37, p37
 
 
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Disease relevance of NUP37

  • An affinity column fraction, containing p37, stimulated HTLV-I transcription approximately 12-fold in vitro [1].
  • We also observed that the detectable levels of p37 and p50 in the infected MOLT-4 cells were greatly reduced after phorbol ester (TPA) treatment under the condition of which HIV-1 gene expression was increased by about fivefold [2].
  • p37 protein is a membrane lipoprotein of Mycoplasma hyorhinis, and our previous work showed that there was high ratio of M. hyorhinis infection in human gastric carcinoma [3].
  • Human gastric cancer cells AGS, after being transfected with the p37 gene, were smaller, more spherical and easy to detach from each other [3].
  • Characterization of platelet agglutinating protein p37 purified from the plasma of a patient with thrombotic thrombocytopenic purpura [4].
 

High impact information on NUP37

  • 14-3-3sigma is a p37 AUF1-binding protein that facilitates AUF1 transport and AU-rich mRNA decay [5].
  • It is proposed that p37 may be a novel adhesive molecule expressed on the surface of a variety of hematopoietic cells that could participate in both homotypic and heterotypic interactions of stromal and progenitor cells [6].
  • This protein, designated p37, could be surface-radiolabeled and thus appeared to be exposed on the cell membrane [6].
  • An apparently identical 37-Kd protein was expressed by three stromal cell lines, by Swiss 3T3 fibroblastic cells, and by FDCP-1 and FDCP-2 progenitor cells. p37 was selectively adsorbed from membrane lysates by a variety of murine hematopoietic cells, including erythrocytes, but not by human erythrocytes [6].
  • Binding of p37 to cells was calcium-dependent, and was not affected by inhibitors of the hematopoietic homing receptor or the cell-binding or heparin-binding functions of fibronectin [6].
 

Chemical compound and disease context of NUP37

 

Biological context of NUP37

  • By combining green fluorescent protein-tagged nucleoporins and specific antibodies, we show that all the constituents of this complex, including Nup37, Nup43, Seh1, and Sec13, are targeted to kinetochores from prophase to anaphase of mitosis [8].
  • In contrast, apparently normal disassembly takes place in cells transfected with cDNA containing mutated p37 kinase phosphorylation sites (thr457:ala/ser458:ala) [9].
  • Lipoprotein p37 from Mycoplasma hyorhinis inhibiting mammalian cell adhesion [3].
  • To investigate the possible functions of p37 in cancer development, the nucleotide sequence of p37 gene was modified and expressed well in transfected cells [3].
  • Their adhesion to matrix was also diminished and cytoskeleton in these stable p37 AGS cell was rearranged and transcription co-factor beta-actin was transferred to nucleolus with down-regulation of ICAM-1 and integrin beta1 [3].
 

Anatomical context of NUP37

  • Like TFIIIA, HeLa cell proteins p37 binds in vitro to 5S RNA and to cloned 5S RNA genes [10].
  • These results suggest that protein p37 fulfils in HeLa cells a function similar to that of TFIIIA in amphibian oocytes, ie control of 5S RNA transcription [10].
  • Contrary to the p34cdc2 mediated N-terminal phosphorylation (at ser-55) which can disassemble vimentin intermediate filaments (IF) in vitro, p37 protein kinase phosphorylates vimentin-IF without obviously affecting its structure in vitro [9].
  • These findings will be helpful for us to elucidate the effects of p37 on eukaryotic cells as well as to better understand the potential relationship between cancer and mycoplasma infection [3].
  • Recombinant p37 enhanced the invasiveness of two prostate carcinoma and two melanoma cell lines in a dose-dependent manner in vitro, but did not have a significant effect on tumor cell growth [11].
 

Associations of NUP37 with chemical compounds

  • Sucrose density gradient ultracentrifugation of a mixture of 125I-PAP p37 and IgG also revealed the fluid-phase complex formation with a sedimentation value of 19S [12].
  • Following renaturation of the proteins isolated from an SDS-containing gel, p37, but not the other protein fractions, was able to specifically bind to DRE 1 [13].
  • Sequence comparisons, followed by three-dimensional molecular modeling, revealed a region of similarity between p37 and influenza hemagglutinin A, a sialic acid-binding protein that plays a critical role in viral entry [11].
  • Preliminary carbohydrate analysis suggested that p37 is a glycoprotein and contained about 11% neutral sugars and 6.6% sialic acid [4].
 

Other interactions of NUP37

  • Here, we identify three WD (Trp-Asp)-repeat nucleoporins as new members of this complex, two of which, Nup37 and Nup43, are specific to higher eukaryotes [8].
 

Analytical, diagnostic and therapeutic context of NUP37

  • Molecular cloning of a cDNA (p37AUF1) corresponding to human p37 predicted a polypeptide containing two non-identical RNA recognition motifs (RRM) and a C-terminal Gln-rich domain [Zhang et al. Mol. Cell. Biol. 13 (1993) 7652-7665] [14].
  • Southern blot data support our assumption of a polymorphism of the factor H-related proteins p39 and p37 [15].
  • In Western immunoblotting p37 binds to purified GPIV and the complex formed between the two proteins was detected by polyclonal antibody to p37 and peroxidase conjugated second antibody [7].

References

  1. Involvement of transcription factor YB-1 in human T-cell lymphotropic virus type I basal gene expression. Kashanchi, F., Duvall, J.F., Dittmer, J., Mireskandari, A., Reid, R.L., Gitlin, S.D., Brady, J.N. J. Virol. (1994) [Pubmed]
  2. Modulation of host cell nuclear proteins that bind to HIV-1 trans-activation-responsive element RNA by phorbol ester. Masuda, T., Harada, S. Virology (1993) [Pubmed]
  3. Lipoprotein p37 from Mycoplasma hyorhinis inhibiting mammalian cell adhesion. Liu, W.B., Zhang, J.Z., Jiang, B.H., Ren, T.T., Gong, M.M., Meng, L., Shou, C.C. J. Biomed. Sci. (2006) [Pubmed]
  4. Characterization of platelet agglutinating protein p37 purified from the plasma of a patient with thrombotic thrombocytopenic purpura. Siddiqui, F.A., Lian, E.C. Biochem. Mol. Biol. Int. (1993) [Pubmed]
  5. 14-3-3sigma is a p37 AUF1-binding protein that facilitates AUF1 transport and AU-rich mRNA decay. He, C., Schneider, R. EMBO J. (2006) [Pubmed]
  6. A novel 37-Kd adhesive membrane protein from cloned murine bone marrow stromal cells and cloned murine hematopoietic progenitor cells. Shiota, Y., Wilson, J.G., Harjes, K., Zanjani, E.D., Tavassoli, M. Blood (1993) [Pubmed]
  7. Platelet-agglutinating protein p37 from a thrombotic thrombocytopenic purpura plasma forms complexes with platelet membrane glycoprotein IV (CD36). Siddiqui, F.A., Lian, E.C. Biochem. Int. (1992) [Pubmed]
  8. The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis. Loïodice, I., Alves, A., Rabut, G., Van Overbeek, M., Ellenberg, J., Sibarita, J.B., Doye, V. Mol. Biol. Cell (2004) [Pubmed]
  9. The relative roles of specific N- and C-terminal phosphorylation sites in the disassembly of intermediate filament in mitotic BHK-21 cells. Chou, Y.H., Opal, P., Quinlan, R.A., Goldman, R.D. J. Cell. Sci. (1996) [Pubmed]
  10. Characterization by human antibodies of two HeLa cell proteins which are related to Xenopus laevis transcription factor TFIIIA. Lagaye, S., Barque, J.P., le Maire, M., Denis, H., Larsen, C.J. Nucleic Acids Res. (1988) [Pubmed]
  11. p37 Induces tumor invasiveness. Ketcham, C.M., Anai, S., Reutzel, R., Sheng, S., Schuster, S.M., Brenes, R.B., Agbandje-McKenna, M., McKenna, R., Rosser, C.J., Boehlein, S.K. Mol. Cancer Ther. (2005) [Pubmed]
  12. Platelet-agglutinating protein P37 from a thrombotic thrombocytopenic purpura plasma forms a complex with human immunoglobulin G. Siddiqui, F.A., Lian, E.C. Blood (1988) [Pubmed]
  13. Sequences downstream of the RNA initiation site regulate human T-cell lymphotropic virus type I basal gene expression. Kashanchi, F., Duvall, J.F., Lindholm, P.F., Radonovich, M.F., Brady, J.N. J. Virol. (1993) [Pubmed]
  14. Characterization of cDNAs encoding the murine A+U-rich RNA-binding protein AUF1. Ehrenman, K., Long, L., Wagner, B.J., Brewer, G. Gene (1994) [Pubmed]
  15. Polymorphism and deficiency of human factor H-related proteins p39 and p37. Feifel, E., Prodinger, W.M., Mölgg, M., Schwaeble, W., Schönitzer, D., Koistinen, V., Misasi, R., Dierich, M.P. Immunogenetics (1992) [Pubmed]
 
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