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Gene Review

PLRG1  -  pleiotropic regulator 1

Homo sapiens

Synonyms: Cwc1, PRL1, PRP46, PRPF46, Pleiotropic regulator 1, ...
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Disease relevance of PLRG1

  • The prl1 mutation localized by T-DNA tagging on Arabidopsis chromosome 4-44 confers hypersensitivity to glucose and sucrose [1].
  • We stably transfected human A549 lung cancer cells with several short hairpin RNAs for PRL-1 and found decreased invasive activity in the resulting clones compared with control cells [2].
  • The present study was undertaken to test the ability of 16K hPRL to inhibit the growth of human HCT116 colon cancer cells transplanted s.c. into Rag1(-/-) mice [3].
  • These findings support the potential of 16K hPRL as a therapeutic agent for the treatment of colorectal cancer [3].
  • These results support the hypothesis that PRL-1 plays an important role in maintaining the malignant phenotype by exploiting Src activation processes, and that PRL-1 could be a promising therapeutic target for cancer metastasis and cell growth [2].

High impact information on PLRG1

  • Crystal structures of SarA, a pleiotropic regulator of virulence genes in S. aureus [4].
  • The prl1 mutation also augments the sensitivity of plants to growth hormones including cytokinin, ethylene, abscisic acid, and auxin; stimulates the accumulation of sugars and starch in leaves; and inhibits root elongation [1].
  • Potential functional conservation of PRL1 homologs found in other eukaryotes is indicated by nuclear localization of PRL1 in monkey COS-1 cells and selective interaction of PRL1 with a nuclear protein kinase C-betaII isoenzyme involved in human insulin signaling [1].
  • NF-kappa B is a pleiotropic regulator of a variety of genes implicated in the cellular response to injury [5].
  • In this study, we evaluated the role of PRL-1 in cell proliferation and metastatic processes in human lung cancer cells [2].

Chemical compound and disease context of PLRG1


Biological context of PLRG1


Anatomical context of PLRG1

  • The human proteins CDC5L (hCDC5) and PLRG1 are both highly conserved components of a multiprotein complex that is a subunit of the spliceosome [13].
  • The M(r) 16,000 NH(2)-terminal fragment of human prolactin (16K hPRL) is a potent antiangiogenic factor inhibiting endothelial cell function in vitro and neovascularization in vivo [3].
  • From the human B-lymphoblastoid cell line IM-9-P, we derived the IM-9-P series of clonal sublines that differ from each other in the degree of human PRL (hPRL) production [12].
  • Here, we examined whether the nuclear factor-kappaB (NF-kappaB) signaling pathway was involved in mediating the apoptotic action of 16K hPRL in bovine adrenal cortex capillary endothelial cells [11].
  • Treatment with recombinant 16K hPRL increased DNA fragmentation in cultured bovine brain capillary endothelial (BBE) and human umbilical vein endothelial (HUVE) cells in a time- and dose-dependent fashion, independent of the serum concentration [14].

Associations of PLRG1 with chemical compounds


Other interactions of PLRG1


Analytical, diagnostic and therapeutic context of PLRG1

  • Transcription of the PRL-1 gene increased in the rat liver remnant within a few minutes after partial hepatectomy and largely explained the increase in steady-state PRL-1 mRNA in the first few hours posthepatectomy [9].
  • When treated with polyclonal anti-hPRL antibodies, all mutants were immunologically indistinguishable from the unmodified hPRL, and circular dichroism analyses indicated that their alpha-helix content was similar to that of the unmodified hormone [20].
  • Each sample contained three distinct hPRL peaks on gel filtration designated as big medium, and small [21].
  • An enriched fraction of human decidual cells that synthesizes and releases human PRL (hPRL) was obtained by isopycnic centrifugation of collagenase- and hyaluronidase-dispersed cells through Percoll [22].
  • Up- and down-regulation of [125I]hPRL binding occurred after pretreatment of EFM-19 cell cultures with subphysiological or higher hPRL concentrations, respectively [23].


  1. Pleiotropic control of glucose and hormone responses by PRL1, a nuclear WD protein, in Arabidopsis. Németh, K., Salchert, K., Putnoky, P., Bhalerao, R., Koncz-Kálmán, Z., Stankovic-Stangeland, B., Bakó, L., Mathur, J., Okrész, L., Stabel, S., Geigenberger, P., Stitt, M., Rédei, G.P., Schell, J., Koncz, C. Genes Dev. (1998) [Pubmed]
  2. PRL-1 tyrosine phosphatase regulates c-Src levels, adherence, and invasion in human lung cancer cells. Achiwa, H., Lazo, J.S. Cancer Res. (2007) [Pubmed]
  3. Expression of the antiangiogenic factor 16K hPRL in human HCT116 colon cancer cells inhibits tumor growth in Rag1(-/-) mice. Bentzien, F., Struman, I., Martini, J.F., Martial, J., Weiner, R. Cancer Res. (2001) [Pubmed]
  4. Crystal structures of SarA, a pleiotropic regulator of virulence genes in S. aureus. Schumacher, M.A., Hurlburt, B.K., Brennan, R.G. Nature (2001) [Pubmed]
  5. Antisense oligonucleotides to the p65 subunit of NF-kappa B block CD11b expression and alter adhesion properties of differentiated HL-60 granulocytes. Sokoloski, J.A., Sartorelli, A.C., Rosen, C.A., Narayanan, R. Blood (1993) [Pubmed]
  6. Involvement of the tyrosine phosphatase early gene of liver regeneration (PRL-1) in cell cycle and in liver regeneration and fibrosis effect of halofuginone. Gnainsky, Y., Spira, G., Paizi, M., Bruck, R., Nagler, A., Genina, O., Taub, R., Halevy, O., Pines, M. Cell Tissue Res. (2006) [Pubmed]
  7. Hormone serum levels during oral cimetidine treatment of patients with peptic ulcers. Spona, J., Weisz, W., Rüdiger, E., Hentschel, E., Schütze, K., Reichel, W., Kerstan, E., Wewalka, F., Lochs, H. Hepatogastroenterology (1981) [Pubmed]
  8. Effects of low and high dose oral cimetidine on hormone serum levels in patients with peptic ulcers. Spona, J., Weiss, W., Rüdiger, E., Hentschel, E., Schütze, K., Reichel, W., Kerstan, E., Pötzi, R.R., Lochs, H. Endocrinol. Exp. (1987) [Pubmed]
  9. Mitogenic up-regulation of the PRL-1 protein-tyrosine phosphatase gene by Egr-1. Egr-1 activation is an early event in liver regeneration. Peng, Y., Du, K., Ramirez, S., Diamond, R.H., Taub, R. J. Biol. Chem. (1999) [Pubmed]
  10. Prevention and treatment of obesity, insulin resistance, and diabetes by bile Acid-binding resin. Kobayashi, M., Ikegami, H., Fujisawa, T., Nojima, K., Kawabata, Y., Noso, S., Babaya, N., Itoi-Babaya, M., Yamaji, K., Hiromine, Y., Shibata, M., Ogihara, T. Diabetes (2007) [Pubmed]
  11. The antiangiogenic factor 16K human prolactin induces caspase-dependent apoptosis by a mechanism that requires activation of nuclear factor-kappaB. Tabruyn, S.P., Sorlet, C.M., Rentier-Delrue, F., Bours, V., Weiner, R.I., Martial, J.A., Struman, I. Mol. Endocrinol. (2003) [Pubmed]
  12. Human prolactin gene expression: positive correlation between site-specific methylation and gene activity in a set of human lymphoid cell lines. Gellersen, B., Kempf, R. Mol. Endocrinol. (1990) [Pubmed]
  13. A direct interaction between the carboxyl-terminal region of CDC5L and the WD40 domain of PLRG1 is essential for pre-mRNA splicing. Ajuh, P., Sleeman, J., Chusainow, J., Lamond, A.I. J. Biol. Chem. (2001) [Pubmed]
  14. The antiangiogenic factor 16K PRL induces programmed cell death in endothelial cells by caspase activation. Martini, J.F., Piot, C., Humeau, L.M., Struman, I., Martial, J.A., Weiner, R.I. Mol. Endocrinol. (2000) [Pubmed]
  15. Thyroid hormone inhibits the human prolactin gene promoter by interfering with activating protein-1 and estrogen stimulations. Pernasetti, F., Caccavelli, L., Van de Weerdt, C., Martial, J.A., Muller, M. Mol. Endocrinol. (1997) [Pubmed]
  16. Interleukin-6 and oncostatin M stimulation of proliferation of prostate cancer 22Rv1 cells through the signaling pathways of p38 mitogen-activated protein kinase and phosphatidylinositol 3-kinase. Godoy-Tundidor, S., Cavarretta, I.T., Fuchs, D., Fiechtl, M., Steiner, H., Friedbichler, K., Bartsch, G., Hobisch, A., Culig, Z. Prostate (2005) [Pubmed]
  17. Phosphatidylinositol 3-kinase and focal adhesion kinase are early signals in the growth factor-like responses to thrombospondin-1 seen in human vascular smooth muscle. Lymn, J.S., Rao, S.J., Clunn, G.F., Gallagher, K.L., O'Neil, C., Thompson, N.T., Hughes, A.D. Arterioscler. Thromb. Vasc. Biol. (1999) [Pubmed]
  18. Induction of IRF-3/-7 kinase and NF-kappaB in response to double-stranded RNA and virus infection: common and unique pathways. Iwamura, T., Yoneyama, M., Yamaguchi, K., Suhara, W., Mori, W., Shiota, K., Okabe, Y., Namiki, H., Fujita, T. Genes Cells (2001) [Pubmed]
  19. Release from quiescence of primitive human hematopoietic stem/progenitor cells by blocking their cell-surface TGF-beta type II receptor in a short-term in vitro assay. Fortunel, N., Hatzfeld, J., Kisselev, S., Monier, M.N., Ducos, K., Cardoso, A., Batard, P., Hatzfeld, A. Stem Cells (2000) [Pubmed]
  20. Alanine-scanning mutagenesis of human prolactin: importance of the 58-74 region for bioactivity. Goffin, V., Norman, M., Martial, J.A. Mol. Endocrinol. (1992) [Pubmed]
  21. Heterogeneous human prolactin from a giant pituitary tumor in a patient with panhypopituitarism. Fang, V.S., Refetoff, S. J. Clin. Endocrinol. Metab. (1978) [Pubmed]
  22. Characterization of the synthesis and release of prolactin by an enriched fraction of human decidual cells. Markoff, E., Zeitler, P., Peleg, S., Handwerger, S. J. Clin. Endocrinol. Metab. (1983) [Pubmed]
  23. In vitro modulation of prolactin binding to human mammary carcinoma cells by steroid hormones and prolactin. Simon, W.E., Pahnke, V.G., Hölzel, F. J. Clin. Endocrinol. Metab. (1985) [Pubmed]
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