The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Prl2c2  -  prolactin family 2, subfamily c, member 2

Mus musculus

Synonyms: MRP-1, Mitogen-regulated protein 1, Mrp1, PLF-1, Plf, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Prl2c2


High impact information on Prl2c2


Biological context of Prl2c2

  • By nucleotide sequence analysis, a strongly hybridizing clone was found to be nearly identical to the proliferin cDNA clone isolated from a library prepared from mRNA of a growing mouse fibroblastic cell line [8].
  • From a cDNA plasmid library prepared from poly(A)+ placental RNA, two types of proliferin-related clones were isolated, differing in intensity of hybridization to proliferin cDNA [8].
  • PLF1 was detected and found to be differentially regulated during myogenesis in the rodent myogenic cell line C2C12 [2].
  • In conclusion, PLF selectively represses myogenic-specific transcription within the actin multigene family by suppressing the level and/or activity of a trans-acting factor (CBF) that modulates multiple muscle-specific genes [2].
  • All of the other genes in this hormone family, including those encoding mPRL, mouse placental lactogens I and II, and mouse proliferin and proliferin-related protein, map to chromosome 13 [9].

Anatomical context of Prl2c2

  • Large cells that expressed the trophoblast giant cell-specific gene Plf (encoding Proliferin) invaded during the early postimplantation period in a pattern tightly associated with spiral arteries [10].
  • We conclude that proliferin is a placental hormone that is synthesized in certain mouse cell lines during active growth [8].
  • These data suggest that cAMP levels can regulate trophoblast giant cell differentiation and, consequently, the amount of PLF and PRP secretion [11].
  • Analyses of cells stably transfected with PLF showed reduced levels of MyoD mRNA, a recently identified gene that is sufficient to convert pluripotential 10T1/2 cells into myoblasts [2].
  • Moreover, the serum concentration of PLF during pregnancy varied directly with the level of PLF mRNA in the placenta and with the number of placentas per animal [12].

Associations of Prl2c2 with chemical compounds


Regulatory relationships of Prl2c2


Other interactions of Prl2c2

  • 5. These cells did not express Plf, but rather expressed the spongiotrophoblast-specific gene Tpbp [10].
  • Proliferin is a recently described, prolactin-related protein whose mRNA appears in several murine cell lines during active growth [8].
  • Individual cells contained both PLF and placental lactogen II [12].
  • Rodents deficient in three known ABC family transporters (MRP1, MRP2, and MDR1a/1b) exhibited urinary arsenic levels similar or greater than those in wild-type rodents; however, administration of MK571, an MRP inhibitor, reduced urinary arsenic excretion by almost 50% [19].
  • Participation of multiple factors, including proliferin, in the inhibition of myogenic differentiation [20].

Analytical, diagnostic and therapeutic context of Prl2c2


  1. Proliferin enhances microvilli formation and cell growth of neuroblastoma cells. Wang, J.W., Jiang, Y.N., Huang, C.Y., Huang, P.Y., Huang, M.C., Cheng, W.T., Shen, C.K., Ju, Y.T. Neurosci. Res. (2006) [Pubmed]
  2. Proliferin, a prolactin/growth hormone-like peptide represses myogenic-specific transcription by the suppression of an essential serum response factor-like DNA-binding activity. Muscat, G.E., Gobius, K., Emery, J. Mol. Endocrinol. (1991) [Pubmed]
  3. Co-localization of elements required for phorbol ester stimulation and glucocorticoid repression of proliferin gene expression. Mordacq, J.C., Linzer, D.I. Genes Dev. (1989) [Pubmed]
  4. Reactivation of proliferin gene expression is associated with increased angiogenesis in a cell culture model of fibrosarcoma tumor progression. Toft, D.J., Rosenberg, S.B., Bergers, G., Volpert, O., Linzer, D.I. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  5. Increase in Mrp1 expression and 4-hydroxy-2-nonenal adduction in heart tissue of Adriamycin-treated C57BL/6 mice. Jungsuwadee, P., Cole, M.P., Sultana, R., Joshi, G., Tangpong, J., Butterfield, D.A., St Clair, D.K., Vore, M. Mol. Cancer Ther. (2006) [Pubmed]
  6. Stimulation and inhibition of angiogenesis by placental proliferin and proliferin-related protein. Jackson, D., Volpert, O.V., Bouck, N., Linzer, D.I. Science (1994) [Pubmed]
  7. Transcriptional regulation of proliferin gene expression in response to serum in transfected mouse cells. Linzer, D.I., Mordacq, J.C. EMBO J. (1987) [Pubmed]
  8. Identification of proliferin mRNA and protein in mouse placenta. Linzer, D.I., Lee, S.J., Ogren, L., Talamantes, F., Nathans, D. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  9. Chromosomal mapping of the prolactin/growth hormone gene family in the mouse. Jackson-Grusby, L.L., Pravtcheva, D., Ruddle, F.H., Linzer, D.I. Endocrinology (1988) [Pubmed]
  10. Interactions between trophoblast cells and the maternal and fetal circulation in the mouse placenta. Adamson, S.L., Lu, Y., Whiteley, K.J., Holmyard, D., Hemberger, M., Pfarrer, C., Cross, J.C. Dev. Biol. (2002) [Pubmed]
  11. Cyclic adenosine 3',5'-monophosphate stimulation of placental proliferin and proliferin-related protein secretion. Yamaguchi, M., Imai, T., Maeda, T., Sakata, M., Miyake, A., Linzer, D.I. Endocrinology (1995) [Pubmed]
  12. Trophoblastic giant cells of the mouse placenta as the site of proliferin synthesis. Lee, S.J., Talamantes, F., Wilder, E., Linzer, D.I., Nathans, D. Endocrinology (1988) [Pubmed]
  13. Proliferin secreted by cultured cells binds to mannose 6-phosphate receptors. Lee, S.J., Nathans, D. J. Biol. Chem. (1988) [Pubmed]
  14. Mitogen-regulated protein/proliferin mRNA induction following single applications of tumor promoters to murine skin. Parfett, C.L. Mol. Carcinog. (2005) [Pubmed]
  15. Apparent lack of Mrp1-mediated efflux at the luminal side of mouse blood-brain barrier endothelial cells. Cisternino, S., Rousselle, C., Lorico, A., Rappa, G., Scherrmann, J.M. Pharm. Res. (2003) [Pubmed]
  16. Regulation of the production of a prolactin-like protein (MRP/PLF) in 3T3 cells and in the mouse placenta. Nilsen-Hamilton, M., Jang, Y.J., Alvarez-Azaustre, E., Hamilton, R.T. Mol. Cell. Endocrinol. (1988) [Pubmed]
  17. Oxidative stress-regulated gene expression and promotion of morphological transformation induced in C3H/10T1/2 cells by ammonium metavanadate. Parfett, C.L., Pilon, R. Food Chem. Toxicol. (1995) [Pubmed]
  18. Overexpression of protein kinase C delta represses expression of proliferin in NIH3T3 cells that regulates cell proliferation. Kang, Y., Park, J.S., Kim, S.H., Shin, Y.J., Kim, W., Joo, H.J., Chun, J.S., Kim, H.J., Ha, M.J. Mol. Cell Biol. Res. Commun. (2000) [Pubmed]
  19. Formation and urinary excretion of arsenic triglutathione and methylarsenic diglutathione. Kala, S.V., Kala, G., Prater, C.I., Sartorelli, A.C., Lieberman, M.W. Chem. Res. Toxicol. (2004) [Pubmed]
  20. Participation of multiple factors, including proliferin, in the inhibition of myogenic differentiation. Wilder, E.L., Linzer, D.I. Mol. Cell. Biol. (1989) [Pubmed]
  21. A novel role for proliferin-2 in the ex vivo expansion of hematopoietic stem cells. Choong, M.L., Tan, A.C., Luo, B., Lodish, H.F. FEBS Lett. (2003) [Pubmed]
WikiGenes - Universities