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Gene Review

Pip  -  prolactin induced protein

Mus musculus

Synonyms: 14 kDa submandibular gland protein, GCDFP-15, GP17, Gross cystic disease fluid protein 15, Prolactin-induced protein, ...
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Disease relevance of Pip


High impact information on Pip

  • 1. Thus, during B-cell activation and differentiation, Pip may function both as an activator to promote B cell-specific gene expression and as a repressor to inhibit the antiproliferative effects of alpha/beta-interferons [6].
  • When stably expressed, the wild-type fused dimer strongly repressed the expression of a rearranged immunoglobulin lambda gene, thereby establishing the functional importance of PU.1-Pip complexes in B cell gene expression [7].
  • In addition, these effects do not reflect a specific insulin requirement for prolactin sensitivity; epidermal growth factor can support prolactin-induced total RNA synthesis as well as insulin can [8].
  • Using electrophoretic mobility shift assays, we found that Pip can bind to the heavy-chain intron enhancer region [3].
  • However, a Pip dominant negative mutant inhibited germ line I micro transcripts [3].

Biological context of Pip


Anatomical context of Pip

  • PIP/SMGP messenger RNA expression was only detected in the lacrimal and submaxillary glands of the rodents [1].
  • PRL had no effect on the regulation of PIP/SMGP in either salivary or lacrimal glands [1].
  • In addition, during early postnatal development, mSMGP/mPIP gene expression was detected in the other two major salivary glands, the sublingual and parotid, as well as in the lacrimal gland and in reproductive tissues [9].
  • In addition, we found that in fibroblasts Pip greatly increased E47 induction of germ line I micro transcripts associated with somatic rearrangement and isotype class switching [3].
  • The inhibitory rates were 16.9%, 36.0%, and 48.3% in stress ulcers; 4.4%, 51.1%, and 64.4% in indometacin ulcers; 19.2%, 41.5%, and 59.6% in HCl ulcers; 4.8%, 11.9%, and 26.2% in pyloric ligation ulcers, respectively; Pip inhibited the volume of gastric juice, gastric acidity, and pepsin A activity [4].

Associations of Pip with chemical compounds

  • Second, a conformational change in the PU.1 PEST domain, apparently mediated by serine phosphorylation, induces a conformational change in Pip enabling it to bind to DNA [11].
  • Ceftriaxone and ticarcillin-clavulanate treatment groups developed persistently high levels of stool VRE compared with both the saline and the piperacillin-tazobactam (Pip-Taz) groups (P<.008) [12].
  • In hypophysectomized ovariectomized animals, the administration of estradiol restored the Hageman factor titer to normal levels, whereas the infusion of prolactin induced a dramatic rise in the Hageman factor titer to the degree observed in nonhypophysectomized estrogen-treated rats [13].
  • In HC11 cells, NF-kappaB p50/p65 activity was inversely correlated with prolactin-induced STAT5 tyrosine phosphorylation, expression of endogenous beta-casein gene, and of a transfected beta-casein gene promoter reporter construct [14].
  • Unlike explants from normal virgin mouse mammary gland, exposure to insulin, hydrocortisone, and prolactin induced an increase in casein synthesis in HAN explant cultures which was independent of DNA synthesis [15].

Regulatory relationships of Pip


Other interactions of Pip


Analytical, diagnostic and therapeutic context of Pip


  1. Tissue-specific androgen-inhibited gene expression of a submaxillary gland protein, a rodent homolog of the human prolactin-inducible protein/GCDFP-15 gene. Myal, Y., Iwasiow, B., Yarmill, A., Harrison, E., Paterson, J.A., Shiu, R.P. Endocrinology (1994) [Pubmed]
  2. Streptogramin-based gene regulation systems for mammalian cells. Fussenegger, M., Morris, R.P., Fux, C., Rimann, M., von Stockar, B., Thompson, C.J., Bailey, J.E. Nat. Biotechnol. (2000) [Pubmed]
  3. Mechanism of e47-Pip interaction on DNA resulting in transcriptional synergy and activation of immunoglobulin germ line sterile transcripts. Nagulapalli, S., Goheer, A., Pitt, L., McIntosh, L.P., Atchison, M.L. Mol. Cell. Biol. (2002) [Pubmed]
  4. Protective action of piperine against experimental gastric ulcer. Bai, Y.F., Xu, H. Acta Pharmacol. Sin. (2000) [Pubmed]
  5. Hepatic clearance and metabolism in the rat of a human breast cancer associated glycoprotein (GCDFP-15). Toth, C.A., Haagensen, D.E., Davis, S., Zamcheck, N., Thomas, P. Breast Cancer Res. Treat. (1988) [Pubmed]
  6. Pip, a lymphoid-restricted IRF, contains a regulatory domain that is important for autoinhibition and ternary complex formation with the Ets factor PU.1. Brass, A.L., Kehrli, E., Eisenbeis, C.F., Storb, U., Singh, H. Genes Dev. (1996) [Pubmed]
  7. Assembly requirements of PU.1-Pip (IRF-4) activator complexes: inhibiting function in vivo using fused dimers. Brass, A.L., Zhu, A.Q., Singh, H. EMBO J. (1999) [Pubmed]
  8. Insulin is essential for accumulation of casein mRNA in mouse mammary epithelial cells. Bolander, F.F., Nicholas, K.R., Van Wyk, J.J., Topper, Y.J. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  9. Expression of the mouse homologue for the human GCDFP-15/PIP gene during pre- and early post-natal development. Lee, B., Modha, G., Watson, P.H., Dodd, J., Troup, S., Blanchard, A., Myal, Y. Mol. Cell. Endocrinol. (2003) [Pubmed]
  10. Transcription factor Pip can enhance DNA binding by E47, leading to transcriptional synergy involving multiple protein domains. Nagulapalli, S., Atchison, M.L. Mol. Cell. Biol. (1998) [Pubmed]
  11. A two-step mechanism for recruitment of Pip by PU.1. Perkel, J.M., Atchison, M.L. J. Immunol. (1998) [Pubmed]
  12. Effect of parenteral antibiotic administration on the establishment of colonization with vancomycin-resistant Enterococcus faecium in the mouse gastrointestinal tract. Donskey, C.J., Hanrahan, J.A., Hutton, R.A., Rice, L.B. J. Infect. Dis. (2000) [Pubmed]
  13. The influence of estrogen and prolactin on Hageman factor (factor XII) titer in ovariectomized and hypophysectomized rats. Gordon, E.M., Douglas, J.G., Ratnoff, O.D., Arafah, B.M. Blood (1985) [Pubmed]
  14. Activation of NF-kappaB p50/p65 is regulated in the developing mammary gland and inhibits STAT5-mediated beta-casein gene expression. Geymayer, S., Doppler, W. FASEB J. (2000) [Pubmed]
  15. Expression of pregnancy-specific genes in preneoplastic mouse mammary tissues from virgin mice. Smith, G.H., Vonderhaar, B.K., Graham, D.E., Medina, D. Cancer Res. (1984) [Pubmed]
  16. Caveolin-1-deficient mice show accelerated mammary gland development during pregnancy, premature lactation, and hyperactivation of the Jak-2/STAT5a signaling cascade. Park, D.S., Lee, H., Frank, P.G., Razani, B., Nguyen, A.V., Parlow, A.F., Russell, R.G., Hulit, J., Pestell, R.G., Lisanti, M.P. Mol. Biol. Cell (2002) [Pubmed]
  17. The MEK inhibitor PD 098059 inhibits prolactin-induced Nb2 cell mitogenesis but not milk product synthesis in cultured mouse mammary tissues. Yu, T.X., Rillema, J.A. Biochim. Biophys. Acta (1998) [Pubmed]
  18. The mechanisms by which nitric oxide affects mammary epithelial growth and differentiation. Bolander, F.F. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  19. Regulation of receptor activator of NF-kappaB ligand-induced tartrate-resistant acid phosphatase gene expression by PU.1-interacting protein/interferon regulatory factor-4. Synergism with microphthalmia transcription factor. Matsumoto, M., Hisatake, K., Nogi, Y., Tsujimoto, M. J. Biol. Chem. (2001) [Pubmed]
  20. Naturally occurring dominant negative variants of Stat5. Wang, D., Stravopodis, D., Teglund, S., Kitazawa, J., Ihle, J.N. Mol. Cell. Biol. (1996) [Pubmed]
  21. Role of tyrosine kinase Jak2 in prolactin-induced differentiation and growth of mammary epithelial cells. Xie, J., LeBaron, M.J., Nevalainen, M.T., Rui, H. J. Biol. Chem. (2002) [Pubmed]
  22. Effects of retinoid glucuronides on mammary gland development in organ culture. Mehta, R.G., Barua, A.B., Olson, J.A., Moon, R.C. Oncology (1991) [Pubmed]
  23. Possible roles of calcium and calmodulin in mammary gland differentiation in vitro. Bolander, F.F. J. Endocrinol. (1985) [Pubmed]
  24. Retinoids inhibit prolactin-induced development of the mammary gland in vitro. Mehta, R.G., Cerny, W.L., Moon, R.C. Carcinogenesis (1983) [Pubmed]
  25. Prolactin analgesia: tolerance and cross-tolerance with morphine. Ramaswamy, S., Viswanathan, S., Bapna, J.S. Eur. J. Pharmacol. (1985) [Pubmed]
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