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Gene Review

LPP  -  LIM domain containing preferred...

Homo sapiens

Synonyms: LIM domain-containing preferred translocation partner in lipoma, Lipoma-preferred partner
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Disease relevance of LPP


High impact information on LPP

  • Here, we have identified the LIM domain protein LPP as a novel coregulatory binding partner for PEA3 [5].
  • LPP can also functionally interact in a similar manner with the related family member ER81 [5].
  • By manipulating LPP levels, we show that it acts to upregulate the transactivation capacity of PEA3 [5].
  • Thus, we have uncovered a novel nuclear function for the LIM domain protein LPP as a transcriptional coactivator [5].
  • As LPP continually shuttles between the cell periphery and the nucleus, it represents a potential novel link between cell surface events and changes in gene expression [5].

Biological context of LPP


Anatomical context of LPP


Associations of LPP with chemical compounds

  • In addition, LPP accumulates in the nucleus of cells upon treatment with leptomycin B, an inhibitor of the export factor CRM1 [7].
  • HPP-CFC were only depleted to 57% of normal at 2 days after FU treatment, whereas the cells responsive to PMUE alone (low proliferative potential, LPP-CFC) were depleted to 1.2%, indicating a marked difference in cycling status of the respective types of progenitor cells [12].
  • Addition of appropriate concentrations of PGE1 to the agar culture assay should improve detection of HPP-CFC by inhibiting the proliferation of LPP-CFC [13].
  • Rats with an estrogen implant had an LPP of 42.5 +/- 16.8 cm H2O, which was significantly greater than rats given sham implants and significantly less than unoperated controls [14].
  • Seven days following nerve crush urethral LPP testing was performed using urethane anesthesia [14].

Physical interactions of LPP


Regulatory relationships of LPP

  • This deletion may bring the BCL6 gene under the control of regulatory elements of the LPP gene or the miRNA-28 gene located in intron 4 of LPP [16].
  • In stented pig coronary vessels, LPP was expressed in the neointima of cells lacking smoothelin and showed expression patterns identical to those of SM alpha-actin [17].

Other interactions of LPP


Analytical, diagnostic and therapeutic context of LPP


  1. LPP, the preferred fusion partner gene of HMGIC in lipomas, is a novel member of the LIM protein gene family. Petit, M.M., Mols, R., Schoenmakers, E.F., Mandahl, N., Van de Ven, W.J. Genomics (1996) [Pubmed]
  2. A novel LPP fusion gene indicates the crucial role of truncated LPP proteins in lipomas and pulmonary chondroid hamartomas. Lemke, I., Rogalla, P., Bullerdiek, J. Cytogenet. Cell Genet. (2001) [Pubmed]
  3. Fusion of the HMGA2 and NFIB genes in lipoma. Nilsson, M., Panagopoulos, I., Mertens, F., Mandahl, N. Virchows Arch. (2005) [Pubmed]
  4. Synergism between human monocyte chemotactic and activating factor and bacterial products for activation of tumoricidal properties in murine macrophages. Singh, R.K., Berry, K., Matsushima, K., Yasumoto, K., Fidler, I.J. J. Immunol. (1993) [Pubmed]
  5. The LIM domain protein LPP is a coactivator for the ETS domain transcription factor PEA3. Guo, B., Sallis, R.E., Greenall, A., Petit, M.M., Jansen, E., Young, L., Van de Ven, W.J., Sharrocks, A.D. Mol. Cell. Biol. (2006) [Pubmed]
  6. The tumor suppressor Scrib interacts with the zyxin-related protein LPP, which shuttles between cell adhesion sites and the nucleus. Petit, M.M., Meulemans, S.M., Alen, P., Ayoubi, T.A., Jansen, E., Van de Ven, W.J. BMC Cell Biol. (2005) [Pubmed]
  7. LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity. Petit, M.M., Fradelizi, J., Golsteyn, R.M., Ayoubi, T.A., Menichi, B., Louvard, D., Van de Ven, W.J., Friederich, E. Mol. Biol. Cell (2000) [Pubmed]
  8. The lipoma preferred partner LPP interacts with alpha-actinin. Li, B., Zhuang, L., Reinhard, M., Trueb, B. J. Cell. Sci. (2003) [Pubmed]
  9. The focal adhesion and nuclear targeting capacity of the LIM-containing lipoma-preferred partner (LPP) protein. Petit, M.M., Meulemans, S.M., Van de Ven, W.J. J. Biol. Chem. (2003) [Pubmed]
  10. LPP, a LIM protein highly expressed in smooth muscle. Gorenne, I., Nakamoto, R.K., Phelps, C.P., Beckerle, M.C., Somlyo, A.V., Somlyo, A.P. Am. J. Physiol., Cell Physiol. (2003) [Pubmed]
  11. Intrapatellar tendon lipoma with chondro-osseous differentiation: detection of HMGA2-LPP fusion gene transcript. Matsui, Y., Hasegawa, T., Kubo, T., Goto, T., Yukata, K., Endo, K., Bando, Y., Yasui, N. J. Clin. Pathol. (2006) [Pubmed]
  12. Detection of primitive macrophage progenitor cells in mouse bone marrow. Bradley, T.R., Hodgson, G.S. Blood (1979) [Pubmed]
  13. The effect of prostaglandins E1 and E2 on macrophage progenitor cells with high proliferative potential in mouse bone marrow in vitro. Kriegler, A.B., Bradley, T.R., Hodgson, G.S. Blood (1984) [Pubmed]
  14. Effect of estrogen on urethral function and nerve regeneration following pudendal nerve crush in the female rat. Ahmed, Y., Lin, D.L., Ferguson, C., Esparza, N., Damaser, M.S. J. Urol. (2006) [Pubmed]
  15. The tumor suppressor Scrib selectively interacts with specific members of the zyxin family of proteins. Petit, M.M., Crombez, K.R., Vervenne, H.B., Weyns, N., Van de Ven, W.J. FEBS Lett. (2005) [Pubmed]
  16. Chromosomal translocations fusing the BCL6 gene to different partner loci are recurrent in primary central nervous system lymphoma and may be associated with aberrant somatic hypermutation or defective class switch recombination. Schwindt, H., Akasaka, T., Zühlke-Jenisch, R., Hans, V., Schaller, C., Klapper, W., Dyer, M.J., Siebert, R., Deckert, M. J. Neuropathol. Exp. Neurol. (2006) [Pubmed]
  17. LPP expression during in vitro smooth muscle differentiation and stent-induced vascular injury. Gorenne, I., Jin, L., Yoshida, T., Sanders, J.M., Sarembock, I.J., Owens, G.K., Somlyo, A.P., Somlyo, A.V. Circ. Res. (2006) [Pubmed]
  18. Human LPP gene is fused to MLL in a secondary acute leukemia with a t(3;11) (q28;q23). Dahéron, L., Veinstein, A., Brizard, F., Drabkin, H., Lacotte, L., Guilhot, F., Larsen, C.J., Brizard, A., Roche, J. Genes Chromosomes Cancer (2001) [Pubmed]
  19. ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E. Murthy, K.K., Clark, K., Fortin, Y., Shen, S.H., Banville, D. J. Biol. Chem. (1999) [Pubmed]
  20. Overexpression of HMGA2-LPP fusion transcripts promotes expression of the alpha 2 type XI collagen gene. Kubo, T., Matsui, Y., Goto, T., Yukata, K., Yasui, N. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  21. An identical HMGIC-LPP fusion transcript is consistently expressed in pulmonary chondroid hamartomas with t(3;12)(q27-28;q14-15). Rogalla, P., Lemke, I., Kazmierczak, B., Bullerdiek, J. Genes Chromosomes Cancer (2000) [Pubmed]
  22. The t(3;12)(q27;q14-q15) with underlying HMGIC-LPP fusion is not determining an adipocytic phenotype. Rogalla, P., Kazmierczak, B., Meyer-Bolte, K., Tran, K.H., Bullerdiek, J. Genes Chromosomes Cancer (1998) [Pubmed]
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