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Gene Review

Prf1  -  perforin 1 (pore forming protein)

Rattus norvegicus

Synonyms: Cyta, Cytolysin, Lymphocyte pore-forming protein, P1, Perforin-1, ...
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Disease relevance of Prf1


High impact information on Prf1

  • The noncytotoxic rat mast cell tumor line RBL was transfected with genes for the cytotoxic lymphocyte granule proteins cytolysin (perforin) and granzyme A, giving transfectants with mRNA and protein expression levels comparable with cloned cytotoxic T lymphocytes [6].
  • With tumor targets, RBL cells expressing cytolysin alone were weakly cytotoxic, but both cytolytic and nucleolytic activity were enhanced by coexpression of granzyme B [1].
  • After permeabilization of mast cells by the bacterial cytolysin streptolysin-O, approximately 60% of the Triton-soluble actin leaks out within 10 min [7].
  • The dense core domains contain secretory proteins thought to play a role in cytolysis, including cytolysin and chondroitin sulfate proteoglycan [8].
  • The granules of natural killer (NK) cells contain cytolysin and serine proteases, proteins that are expressed specifically in cytolytic cells and are released in response to target binding [9].

Biological context of Prf1


Anatomical context of Prf1


Associations of Prf1 with chemical compounds


Other interactions of Prf1

  • Three stages of cytokine mRNA expression could be distinguished: (i) interleukin (IL)-12, tumor necrosis factor (TNF)-beta (= lymphotoxin-alpha) and cytolysin appeared early and before onset of clinical signs of EAE; (ii) TNF-alpha peaked at height of clinical signs of EAE; (iii) IL-10 appeared increasingly at and after clinical recovery [2].
  • On the contrary, LPS strongly inhibited IFN-gamma-mediated cytolysin mRNA expression in microglia, astrocytes and oligodendrocytes [3].

Analytical, diagnostic and therapeutic context of Prf1


  1. Synergistic roles of granzymes A and B in mediating target cell death by rat basophilic leukemia mast cell tumors also expressing cytolysin/perforin. Nakajima, H., Park, H.L., Henkart, P.A. J. Exp. Med. (1995) [Pubmed]
  2. Cytokine production in the central nervous system of Lewis rats with experimental autoimmune encephalomyelitis: dynamics of mRNA expression for interleukin-10, interleukin-12, cytolysin, tumor necrosis factor alpha and tumor necrosis factor beta. Issazadeh, S., Ljungdahl, A., Höjeberg, B., Mustafa, M., Olsson, T. J. Neuroimmunol. (1995) [Pubmed]
  3. Induction of cytolysin mRNA in glial cells by IFN-gamma: a possible cytotoxic pathway in the CNS. Xiao, B.G., Bao, W.J., Bai, X.F., Link, H. Neuroreport (1996) [Pubmed]
  4. Mechanism of lysis by large granular lymphocyte granule cytolysin: generation of a stable cytolysin-RBC intermediate. Kuta, A.E., Reynolds, C.R., Henkart, P.A. J. Immunol. (1989) [Pubmed]
  5. Purinergic agonists stimulate the secretion of endothelin-1 in rat thyroid FRTL-5 cells. Vainio, M., Saijonmaa, O., Fyhrquist, F., Törnquist, K. J. Cell. Physiol. (1996) [Pubmed]
  6. Cytotoxicity with target DNA breakdown by rat basophilic leukemia cells expressing both cytolysin and granzyme A. Shiver, J.W., Su, L., Henkart, P.A. Cell (1992) [Pubmed]
  7. Changes in the state of actin during the exocytotic reaction of permeabilized rat mast cells. Koffer, A., Tatham, P.E., Gomperts, B.D. J. Cell Biol. (1990) [Pubmed]
  8. The lytic granules of natural killer cells are dual-function organelles combining secretory and pre-lysosomal compartments. Burkhardt, J.K., Hester, S., Lapham, C.K., Argon, Y. J. Cell Biol. (1990) [Pubmed]
  9. Two proteins targeted to the same lytic granule compartment undergo very different posttranslational processing. Burkhardt, J.K., Hester, S., Argon, Y. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  10. Molecular cloning of rat cytolysin. Ishikawa, H., Shinkai, Y., Yagita, H., Yue, C.C., Henkart, P.A., Sawada, S., Young, H.A., Reynolds, C.W., Okumura, K. J. Immunol. (1989) [Pubmed]
  11. Cytolysin gene expression in the islets of diabetic BioBreeding/Worcester rats. Jiang, Z., Makowiecki, J., Mordes, J.P., Woda, B.A. J. Immunol. (1994) [Pubmed]
  12. Sequential expression of nucleoproteins during rat spermiogenesis. Kistler, W.S., Henriksén, K., Mali, P., Parvinen, M. Exp. Cell Res. (1996) [Pubmed]
  13. Stable, conserved outer membrane epitope of strains of Haemophilus influenzae biogroup aegyptius associated with Brazilian purpuric fever. Lesse, A.J., Gheesling, L.L., Bittner, W.E., Myers, S.D., Carlone, G.M. Infect. Immun. (1992) [Pubmed]
  14. Liposomes as targets for granule cytolysin from cytotoxic large granular lymphocyte tumors. Blumenthal, R., Millard, P.J., Henkart, M.P., Reynolds, C.W., Henkart, P.A. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  15. Nongranular proteolytic enzymes of rat IL-2-activated natural killer cells. I. Subcellular localization and functional role. Goldfarb, R.H., Wasserman, K., Herberman, R.B., Kitson, R.P. J. Immunol. (1992) [Pubmed]
  16. Nicotinamide adenine dinucleotide (NAD) and its metabolites inhibit T lymphocyte proliferation: role of cell surface NAD glycohydrolase and pyrophosphatase activities. Bortell, R., Moss, J., McKenna, R.C., Rigby, M.R., Niedzwiecki, D., Stevens, L.A., Patton, W.A., Mordes, J.P., Greiner, D.L., Rossini, A.A. J. Immunol. (2001) [Pubmed]
  17. Expression of epidermal growth factor in the developing rat kidney. Jung, J.Y., Song, J.H., Li, C., Yang, C.W., Kang, T.C., Won, M.H., Jeong, Y.G., Han, K.H., Choi, K.B., Lee, S.H., Kim, J. Am. J. Physiol. Renal Physiol. (2005) [Pubmed]
  18. Tissue-specific regulation of the expression of rat kallikrein gene family members by thyroid hormone. Clements, J.A., Matheson, B.A., Funder, J.E. Biochem. J. (1990) [Pubmed]
  19. Demonstration of trans-acting factors binding to the promoter region of the testis-specific rat protamine P1 gene. Queralt, R., Oliva, R. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
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