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

PTN  -  pleiotrophin

Bos taurus

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 PTN

  • These experiments demonstrated that antisense inhibition of the expression of p18 in K562 erythroleukemia cells is associated with a decrease in cellular proliferation and accumulation of cells in the G2-M phases of the cycle [1].
  • We have determined the redox status and the disulfide arrangement of the cysteine residues in HBNF from bovine brain and refolded human recombinant protein produced in E. coli [2].

High impact information on PTN


Biological context of PTN


Anatomical context of PTN

  • A novel 17 kD heparin-binding growth factor (HBGF-8) in bovine uterus: purification and N-terminal amino acid sequence [8].
  • SDS-page and glycosaminoglycan (GAG) analysis of sulfate-radiolabeled proteoglycans isolated from the medium of mature cultured chondrocytes treated with PTN showed a threefold increase in the levels of proteoglycan synthesis [5].
  • The concentrations of MK and PTN in the bovine follicular fluid were estimated to be 125 micrograms/l and 400 micrograms/l, respectively [9].
  • An abundant protein that is identical to the growth-associated protein pleiotrophin (PTN) has been isolated from dissociative extracts of bovine nasal and fetal epiphyseal cartilage [10].
  • PTN was absent or was present only in trace amounts in mature articular cartilage [10].

Associations of PTN with chemical compounds

  • A neurite-promoting factor (p18) was isolated from bovine brain using ammonium sulfate fractionation, sulfated Sephadex G-50 chromatography, heparin-Sepharose gel chromatography, and reverse phase high performance liquid chromatography [4].
  • The complete amino acid sequence of p18 was determined by automated Edman degradation of S-pyridylethylated p18, and its peptide fragments produced by cyanogen bromide cleavage and by digestion with specific endoproteinases [4].
  • Pleiotrophin (PTN) is a secreted heparin-binding, developmentally regulated protein that is found in abundance in fetal, but not mature, cartilage [5].
  • An analysis of tryptic fragments of PTN, held together with disulfide bonds, did not indicate any set pattern of cystine cross-links, which suggests a propensity for rapid refolding of the protein [10].
  • More than 12 different phosphorylation products of p18 have been identified in different cells by high resolution two-dimensional polyacrylamide gel electrophoresis [1].

Other interactions of PTN


Analytical, diagnostic and therapeutic context of PTN

  • Capillary electrophoresis of chondroitinase ABC-digested proteoglycans isolated from mature chondrocytes showed 2-4-fold increases in the amounts of the 4S- and 6S-substituted GAG chains for the PTN-treated chondrocytes [5].
  • ULF contained several proteins that were detected on Western blots by an antibody raised against the N-terminal 14 amino acids of rat pleiotrophin (PTN) [12].
  • The disulfide linkages of human recombinant and bovine brain HBNF, as determined after proteolytic digestions of the non-reduced proteins by peptide mapping and sequence analysis are: Cys15-Cys44, Cys23-Cys53, Cys30-Cys57, Cys67-Cys99 and Cys77-Cys109 [2].


  1. Regulation of phosphoprotein p18 in leukemic cells. Cell cycle regulated phosphorylation by p34cdc2 kinase. Luo, X.N., Mookerjee, B., Ferrari, A., Mistry, S., Atweh, G.F. J. Biol. Chem. (1994) [Pubmed]
  2. Comparison of the disulfide bond arrangements of human recombinant and bovine brain heparin binding neurite-promoting factors. Hulmes, J.D., Seddon, A.P., Decker, M.M., Böhlen, P. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  3. Signal transduction pathways involved in the mitogenic activity of pleiotrophin. Implication of mitogen-activated protein kinase and phosphoinositide 3-kinase pathways. Souttou, B., Ahmad, S., Riegel, A.T., Wellstein, A. J. Biol. Chem. (1997) [Pubmed]
  4. Amino acid sequence and characterization of a heparin-binding neurite-promoting factor (p18) from bovine brain. Kuo, M.D., Oda, Y., Huang, J.S., Huang, S.S. J. Biol. Chem. (1990) [Pubmed]
  5. Pleiotrophin inhibits chondrocyte proliferation and stimulates proteoglycan synthesis in mature bovine cartilage. Tapp, H., Hernandez, D.J., Neame, P.J., Koob, T.J. Matrix Biol. (1999) [Pubmed]
  6. Pleiotrophin regulates bone morphogenetic protein (BMP)-induced ectopic osteogenesis. Sato, Y., Takita, H., Ohata, N., Tamura, M., Kuboki, Y. J. Biochem. (2002) [Pubmed]
  7. Mitogenic properties of a new endothelial cell growth factor related to pleiotrophin. Courty, J., Dauchel, M.C., Caruelle, D., Perderiset, M., Barritault, D. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  8. A novel 17 kD heparin-binding growth factor (HBGF-8) in bovine uterus: purification and N-terminal amino acid sequence. Milner, P.G., Li, Y.S., Hoffman, R.M., Kodner, C.M., Siegel, N.R., Deuel, T.F. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
  9. Isolation and identification of midkine and pleiotrophin in bovine follicular fluid. Ohyama, Y., Miyamoto, K., Minamino, N., Matsuo, H. Mol. Cell. Endocrinol. (1994) [Pubmed]
  10. Pleiotrophin is an abundant protein in dissociative extracts of bovine fetal epiphyseal cartilage and nasal cartilage from newborns. Neame, P.J., Young, C.N., Brock, C.W., Treep, J.T., Ganey, T.M., Sasse, J., Rosenberg, L.C. J. Orthop. Res. (1993) [Pubmed]
  11. Construction and biological characterization of an HB-GAM/FGF-1 chimera for vascular tissue engineering. Xue, L., Tassiopoulos, A.K., Woloson, S.K., Stanton, D.L., Ms, C.S., Hampton, B., Burgess, W.H., Greisler, H.P. J. Vasc. Surg. (2001) [Pubmed]
  12. Pig uterine luminal fluid contains the developmentally regulated neurotrophic factor, pleiotrophin. Brigstock, D.R., Kim, G.Y., Steffen, C.L. J. Endocrinol. (1996) [Pubmed]
WikiGenes - Universities