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Gene Review

TNAP  -  TRAFs and NIK-associated protein

Homo sapiens

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Disease relevance of TNAP


High impact information on TNAP

  • We have identified a novel NIK interacting protein, TNAP (for TRAFs and NIK-associated protein) [3].
  • Knockdown of TNAP by lentiviral-mediated small interference RNA potentiates TNF-alpha-induced NF-kappaB activation [3].
  • 8. We also determined the ability of the mutants to metabolize two natural substrates of TNAP, that is, pyridoxal-5'-phosphate (PLP) and inorganic pyrophosphate (PPi), at physiological pH [1].
  • After introducing each single hypophosphatasia mutation, the setTNAP and mutant TNAP cDNAs were expressed in COS-1 cells and the recombinant flagged enzymes were affinity purified [1].
  • We have analyzed the role of the N-terminus and its microenvironment in determining the enzyme stability and catalysis using human placental (PLAP) and tissue-nonspecific AP (TNAP) as paradigms [4].

Biological context of TNAP

  • In addition, retinoic acid plays an essential role in the superinduction of TNAP gene expression by enabling dexamethasone to exert its agonist activity, which otherwise has no effect [5].
  • RESULTS: No difference was observed in the allele or genotype frequencies between patients and controls at either ENPP1 or TNAP [2].
  • METHODS: Exons, untranslated regions (UTR) and exon-intron boundaries of ENPP1 and TNAP were sequenced using ABI Big Dye chemistry on automated sequencers [2].
  • Sixteen variants were identified (3 in ENPP1 and 13 in TNAP) and were subsequently genotyped in 128 sporadic Caucasian CPPD CC patients and 600 healthy controls using a combination of polymerase chain reaction/restriction fragment-length polymorphism analysis or using Taqman [2].

Anatomical context of TNAP


Associations of TNAP with chemical compounds

  • However, the ability of RU486 to antagonize the action of glucocorticoid was greatly compromised in dexamethasone-mediated superinduction of TNAP activity [5].
  • Interestingly, TNAP was found to be the only isozyme activity superinduced when the cells were costimulated with retinoic acid and dexamethasone [5].

Other interactions of TNAP

  • These data suggest that TNAP is a repressor of NIK activity and regulates both the classical and alternative NF-kappaB signaling pathways [3].

Analytical, diagnostic and therapeutic context of TNAP

  • Site-directed mutagenesis was used to introduce a sequence tag into the TNAP cDNA and eliminate the glycosylphosphatidylinositol (GPI)-anchor recognition sequence to produce a secreted epitope-tagged TNAP (setTNAP) [1].
  • Northern blot and RT-PCR analysis were then used to demonstrate that the steady-state TNAP mRNA level was also superinduced, which indicates that the superinduction is regulated at the transcriptional or post-transcriptional levels [5].


  1. Kinetic characterization of hypophosphatasia mutations with physiological substrates. Di Mauro, S., Manes, T., Hessle, L., Kozlenkov, A., Pizauro, J.M., Hoylaerts, M.F., Millán, J.L. J. Bone Miner. Res. (2002) [Pubmed]
  2. Investigation of the role of ENPP1 and TNAP genes in chondrocalcinosis. Zhang, Y., Brown, M.A., Peach, C., Russell, G., Wordsworth, B.P. Rheumatology (Oxford, England) (2007) [Pubmed]
  3. TNAP, a novel repressor of NF-kappaB-inducing kinase, suppresses NF-kappaB activation. Hu, W.H., Mo, X.M., Walters, W.M., Brambilla, R., Bethea, J.R. J. Biol. Chem. (2004) [Pubmed]
  4. Mammalian alkaline phosphatase catalysis requires active site structure stabilization via the N-terminal amino acid microenvironment. Hoylaerts, M.F., Ding, L., Narisawa, S., Van Kerckhoven, S., Millan, J.L. Biochemistry (2006) [Pubmed]
  5. Expression and regulation of alkaline phosphatases in human breast cancer MCF-7 cells. Tsai, L.C., Hung, M.W., Chen, Y.H., Su, W.C., Chang, G.G., Chang, T.C. Eur. J. Biochem. (2000) [Pubmed]
  6. The presence of PHOSPHO1 in matrix vesicles and its developmental expression prior to skeletal mineralization. Stewart, A.J., Roberts, S.J., Seawright, E., Davey, M.G., Fleming, R.H., Farquharson, C. Bone (2006) [Pubmed]
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