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Gene Review

TPI1  -  triosephosphate isomerase 1

Bos taurus

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High impact information on TPI1

  • Flow cytometric analysis of DNA content and synthesis in BASMCs treated with TPI-1 or calpeptin additionally revealed the presence of a distinct cell cycle block in the G2-M compartment [1].
  • By Northern analysis of mRNA after serum addition, TPI-1 caused a fourfold decrease in the transient elevation of fos and myc proto-oncogene as well as a decrease in the levels of both muscle and nonmuscle actin mRNA induced early after serum addition [1].
  • The kinetics of the reverse reaction were studied by coupling the phosphatase reaction to the aldolase, triosephosphate isomerase, and glycerolphosphate dehydrogenase reactions [2].
  • The strong inhibition of triosephosphate isomerase by the natural beta-carbolines may explain their neurotoxic actions [3].
  • The location of the triose phosphate isomerase (TPI1) gene and one of the nucleolar organizer regions (RNR) on sheep 3q was confirmed by Southern analysis [4].

Biological context of TPI1

  • The cell cycle progression block was gradually lost as the delay from serum to TPI-1 application was increased from 6 to 12 hours [1].

Anatomical context of TPI1


  1. Effects of thiol protease inhibitors on cell cycle and proliferation of vascular smooth muscle cells in culture. March, K.L., Wilensky, R.L., Roeske, R.W., Hathaway, D.R. Circ. Res. (1993) [Pubmed]
  2. Kinetic studies of bovine liver fructose-1,6-bisphosphatase. Casazza, J.P., Stone, S.R., Fromm, H.J. J. Biol. Chem. (1979) [Pubmed]
  3. The strong inhibition of triosephosphate isomerase by the natural beta-carbolines may explain their neurotoxic actions. Bonnet, R., Pavlovic, S., Lehmann, J., Rommelspacher, H. Neuroscience (2004) [Pubmed]
  4. Mapping of MYF5, C1R, MYHL, TPI1, IAPP, A2MR and RNR onto sheep chromosome 3q. Broad, T.E., Burkin, D.J., Jones, C., Lewis, P.E., Ansari, H.A., Pearce, P.D. Anim. Genet. (1993) [Pubmed]
  5. Thermostability characteristics of glucosephosphate and triosephosphate isomerase in erythrocytes from several species. Naidu, J.M., Turner, T.R., Mohrenweiser, H.W. Comp. Biochem. Physiol., B (1984) [Pubmed]
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