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Gene Review

Acp5  -  acid phosphatase 5, tartrate resistant

Rattus norvegicus

Synonyms: TR-AP, TTRRAP, Tartrate-resistant acid ATPase, Tartrate-resistant acid phosphatase type 5, TrATPase, ...
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Disease relevance of Acp5

  • Our observation of extracellular localization, in particular accumulation of TrATPase in bone matrix facing the ruffled border area of the osteoclasts, favors the view that the enzyme is exported to areas of active bone resorption, thereby indicating a potential role for the enzyme in this process [1].

High impact information on Acp5

  • Thus, despite the apparent similarity of this osteoclastic TRAP/TrATPase with type 5, tartrate-resistant and purple, acid phosphatases expressed in other mammalian tissues, this gene appears to be preferentially expressed at skeletal sites [2].
  • We now report the isolation of a 1397-base pair (bp) full-length TRAP/tartrate-resistant acid ATPase (TrATPase) cDNA clone from a neonatal rat calvaria lambda gt11 cDNA library [2].
  • In neonatal rats, TRAP/TrATPase mRNA was highly expressed in skeletal tissues, with much lower (less than 10%) levels detected in spleen, thymus, liver, skin, brain, kidney, brain, lung, and heart [2].
  • The findings that TrATPase has a spherical shape and binds low amounts of detergent suggest that the enzyme is a soluble protein, compatible with the view that TrATPase is secreted by the osteoclast [3].
  • Current histochemical, immunohistochemical, and in situ hybridization studies of rat and canine bones confirmed TRAP enzyme activity, TRAP immunoreactivity, and the expression of Trap mRNA signals in osteocytes located close to the bone-resorbing surface [4].

Biological context of Acp5

  • Spatial and temporal patterns of TRAP/Trap expression in the osteocytes should serve as a valuable parameter for further analyses of biological interactions between the osteocytes and the osteoclasts associated with bone remodeling [4].
  • TRAP/Trap- positive osteocytes thus identified were confined to the areas no further than 200 microm from the bone-resorbing surface and showed apparent upregulation of TRAP/Trap expression toward the active osteoclasts [4].

Anatomical context of Acp5

  • Combined with the Purge and Trap using a gas chromatography-mass spectrometry (GC-MS) system, it is very useful to detect the trace amounts of metabolites in primary rat hepatocytes [5].
  • Comparison of the biochemically measured TRAP and TrATPase activities showed that bone had the highest specific activity for both enzymes followed by the bone marrow and spleen [6].

Other interactions of Acp5


  1. Ultrastructural localization of a tartrate-resistant acid ATPase in bone. Reinholt, F.P., Widholm, S.M., Ek-Rylander, B., Andersson, G. J. Bone Miner. Res. (1990) [Pubmed]
  2. Cloning, sequence, and developmental expression of a type 5, tartrate-resistant, acid phosphatase of rat bone. Ek-Rylander, B., Bill, P., Norgård, M., Nilsson, S., Andersson, G. J. Biol. Chem. (1991) [Pubmed]
  3. Characterization of a tartrate-resistant acid phosphatase (ATPase) from rat bone: hydrodynamic properties and N-terminal amino acid sequence. Ek-Rylander, B., Bergman, T., Andersson, G. J. Bone Miner. Res. (1991) [Pubmed]
  4. Eccentric localization of osteocytes expressing enzymatic activities, protein, and mRNA signals for type 5 tartrate-resistant acid phosphatase (TRAP). Nakano, Y., Toyosawa, S., Takano, Y. J. Histochem. Cytochem. (2004) [Pubmed]
  5. Metabolites of diallyl disulfide and diallyl sulfide in primary rat hepatocytes. Sheen, L.Y., Wu, C.C., Lii, C.K., Tsai, S.J. Food Chem. Toxicol. (1999) [Pubmed]
  6. Histochemistry and biochemistry of tartrate-resistant acid phosphatase (TRAP) and tartrate-resistant acid adenosine triphosphatase (TrATPase) in bone, bone marrow and spleen: implications for osteoclast ontogeny. Lindunger, A., MacKay, C.A., Ek-Rylander, B., Andersson, G., Marks, S.C. Bone and mineral. (1990) [Pubmed]
  7. The effects of colony-stimulating factor-1 on tooth eruption in the toothless (osteopetrotic) rat in relation to the critical periods for bone resorption during tooth eruption. Iizuka, T., Cielinski, M., Aukerman, S.L., Marks, S.C. Arch. Oral Biol. (1992) [Pubmed]
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