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Gene Review

Ppp6c  -  protein phosphatase 6, catalytic subunit

Mus musculus

Synonyms: 2310003C10Rik, PP6C, Serine/threonine-protein phosphatase 6 catalytic subunit
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Disease relevance of Ppp6c

  • PP6, a representative of the first group, recognizes an epitope shared by smooth-type Bordetella parapertussis and Bordetella bronchiseptica lipopolysaccharides (LPS) [1].

High impact information on Ppp6c

  • We measured in rat aorta rings the relaxant activity of a number of peptides derived from the activating sequence (SLIGRL, or PP6) of the proteinase-activated receptor-2 (PAR-2) [2].
  • 6. The contractile actions of PP6 and PP6-NH2 in the rat gastric preparation required the presence of extracellular calcium, were inhibited by nifedipine and were blocked by the cyclo-oxygenase inhibitor, indomethacin and by the tyrosine kinase inhibitor, genistein, but not by the kinase C inhibitor, GF109203X [3].
  • Between days 2-7 post-transplant, both allogenic fibroblasts and PP6 myogenic stem cells maintained survivability in similar numbers [4].
  • Outside the pancreas, no localizations were obtained with anti-hPP antiserum, whereas antiserum to PP6 demonstrated immunoreactivity in a variety of tissues including gut glucagon cells, adrenal chromaffin cells, and nerve fibres in the gastrointestinal tract and adrenal gland [5].
  • The protein serine/threonine phosphatase (PP) type 2A family consists of three members: PP2A, PP4, and PP6 [6].

Biological context of Ppp6c

  • PP2A, PP4, and PP6 catalytic subunits (PP2A(C), PP4(C), and PP6(C), respectively) were detected in all rat tissue extracts examined and exhibited some differences in their levels of expression [6].


  1. Specific and cross-reacting monoclonal antibodies to Bordetella parapertussis and Bordetella bronchiseptica lipopolysaccharides. Le Blay, K., Caroff, M., Richards, J.C., Perry, M.B., Chaby, R. Microbiology (Reading, Engl.) (1994) [Pubmed]
  2. Proteinase-activated receptor-2 in rat aorta: structural requirements for agonist activity of receptor-activating peptides. Hollenberg, M.D., Saifeddine, M., al-Ani, B. Mol. Pharmacol. (1996) [Pubmed]
  3. Rat proteinase-activated receptor-2 (PAR-2): cDNA sequence and activity of receptor-derived peptides in gastric and vascular tissue. Saifeddine, M., al-Ani, B., Cheng, C.H., Wang, L., Hollenberg, M.D. Br. J. Pharmacol. (1996) [Pubmed]
  4. Transplantation of virally transduced cells into the dermis of immunocompetent and immunodeficient (SCID) mice to determine gene expression profile and differential donor cell survival. Radfar, A.J., Robbins, P.D., Huard, J., Rosas, F.R., Dohar, J.E., Hebda, P.A. Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society. (2000) [Pubmed]
  5. Demonstration of carboxyl-terminal PP-like peptides in endocrine cells and nerves. Vaillant, C., Taylor, I.L. Peptides (1981) [Pubmed]
  6. Parallel purification of three catalytic subunits of the protein serine/threonine phosphatase 2A family (PP2A(C), PP4(C), and PP6(C)) and analysis of the interaction of PP2A(C) with alpha4 protein. Kloeker, S., Reed, R., McConnell, J.L., Chang, D., Tran, K., Westphal, R.S., Law, B.K., Colbran, R.J., Kamoun, M., Campbell, K.S., Wadzinski, B.E. Protein Expr. Purif. (2003) [Pubmed]
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