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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

Prss8  -  protease, serine 8 (prostasin)

Mus musculus

Synonyms: 2410039E18Rik, AI313909, C79772, CAP1, Cap1, ...
 
 
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High impact information on Prss8

  • The epidermal barrier function is dependent on the serine protease CAP1/Prss8 [1].
  • Here we use a retroviral expression system to identify Cap1, a 31-kDa protein from C. trachomatis recognized by protective CD8(+) T cells [2].
  • The pyrophosphatase and alkaline phosphatase digestion products of the globin Cap 1 and Cap 2 core structures were analyzed by high voltage electrophoresis and paper chromatography and found to be 7-methyiguanosine (m7G) and the dimethylated nucleoside 6-methyl-2'-O-methyladenosine (N6mAm) [3].
  • It is concluded that auto- and heterocatalytic requirements are specific for each CAP and that endogenous partners are a necessity for activation of ENaC by mCAP in the Xenopus oocyte expression system [4].
  • Mouse channel activating proteases 1, 2, and 3 (mCAP1, mCAP2, and mCAP3) were described recently as regulators of the epithelial sodium channel (ENaC) [4].
 

Biological context of Prss8

  • Various point mutations were introduced in the catalytic or protein-protein interacting domains of mCAP and wild-type and mutant enzymes were expressed in the Xenopus oocyte expression system to test for ability to activate ENaC [4].
 

Anatomical context of Prss8

  • Recent in vitro and in vivo experiments indicate that membrane-bound serine proteases (channel activating proteases [CAP-1, -2, or-3]) may be of critical importance in the activation of ENaC in different organs, such as the kidney, the lung or the cochlea [5].
 

Other interactions of Prss8

  • Synergistic activation of ENaC by three membrane-bound channel-activating serine proteases (mCAP1, mCAP2, and mCAP3) and serum- and glucocorticoid-regulated kinase (Sgk1) in Xenopus Oocytes [6].
 

Analytical, diagnostic and therapeutic context of Prss8

  • Immunofluorescence microscopy by using Cap1-specific antibody demonstrates that this protein is localized to the vacuolar membrane [2].
  • Specific antibodies against each mCAP were developed to distinguish between proenzyme and active protease by Western blot analysis [4].

References

  1. The epidermal barrier function is dependent on the serine protease CAP1/Prss8. Leyvraz, C., Charles, R.P., Rubera, I., Guitard, M., Rotman, S., Breiden, B., Sandhoff, K., Hummler, E. J. Cell Biol. (2005) [Pubmed]
  2. CD8+ T cells recognize an inclusion membrane-associated protein from the vacuolar pathogen Chlamydia trachomatis. Fling, S.P., Sutherland, R.A., Steele, L.N., Hess, B., D'Orazio, S.E., Maisonneuve, J., Lampe, M.F., Probst, P., Starnbach, M.N. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  3. Methylated nucleosides in globin mRNA from mouse nucleated erythroid cells. Heckle, W.L., Fenton, R.G., Wood, T.G., Merkel, C.G., Lingrel, J.B. J. Biol. Chem. (1977) [Pubmed]
  4. Activation of epithelial sodium channels by mouse channel activating proteases (mCAP) expressed in Xenopus oocytes requires catalytic activity of mCAP3 and mCAP2 but not mCAP1. Andreasen, D., Vuagniaux, G., Fowler-Jaeger, N., Hummler, E., Rossier, B.C. J. Am. Soc. Nephrol. (2006) [Pubmed]
  5. The epithelial sodium channel: activation by membrane-bound serine proteases. Rossier, B.C. Proceedings of the American Thoracic Society. (2004) [Pubmed]
  6. Synergistic activation of ENaC by three membrane-bound channel-activating serine proteases (mCAP1, mCAP2, and mCAP3) and serum- and glucocorticoid-regulated kinase (Sgk1) in Xenopus Oocytes. Vuagniaux, G., Vallet, V., Jaeger, N.F., Hummler, E., Rossier, B.C. J. Gen. Physiol. (2002) [Pubmed]
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