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Gene Review

Cpa1  -  carboxypeptidase A1 (pancreatic)

Rattus norvegicus

Synonyms: Carboxypeptidase A1, Cpa
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Disease relevance of Cpa1


High impact information on Cpa1


Biological context of Cpa1


Anatomical context of Cpa1


Associations of Cpa1 with chemical compounds


Other interactions of Cpa1

  • Glucagon1-21 has been prepared by treating native glucagon with carboxypeptidase A. Purified glucagon1-21 did not contain detectable methionine (less than 0.001 residue/mol) and the activity of the compound did not change after treatment with cyanogen bromide as has been shown with native glucagon [19].
  • Only one of the exon/intron junctions of the rat CPE gene is present in a comparable position within the genes for carboxypeptidase-A and -B, both of which are only 17-21% homologous to CPE at the amino acid level [20].
  • Enkephalinase, a zinc-containing metallo enzyme, displays homology with other zinc metallo enzymes such as carboxypeptidase A, B and E, suggesting enzymatic similarities in these enzymes [21].
  • On the other hand, selective inhibition of granule chymase (leaving carboxypeptidase A active) totally abolished the proteolytic degradation of LDL [22].
  • The results are consistent with a model according to which the proteolytic degradation of LDL by mast cell granules results from coordinated action of the two granule-bound enzymes, whereby the chymase first cleaves peptides from the apolipoprotein B of LDL, and thereafter the carboxypeptidase A cleaves amino acids from the peptides formed [22].

Analytical, diagnostic and therapeutic context of Cpa1


  1. Rat preprocarboxypeptidase A: cDNA sequence and preliminary characterization of the gene. Quinto, C., Quiroga, M., Swain, W.F., Nikovits, W.C., Standring, D.N., Pictet, R.L., Valenzuela, P., Rutter, W.J. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  2. Stimulation of rat peritoneal mast cell migration by tumor-derived peptides. Poole, T.J., Zetter, B.R. Cancer Res. (1983) [Pubmed]
  3. Site-directed mutagenesis shows that tyrosine 248 of carboxypeptidase A does not play a crucial role in catalysis. Gardell, S.J., Craik, C.S., Hilvert, D., Urdea, M.S., Rutter, W.J. Nature (1985) [Pubmed]
  4. Substrate specificity of the chymotrypsin-like protease in secretory granules isolated from rat mast cells. Le Trong, H., Neurath, H., Woodbury, R.G. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  5. Cerebral cortical specification by early potential restriction of progenitor cells and later phenotype control of postmitotic neurons. Arimatsu, Y., Ishida, M., Takiguchi-Hayashi, K., Uratani, Y. Development (1999) [Pubmed]
  6. Arginine 127 stabilizes the transition state in carboxypeptidase. Phillips, M.A., Fletterick, R., Rutter, W.J. J. Biol. Chem. (1990) [Pubmed]
  7. Carboxypeptidase A isoforms produced by distinct genes or alternative splicing in brain and other extrapancreatic tissues. Normant, E., Gros, C., Schwartz, J.C. J. Biol. Chem. (1995) [Pubmed]
  8. Rat mast cell carboxypeptidase: amino acid sequence and evidence of enzyme activity within mast cell granules. Cole, K.R., Kumar, S., Trong, H.L., Woodbury, R.G., Walsh, K.A., Neurath, H. Biochemistry (1991) [Pubmed]
  9. Localization of the rat T-cell receptor beta-chain and carboxypeptidase A1 loci to chromosome 4. Dissen, E., Hunt, S.V., Rolstad, B., Fossum, S. Immunogenetics (1993) [Pubmed]
  10. Properties of fructose-1,6-bisphosphate aldolase inactivating enzymes in rat liver lysosomes. Kominami, E., Hashida, S., Katunuma, N. Biochim. Biophys. Acta (1981) [Pubmed]
  11. Changes in carboxypeptidase A, dipeptidase and Na+/K+ ATPase activities in the intestine of rats orally exposed to different doses of cadmium. Eriyamremu, G.E., Asagba, S.O., Onyeneke, E.C., Adaikpoh, M.A. Biometals (2005) [Pubmed]
  12. Localization of carboxypeptidase A to the macromolecular heparin proteoglycan-protein complex in secretory granules of rat serosal mast cells. Schwartz, L.B., Riedel, C., Schratz, J.J., Austen, K.F. J. Immunol. (1982) [Pubmed]
  13. Latexin, a carboxypeptidase A inhibitor, is expressed in rat peritoneal mast cells and is associated with granular structures distinct from secretory granules and lysosomes. Uratani, Y., Takiguchi-Hayashi, K., Miyasaka, N., Sato, M., Jin, M., Arimatsu, Y. Biochem. J. (2000) [Pubmed]
  14. Regulation of proteolytic enzyme activities and mRNA concentrations in rat pancreas by food content. Giorgi, D., Renaud, W., Bernard, J.P., Dagorn, J.C. Biochem. Biophys. Res. Commun. (1985) [Pubmed]
  15. Localization of carboxypeptidase A-like enzyme in rat kidney. Igić, R., Garber, S., Sekosan, M., Urbanska, R.A., Behnia, R. Peptides (2003) [Pubmed]
  16. Rat muscle 5'-adenylic acid aminohydrolase. I. Purification and subunit structure. Coffee, C.J., Kofke, W.A. J. Biol. Chem. (1975) [Pubmed]
  17. Divalent cation and prenyl pyrophosphate specificities of the protein farnesyltransferase from rat brain, a zinc metalloenzyme. Reiss, Y., Brown, M.S., Goldstein, J.L. J. Biol. Chem. (1992) [Pubmed]
  18. S-Adenosylhomocysteinase from rat liver. Evidence for structurally identical and catalytically equivalent subunits. Gomi, T., Ishiguro, Y., Fujioka, M. J. Biol. Chem. (1985) [Pubmed]
  19. A reassessment of structure-function relationships in glucagon. Glucagon1-21 is a full agonist. Wright, D.E., Hruby, V.J., Rodbell, M. J. Biol. Chem. (1978) [Pubmed]
  20. Structural characterization of the rat carboxypeptidase-E gene. Jung, Y.K., Kunczt, C.J., Pearson, R.K., Dixon, J.E., Fricker, L.D. Mol. Endocrinol. (1991) [Pubmed]
  21. Molecular cloning and amino acid sequence of rat enkephalinase. Malfroy, B., Schofield, P.R., Kuang, W.J., Seeburg, P.H., Mason, A.J., Henzel, W.J. Biochem. Biophys. Res. Commun. (1987) [Pubmed]
  22. Low density lipoprotein degradation by secretory granules of rat mast cells. Sequential degradation of apolipoprotein B by granule chymase and carboxypeptidase A. Kokkonen, J.O., Vartiainen, M., Kovanen, P.T. J. Biol. Chem. (1986) [Pubmed]
  23. Intracellular activation of digestive zymogens in rat pancreatic acini. Stimulation by high doses of cholecystokinin. Leach, S.D., Modlin, I.M., Scheele, G.A., Gorelick, F.S. J. Clin. Invest. (1991) [Pubmed]
  24. Immunohistochemical localization of pancreatic exocrine enzymes in normal and neoplastic pancreatic acinar epithelium of rat. Hansen, L.J., Mangkornkanok/Mark, M., Reddy, J.K. J. Histochem. Cytochem. (1981) [Pubmed]
  25. Conversion of Met-enkephalin-Arg6-Phe7 by a purified brain carboxypeptidase (cathepsin A). Marks, N., Sachs, L., Stern, F. Peptides (1981) [Pubmed]
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