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Gene Review

GUCA2A  -  guanylate cyclase activator 2A (guanylin)

Homo sapiens

Synonyms: GCAP-I, GUCA2, Guanylate cyclase activator 2A, Guanylate cyclase-activating protein 1, Guanylate cyclase-activating protein I, ...
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Disease relevance of GUCA2A


High impact information on GUCA2A


Chemical compound and disease context of GUCA2A


Biological context of GUCA2A


Anatomical context of GUCA2A

  • CONCLUSIONS: Based on the present findings and on the functional role of guanylin in other epithelia, it is likely that gallbladder epithelial cells synthesize and release guanylin into the bile to regulate electrolyte secretion by a paracrine/luminocrine signaling pathway [19].
  • RESULTS: Guanylin and its affiliated signaling proteins are highly expressed in the human gallbladder [19].
  • A 15-amino acid peptide, guanylin, was recently purified from rat jejunum and proposed to be a potential endogenous activator of this receptor [14].
  • Thus, guanylin is synthesized by gut enterochromaffin cells as a prohormone of 115 amino acids and is processed to the molecular form of 94 amino acids circulating in the blood [15].
  • Northern blot and in situ hybridization show high-level expression of guanylin mRNA restricted to the intestine, with localization to Paneth cells at the base of the small intestinal crypts [14].

Associations of GUCA2A with chemical compounds


Physical interactions of GUCA2A


Regulatory relationships of GUCA2A

  • Pretreatment with ANP (0.03 nM) enhanced guanylin (0.19 muM) natriuretic activity (%ENa(+); from 18.5+/-4.25 to 31.5+/-1.69, P<0.05, 120 min) and its kaliuretic activity (%EK(+); from 24.5+/-4.43 to 50.6+/-3.84, P<0.05, 120 min) [24].
  • UROD (0.03 nM) also enhanced the guanylin-induced natriuresis (to %ENa(+)=31.0+/-1.93, P<0.05, 120 min) and kaliuresis (to %EK(+)=54.2+/-3.61, P<0.05, 120 min), and inhibited the %ENa(+) of uroguanylin (0.31 muM) to 17.9+/-1.67 as well as its %EK(+) to 24.3+/-3.13 (both at 120 min, P<0.05) [24].

Other interactions of GUCA2A


Analytical, diagnostic and therapeutic context of GUCA2A


  1. Guanylin and functional coupling proteins in the human salivary glands and gland tumors : expression, cellular localization, and target membrane domains. Kulaksiz, H., Rehberg, E., Stremmel, W., Cetin, Y. Am. J. Pathol. (2002) [Pubmed]
  2. Receptors for Escherichia coli heat stable enterotoxin in human intestine and in a human intestinal cell line (Caco-2). Cohen, M.B., Jensen, N.J., Hawkins, J.A., Mann, E.A., Thompson, M.R., Lentze, M.J., Giannella, R.A. J. Cell. Physiol. (1993) [Pubmed]
  3. Uroguanylin treatment suppresses polyp formation in the Apc(Min/+) mouse and induces apoptosis in human colon adenocarcinoma cells via cyclic GMP. Shailubhai, K., Yu, H.H., Karunanandaa, K., Wang, J.Y., Eber, S.L., Wang, Y., Joo, N.S., Kim, H.D., Miedema, B.W., Abbas, S.Z., Boddupalli, S.S., Currie, M.G., Forte, L.R. Cancer Res. (2000) [Pubmed]
  4. Targeted inactivation of the mouse guanylin gene results in altered dynamics of colonic epithelial proliferation. Steinbrecher, K.A., Wowk, S.A., Rudolph, J.A., Witte, D.P., Cohen, M.B. Am. J. Pathol. (2002) [Pubmed]
  5. Uroguanylin and guanylin peptides: pharmacology and experimental therapeutics. Forte, L.R. Pharmacol. Ther. (2004) [Pubmed]
  6. Turned on by Ca2+! The physiology and pathology of Ca(2+)-binding proteins in the retina. Polans, A., Baehr, W., Palczewski, K. Trends Neurosci. (1996) [Pubmed]
  7. Regulation of taurine transport by Escherichia coli heat-stable enterotoxin and guanylin in human intestinal cell lines. Brandsch, M., Ramamoorthy, S., Marczin, N., Catravas, J.D., Leibach, J.W., Ganapathy, V., Leibach, F.H. J. Clin. Invest. (1995) [Pubmed]
  8. Guanylin stimulation of Cl- secretion in human intestinal T84 cells via cyclic guanosine monophosphate. Forte, L.R., Eber, S.L., Turner, J.T., Freeman, R.H., Fok, K.F., Currie, M.G. J. Clin. Invest. (1993) [Pubmed]
  9. Differential role of cyclic GMP-dependent protein kinase II in ion transport in murine small intestine and colon. Vaandrager, A.B., Bot, A.G., Ruth, P., Pfeifer, A., Hofmann, F., De Jonge, H.R. Gastroenterology (2000) [Pubmed]
  10. Guanylin stimulates regulated secretion from human neuroendocrine pancreatic cells. John, M., Wiedenmann, B., Kruhøffer, M., Adermann, K., Ankorina-Stark, I., Schlatter, E., Ahnert-Hilger, G., Forssmann, W.G., Kuhn, M. Gastroenterology (1998) [Pubmed]
  11. A role for guanylate cyclase C in acid-stimulated duodenal mucosal bicarbonate secretion. Rao, S.P., Sellers, Z., Crombie, D.L., Hogan, D.L., Mann, E.A., Childs, D., Keely, S., Sheil-Puopolo, M., Giannella, R.A., Barrett, K.E., Isenberg, J.I., Pratha, V.S. Am. J. Physiol. Gastrointest. Liver Physiol. (2004) [Pubmed]
  12. Circulating and tissue guanylin immunoreactivity in intestinal secretory diarrhoea. Kuhn, M., Kulaksiz, H., Cetin, Y., Frank, M., Nold, R., Arnold, R., Böker, K., Bischoff, S.C., Manns, M.P., Forssmann, W.G. Eur. J. Clin. Invest. (1995) [Pubmed]
  13. Tissue distribution and plasma concentration of human guanylin. Date, Y., Nakazato, M., Yamaguchi, H., Miyazato, M., Matsukura, S. Intern. Med. (1996) [Pubmed]
  14. Precursor structure, expression, and tissue distribution of human guanylin. de Sauvage, F.J., Keshav, S., Kuang, W.J., Gillett, N., Henzel, W., Goeddel, D.V. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  15. Analysis of the human guanylin gene and the processing and cellular localization of the peptide. Hill, O., Kuhn, M., Zucht, H.D., Cetin, Y., Kulaksiz, H., Adermann, K., Klock, G., Rechkemmer, G., Forssmann, W.G., Mägert, H.J. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  16. Guanylin and uroguanylin regulate electrolyte transport in isolated human cortical collecting ducts. Sindić, A., Hirsch, J.R., Velic, A., Piechota, H., Schlatter, E. Kidney Int. (2005) [Pubmed]
  17. GCAP-II: isolation and characterization of the circulating form of human uroguanylin. Hess, R., Kuhn, M., Schulz-Knappe, P., Raida, M., Fuchs, M., Klodt, J., Adermann, K., Kaever, V., Cetin, Y., Forssmann, W.G. FEBS Lett. (1995) [Pubmed]
  18. Human guanylin: cDNA isolation, structure, and activity. Wiegand, R.C., Kato, J., Huang, M.D., Fok, K.F., Kachur, J.F., Currie, M.G. FEBS Lett. (1992) [Pubmed]
  19. Guanylin regulates chloride secretion in the human gallbladder via the bile fluid. Kulaksiz, H., Schlenker, T., Rost, D., Stiehl, A., Volkmann, M., Lehnert, T., Cetin, Y., Stremmel, W. Gastroenterology (2004) [Pubmed]
  20. Guanylin, uroguanylin, and heat-stable euterotoxin activate guanylate cyclase C and/or a pertussis toxin-sensitive G protein in human proximal tubule cells. Sindiće, A., Başoglu, C., Cerçi, A., Hirsch, J.R., Potthast, R., Kuhn, M., Ghanekar, Y., Visweswariah, S.S., Schlatter, E. J. Biol. Chem. (2002) [Pubmed]
  21. Solution structure of human proguanylin: the role of a hormone prosequence. Lauber, T., Neudecker, P., Rösch, P., Marx, U.C. J. Biol. Chem. (2003) [Pubmed]
  22. Escherichia coli heat-stable enterotoxins, guanylins, and their receptors: what are they and what do they do? Giannella, R.A. J. Lab. Clin. Med. (1995) [Pubmed]
  23. Guanylin mRNA expression in human intestine and colorectal adenocarcinoma. Cohen, M.B., Hawkins, J.A., Witte, D.P. Lab. Invest. (1998) [Pubmed]
  24. Interaction of atrial natriuretic peptide, urodilatin, guanylin and uroguanylin in the isolated perfused rat kidney. Santos-Neto, M.S., Carvalho, A.F., Monteiro, H.S., Forte, L.R., Fonteles, M.C. Regul. Pept. (2006) [Pubmed]
  25. Mutations in the gene coding for guanylate cyclase-activating protein 2 (GUCA1B gene) in patients with autosomal dominant retinal dystrophies. Sato, M., Nakazawa, M., Usui, T., Tanimoto, N., Abe, H., Ohguro, H. Graefes Arch. Clin. Exp. Ophthalmol. (2005) [Pubmed]
  26. Uroguanylin: gene structure, expression, processing as a peptide hormone, and co-storage with somatostatin in gastrointestinal D-cells. Mägert, H.J., Reinecke, M., David, I., Raab, H.R., Adermann, K., Zucht, H.D., Hill, O., Hess, R., Forssmann, W.G. Regul. Pept. (1998) [Pubmed]
  27. Identification and functional consequences of a new mutation (E155G) in the gene for GCAP1 that causes autosomal dominant cone dystrophy. Wilkie, S.E., Li, Y., Deery, E.C., Newbold, R.J., Garibaldi, D., Bateman, J.B., Zhang, H., Lin, W., Zack, D.J., Bhattacharya, S.S., Warren, M.J., Hunt, D.M., Zhang, K. Am. J. Hum. Genet. (2001) [Pubmed]
  28. Detailed localization of photoreceptor guanylate cyclase activating protein-1 and -2 in mammalian retinas using light and electron microscopy. Kachi, S., Nishizawa, Y., Olshevskaya, E., Yamazaki, A., Miyake, Y., Wakabayashi, T., Dizhoor, A., Usukura, J. Exp. Eye Res. (1999) [Pubmed]
  29. The destabilization of human GCAP1 by a proline to leucine mutation might cause cone-rod dystrophy. Newbold, R.J., Deery, E.C., Walker, C.E., Wilkie, S.E., Srinivasan, N., Hunt, D.M., Bhattacharya, S.S., Warren, M.J. Hum. Mol. Genet. (2001) [Pubmed]
  30. A novel guanylin family (guanylin, uroguanylin, and renoguanylin) in eels: possible osmoregulatory hormones in intestine and kidney. Yuge, S., Inoue, K., Hyodo, S., Takei, Y. J. Biol. Chem. (2003) [Pubmed]
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