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Volumn 278, Issue 2 47-2, 2000, Pages

Guanylin peptides: Renal actions mediated by cyclic GMP

Author keywords

Guanylate cyclase; Heat stable enterotoxins of Escherichia coli; Intestinal natriuretic peptides; Intestine; Urinary sodium excretion

Indexed keywords

BICARBONATE; CELL SURFACE RECEPTOR; CHLORIDE; CYCLIC GMP; ESCHERICHIA COLI ENTEROTOXIN; GUANYLATE CYCLASE; GUANYLIN; UROGUANYLIN;

EID: 0034094386     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.2000.278.2.f180     Document Type: Review
Times cited : (68)

References (71)
  • 1
    • 0028402534 scopus 로고
    • Characterization of a chymotrypsin-like hydrolytic activity in the opossum kidney cell
    • Arao, M., T. Yamaguchi, T. Sugimoto, M. Fukase, and K. Chihara. Characterization of a chymotrypsin-like hydrolytic activity in the opossum kidney cell. Biochem. Cell Biol. 72: 157-162, 1994.
    • (1994) Biochem. Cell Biol. , vol.72 , pp. 157-162
    • Arao, M.1    Yamaguchi, T.2    Sugimoto, T.3    Fukase, M.4    Chihara, K.5
  • 2
    • 0032509484 scopus 로고    scopus 로고
    • Neurobiology of the Caenorhabditis elegans genome
    • Bargmann, C. I. Neurobiology of the Caenorhabditis elegans genome. Science 282: 2028-2033, 1998.
    • (1998) Science , vol.282 , pp. 2028-2033
    • Bargmann, C.I.1
  • 3
    • 0018188478 scopus 로고
    • Evidence for a splanchnic sodium input monitor regulating renal sodium excretion in man: Lack of dependence upon aldosterone
    • Carey, R. M. Evidence for a splanchnic sodium input monitor regulating renal sodium excretion in man: lack of dependence upon aldosterone. Circ. Res. 43: 19-23, 1978.
    • (1978) Circ. Res. , vol.43 , pp. 19-23
    • Carey, R.M.1
  • 4
    • 0027432394 scopus 로고
    • The Escherichia coli heat-stable enterotoxin is a long-lived superagonist of guanylin
    • Carpick, B. W., and J. Gariepy. The Escherichia coli heat-stable enterotoxin is a long-lived superagonist of guanylin. Infect. Immun. 61: 4710-4715, 1993.
    • (1993) Infect. Immun. , vol.61 , pp. 4710-4715
    • Carpick, B.W.1    Gariepy, J.2
  • 6
    • 0028199621 scopus 로고
    • Enterochromaffin cells of the digestive system: Cellular source of guanylin, a guanylate cyclase-activating peptide
    • Cetin, Y., M. Kuhn, H. Kulaksiz, K. Adermann, G. Bargsten, D. Grube, and W-G. Forssmann. Enterochromaffin cells of the digestive system: cellular source of guanylin, a guanylate cyclase-activating peptide. Proc. Natl. Acad. Sci. USA. 91: 2935-2939, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2935-2939
    • Cetin, Y.1    Kuhn, M.2    Kulaksiz, H.3    Adermann, K.4    Bargsten, G.5    Grube, D.6    Forssmann, W.-G.7
  • 7
    • 0026727720 scopus 로고
    • A gradient in expression of the Escherichia coli heat-stable enterotoxin receptor exists along the villus-to-crypt axis of rat small intestine
    • Cohen, M. B., E. A. Mann, C. Lau, S. J. Henning, and R. A. Giannella. A gradient in expression of the Escherichia coli heat-stable enterotoxin receptor exists along the villus-to-crypt axis of rat small intestine. Biochem. Biophys. Res. Commun. 189: 483-490, 1992.
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 483-490
    • Cohen, M.B.1    Mann, E.A.2    Lau, C.3    Henning, S.J.4    Giannella, R.A.5
  • 8
    • 0029052539 scopus 로고
    • Immunohistochemical localization of guanylin in the rat small intestine and colon
    • Cohen, M. B., D. P. Witte, J. A. Hawkins, and M. G. Currie. Immunohistochemical localization of guanylin in the rat small intestine and colon. Biochem. Biophys. Res. Commun. 209: 803-808, 1995.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 803-808
    • Cohen, M.B.1    Witte, D.P.2    Hawkins, J.A.3    Currie, M.G.4
  • 11
    • 0019352579 scopus 로고
    • A rapid and potent natriuretic response to intravenous injection of atrial myocardial extract in rats
    • De Bold, A. J., H. B. Borenstein, A. T. Veress, and H. Sonnenberg. A rapid and potent natriuretic response to intravenous injection of atrial myocardial extract in rats. Life Sci. 28: 89-94, 1981.
    • (1981) Life Sci. , vol.28 , pp. 89-94
    • De Bold, A.J.1    Borenstein, H.B.2    Veress, A.T.3    Sonnenberg, H.4
  • 13
    • 0029985322 scopus 로고    scopus 로고
    • Uroguanylin: Cloning of preprouroguanylin cDNA, mRNA expression in the intestine and heart and isolation of uroguanylin and prouroguanylin from plasma
    • Fan, X., F. K. Hamra, R. H. Freeman, S. L. Eber, W. J. Krause, R. W. Lim, V. M. Pace, M. G. Currie, and L. R. Forte. Uroguanylin: cloning of preprouroguanylin cDNA, mRNA expression in the intestine and heart and isolation of uroguanylin and prouroguanylin from plasma. Biochem. Biophys. Res. Commun. 219: 457-462, 1996.
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 457-462
    • Fan, X.1    Hamra, F.K.2    Freeman, R.H.3    Eber, S.L.4    Krause, W.J.5    Lim, R.W.6    Pace, V.M.7    Currie, M.G.8    Forte, L.R.9
  • 15
    • 0030830202 scopus 로고    scopus 로고
    • Signaling pathways for guanylin and uroguanylin in the digestive, renal, central nervous, reproductive and lymphoid systems
    • Fan, X., Y. Wang, R. M. London, S. L. Eber, W. J. Krause, R. H. Freeman, and L. R. Forte. Signaling pathways for guanylin and uroguanylin in the digestive, renal, central nervous, reproductive and lymphoid systems. Endocrinology 138: 4636-4648, 1997.
    • (1997) Endocrinology , vol.138 , pp. 4636-4648
    • Fan, X.1    Wang, Y.2    London, R.M.3    Eber, S.L.4    Krause, W.J.5    Freeman, R.H.6    Forte, L.R.7
  • 16
    • 0011155218 scopus 로고
    • Heat-stable enterotoxin of Escherichia coli: In vitro effects on guanylate cyclase activity, cyclic GMP concentration, and ion transport in small intestine
    • Field, M., L. H. Graf, Jr., W. J. Laird, and P. L. Smith. Heat-stable enterotoxin of Escherichia coli: in vitro effects on guanylate cyclase activity, cyclic GMP concentration, and ion transport in small intestine. Proc. Natl. Acad. Sci. USA 75: 2800-2804, 1978.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 2800-2804
    • Field, M.1    Graf Jr., L.H.2    Laird, W.J.3    Smith, P.L.4
  • 17
    • 4243308785 scopus 로고    scopus 로고
    • Natriuretic activity of lymphoguanylin in the isolated perfused rat kidney
    • Fonteles, M. C., A. F. Carvalho, G. R. Coelho, H. A. S. Monteiro, and L. R. Forte. Natriuretic activity of lymphoguanylin in the isolated perfused rat kidney (Abstract). FASEB J. 13: A727, 1999.
    • (1999) FASEB J. , vol.13
    • Fonteles, M.C.1    Carvalho, A.F.2    Coelho, G.R.3    Monteiro, H.A.S.4    Forte, L.R.5
  • 23
    • 0028784412 scopus 로고
    • Isotype-specific activation of cystic fibrosis transmembrane conductance regulator-chloride channels by cGMP-dependent protein kinase II
    • French, P. J., J. Bijman, M. Edixhoven, A. B. Vaandrager, B. J. Scholte, S. M. Lohmann, A. C. Nairn, and H. R. de Jonge. Isotype-specific activation of cystic fibrosis transmembrane conductance regulator-chloride channels by cGMP-dependent protein kinase II. J. Biol. Chem. 270: 26626-26631, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26626-26631
    • French, P.J.1    Bijman, J.2    Edixhoven, M.3    Vaandrager, A.B.4    Scholte, B.J.5    Lohmann, S.M.6    Nairn, A.C.7    De Jonge, H.R.8
  • 24
    • 0031157166 scopus 로고    scopus 로고
    • Comparison of effects of uroguanylin, guanylin, Escherichia coli heat-stable enterotoxin STa in mouse intestine and kidney: Evidence that uroguanylin is an intestinal natriuretic hormone
    • Greenberg, R. N., M. Hill, J. Crytzer, W. J. Krause, S. L. Eber, F. K. Hamra, and L. R. Forte. Comparison of effects of uroguanylin, guanylin, Escherichia coli heat-stable enterotoxin STa in mouse intestine and kidney: evidence that uroguanylin is an intestinal natriuretic hormone. J. Invest. Med. 45: 276-282, 1997.
    • (1997) J. Invest. Med. , vol.45 , pp. 276-282
    • Greenberg, R.N.1    Hill, M.2    Crytzer, J.3    Krause, W.J.4    Eber, S.L.5    Hamra, F.K.6    Forte, L.R.7
  • 26
    • 0030025049 scopus 로고    scopus 로고
    • Prouroguanylin and proguanylin: Purification from colon, structure, and modulation of bioactivity by proteases
    • Hamra, F. K., X. Fan, W. J. Krause, R. H. Freeman, D. T. Chin, C. E. Smith, M. G. Currie, and L. R. Forte. Prouroguanylin and proguanylin: purification from colon, structure, and modulation of bioactivity by proteases. Endocrinology 137: 257-265, 1996.
    • (1996) Endocrinology , vol.137 , pp. 257-265
    • Hamra, F.K.1    Fan, X.2    Krause, W.J.3    Freeman, R.H.4    Chin, D.T.5    Smith, C.E.6    Currie, M.G.7    Forte, L.R.8
  • 29
    • 0014670941 scopus 로고
    • Guanyl cyclase, an enzyme catalyzing the formation of guanosine 3′,5′-monophosphate from guanosine triphosphate
    • Hardman, J. G., and E. W. Sutherland. Guanyl cyclase, an enzyme catalyzing the formation of guanosine 3′,5′-monophosphate from guanosine triphosphate. J. Biol. Chem. 244: 6363-6370, 1969.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6363-6370
    • Hardman, J.G.1    Sutherland, E.W.2
  • 31
    • 0028826899 scopus 로고
    • A new human guanylate cyclase-activating peptide (uroguanylin): Precursor cDNA and colonic expression
    • Hill, O., Y. Cetin, A. Cieslak, H-J. Magert, and W-G. Forssmann. A new human guanylate cyclase-activating peptide (uroguanylin): precursor cDNA and colonic expression. Biochim. Biophys. Acta 1253: 146-149, 1995.
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 146-149
    • Hill, O.1    Cetin, Y.2    Cieslak, A.3    Magert, H.-J.4    Forssmann, W.-G.5
  • 32
    • 0018100207 scopus 로고
    • Role of cyclic GMP in the action of heat-stable enterotoxin of Escherichia coli
    • Hughes, J. M., F. Murad, B. Chang, and R. L. Guerrant. Role of cyclic GMP in the action of heat-stable enterotoxin of Escherichia coli. Nature 271: 755-756, 1978.
    • (1978) Nature , vol.271 , pp. 755-756
    • Hughes, J.M.1    Murad, F.2    Chang, B.3    Guerrant, R.L.4
  • 34
    • 0033034327 scopus 로고    scopus 로고
    • Plasma and urine levels of uroguanylin, a new natriuretic peptide, in nephrotic syndrome
    • Kinoshita, H., S. Fujimoto, H. Fukae, N. Yokota, S. Hisanaga, M. Nakazato, and T. Eto. Plasma and urine levels of uroguanylin, a new natriuretic peptide, in nephrotic syndrome. Nephron 81: 160-164, 1999.
    • (1999) Nephron , vol.81 , pp. 160-164
    • Kinoshita, H.1    Fujimoto, S.2    Fukae, H.3    Yokota, N.4    Hisanaga, S.5    Nakazato, M.6    Eto, T.7
  • 38
    • 0025257617 scopus 로고
    • Autoradiographic demonstration of specific binding sites for E. coli enterotoxin in various epithelia of the North American opossum
    • Krause, W. J., R. H. Freeman, and L. R. Forte. Autoradiographic demonstration of specific binding sites for E. coli enterotoxin in various epithelia of the North American opossum. Cell Tissue Res. 260: 387-394, 1990.
    • (1990) Cell Tissue Res. , vol.260 , pp. 387-394
    • Krause, W.J.1    Freeman, R.H.2    Forte, L.R.3
  • 39
    • 0031393324 scopus 로고    scopus 로고
    • The guanylin and uroguanylin peptide hormones and their receptors
    • Krause, W. J., R. M. London, R. H. Freeman, and L. R. Forte. The guanylin and uroguanylin peptide hormones and their receptors. Acta Anat. 160: 213-231, 1997.
    • (1997) Acta Anat. , vol.160 , pp. 213-231
    • Krause, W.J.1    London, R.M.2    Freeman, R.H.3    Forte, L.R.4
  • 41
    • 0016581943 scopus 로고
    • Comparison of natriuresis after oral and intravenous sodium loading in sodium-depleted rabbits: Evidence for a gastrointestinal or portal monitor of sodium intake
    • Lennane, R. J., W. S. Peart, R. M. Carey, and J. Shaw. Comparison of natriuresis after oral and intravenous sodium loading in sodium-depleted rabbits: evidence for a gastrointestinal or portal monitor of sodium intake. Clin. Sci. Mol. Med. 49: 433-436, 1975.
    • (1975) Clin. Sci. Mol. Med. , vol.49 , pp. 433-436
    • Lennane, R.J.1    Peart, W.S.2    Carey, R.M.3    Shaw, J.4
  • 42
    • 0027325558 scopus 로고
    • Peptide-regulated guanylate cyclase pathways in rat colon: In situ localization of GCA, GCC, and guanylin mRNA
    • Li, Z., and M. F. Goy. Peptide-regulated guanylate cyclase pathways in rat colon: in situ localization of GCA, GCC, and guanylin mRNA. Am. J. Physiol. Gastrointest. Liver Physiol. 265: G394-G402, 1993.
    • (1993) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.265
    • Li, Z.1    Goy, M.F.2
  • 43
    • 0031568228 scopus 로고    scopus 로고
    • Purification, cDNA sequence, and tissue distribution of rat uroguanylin
    • Li, Z., A. G. Perkins, M. F. Peters, M. J. Campa, and M. F. Goy. Purification, cDNA sequence, and tissue distribution of rat uroguanylin. Reg. Peptides 68: 45-56, 1997.
    • (1997) Reg. Peptides , vol.68 , pp. 45-56
    • Li, Z.1    Perkins, A.G.2    Peters, M.F.3    Campa, M.J.4    Goy, M.F.5
  • 44
    • 0026586940 scopus 로고
    • The effects of Escherichia coli heat-stable enterotoxin in renal sodium tubular transport
    • Lima, A. A. M., H. S. A. Monteiro, and M. C. Fonteles. The effects of Escherichia coli heat-stable enterotoxin in renal sodium tubular transport. Pharmacol. Toxicol. 70: 163-167, 1992.
    • (1992) Pharmacol. Toxicol. , vol.70 , pp. 163-167
    • Lima, A.A.M.1    Monteiro, H.S.A.2    Fonteles, M.C.3
  • 47
    • 0040030724 scopus 로고    scopus 로고
    • Uroguanylin: Gene structure, expression, processing as a peptide hormone, and co-storage with somatostatin in gastrointestinal D-cells
    • Magert, H.-J., M. Reinecke, I. David, H.-R. Raab, K. Adermann, H-D. Zucht, O. Hill, R. Hess, and W.-G. Forssmann. Uroguanylin: gene structure, expression, processing as a peptide hormone, and co-storage with somatostatin in gastrointestinal D-cells. Reg. Peptides 73: 165-176, 1998.
    • (1998) Reg. Peptides , vol.73 , pp. 165-176
    • Magert, H.-J.1    Reinecke, M.2    David, I.3    Raab, H.-R.4    Adermann, K.5    Zucht, H.-D.6    Hill, O.7    Hess, R.8    Forssmann, W.-G.9
  • 48
    • 0031581108 scopus 로고    scopus 로고
    • Mice lacking the guanylyl cyclase C receptor are resistant to STa-induced intestinal secretion
    • Mann, E. A., M. L. Jump, J. Wu, E. Yee, and R. A. Giannella. Mice lacking the guanylyl cyclase C receptor are resistant to STa-induced intestinal secretion. Biochem. Biophys. Res. Commun. 239: 463-466, 1997.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 463-466
    • Mann, E.A.1    Jump, M.L.2    Wu, J.3    Yee, E.4    Giannella, R.A.5
  • 49
    • 0030566808 scopus 로고    scopus 로고
    • Uroguanylin gene expression in the alimentary tract and extra-gastrointestinal tissues
    • Miyazato, M., M. Nakazato, S. Matsukura, K. Kangawa, and H. Matsuo. Uroguanylin gene expression in the alimentary tract and extra-gastrointestinal tissues. FEBS Lett. 398: 170-174, 1996.
    • (1996) FEBS Lett. , vol.398 , pp. 170-174
    • Miyazato, M.1    Nakazato, M.2    Matsukura, S.3    Kangawa, K.4    Matsuo, H.5
  • 52
    • 0029975375 scopus 로고    scopus 로고
    • Identification of biologically active and inactive human uroguanylins in plasma and urine and their increases in renal insufficiency
    • Nakazato, M., H. Yamaguchi, H. Kinoshita, K. Kangawa, H. Matsuo, N. Chino, and S. Matsukura. Identification of biologically active and inactive human uroguanylins in plasma and urine and their increases in renal insufficiency. Biochem. Biophys. Res. Commun. 220: 586-593, 1996.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 586-593
    • Nakazato, M.1    Yamaguchi, H.2    Kinoshita, H.3    Kangawa, K.4    Matsuo, H.5    Chino, N.6    Matsukura, S.7
  • 53
    • 0028585922 scopus 로고
    • Identification of 10-kDa proguanylin as a major guanylin molecule in human intestine and plasma and its increase in renal insufficiency
    • Nakazato, M., H. Yamaguchi, K. Shiomi, Y. Date, S. Fujimoto, K. Kangawa, H. Matsuo, and S. Matsukura. Identification of 10-kDa proguanylin as a major guanylin molecule in human intestine and plasma and its increase in renal insufficiency. Biochem: Biophys. Res. Commun. 205: 1966-1975, 1994.
    • (1994) Biochem: Biophys. Res. Commun. , vol.205 , pp. 1966-1975
    • Nakazato, M.1    Yamaguchi, H.2    Shiomi, K.3    Date, Y.4    Fujimoto, S.5    Kangawa, K.6    Matsuo, H.7    Matsukura, S.8
  • 54
    • 0030801587 scopus 로고    scopus 로고
    • Epitope conservation and immunohistochemical localization of the guanylin/stable toxin peptide receptor, guanylyl cyclase C
    • Nandi, A., R. Bhandari, and S. S. Visweswariah. Epitope conservation and immunohistochemical localization of the guanylin/stable toxin peptide receptor, guanylyl cyclase C. J. Cell. Biochem. 66: 500-511, 1997.
    • (1997) J. Cell. Biochem. , vol.66 , pp. 500-511
    • Nandi, A.1    Bhandari, R.2    Visweswariah, S.S.3
  • 55
    • 0030823669 scopus 로고    scopus 로고
    • Uroguanylin is expressed by enterochromaffin cells in the rat gastrointestinal tract
    • Perkins, A., M. F. Goy, and Z. Li. Uroguanylin is expressed by enterochromaffin cells in the rat gastrointestinal tract. Gastroenterology 113: 1007-1014, 1997.
    • (1997) Gastroenterology , vol.113 , pp. 1007-1014
    • Perkins, A.1    Goy, M.F.2    Li, Z.3
  • 56
    • 0030452310 scopus 로고    scopus 로고
    • Intestinal secretory defects and dwarfism in mice lacking cGMP-dependent protein kinase II
    • Pfeifer, A., A. Aszodi, U. Seidler, P. Ruth, F. Hofmann, and R. Fassler. Intestinal secretory defects and dwarfism in mice lacking cGMP-dependent protein kinase II. Science 274: 2082-2086, 1996.
    • (1996) Science , vol.274 , pp. 2082-2086
    • Pfeifer, A.1    Aszodi, A.2    Seidler, U.3    Ruth, P.4    Hofmann, F.5    Fassler, R.6
  • 57
    • 0032272276 scopus 로고    scopus 로고
    • Does your gut taste? Sensory transduction in the gastrointestinal tract
    • Raybould, H. E. Does your gut taste? Sensory transduction in the gastrointestinal tract. NIPS 13: 75-280, 1998.
    • (1998) NIPS , vol.13 , pp. 75-280
    • Raybould, H.E.1
  • 60
    • 0030444557 scopus 로고    scopus 로고
    • Structure, glycosylation, and localization of rat intestinal guanylyl cyclase C: Modulation by fasting
    • Scheving, L. A., W. E. Russell, and K. Chong. Structure, glycosylation, and localization of rat intestinal guanylyl cyclase C: modulation by fasting. Am. J. Physiol. Gastrointest. Liver Physiol. 271: G959-G968, 1996.
    • (1996) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.271
    • Scheving, L.A.1    Russell, W.E.2    Chong, K.3
  • 61
    • 0025647794 scopus 로고
    • Guanylyl cyclase is a heat-stable enterotoxin receptor
    • Schulz, S., C. K. Green, P. S. T. Yuen, and D. L. Garbers. Guanylyl cyclase is a heat-stable enterotoxin receptor. Cell 63: 941-948, 1990.
    • (1990) Cell , vol.63 , pp. 941-948
    • Schulz, S.1    Green, C.K.2    Yuen, P.S.T.3    Garbers, D.L.4
  • 62
    • 0030779011 scopus 로고    scopus 로고
    • Disruption of the guanylyl cyclase-C gene leads to a paradoxical phenotype of viable but heat-stable enterotoxin-resistant mice
    • Schulz, S., M. J. Lopez, M. Kuhn, and D. L. Garbers. Disruption of the guanylyl cyclase-C gene leads to a paradoxical phenotype of viable but heat-stable enterotoxin-resistant mice. J. Clin. Invest. 100: 1590-1595, 1997.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1590-1595
    • Schulz, S.1    Lopez, M.J.2    Kuhn, M.3    Garbers, D.L.4
  • 63
    • 0001337601 scopus 로고    scopus 로고
    • The guanylin/STa receptor is expressed in crypts and apical epithelium throughout the mouse intestine
    • Swenson, E. S., E. A. Mann, M. L. Jump, D. P. Witte, and R. A. Giannella. The guanylin/STa receptor is expressed in crypts and apical epithelium throughout the mouse intestine. Biochem. Biophys. Res. Commun. 225: 1009-1014, 1996.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 1009-1014
    • Swenson, E.S.1    Mann, E.A.2    Jump, M.L.3    Witte, D.P.4    Giannella, R.A.5
  • 66
    • 0027935285 scopus 로고
    • Pig intestinal membrane-bound receptor (guanylyl cyclase) for heat-stable enterotoxin: cDNA cloning functional expression, and characterization
    • Wada, A., T. Hirayama, S. Kitao, J. Fujisawa, Y. Hidaka, and Y. Shimonishi. Pig intestinal membrane-bound receptor (guanylyl cyclase) for heat-stable enterotoxin: cDNA cloning functional expression, and characterization. Microbiol. Immunol. 38: 535-541, 1994.
    • (1994) Microbiol. Immunol. , vol.38 , pp. 535-541
    • Wada, A.1    Hirayama, T.2    Kitao, S.3    Fujisawa, J.4    Hidaka, Y.5    Shimonishi, Y.6
  • 67
    • 0030880743 scopus 로고    scopus 로고
    • Uroguanylin and guanylin: Distinct but overlapping patterns of messenger RNA expression in mouse intestine
    • Whitaker, T. L., D. P. Witte, M. C. Scott, and M. B. Cohen. Uroguanylin and guanylin: distinct but overlapping patterns of messenger RNA expression in mouse intestine. Gastroenterology 113: 1000-1006, 1997.
    • (1997) Gastroenterology , vol.113 , pp. 1000-1006
    • Whitaker, T.L.1    Witte, D.P.2    Scott, M.C.3    Cohen, M.B.4
  • 68
    • 0014641807 scopus 로고
    • Detection of guanyl cyclase in mammalian tissues
    • White, A.A., and G. D. Aurbach. Detection of guanyl cyclase in mammalian tissues. Biochim. Biophys. Acta 191: 686-687, 1969.
    • (1969) Biochim. Biophys. Acta , vol.191 , pp. 686-687
    • White, A.A.1    Aurbach, G.D.2
  • 69
    • 0024536091 scopus 로고
    • Opossum kidney contains a functional receptor for the Escherichia coli heat-stable enterotoxin
    • White, A. A., W. J. Krause, J. T. Turner, and L. R. Forte. Opossum kidney contains a functional receptor for the Escherichia coli heat-stable enterotoxin. Biochem. Biophys. Res. Commun. 159: 363-367, 1989.
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 363-367
    • White, A.A.1    Krause, W.J.2    Turner, J.T.3    Forte, L.R.4
  • 70
    • 0026724202 scopus 로고
    • Rat guanylin cDNA: Characterization of the precursor of the endogenous activator of intestinal guanylate cyclase
    • Wiegand, R. C., J. Kato, and M. G. Currie. Rat guanylin cDNA: characterization of the precursor of the endogenous activator of intestinal guanylate cyclase. Biochem. Biophys. Res. Commun. 185: 812-817, 1992.
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 812-817
    • Wiegand, R.C.1    Kato, J.2    Currie, M.G.3


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