Literature DB >> 19960363

Receptor guanylyl cyclase C (GC-C): regulation and signal transduction.

Nirmalya Basu1, Najla Arshad, Sandhya S Visweswariah.   

Abstract

Receptor guanylyl cyclase C (GC-C) is the target for the gastrointestinal hormones, guanylin, and uroguanylin as well as the bacterial heat-stable enterotoxins. The major site of expression of GC-C is in the gastrointestinal tract, although this receptor and its ligands play a role in ion secretion in other tissues as well. GC-C shares the domain organization seen in other members of the family of receptor guanylyl cyclases, though subtle differences highlight some of the unique features of GC-C. Gene knock outs in mice for GC-C or its ligands do not lead to embryonic lethality, but modulate responses of these mice to stable toxin peptides, dietary intake of salts, and development and differentiation of intestinal cells. It is clear that there is much to learn in future about the role of this evolutionarily conserved receptor, and its properties in intestinal and extra-intestinal tissues.

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Year:  2009        PMID: 19960363     DOI: 10.1007/s11010-009-0324-x

Source DB:  PubMed          Journal:  Mol Cell Biochem        ISSN: 0300-8177            Impact factor:   3.396


  157 in total

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3.  Autoradiographic demonstration of specific binding sites for E. coli enterotoxin in various epithelia of the North American opossum.

Authors:  W J Krause; R H Freeman; L R Fort
Journal:  Cell Tissue Res       Date:  1990-05       Impact factor: 5.249

4.  Gastrointestinal control of sodium excretion in sodium-depleted conscious rabbits.

Authors:  R M Carey; J R Smith; E M Ortt
Journal:  Am J Physiol       Date:  1976-06

5.  Activation of particulate guanylate cyclase by Escherichia coli heat-stable enterotoxin is regulated by adenine nucleotides.

Authors:  H Gazzano; H I Wu; S A Waldman
Journal:  Infect Immun       Date:  1991-04       Impact factor: 3.441

6.  Dominant negative mutations of the guanylyl cyclase-A receptor. Extracellular domain deletion and catalytic domain point mutations.

Authors:  D K Thompson; D L Garbers
Journal:  J Biol Chem       Date:  1995-01-06       Impact factor: 5.157

7.  Structural characteristics for biological activity of heat-stable enterotoxin produced by enterotoxigenic Escherichia coli: X-ray crystallography of weakly toxic and nontoxic analogs.

Authors:  T Sato; H Ozaki; Y Hata; Y Kitagawa; Y Katsube; Y Shimonishi
Journal:  Biochemistry       Date:  1994-07-26       Impact factor: 3.162

8.  Biochemical characterization of the intracellular domain of the human guanylyl cyclase C receptor provides evidence for a catalytically active homotrimer.

Authors:  K Vijayachandra; M Guruprasad; R Bhandari; U H Manjunath; B P Somesh; N Srinivasan; K Suguna; S S Visweswariah
Journal:  Biochemistry       Date:  2000-12-26       Impact factor: 3.162

9.  Comparison of receptors for Escherichia coli heat-stable enterotoxin: novel receptor present in IEC-6 cells.

Authors:  E A Mann; M B Cohen; R A Giannella
Journal:  Am J Physiol       Date:  1993-01

10.  The crystal structure of the catalytic domain of a eukaryotic guanylate cyclase.

Authors:  Jonathan A Winger; Emily R Derbyshire; Meindert H Lamers; Michael A Marletta; John Kuriyan
Journal:  BMC Struct Biol       Date:  2008-10-07
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5.  Intestinal cell proliferation and senescence are regulated by receptor guanylyl cyclase C and p21.

Authors:  Nirmalya Basu; Sayanti Saha; Imran Khan; Subbaraya G Ramachandra; Sandhya S Visweswariah
Journal:  J Biol Chem       Date:  2013-11-11       Impact factor: 5.157

6.  Activation of guanylate cyclase-C attenuates stretch responses and sensitization of mouse colorectal afferents.

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7.  Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.

Authors:  Najla Arshad; Suhas Ballal; Sandhya S Visweswariah
Journal:  J Biol Chem       Date:  2012-12-26       Impact factor: 5.157

8.  Guanylate cyclase 2C agonism corrects CFTR mutants.

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9.  Plecanatide and dolcanatide, novel guanylate cyclase-C agonists, ameliorate gastrointestinal inflammation in experimental models of murine colitis.

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10.  Guanylyl cyclase C as a biomarker for immunotherapies for the treatment of gastrointestinal malignancies.

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