Segmental differences in the effects of guanylin and Escherichia coli heat‐stable enterotoxin on Cl‐ secretion in human gut.

Kühn, Michaela; Adermann, Knut; Jähne, J.; Forssmann, Wolf‐Georg; G, Rechkemmer

doi:10.1113/jphysiol.1994.sp020307

Cited by 64 publications

(42 citation statements)

References 21 publications

(25 reference statements)

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“…In fractions 29-31 a strongly stained peptide band in the range of 10-11 kDa was identified. Further immunoreactive bands were observed above 20 kDa, appearing in a wide range of the HPLC fractions. The fractions showing'only the high molecular mass substance contained no measurable bioactive guanylin, suggesting a nonspecific crossreaction.…”

Section: Resultsmentioning

confidence: 94%

“…Ussing chamber studies. Mucosal sheets from rat proximal colon were dissected, mounted in Ussing chambers, and automatically voltage clamped (20 Immunohistochemistry. Specimens of human small intestine obtained from patients undergoing major gut surgery were fixed in Bouin fluid (without acetic acid) for 20 h. They were dehydrated with ethanol, cleared in xylene, and embedded in paraffin.…”

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confidence: 99%

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Analysis of the human guanylin gene and the processing and cellular localization of the peptide.

Hill¹,

Kühn²,

Zucht³

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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The complete cell biological analysis of human guanylin, a recently discovered regulatory peptide, is offered in this investigation: (i) the nucleotide sequence of the gene, (ii) the isolation and characterization of its circulating molecular form, and (iii) its localization in enterochromaffin cells of the gut. As determined by molecular cloning, DNA sequencing, and comparison with the known cDNA sequence, the approximately 2.6-kbp large gene consists of three exons interrupted by two introns. The putative promoter region contains a TTTAAAA sequence motif and several potential binding sites for transcription factors such as AP-1, AP-2, Sp 1, and glucocorticoid receptors. The isolated hormonal form of guanylin is a 94-amino acid peptide with a molecular mass of 10.3 kDa. Western blot analysis of RP-HPLC fractions from blood plasma confirms this molecular form. 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.

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Section: Resultsmentioning

confidence: 94%

mentioning

confidence: 99%

Analysis of the human guanylin gene and the processing and cellular localization of the peptide.

Hill¹,

Kühn²,

Zucht³

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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“…Tissues used for experimental studies were taken from macroscopically normal areas distant from the pathologically affected tissue. After dissection of muscle layers, sheets of isolated mucosa were mounted in Ussing chambers and automatically voltage-clamped as described previously [13]. Short-circuit current (Isc) was continuously recorded.…”

Section: Ussing Chamber Experimentsmentioning

confidence: 99%

GCAP‐II: Isolation and characterization of the circulating form of human uroguanylin

Hess¹,

Kühn²,

Schulz‐Knappe³

et al. 1995

FEBS Letters

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The systematic isolation of circulating regulatory peptides which generate cGMP as second messenger resulted in the identification of a novel member of the gnanylin family. In the present study we describe the purification and amino acid sequence of a new guanylate cyclase C activating peptide (GCAP-II). GCAP-II contains 24 amino acids in the following sequence: FKTLRTIANDDCELCVNVACTGCL. Its molecular mass is 2597.7 Da. The 16 C-terminal amino acids are identical to uroguanylin from human urine. Native and synthetic GCAP-II activate GC-C, the specific gnanylate cyclase receptor, of cultured human colon carcinoma (T84) cells. GCAP-II stimulates chloride secretion in isolated human intestinal mucosa mediated by intracellular cGMP increase. GCAP-II specific antibodies were used to localize the peptide by immunohistochemistry in entero-endocrine cells of the colonic mucosa. Key words':Guanylate cyclase activating peptide II; Uroguanylin; Guanylin; cGMP; Intestinal chloride secretion; Entero-endocrine cell intestinal tissues, such as kidney, liver, reproductive tract, adrenals, airway epithelia, and pancreas [4,5]. In addition, a larger molecular form of this peptide, namely guanylin-22-115, circulates as a bioactive peptide in human blood, suggesting that this peptide regulates the function of different target organs by an endocrine interaction [8].Uroguanylin, a second ligand of the GC-C receptor, has been recently purified from human and opossum urine [9,10]. The structural homology and the similar biological activity of guanylin and uroguanylin suggest that they are members of a peptide family, the main function of which is the activation of GC-C in the intestine and in other tissues. With regard to putative endocrine interactions of this system we initiated a systematic search for further endogenous activators of GC-C circulating in human blood. Here we report the isolation, the biochemical and functional characterization, and the immunohistochemical localization of a new GCAP related to uroguanylin.

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“…Par exemple, comparativement au récepteur ubiquitaire GM1 de CT et LT, le récepteur GC-C de STa est présent uniquement dans l'intestin. La stimulation de GC-C par STa est plus grande dans l'intestin grêle que dans le côlon [58,92] et, en général, moins de récepteurs à STa sont trouvés dans le côlon [21,90]. En revanche, la réponse à STa en flux d'électrolytes, telle que mesurée en chambre d'Ussing, est plus forte dans le côlon [92].…”

Section: Sites D'attachement Multifactorielsunclassified

“…La stimulation de GC-C par STa est plus grande dans l'intestin grêle que dans le côlon [58,92] et, en général, moins de récepteurs à STa sont trouvés dans le côlon [21,90]. En revanche, la réponse à STa en flux d'électrolytes, telle que mesurée en chambre d'Ussing, est plus forte dans le côlon [92]. Il est possible que la toxine STa soit inactivée à différents niveaux dans différentes régions de l'intestin, comme il a été montré dans le jéjunum et l'iléon [22].…”

Section: Sites D'attachement Multifactorielsunclassified

Les récepteurs des entérotoxines bactériennes

Rousset

2000

Vet. Res.

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-Bacterial enterotoxin receptors. Enteric bacterial toxins display a great diversity in their structure, molecular weight and mechanism of action. The interaction of enterotoxins with the intestinal mucosa either leads to a direct effect on the cell membrane or an effect on signal transduction within eukaryotic cells. However, before a toxin can affect a cell, it must after its secretion by a microorganism, recognise and bind to a specific surface molecule, its receptor. Membrane receptors of bacterial enterotoxins have been identified as protein, glycoprotein or glycolipid in nature. The chemical nature of the molecules acting as receptors is crucial and during evolution they have been carefully selected. Some toxins, after their interaction with a receptor molecule, will transduce a signal across the cell membrane while remaining at the cell surface. Other toxins, after this initial binding step with a receptor, will be internalised. Others can form pores leading to leakage of cellular components and cell lysis. Receptors that have been identified often comprise a saccharidic chain that is directly involved in the recognition and binding of the toxin. Today, models explaining toxin-receptor interactions are more complex, including multistep events. This review summarises the knowledge of the interactions between bacterial toxins and membrane receptors present on intestinal mucosa. receptor / intestine / enterotoxin / binding epitope / glycosphingolipidRésumé -Les toxines bactériennes entériques présentent une grande diversité autant dans leur structure que dans leur poids moléculaire et leur mécanisme d'action. L'interaction des entérotoxines avec la muqueuse intestinale conduit soit à un effet direct sur la paroi cellulaire de la cellule hôte, soit à un dérèglement des voies de signalisation de celle-ci. Toutefois, avant même d'affecter la cellule cible, la toxine sécrétée par le micro-organisme devra reconnaître et s'attacher à une molécule présente à la surface cellulaire, son récepteur. Les récepteurs membranaires des entérotoxines bactériennes peuvent être de nature protéique, glycoprotéique ou glycolipidique. La nature chimique de ces récepteurs, sur laquelle repose la spécificité, est primordiale et au cours de l'évolution ceuxci ont été soigneusement sélectionnés. Certaines toxines, une fois en contact avec leur récepteur, envoient un signal à l'intérieur de la cellule tout en demeurant à la surface alors que d'autres toxines sont internalisées. Enfin, certaines toxines bactériennes peuvent former des pores dans la membrane Vet. Res. 31 (2000)

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Segmental differences in the effects of guanylin and Escherichia coli heat‐stable enterotoxin on Cl‐ secretion in human gut.

Cited by 64 publications

References 21 publications

Analysis of the human guanylin gene and the processing and cellular localization of the peptide.

Analysis of the human guanylin gene and the processing and cellular localization of the peptide.

GCAP‐II: Isolation and characterization of the circulating form of human uroguanylin

Les récepteurs des entérotoxines bactériennes

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