Enterochromaffin cells of the digestive system: cellular source of guanylin, a guanylate cyclase-activating peptide.

Cetin, Yalcin; Kühn, Michaela; Kulaksiz, Hasan; Adermann, Knut; Bargsten, Gerhard; Grube, D.; Forssmann, Wolf‐Georg

doi:10.1073/pnas.91.8.2935

Cited by 96 publications

(136 citation statements)

References 38 publications

Supporting

Mentioning

132

Contrasting

Order By: Relevance

“…Northern analysis confirms that guanylin is synthesized in the gut, especially in its distal segments (5). Guanylin is thought to modulate intestinal water/electrolyte transport in a paracrine mode (3,4,7,8). This investigation reports data on the structure of the human genesl and the circulating form of its product as well as the identification of the guanylin-containing cells in the human intestine.…”

mentioning

confidence: 69%

“…7 and 15). In addition, antisera against serotonin and chromogranin A (7,16,17) were used for the identification of endocrine cells.…”

mentioning

confidence: 99%

“…According to the published human proguanylin sequence (5,6,14) the peptides guanylin-(25-37), guanylin-(34-46), and [Lys'00]guanylin-(101-115) were synthesized as described previously (7). Polyclonal rabbit antisera K39 [recognizing guanylin-(25-37)], K42 [recognizing guanylin-(34-46)], and K605 [recognizing guanylin-(101-115)] were raised (for details, see refs.…”

mentioning

confidence: 99%

See 2 more Smart Citations

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.

Self Cite

View full text Add to dashboard Cite

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.

show abstract

mentioning

confidence: 69%

“…7 and 15). In addition, antisera against serotonin and chromogranin A (7,16,17) were used for the identification of endocrine cells.…”

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

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.

Self Cite

View full text Add to dashboard Cite

show abstract

“…Antisera were raised in rabbits and used to localize the peptide in various tissues such as colon, liver, kidney, and stomach. Controls were carried out as routinely [6], for preabsorption tests the entire synthetic GCAP-II as well as the MAP and the linear undecapeptide were used in excess.…”

Section: Immunohistochemistrymentioning

confidence: 99%

“…Northern blot and immunohistochemical analysis have revealed that guanylin occurs in the mucosa of the mammalian intestine (see reviews [4] and [5]). The peptide is probably released from entero-endocrine cells [6,7] into the intestinal lumen to activate the GC-C and consequently the chloride transport in enterocytes by means of a paracrine interaction [5]. However, several data indicate that the guanylin/GC-C system is not exclusively confined to the intestine.…”

Section: Introductionmentioning

confidence: 99%

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

Hess¹,

Kühn²,

Schulz‐Knappe³

et al. 1995

FEBS Letters

View full text Add to dashboard Cite

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.

show abstract

Natriuretic Peptides

Bold¹,

Bruneau²

2000

Comprehensive Physiology

View full text Add to dashboard Cite

The sections in this article are: Historical Perspectives Primary Structure Assay Methods The Endocrine Heart Functional Morphology Biological Properties of Natriuretic Peptides and Their Receptors Natriuretic Peptide Gene Structure Mechanical and Neuroendocrine Control of Natriuretic Peptide Gene Expression and Release Contribution of Natriuretic Peptides to Cardiovascular Homeostasis

show abstract

Enterochromaffin cells of the digestive system: cellular source of guanylin, a guanylate cyclase-activating peptide.

Abstract: Guanylin, a bioactive peptide, has recently been isolated from the intet; this peptide activates intestinal guanylate cydase (i.e., guanylate cyclase C) and thus is poten-

Cited by 96 publications

References 38 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

Natriuretic Peptides

Contact Info

Product

Resources

About