The trefoil peptides spasmolytic polypeptide and intestinal trefoil factor are major secretory products of the rat gut

Peptides ◽  
1995 ◽  
Vol 16 (6) ◽  
pp. 1001-1005 ◽  
Author(s):  
D.R. Taupin ◽  
K.C. Pang ◽  
S.P. Green ◽  
A.S. Giraud
Keyword(s):  
Trefoil Factor ◽  
Intestinal Trefoil Factor ◽  
Trefoil Peptides ◽  
Spasmolytic Polypeptide ◽  
Secretory Products ◽  
Rat Gut

scholarly journals cDNA cloning of rat pS2 peptide and expression of trefoil peptides in acetic acid-induced colitis

1996 ◽  
Vol 318 (3) ◽  
pp. 939-944 ◽  
Author(s):  
Hiroshi ITOH ◽  
Masaki TOMITA ◽  
Hirofumi UCHINO ◽  
Takahiko KOBAYASHI ◽  
Hiroaki KATAOKA ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Acute Phase ◽  
Recovery Phase ◽  
Intestinal Epithelial ◽  
Trefoil Factor ◽  
Intestinal Trefoil Factor ◽  
Reverse Transcription Pcr ◽  
Trefoil Peptides ◽  
Rapid Amplification ◽  
Normal Controls

By using a combination of the methods of reverse transcription-PCR and rapid amplification of cDNA ends, a cDNA for rat pS2 peptide (rpS2) was successfully cloned and sequenced from rat stomach. By RNA blot analysis, the gene was shown to be expressed abundantly in the stomach and only faintly in the duodenum, but not in other tissues including the distal small and large intestines. rpS2 expression was also examined in the rectum during the course of acetic acid-induced colitis; rpS2 mRNA was detected during the acute phase of colitis but not in normal controls or during the recovery phase. On the other hand, expression of rat intestinal trefoil factor (rITF) was down-regulated during the acute phase of colitis and then up-regulated during the recovery phase, whereas rat spasmolytic peptide was not detectable throughout the course of the induced colitis. These results indicate that the patterns and timing of the expression of these trefoil peptides are different from each other. rpS2 may play an important role in the proliferation of intestinal epithelial cells during the acute phase of mucosal ulceration, whereas rITF may be involved in differentiation of the cells, particularly to form goblet cells, during the recovery phase.

scholarly journals Trefoil peptide TFF2 (spasmolytic polypeptide) potently accelerates healing and reduces inflammation in a rat model of colitis

Gut ◽  
1999 ◽  
Vol 44 (5) ◽  
pp. 636-642 ◽  
Author(s):  
C P Tran ◽  
G A Cook ◽  
N D Yeomans ◽  
L Thim ◽  
A S Giraud
Keyword(s):  
Rat Model ◽  
Therapeutic Potential ◽  
Active Phase ◽  
Gastric Injury ◽  
Myeloperoxidase Activity ◽  
Intestinal Trefoil Factor ◽  
Inflammatory Index ◽  
Trefoil Peptides ◽  
Trefoil Peptide ◽  
Spasmolytic Polypeptide

BACKGROUNDThe trefoil peptides are major secretory products of mucus cells of the gastrointestinal tract and show increased expression after inflammatory or ulcerative damage. Recombinant human TFF2 (spasmolytic polypeptide) has been shown to be cytoprotective, and enhances repair in models of gastric injury.AIMSTo test the healing effects of recombinant human (h)TFF2 in a rat model of chronic colitis.METHODSColitis was induced by intracolonic administration of dinitrobenzene sulphonic acid in ethanol. Mucosal repair was quantified macroscopically, microscopically by image analysis of tissue histology, and by measuring myeloperoxidase activity.RESULTSInitial validation studies showed that maximal injury and inflammation occurred at the end of the first week after colitis induction (active phase), and that spontaneous healing was complete by eight weeks. Once daily intrarectal application of hTFF2 (2.5 mg/kg; approximately 0.5 mg/rat) for five days after maximal damage had been sustained, reduced both microscopic and macroscopic injury by 80% and inflammatory index by 50% compared with vehicle controls. In addition, endogenous concentrations of rat TFF2 and TFF3 (intestinal trefoil factor) were increased in the active phase of colitis and were reduced to basal levels by hTFF2 treatment.CONCLUSIONSThis study has shown that hTFF2 enhances the rate of colonic epithelial repair, and reduces local inflammation in a rat model of colitis, and suggests that luminal application of trefoil peptides may have therapeutic potential in the treatment of inflammatory bowel disease.

Trefoil peptides: a newly recognized family of epithelial mucin-associated molecules

1993 ◽  
Vol 265 (2) ◽  
pp. G205-G213 ◽  
Author(s):  
R. Poulsom ◽  
N. A. Wright
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Cultured Cells ◽  
Cell Lineage ◽  
Smooth Muscle Contraction ◽  
Mucosal Healing ◽  
Intestinal Trefoil Factor ◽  
Trefoil Peptides ◽  
Spasmolytic Polypeptide ◽  
Glandular Structures

Members of the trefoil family of peptides are generally small stable secreted molecules, structurally related by the presence of one, or up to six, compact 6-cysteine motifs. Several trefoil peptides are expressed in mammalian gut and Xenopus gut and skin, often in association with mucins. Chronic ulcerative conditions of the gut, such as Crohn's disease, result in the growth of glandular structures of the ulcer-associated cell lineage (UACL) that secrete epidermal growth factor/urogastrone, transforming growth factor-alpha, and at least three trefoil peptides [pS2, human spasmolytic polypeptide (hSP), and intestinal trefoil factor (hITF/hP1.B)]. Neuroendocrine and goblet cells near the UACL are "recruited" into expressing pS2 and hSP, but the purpose of this concerted expression is unclear. A role in mucosal healing has been proposed. Biological functions of trefoil peptides have been difficult to establish. Pancreatic spasmolytic polypeptide of porcine origin inhibits gastric acid secretion and smooth muscle contraction and is a growth factor for some cultured cells, but pS2, once thought to be breast cancer specific, is not a mitogen. Recombinant trefoil peptides have allowed localization of binding sites and will allow structure-activity relationships to be studied, once the functions are clear.

Characterisation of the single copy trefoil peptides intestinal trefoil factor and pS2 and their ability to form covalent dimers

FEBS Letters ◽  
1995 ◽  
Vol 357 (1) ◽  
pp. 50-54 ◽  
Author(s):  
Rebecca Chinery ◽  
Paul A. Bates ◽  
Amitabha De ◽  
Paul S. Freemont
Keyword(s):  
Single Copy ◽  
Trefoil Factor ◽  
Intestinal Trefoil Factor ◽  
Trefoil Peptides

scholarly journals Localization of intestinal trefoil-factor mRNA in rat stomach and intestine by hybridization in situ

1992 ◽  
Vol 285 (1) ◽  
pp. 5-8 ◽  
Author(s):  
R Chinery ◽  
R Poulsom ◽  
L A Rogers ◽  
R E Jeffery ◽  
J M Longcroft ◽  
...  
Keyword(s):  
Gastric Mucosa ◽  
Pcr Amplification ◽  
Trefoil Factor ◽  
Intestinal Trefoil Factor ◽  
Trefoil Peptides ◽  
Cardiac Region ◽  
Hybridization In Situ ◽  
Acid Mucins ◽  
Formed Part

A cDNA encoding rat intestinal trefoil factor (rITF) was prepared by reverse transcription and PCR amplification. The sequence obtained was well conserved with that of other trefoil peptides. An antisense riboprobe produced from the clone was used to localize the sites of ITF expression in the rat gastrointestinal tract using hybridization in situ. We found rITF mRNA in goblet cells in the small intestine and colon; a gradient of signal strength greatest near the crypt base was sometimes present. We found no evidence for rITF expression in Brunner's glands, the pancreas, or most regions of the gastric mucosa. Surprisingly, strong signals for rITF mRNA were detected in a region of stomach at the junction of the squamous fore-stomach with the glandular gastric mucosa. This region, which may correspond to the cardiac region, formed part of a larger area of cells staining positive for acid mucins. We hypothesize that concerted expression occurs of particular trefoil peptides with specific mucins, and that this organization reflects a functional relationship between mucins and trefoil peptides.

scholarly journals Molecular cloning of mouse intestinal trefoil factor and its expression during goblet cell changes

1995 ◽  
Vol 311 (1) ◽  
pp. 293-297 ◽  
Author(s):  
M Tomita ◽  
H Itoh ◽  
N Ishikawa ◽  
A Higa ◽  
H Ide ◽  
...  
Keyword(s):  
Goblet Cell ◽  
Goblet Cells ◽  
Recovery Phase ◽  
Nippostrongylus Brasiliensis ◽  
Trefoil Factor ◽  
Intestinal Trefoil Factor ◽  
Cell Hyperplasia ◽  
Reverse Transcription Pcr ◽  
Rapid Amplification ◽  
Mitf Expression

A cDNA encoding mouse intestinal trefoil factor (mITF) was successfully cloned and sequenced from the small intestine of C57BL/6 mouse by using the combination of reverse transcription-PCR and rapid amplification of cDNA ends methods. The gene was, similar to rat and human ITFs, mainly expressed in the small and large intestine. The mITF expression was up-regulated during the recovery phase after depletion of goblet cells in acetic acid-induced colitis. On the other hand, the expression in the jejunum was not altered, while goblet cell hyperplasia was induced by Nippostrongylus brasiliensis infection. These results suggest that the mITF expression did not simply correlate with the number of goblet cells. The mITF may play an important role in the maintenance and repair of mucosal function of the rectum. Additionally, the mITF in the jejunum may play a role in alteration of the physicochemical nature of goblet cell mucins, thereby affecting the establishment of intestinal helminths.

scholarly journals Selective reduction of intestinal trefoil factor in untreated coeliac disease

2002 ◽  
Vol 130 (3) ◽  
pp. 526-531 ◽  
Author(s):  
C. CIACCI ◽  
D. DI VIZIO ◽  
R. SETH ◽  
G. INSABATO ◽  
G. MAZZACCA ◽  
...  
Keyword(s):  
Coeliac Disease ◽  
Selective Reduction ◽  
Trefoil Factor ◽  
Intestinal Trefoil Factor
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