Редактирование: TFF2 (раздел)

==Publications==

{{medline-entry
|title=Human pancreatic polypeptide has a marked diurnal rhythm that is affected by ageing and is associated with the gastric [[TFF2]] circadian rhythm.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/16359755
|abstract=Normal circadian variations in vasoactive intestinal polypeptide, somatostatin, cholecystokinin and pancreatic polypeptide were measured to determine if these alter with aging and to identify gastrointestinal regulatory hormones that might control the dramatic diurnal variation in the gastric cytoprotective trefoil protein [[TFF2]]. Plasma pancreatic polypeptide concentrations showed a marked diurnal rhythm (p < 0.0001). Basal and postprandial pancreatic polypeptide concentrations increased with age (p < 0.01). The timing of the diurnal rhythm was consistent with pancreatic polypeptide inhibiting [[TFF2]] secretion and there was a negative association between pancreatic polypeptide and [[TFF2]] concentrations (p < 0.002). The much higher pancreatic polypeptide concentrations in older people will induce increased satiety that may contribute to 'anorexia of ageing'. These results identify potential therapies for treatment of gastric mucosal morbidity and age-associated loss of appetite.
|mesh-terms=* Adolescent
* Adult
* Age Factors
* Aged
* Aged, 80 and over
* Aging
* Circadian Rhythm
* Feeding Behavior
* Gastric Mucosa
* Humans
* Middle Aged
* Pancreatic Polypeptide
* Peptides
* Time Factors
* Trefoil Factor-2

|full-text-url=https://sci-hub.do/10.1016/j.peptides.2005.11.002
}}
{{medline-entry
|title=The diurnal rhythm of the cytoprotective human trefoil protein [[TFF2]] is reduced by factors associated with gastric mucosal damage: ageing, Helicobacter pylori infection, and sleep deprivation.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/15984970
|abstract=To determine if the normal [[TFF2]] diurnal rhythm is disrupted in those with increased risk of gastric morbidity. Trefoil proteins protect the gastrointestinal mucosa from damage and aid its repair. [[TFF2]] is considered the major cytoprotective gastric trefoil protein. There is a marked circadian variation in gastric luminal [[TFF2]] in young healthy volunteers with peak levels present during the night. Gastric juice was aspirated at two hourly intervals over a 24-h period via a nasogastric tube. [[TFF2]] was measured by quantitative western transfer analysis. Helicobacter pylori (H. pylori) status was measured by C13 urea breath test and by serology. The effects of H. pylori infection, sleep deprivation, and ageing, which cause increased gastric morbidity, on the [[TFF2]] circadian rhythm were tested. H. pylori infection attenuated the increase in [[TFF2]] that occurs during the night. The [[TFF2]] diurnal rhythm was reduced in older people and both the [[TFF2]] level reached and the time at which the maximum [[TFF2]] concentration occurs were associated inversely with age (p < 0.005). Sleep deprivation delayed the normal night time increase in gastric [[TFF2]] and resulted in an overall reduction in [[TFF2]] secretion. H. pylori infection, ageing, and sleep deprivation cause a reduction in the [[TFF2]] diurnal rhythm. The demonstration that the [[TFF2]] rhythm is impaired in cohorts of individuals known to suffer gastric symptoms suggests that interventions to restore the normal [[TFF2]] rhythm in those with poor mucosal protection could reduce morbidity.
|mesh-terms=* Adolescent
* Adult
* Aged
* Aged, 80 and over
* Aging
* Circadian Rhythm
* Cytoprotection
* Gastric Mucosa
* Helicobacter Infections
* Helicobacter pylori
* Humans
* Middle Aged
* Mucins
* Muscle Proteins
* Peptides
* Sleep
* Trefoil Factor-2

|full-text-url=https://sci-hub.do/10.1111/j.1572-0241.2005.41859.x
}}
{{medline-entry
|title=Immunoassays of human trefoil factors 1 and 2: measured on serum from patients with inflammatory bowel disease.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/15115253
|abstract=The trefoil factors ([[TFF1]]-3) are cysteine-rich peptides expressed in the gastrointestinal tract where they play a critical role in mucosal protection and repair. The expression is up-regulated at sites of ulceration in various chronic inflammatory diseases. Recently, we presented an ELISA method for measurement of [[TFF3]]. The aims of the present study were to develop and evaluate ELISAs for the other two known human trefoil peptides, [[TFF1]] and [[TFF2]], and to carry out a cross-sectional study on serum TFF levels in patients with inflammatory bowel disease (IBD). The [[TFF1]]-ELISA was based on two polyclonal rabbit antibodies and the [[TFF2]]-ELISA on a monoclonal mouse antibody and a polyclonal rabbit antibody. Rh[[TFF1]] and 2 were employed to prepare the calibrators. [[TFF1]]-3 were assayed in serum from IBD patients (n=41) and controls (n=13). The [[TFF1]]- ([[TFF2]]-) ELISA had a detection limit of 3 pmol/L (6 pmol/L) and an analytical imprecision (CV(A)) of 7.0-8.8 for mean concentrations of 24-120 pmol/L (6.1-8.0 for mean concentrations of 17-77 pmol/L). The central reference intervals (n=300) were 140-1400 pmol/L (37-190 pmol/L). There was no variation with age and menstrual cycle. Food intake reduced concentrations of [[TFF1]] by approximately 15%, but did not influence concentrations of [[TFF2]]. [[TFF1]] and [[TFF3]] were increased in serum from IBD patients. We have developed assays for measuring [[TFF1]] and [[TFF2]]. Finding increased TFF concentrations in serum from IBD patients suggests that measurements of trefoil peptides may be of clinical relevance in IBD.
|mesh-terms=* Adolescent
* Adult
* Aged
* Aging
* Enzyme-Linked Immunosorbent Assay
* Female
* Health
* Humans
* Immunoassay
* Inflammatory Bowel Diseases
* Male
* Middle Aged
* Mucins
* Muscle Proteins
* Peptides
* Proteins
* Sensitivity and Specificity
* Trefoil Factor-1
* Trefoil Factor-2
* Trefoil Factor-3
* Tumor Suppressor Proteins

|full-text-url=https://sci-hub.do/10.1080/00365510410001176
}}
{{medline-entry
|title=Metaplasia of the duodenum shows a Helicobacter pylori-correlated differentiation into gastric-type protein expression.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/12612884
|abstract=The origin of gastric metaplasia of the duodenum (GMD) remains enigmatic. We studied expression of mucins and trefoil peptides in GMD to gain insight into its phenotype and origin. We examined duodenal tissue of 95 patients (0 to 83 years old, 26 with gastric Helicobacter pylori infection) for the presence of GMD. Expression was examined immunohistochemically of secretory mucins ([[MUC2]], [[MUC5AC]], [[MUC5B]], and [[MUC6]]), trefoil peptides ([[TFF1]], [[TFF2]], and [[TFF3]]), and sucrase-isomaltase ([[SI]]). GMD, found in 37 patients, correlated positively to gastric H. pylori infection, age, and villus atrophy. [[MUC2]] and [[TFF3]], expressed in normal goblet cells, were absent from 100% and 87% of GMD, respectively. GMD ubiquitously expressed [[MUC5AC]], whereas [[MUC5AC]] expression in adjacent goblet cells was closely correlated with the extent of GMD. [[TFF1]], [[TFF2]], and [[MUC6]] were found in 84%, 92%, and 65% of GMD, respectively. [[MUC5B]] was absent from epithelium and GMD. [[SI]], expressed by villus enterocytes, was absent from GMD. Brunner's glands ubiquitously expressed [[MUC5B]], [[MUC6]], and [[TFF2]]. GMD was characterized by the expression of gastric-type proteins [[MUC5AC]], [[MUC6]], [[TFF1]], and [[TFF2]] and the absence of intestinal markers [[MUC2]], [[TFF3]], and [[SI]]. In terms of the location of metaplastic cells, our results suggest that epithelial cells migrating toward villus tips switch to gastric-type secretory cells. Positive correlation with infection suggests an inductive role H. pylori in the development of GMD.
|mesh-terms=* Adolescent
* Adult
* Aged
* Aged, 80 and over
* Aging
* Brunner Glands
* Cell Differentiation
* Child
* Child, Preschool
* Duodenum
* Gastric Mucosa
* Goblet Cells
* Growth Substances
* Helicobacter Infections
* Helicobacter pylori
* Humans
* Infant
* Metaplasia
* Middle Aged
* Mucin 5AC
* Mucin-2
* Mucin-5B
* Mucin-6
* Mucins
* Muscle Proteins
* Neuropeptides
* Peptides
* Proteins
* Stomach Diseases
* Trefoil Factor-1
* Trefoil Factor-2
* Trefoil Factor-3
* Tumor Suppressor Proteins

|full-text-url=https://sci-hub.do/10.1053/hupa.2003.15
}}