Редактирование: TFF3 (раздел)

==Publications==

{{medline-entry
|title=Aging in the absence of [[TLR2]] is associated with reduced IFN-gamma responses in the large intestine and increased severity of induced colitis.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/18223102
|abstract=Age-associated changes in immune function and their implications for intestinal inflammation are poorly understood. Defects in innate immunity have been shown to enhance intestinal inflammation and have been demonstrated upon aging. This study aimed to determine the consequences of aging in the presence and absence of [[TLR2]] on intestinal inflammation. Young and aged (>60 weeks), control C57Bl/6 and [[TLR2]]-deficient ([[TLR2]](-/-)) mice were examined. The cecum and mid-colon were analyzed for tissue damage, cytokine profiles, and trefoil factor 3 ([[TFF3]]) expression at baseline or after 5 days of treatment with dextran sodium sulfate (DSS) and 5 or 13 days recovery. Untreated, aged [[TLR2]](-/-) mice had no significant intestinal inflammation but had reduced colonic IFN-gamma and IL-10 compared with younger mice. Aged [[TLR2]](-/-) mice developed more severe colitis than other groups, as indicated by histological examination and overall weight loss. There were significant increases in colonic IFN-gamma following DSS treatment in young but not in aged mice. [[TFF3]] was substantially reduced in the cecum and increased in the colon of aged but not younger [[TLR2]](-/-) mice following DSS treatment. These results demonstrate that even upon aging, [[TLR2]]-deficient animals did not develop intestinal disease. However, they failed to respond appropriately to an inflammatory insult, and the consequences of this were most severe in aged animals. Cytokine and [[TFF3]] changes associated with aging may contribute to more severe intestinal inflammation.
|mesh-terms=* Aging
* Animals
* Cecum
* Colitis
* Colon
* Dextran Sulfate
* Genetic Predisposition to Disease
* Interferon-gamma
* Mice
* Mice, Inbred C57BL
* Mice, Knockout
* Toll-Like Receptor 2

|full-text-url=https://sci-hub.do/10.1189/jlb.0807557
}}
{{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=The therapeutic effect of recombinant human trefoil factor 3 on hypoxia-induced necrotizing enterocolitis in immature rat.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/14599715
|abstract=Trefoil peptides are a new class of regulatory peptides involved in mucosal protection and repair in the gastrointestinal tract. Among them, trefoil factor 3 ([[TFF3]]) (intestinal trefoil factor) is known to be cytoprotective in the gut. The aim of this study was to determine the effect of recombinant human trefoil factor 3 (rh[[TFF3]]) on hypoxia-induced necrotizing enterocolitis (NEC) in immature rats. In the present study, thirty-two 1-day-old Wistar rat pups were randomly divided into four groups. Group 1 served as nonhypoxic controls. Group 2 rats were subjected to hypoxia reoxygenation (H/O) and then were returned to their mothers. Groups 3 and 4 rats were subjected to H/O, were returned to their mothers, and were treated with rh[[TFF3]] intraperitoneally (0.5 mg) and subcutaneously (0.2 mg), respectively, for the next 3 days. All animals were killed on day 4, and intestine specimens were obtained to determine the histological changes, tissue level of interleukin-8 (IL-8), tumor necrosis factor-alpha (TNF-alpha), malondialdehyde (MDA), prostaglandin E2 (PGE2), tromboxane B2 (TXB2), and nitric oxide (NO). In addition, the effects of rh[[TFF3]] on abundance of inducible nitric oxide synthase (iNOS) and cyclooxygenase 2 (COX-2) were also investigated. In neonatal NEC (group 2), necrosis of villi and crypts and, in some cases, transmural necrosis was observed under light microscopy. Tissue level of interleukin-8, tumor necrosis factor-alpha, malondialdehyde, prostaglandin E2, tromboxane B2, and nitric oxide were significantly higher than group 1. In addition, abundance of inducible nitric oxide synthase and cyclooxygenase 2 was markedly increased. In groups 3 and 4, only very slight intestinal injury was observed. The tissue level of interleukin-8, tumor necrosis factor-alpha, malondialdehyde, prostaglandin E2, tromboxane B2, and nitric oxide were significantly decreased in comparison to the group 2. Meanwhile, the abundance of inducible nitric oxide synthase and cyclooxygenase 2 was also marked decreased in comparison to group 2. The current study suggests a therapeutic role of [[TFF3]] in an experimental model of NEC. Our findings may open a new insight into the treatment of NEC in newborns.
|mesh-terms=* Aging
* Animals
* Cyclooxygenase 2
* Enterocolitis, Necrotizing
* Gene Expression Regulation
* Humans
* Hypoxia
* Immunohistochemistry
* Intestine, Small
* Isoenzymes
* Membrane Proteins
* Mucins
* Muscle Proteins
* Nitric Oxide Synthase
* Nitric Oxide Synthase Type II
* Peptides
* Prostaglandin-Endoperoxide Synthases
* Rats
* Trefoil Factor-3

|full-text-url=https://sci-hub.do/10.1016/s0167-0115(03)00177-0
}}
{{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
}}