Trefoil factor 1

From Wikipedia, the free encyclopedia

Trefoil factor 1

PDB rendering based on 1hi7.

Available structures: 1hi7, 1ps2

Identifiers

Symbol(s)

TFF1; BCEI; D21S21; HP1.A; HPS2; pNR-2; pS2

External IDs

OMIM: 113710 MGI: 88135 HomoloGene: 2426

Gene ontology
Molecular Function:	• protein binding • growth factor activity
Biological Process:	• carbohydrate metabolic process • defense response • digestion • negative regulation of cell proliferation • cell differentiation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003225 (mRNA)
NP_003216 (protein)

NM_009362 (mRNA)
NP_033388 (protein)

Location

Chr 21: 42.66 - 42.66 Mb

Chr 17: 30.87 - 30.89 Mb

Pubmed search

[1]

[2]

Trefoil factor 1, also known as TFF1, is a human gene.^[1]

Members of the trefoil family are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides. They are stable secretory proteins expressed in gastrointestinal mucosa. Their functions are not defined, but they may protect the mucosa from insults, stabilize the mucus layer, and affect healing of the epithelium. This gene, which is expressed in the gastric mucosa, has also been studied because of its expression in human tumors. This gene and two other related trefoil family member genes are found in a cluster on chromosome 21.^[1]

[edit] References

^ ^a ^b Entrez Gene: TFF1 trefoil factor 1.

[edit] Further reading

Langer G, Jagla W, Behrens-Baumann W, et al. (2003). "Ocular TFF-peptides: new mucus-associated secretory products of conjunctival goblet cells.". Adv. Exp. Med. Biol. 506 (Pt A): 313–6. PMID 12613926.
Piggott NH, Henry JA, May FE, Westley BR (1991). "Antipeptide antibodies against the pNR-2 oestrogen-regulated protein of human breast cancer cells and detection of pNR-2 expression in normal tissues by immunohistochemistry.". J. Pathol. 163 (2): 95–104. doi:10.1002/path.1711630204. PMID 1707960.
Mori K, Fujii R, Kida N, et al. (1990). "Complete primary structure of the human estrogen-responsive gene (pS2) product.". J. Biochem. 107 (1): 73–6. PMID 2185238.
Tomasetto C, Rio MC, Gautier C, et al. (1990). "hSP, the domain-duplicated homolog of pS2 protein, is co-expressed with pS2 in stomach but not in breast carcinoma.". EMBO J. 9 (2): 407–14. PMID 2303034.
Takahashi H, Kida N, Fujii R, et al. (1990). "Expression of the pS2 gene in human gastric cancer cells derived from poorly differentiated adenocarcinoma.". FEBS Lett. 261 (2): 283–6. PMID 2311759.
Rio MC, Bellocq JP, Daniel JY, et al. (1988). "Breast cancer-associated pS2 protein: synthesis and secretion by normal stomach mucosa.". Science 241 (4866): 705–8. PMID 3041593.
Rio MC, Lepage P, Diemunsch P, et al. (1989). "[Primary structure of human protein pS2]". C. R. Acad. Sci. III, Sci. Vie 307 (19): 825–31. PMID 3146413.
Mori K, Fujii R, Kida N, et al. (1988). "Identification of a polypeptide secreted by human breast cancer cells (MCF-7) as the human estrogen-responsive gene (pS2) product.". Biochem. Biophys. Res. Commun. 155 (1): 366–72. PMID 3261981.
Jeltsch JM, Roberts M, Schatz C, et al. (1987). "Structure of the human oestrogen-responsive gene pS2.". Nucleic Acids Res. 15 (4): 1401–14. PMID 3822834.
Prud'homme JF, Fridlansky F, Le Cunff M, et al. (1985). "Cloning of a gene expressed in human breast cancer and regulated by estrogen in MCF-7 cells.". DNA 4 (1): 11–21. PMID 3838275.
Jakowlew SB, Breathnach R, Jeltsch JM, et al. (1984). "Sequence of the pS2 mRNA induced by estrogen in the human breast cancer cell line MCF-7.". Nucleic Acids Res. 12 (6): 2861–78. PMID 6324130.
Hanby AM, Poulsom R, Singh S, et al. (1993). "Spasmolytic polypeptide is a major antral peptide: distribution of the trefoil peptides human spasmolytic polypeptide and pS2 in the stomach.". Gastroenterology 105 (4): 1110–6. PMID 8405856.
Polshakov VI, Frenkiel TA, Westley B, et al. (1996). "NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure.". Eur. J. Biochem. 233 (3): 847–55. PMID 8521850.
Gött P, Beck S, Machado JC, et al. (1997). "Human trefoil peptides: genomic structure in 21q22.3 and coordinated expression.". Eur. J. Hum. Genet. 4 (6): 308–15. PMID 9043862.
Seib T, Blin N, Hilgert K, et al. (1997). "The three human trefoil genes TFF1, TFF2, and TFF3 are located within a region of 55 kb on chromosome 21q22.3.". Genomics 40 (1): 200–2. doi:10.1006/geno.1996.4511. PMID 9070946.
Polshakov VI, Williams MA, Gargaro AR, et al. (1997). "High-resolution solution structure of human pNR-2/pS2: a single trefoil motif protein.". J. Mol. Biol. 267 (2): 418–32. doi:10.1006/jmbi.1997.0896. PMID 9096235.
Chadwick MP, Westley BR, May FE (1997). "Homodimerization and hetero-oligomerization of the single-domain trefoil protein pNR-2/pS2 through cysteine 58.". Biochem. J. 327 ( Pt 1): 117–23. PMID 9355742.
Chen H, Lin RJ, Xie W, et al. (1999). "Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase.". Cell 98 (5): 675–86. PMID 10490106.
Newton JL, Allen A, Westley BR, May FE (2000). "The human trefoil peptide, TFF1, is present in different molecular forms that are intimately associated with mucus in normal stomach.". Gut 46 (3): 312–20. PMID 10673290.
Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21.". Nature 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953.