High impact information on Tuft1

• Tuftelin-interacting protein (TFIP11) was first identified in a yeast two-hybrid screening as a protein interacting with tuftelin [1].
• 9. Comparison of the bovine, mouse, and porcine cDNAs supports the revised bovine tuftelin amino acid sequence and suggests that the bovine tuftelin translation initiation codon be re-assigned to a more 5' ATG [2].
• DNA sequence characterization of an RT-PCR amplification product confirmed expression of tuftelin in kidney, and identified an alternatively spliced mouse tuftelin mRNA lacking exon 2 [2].
• Published sequences for bovine tuftelin cDNA and genomic clones proposed different reading frames that radically affected the derived amino acid sequence of the tuftelin carboxyl-terminus [2].
• Northern blot analysis reveals that tuftelin is not ameloblast-specific but is expressed in multiple tissues, including kidney, lung, liver, and testis [2].

Biological context of Tuft1

• Our results showed the initial detection of tuftelin transcripts within proliferating inner enamel epithelial cells at very early stages of tooth development (13 days of embryonic development equivalent to the bud stage of tooth development) [3].
• The ameloblast phenotype has been characterized as consisting of two major classes of proteins: amelogenins and non-amelogenin proteins such as anionic enamel proteins (enamelins, tuft proteins, tuftelin, sulfated proteins) and enamel proteases [3].
• Using fluorescent-tagged tuftelin and amelogenin plasmid constructs we saw little evidence that these two enamel proteins colocalize in ameloblast-like LS-8 cells [4].
• In an attempt to better define a physiological function for tuftelin during amelogenesis, we have produced transgenic mice that overexpress tuftelin in ameloblasts and subsequently the enamel matrix [4].
• These studies also suggest that the regulatory mechanisms controlling tuftelin gene expression are different than the mechanisms regulating ameloblastin and amelogenin transcription [5].

Anatomical context of Tuft1

• Tuftelin was detected within the odontoblast processes during earlier stages of development (E19 and 1 day postnatal), whereas during later stages (3-11 days) it was recognized in a portion of the enamel layer adjacent to the dentine-enamel junction [6].
• In the present study, we designed experiments to characterize one of the anionic enamel proteins from mouse molars, tuftelin, and to determine the timing of expression of this protein during molar tooth development [3].
• In addition, tuftelin was found to be synthesized also by dental papilla mesenchyme cells suggesting that this protein is not enamel-specific [3].
• Using immunohistochemistry, amelogenin and tuftelin enamel proteins were detected in the enamel organ of many species investigated, but tuftelin epitopes were also found in other tissues [7].

Associations of Tuft1 with chemical compounds

• It might also suggest a possible different role for tuftelin than nucleator of hydroxyapatite crystals [3].

Other interactions of Tuft1

• Adjacent sections were exposed to antibodies against either tuftelin or various amelogenin epitopes [6].
• The established cell line (ameloblast-lineage cell; ALC) maintained the expression of several ameloblast specific genes (Amelogenin, Tuftelin, and Enamelin) in long-term culture [8].
• In conclusion, our studies showed that the increase in enamel matrix formation by overexpression of IGFs is the result of transcriptional regulation of enamel specific proteins like amelogenin and ameloblastin but not tuftelin [5].

References