Effect of compressive force combined with vibration on CCL2 and CCL5 in human periodontal ligament cells.

Purpose: To investigate the effect of compressive force combined with vibration on expression of CC-chemokine ligand 2 (CCL2) and 5 (CCL5) in human periodontal ligament (hPDL) cells.

Methods: Human PDL cells were cultured and assigned into four groups: control (Con), compressive force 2.0 g/cm for 24 h and 48 h (C), vibration 0.

Biocompatibility and mineralization activity of modified glass ionomer cement in human dental pulp stem cells.

Background/purpose: Fortilin is a multi-functional protein involved in several cellular processes. It has been shown promising potential to be a bioactive molecule that can be incorporated in the dental materials. This study aimed to compare the biocompatibility and mineralization activities of modified glass ionomer cement (Bio-GIC) and Biodentine by direct and indirect method on human dental pulp stem cells (hDPSCs).

Biological Activities of Glass Ionomer Cement Supplemented with Fortilin on Human Dental Pulp Stem Cells.

This study aimed to determine the most suitable recombinant fortilin and evaluate the biological activities of glass ionomer cement (GIC) incorporated with fortilin on human dental pulp stem cells (hDPSCs). Full-length and three fragments of fortilin were cloned and examined for their proliferative and cytoprotective effects on hDPSCs by MTT (3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide) assay. Human DPSCs were cultured with GIC supplemented with fortilin, tricalcium phosphate, or a combination of tricalcium phosphate and fortilin, designated as GIC + FL, GIC + TCP, and GIC + TCP + FL, respectively ( = 4 for each group).

Long-Term Effect of Modified Glass Ionomer Cement with Mimicked Biological Property of Recombinant Translationally Controlled Protein.

This study modified glass ionomer cement (GIC) by adding mimicked biological molecules to reduce cell death. GIC was modified to BIOGIC by adding chitosan and bovine serum albumin for enhancing protein release. The BIOGIC was supplemented with tricalcium phosphate (TCP) and recombinant translationally controlled tumor protein (TCTP) to improve its biological properties.

Effects of tannin-fluoride and milk-fluoride mixture on human enamel erosion from inappropriately chlorinated pool water.

This in vitro study aimed to investigate the efficacy of tannin-fluoride and milk-fluoride mixtures on human enamel erosion after exposure to inappropriately chlorinated pool water. Enamel specimens were immersed in swimming pool water (pH 2.7) for 30 min and in each test reagent for 4 min once a day for 60 consecutive days (group I: control, group II: tannin-fluoride, group III: milk-fluoride, group IV: tannin-fluoride before and milk-fluoride after erosive challenge, and group V: milk containing tannin-fluoride before and after erosive exposure).

Expression of translationally controlled tumor protein in heat-stressed human dental pulp cells.

Objective: The aim of this study was to investigate the effects of heat stress on cell viability, translationally controlled tumor protein (TCTP) expression, and the effects of recombinant TCTP on heat-stressed human dental pulp cells (HDPCs).

Methods: HDPCs were isolated from human teeth and cultured at 37°C. For heat stress, HPDCs were incubated at 43°C for 45min.

Identification of a novel nuclear localization signal and speckle-targeting sequence of tuftelin-interacting protein 11, a splicing factor involved in spliceosome disassembly.

Tuftelin-interacting protein 11 (TFIP11) is a protein component of the spliceosome complex that promotes the release of the lariat-intron during late-stage splicing through a direct recruitment and interaction with DHX15/PRP43. Expression of TFIP11 is essential for cell and organismal survival. TFIP11 contains a G-patch domain, a signature motif of RNA-processing proteins that is responsible for TFIP11-DHX15 interactions.

TFIP11 interacts with mDEAH9, an RNA helicase involved in spliceosome disassembly.

Yeast proteins Ntr1, Ntr2 and Prp43 function in spliceosome disassembly. An Ntr1-Ntr2 protein complex recruits Prp43 to allow the removal of the lariat-intron in late-stage RNA splicing activity. Based on amino-acid sequence similarities across species, TFIP11 and mDEAH9/Dhx15 have been identified as homologues of yeast Ntr1 and Prp43, respectively.

TFIP11, CCNL1 and EWSR1 Protein-protein Interactions, and Their Nuclear Localization.

Previous studies using the yeast two-hybrid assay (Y2H) have identified cyclin L1 (CCNL1) and Ewing sarcoma breakpoint region 1 protein (EWSR1) as being interacting partners of tuftelin-interacting protein 11 (TFIP11). All three proteins are functionally related to the spliceosome and involved in pre-mRNA splicing activities. The spliceosome is a dynamic ribonucleoprotein complex responsible for pre-mRNA splicing of intronic regions, and is composed of five small nuclear RNAs (snRNAs) and μ140 proteins.

Using the yeast two-hybrid assay to discover protein partners for the leucine-rich amelogenin peptide and for tuftelin-interacting protein 11.

The established structural proteins of the enamel matrix are amelogenin, ameloblastin, and enamelin. Historically, tuftelin and tuftelin-interacting protein 11 (TFIP11) have also been discussed as possible enamel proteins. Protein complexes are achieved by protein-protein interactions, and it is protein complexes that control biomineralization.

An amelogenin minigene to study alternative splicing.

Diversity in gene expression is commonly observed as a result of alternative splicing of RNA transcripts. This is true in the case of amelogenin, one of the enamel matrix proteins. Our hypothesis is that additional amelogenin mRNA transcripts are generated in vivo, but these transcripts have yet to be observed because of the limitations of currently used detection methodologies.

Enamel matrix protein interactions.

Unlabelled: The recognized structural proteins of the enamel matrix are amelogenin, ameloblastin, and enamelin. While a large volume of data exists showing that amelogenin self-assembles into multimeric units referred to as nanospheres, other reports of enamel matrix protein-protein interactions are scant. We believe that each of these enamel matrix proteins must interact with other organic components of ameloblasts and the enamel matrix.