Comparison of vertical bone resorption following various types of autologous block bone grafts.

BACKGROUND: This study aims to measure and compare the differences in vertical bone resorption after vertical augmentation using different types of autologous block bone. METHODS: Data were collected from 38 patients who had undergone vertical ridge augmentation using an autologous block bone before implant insertion. The patients were divided into three groups based on the donor sites: ramus bone (RB), chin bone (CB), and iliac crestal bone (IB). RESULTS: The surgical outcome of the augmentation was evaluated at the follow-up periods up to 60 months. In 38 patients, the mean amount of vertical bone gain was 8.36 ± 1.51 mm in the IB group, followed by the RB group (4.17 ± 1.31 mm) and the CB group (3.44 ± 1.08 mm). There is a significant difference in vertical bone resorption between the groups (p < 0.001), and the RB group demonstrated significantly lower resorption than the CB and IB groups (p = 0.011 and p < 0.001, respectively). The most common postoperative complications included neurosensory disturbance in the CB graft and gait disturbance in the IB graft. Out of the 92 implants inserted after augmentation, four implants were lost during the study period, resulting in an implant success rate of 95.65%. CONCLUSIONS: The RB graft might be the most suitable option for vertical augmentation in terms of maintaining postoperative vertical height and reducing morbidity, although the initial gain was greater with the IB graft compared to other block bones.

How much does fat mass change affect serum uric acid levels among apparently clinically healthy Korean men?

OBJECTIVE: The aim of this study was to examine the impact of fat mass alteration on serum uric acid (SUA) levels in apparently clinically healthy men. METHODS: We evaluated 27,387 men who consecutively underwent health check ups between 2015 and 2017. We assessed the likelihood of achieving a SUA level of <0.41 mmol/L and compared the SUA levels according to fat mass changes. RESULTS: Compared with those without fat mass change (the reference group), the odds ratios (95% confidence interval) of achieving a SUA level of <0.41 mmol/L for fat mass decreases of ⩾2.5, 1.5-2.5, and 0.5-1.5 kg were 1.63 (1.45-1.82), 1.19 (1.06-1.34), and 1.07 (0.97-1.18), respectively, while those for a fat mass increase of ⩾2.5, 1.5-2.5, and 0.5-1.5 kg were 0.71 (0.64-0.78), 0.87 (0.79-0.97), and 0.95 (0.86-1.04), respectively. The corresponding beta-coefficients of SUA levels (mmol/L) were -0.26 [-0.29-(-0.23)], -0.12 [-0.16-(-0.09)], and -0.09 [-0.12-(-0.06)] for fat mass decreases of ⩾2.5, 1.5-2.5, and 0.5-1.5 kg, respectively. Every 1-kg fat mass reduction was associated with 9% increased odds of achieving the target SUA level. The multivariate SUA level difference per 1-kg fat mass gain was 2.97 µmol/L. Similar levels of association persisted among the prespecified subgroups. CONCLUSION: We quantitatively demonstrated that fat mass reduction contributes to a clinically relevant decrease in SUA levels and a significant increase in the likelihood of achieving target SUA levels. Our findings may help to provide clear clinical guidance on fat mass alteration to reduce SUA levels in patients with hyperuricemia.

A missense mutation (c.1963A

Serum Ca(++) levels play important roles in the humoral immunity. The aim of this study was to detect quantitative trait loci and the associated positional candidate genes affecting baseline serum Ca(++) concentrations. A genome-wide association study was conducted in an F(2) intercross population between Landrace and Korean native pigs using the porcine single nucleotide polymorphism (SNP) 60 K beadchip and the PLINK program based on linear regression. Data used in the study included 410 F(2) pigs. All experimental animals were genotyped with 36,613 SNP markers located throughout the pig autosomes. We identified a strong association between a SNP marker on chromosome 7 and serum Ca(++) levels (DIAS0002191, genomic control-corrected P = 7.7 × 10(-5)). The position of DIAS0002191 was closely located to SLA class III region containing the C2 gene encoding the complementary component 2 protein, a protein which is important in the humoral immune responses. De novo sequencing of the porcine C2 gene revealed a missense mutation [c.1963A

Rapid analysis of proteomic biomarkers expressed in human endometrial stromal cells during decidualization.

Decidualization of human endometrial stromal (ES) cells plays a critical role in successful uterine implantation. Therefore, monitoring of the behavior of human ES cells may provide the clue for early detection of a uterine abnormality such as sterility and abortion. Monitoring of decidualization in vitro cell culture system fundamentally depends on expression of the definite biomarkers. In this study, we tried to uncover novel marker proteins of 8-bromo-cyclic adenosine monophosphate (8-Br-cAMP)-induced decidualization in human ES cells using the surface enhanced laser desorption/ionization time-of-flight mass spectrometry (SELDI-TOF-MS). Samples were divided into three groups; control human ES cells (n=7), ES cells treated with 8-Br-cAMP (n=7 per each treatment, treated for 3, 6, 9, or 12 days), and cells from which 8-Br-cAMP was withdrawn for 3 days (n=7) or 6 days (n=7) after 8-Br-cAMP treatment for 6 days. Differential expressions between non-decidual control cells and 8-Br-cAMP-induced decidual cells were observed in the peaks of 9787.058 Da, 10115.45 Da, and 24031.25 Da, detected by H4 ProteinChip, and in the peaks of 10833.08 Da, 22440.88 Da, and 32777.38 Da, detected by CM10 ProteinChip. The expression patterns of these decidual markers are expected to provide invaluable information in monitoring cellular development, and further identification of these proteins may hopefully offer precious means for clinical research and therapeutic purposes.

Activation of phospholipase D by 8-Br-cAMP occurs through novel pathway involving Src, Ras, and ERK in human endometrial stromal cells.

We investigated the mechanism of 8-Br-cAMP-mediated phospholipase D (PLD) activation using a primary cell culture system of human endometrial stromal cells (ES cells). PLD activity was increased by the treatment of ES cells with 8-Br-cAMP, maximally at 5 min. To determine whether the effects of 8-Br-cAMP on PLD occurred as a consequence of PKC activation, ES cells were preincubated for 15 min with RO320432 (1 microM) and GF109203X (1 microM), the PKC inhibitors, or they were pretreated for 24h with phorbol myristate acetate (100 nM) to downregulate PKC. However, these treatments had no effects on PLD activation induced by 8-Br-cAMP. Furthermore, 8-Br-cAMP had no effects on the subcellular distribution of PKC alpha and PKC betaI, confirming no involvement of PKC. 8-Br-cAMP activated ERK1/2, maximally at 5 min, and PD98059 (MEK inhibitor: 50 microM) and transfection of ES cells with dominant negative (DN)-MEK completely inhibited 8-Br-cAMP-induced PLD activation, suggesting that ERK1/2 mediates the PLD activation. To investigate the involvement of protein kinase A (PKA), Src, and Ras in 8-Br-cAMP-induced PLD activation, we used PKA inhibitor, H89 and Rp-cAMPs, and transfections of DN-Src and DN-Ras. H-89 and Rp-cAMPs completely blocked 8-Br-cAMP-mediated PLD and ERK activation, implying the involvement of PKA in this PLD activation. In addition, transfection of ES cells with DN-Src, or DN-Ras partially inhibited 8-Br-cAMP-induced ERK1/2 and consequently PLD activation, whereas cotransfection of DN-Src and DN-Ras completely inhibited ERK1/2 and PLD activation, suggesting that Src and Ras independently regulate ERK/PLD activation. Taken together, these results demonstrate a novel pathway in ES cells that 8-Br-cAMP activate PLD through PKA and ERK1/2 and this ERK/PLD activation by 8-Br-cAMP is mediated by Src and Ras, separately.