Does the Rigid External Distraction Device Alter Maxillary Pitch in Cleft Maxillary Distraction?

The rigid external distraction (RED) device is reported to have the ability to three-dimensionally reposition the maxilla. The purpose of this study is to assess the ability of RED to intentionally alter the maxillary pitch.Retrospective cohort study.Institutional practice.A retrospective chart review was completed over the past 12 years and a total of 50 patients met the inclusion criteria.Cephalometric changes and alteration in palatal plane angle.Cephalometric analysis of standardized landmarks was completed on calibrated, standardized lateral cephalograms. Pre-distraction and post-consolidation variables were compared via a two-tailed paired t-test.The mean age at surgery of 12.2 ± 3.2 years. Through distraction osteogenesis (DO), the maxilla was moved anteriorly with a mean distraction distance of 8.4 ± 4.8 mm. The mean change in the angles sella-nasion-A-point angle (SNA), sella-nasion-B-point angle (SNB), and A-point-nasion-B-point angle (ANB) were 10.2 ± 4.8, 0.9 ± 2.7, and 9.3 ± 4.1, respectively. The mean change in the palatal plane angle was -4.4 ± 3.7. The mean change in the vertical position of the anterior nasal spine (ANS) and posterior nasal spine (PNS) in relation to the Frankfort horizontal (FH) were -2.0 ± 4.1 mm and 1.7 ± 3.8 mm, respectively.This study documents short-term findings of RED in a large cleft lip and palate (CLP) population. Despite positioning of distraction eyelets superior to the theoretical center of resistance, a counterclockwise (CCW) rotation of the palatal plane occurred. This suggests that adjunctive methods of vector control should be considered if clockwise (CW) rotation of the palatal plane is intended with the RED device.

The mammalian phosphate carrier SLC25A3 is a mitochondrial copper transporter required for cytochrome c oxidase biogenesis.

Copper is required for the activity of cytochrome c oxidase (COX), the terminal electron-accepting complex of the mitochondrial respiratory chain. The likely source of copper used for COX biogenesis is a labile pool found in the mitochondrial matrix. In mammals, the proteins that transport copper across the inner mitochondrial membrane remain unknown. We previously reported that the mitochondrial carrier family protein Pic2 in budding yeast is a copper importer. The closest Pic2 ortholog in mammalian cells is the mitochondrial phosphate carrier SLC25A3. Here, to investigate whether SLC25A3 also transports copper, we manipulated its expression in several murine and human cell lines. SLC25A3 knockdown or deletion consistently resulted in an isolated COX deficiency in these cells, and copper addition to the culture medium suppressed these biochemical defects. Consistent with a conserved role for SLC25A3 in copper transport, its heterologous expression in yeast complemented copper-specific defects observed upon deletion of PIC2 Additionally, assays in Lactococcus lactis and in reconstituted liposomes directly demonstrated that SLC25A3 functions as a copper transporter. Taken together, these data indicate that SLC25A3 can transport copper both in vitro and in vivo.