Soft-tissue changes after maxillomandibular advancement surgery assessed with cone-beam computed tomography.

INTRODUCTION: The purpose of this study was to quantify anteroposterior and transverse facial soft-tissue changes with respect to underlying skeletal movements after maxillomandibular advancements by using cone-beam computed tomography. METHODS: Thirty white patients were treated by maxillomandibular advancements after LeFort I osteotomies and bilateral sagittal split osteotomies. The patients were scanned by using cone-beam computed tomography within 1 week before the surgery, within 1 week after the surgery, and a minimum of 8 weeks postsurgery. We measured the differences between the first and last images and calculated ratios for anteroposterior and transverse soft-to-hard tissue movements. Changes in the greatest interalar width were also measured. RESULTS: There was a statistically significant difference in the greatest interalar width change between patients receiving maxillary advancements greater than 4 mm and those having advancements less than or equal to 4 mm (P <0.023). Mean ratios of anteroposterior soft-to-hard tissue movements were 84.9% +/- 38.0% in the malar region, 96.1% +/- 15.5% in the chin, and 101.1% +/- 27.3% in the subcommissural region. Mean ratios of transverse soft-to-hard tissue movements were 39.4% +/- 19.7% in the malar region and 82.5% +/- 56.7% in the subcommissural region. CONCLUSIONS: The amount of maxillary advancement most likely plays a role in the postsurgical increase in interalar width. In addition, facial soft tissues appear to respond more to anterior movement of the jaws than to an increase in transverse dimensions after maxillomandibular advancements.

Identification of a novel membrane-associated gene product that suppresses toxicity of a TrfA peptide from plasmid RK2 and its relationship to the DnaA host initiation protein.

The toxicity of a peptide derived from the amino-terminal portion of 33-kDa TrfA, one of the initiation proteins encoded by the broad-host-range plasmid RK2, was suppressed by a host protein related to DnaA, the initiation protein of Escherichia coli. The newly identified 28.4-kDa protein, termed a DnaA paralog (Dp) because it is similar to a region of DnaA but likely has a different function in initiation of plasmid RK2 replication, interacts physically with the 33-kDa TrfA initiation protein, including the initiation-active monomeric form. The Dp has a cellular distribution similar to that of the 33-kDa TrfA initiation protein, being found primarily in the inner membrane fraction, with lesser amounts detected in the outer membrane fraction and almost none in the soluble fraction of E. coli. Maintenance and inner membrane-associated replication of plasmid RK2 were enhanced in a Dp knockout strain and inhibited in strains containing extra copies of the Dp gene or in membrane extracts to which a tagged form of Dp was added. Recently, the Dp was independently shown to help prevent overinitiation in E. coli and was termed Hda (S. Kato and T. Katayama, EMBO J. 20:4253-4262, 2001).