Relapse in Angle Class II Division 1 Malocclusion treated by tandem mechanics without extraction of permanent teeth: A retrospective analysis.

Ideal orthodontic treatment should achieve long-term stability of the occlusion. The mandibular incisor segment has been described as the segment that is most likely to exhibit relapse after treatment and retention. Therefore, relapse of this is a challenge that clinicians need to address. The purpose of this study is to evaluate the amount of relapse that may occur in Angle Class II Division 1 patients, treated orthodontically with tandem mechanics. All cases in this study were treated without extraction of permanent teeth, and the patients were followed for at least 2 years after the end of the retention phase of treatment. Six predictors were investigated at pretreatment, posttreatment, and postretention periods. A synopsis of this study shows the correction of lower incisor crowding as measured by the irregularity index was stable over 5.2 years of postretention follow-up; but longer follow-up time revealed increased relapse of incisor irregularity. Intermolar width increased during treatment and remained stable in the follow-up period. Overjet and overbite corrections and changes in the lower incisor to mandibular plane angle were also stable in the follow-up period. In addition, the amounts of overjet correction and loss of expansion of intercanine distance after treatment were associated with increased irregularity index in the follow-up period. It appears the discrepancies between this and previously published works are sufficiently dramatic that the whole question of treatment philosophy and long-term stability may need to be reevaluated.

A retrospective study of Angle Class I malocclusions treated orthodontically without extractions using two palatal expansion methods.

The correction and relapse of mandibular anterior crowding was evaluated in a population of 58 patients with Angle Class I malocclusion who were treated orthodontically without extraction of permanent teeth. The subjects were retrospectively evaluated from records taken before treatment, posttreatment, and postretention. The postretention period averaged 8 years (minimum of 4 and maximum of 20 years). All cases in Groups A and B were given orthopedic treatment to develop the maxillary apical base in the transverse and anteroposterior planes. Group A was treated with expansion of the inner bow of the face bow appliance (Kloehn), and Group B was treated with the Haas palatal expansion appliance. Both groups were then treated orthodontically with tandem mechanics. The response variables measured were: overbite, overjet, intercanine distance, intermolar distance, and irregularity index. Study groups A and B were not significantly different for subject age, retention, or postretention time. Moreover, the groups did not show significant difference for any of the response variables before treatment. However, there was a statistically significant difference in the treatment times (P =.0133). A statistically significant treatment effect was observed for most response variables in the groups. Overbite, overjet, and irregularity index were significantly reduced, intermolar distance was significantly increased, and intercanine distance showed no significant change in Groups A and B. In the postretention period, there was a tendency for variables to change slightly toward their before treatment values but no compromise of orthodontic correction was noted. The irregularity index in Group A was corrected from 4.8 to 1.1 mm and remained at 1.1 mm in the postretention period. The irregularity index in Group B was corrected from 5.1 to 1.2 mm (P =.0001) and changed slightly from 1. 2 to 1.7 mm (P =.0540) in the postretention period. We concluded that mandibular incisors tended to become more crowded postretention. However, in contrast to previous reports, we calculate this relapse to be small. Neither before treatment nor posttreatment variables were predictive of relapse.

Trichohyalin: a structural protein of hair, tongue, nail, and epidermis.

In the course of studies of desmosomes, we found trichohyalin, a 200-kDa protein of the inner root sheath and medulla, in a citric acid-insoluble fraction ("desmosome preparation") from tongue epithelium. Pig tongue epithelium yielded milligram quantities of pure trichohyalin from about 100 g of keratomed epithelium. The protein has an extended shape as determined by gel filtration, ultracentrifugation, and electron microscopy, with a rod domain and a globular domain at one end and overall dimensions of about 85 nm. Crosslinking studies suggest that the protein may be dimeric in solution. The protein is a doublet in some animals but apparently is a single polypeptide of 220 kDa in humans. Immunofluorescence studies showed that it is a major protein of the filiform papillae of the tongue of mammals and is present in isolated cells of the stratum granulosum of some regions of epidermis in a subset of cells containing filaggrin and in the nail matrix. Similarly, in filiform papillae some cells contain granules that stain for both trichohyalin and filaggrin. Immunoblotting confirmed that trichohyalin is present in tongue and epidermis. Polymerase chain reaction with human genomic DNA using oligonucleotide primers based on sheep trichohyalin resulted in synthesis of multiple DNAs, from which a 504-bp fragment was subcloned and sequenced and found to resemble closely the carboxyl terminus of sheep trichohyalin. Studies with antibody to the carboxyl-terminal 14 amino acids of the human sequence show that, whereas the carboxyl-terminal epitope is present only in the stratum granulosum, in epidermis epitopes detected by a monoclonal antibody are demonstrated in both the stratum granulosum and stratum corneum, suggesting that the carboxyl terminus is cleaved in the stratum corneum.

Trichohyalin: purification from porcine tongue epithelium and characterization of the native protein.

Trichohyalin, a protein of Mr between 190 and 220 kDa in different species, was first demonstrated in large granules of the inner root sheath and medulla of hair follicles and may provide a matrix for keratin filaments. We have purified trichohyalin in milligram quantities from a citric acid-insoluble fraction derived from pig tongue epithelium. Trichohyalin was extracted under conditions of low ionic strength from the citric acid-insoluble fraction, separated by gel-filtration chromatography in buffer containing 1 M NaBr, and concentrated by ion-exchange chromatography in buffer containing 4 M urea. The purified material, which is soluble in buffers containing 1 M NaBr, was considered to be trichohyalin because of its characteristic molecular weight and amino acid composition and its localization to hair follicle inner root sheath and medulla by indirect immunofluorescence using antibodies against the purified protein. Immunofluorescence showed that trichohyalin is a major protein of filiform papillae of the tongue. Unlike trichohyalin from other animals examined, the porcine protein is a doublet on SDS polyacrylamide gels of 195 and 210 kDa; both bands are recognized by different antibodies, their two-dimensional peptide maps are nearly identical, and they have nearly identical isoelectric points of about 6.6. Trichohyalin has a Stokes radius of 124 A on gel filtration and a Svedberg constant of 6, consistent with an extended structure. The protein probably associates reversibly in solution, and the native protein we have isolated may be dimeric, because crosslinking of the iodinated purified protein with disuccinimidyl suberate demonstrated the presence of a dimer, which could be dissociated in the presence of high concentrations of urea. Rotary shadowing electron microscopy of the native protein showed a filamentous structure averaging 85 nm in length with a single globular-appearing end-domain. The purification of native trichohyalin provides a basis for future functional studies.

Trichohyalin: presence in the granular layer and stratum corneum of normal human epidermis.

Trichohyalin, a protein contained in granules in the cells of the hair-follicle inner root sheath and in the medulla of the hair shaft, has been purified previously from sheep hair bulbs and is also a major protein of filiform papillae of tongue epithelium. Polyclonal affinity-purified antibodies and a monoclonal antibody raised to purified pig tongue trichohyalin both stained the inner root sheath of hair follicles and the medulla of hair fibers and identified human trichohyalin as a single 220-kDa band on immunoblots of human hair bulb proteins. These antibodies were used to examine human epidermis by immunofluorescence and immunoblotting. The antibodies decorate granules in cells in the granular layer and stratum corneum of non-hair-bearing human skin, and immunoblots identify a protein in epidermis comigrating with trichohyalin from human hair and human tongue epithelium. Absorption of antibody to trichohyalin on a trichohyalin affinity column abrogated staining of the epidermis and the bands on the immunoblots. Trypsin-separated epidermis contained 220 and 160 kDa bands identified as trichohyalin, but epidermis shaved from skin and quickly frozen showed only a single 220-kDa band, indicating that the 160-kDa protein was generated by proteolysis. Double immunofluorescence for trichohyalin and filaggrin showed that some cells containing filaggrin also contain trichohyalin. These studies show that trichohyalin is not limited to hair and tongue but is present in isolated cells in the granular layer and stratum corneum of normal epidermis.