A prospective evaluation of Bass, Bionator and Twin Block appliances. Part I--The hard tissues

A prospective clinical study with a random allocation of 47 adolescent patients to three different functional appliance groups was established and compared with an untreated control group over a 9-month period. Treatment was undertaken with either a Bionator, Twin Block, or Bass appliance. Pre- and post-treatment cephalograms were used to quantify the skeletal and dentoalveolar changes produced by the appliances and compared with those observed in the control group as a result of growth. Both the Bionator and Twin Block appliances demonstrated a statistically significant increase in mandibular length (3.9 +/- 2.7 mm; 3.7 +/- 2.1 mm, respectively) compared with the control group (P < 0.05), with an anterior movement of pogonion and point B. Highly statistically significant increases (P < 0.01) were seen in lower face heights for all the appliance groups compared with the control group. The Twin Block group showed the least forward movement of point A due to a change in the inclination of the maxillary plane. The Bionator and Twin Block groups showed statistically significant reductions in the inclination of the upper incisors to the maxillary plane (P < 0.05). The Bass group showed minimal change in the inclination of the lower labial segment to the mandibular plane. The Bionator group demonstrated the greatest proclination of the lower labial segment (4.0 +/- 3.6 degrees). Clinically important changes were measured in all the appliance groups when compared with the control group. Differences were also identified between the functional appliance groups. The Twin Block appliance and, to a lesser extent, the Bionator appeared the most effective in producing sagittal and vertical changes.     

Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes

Immunoprecipitation of unactivated avian progesterone receptor results in the copurification of hsp90, hsp70, and three additional proteins, p54, p50, and p23. p23 is also present in immunoaffinity-purified hsp90 complexes along with hsp70 and another protein, p60. Antibody and cDNA probes for p23 were prepared in an effort to elucidate the significance and function of this protein. Antibodies to p23 detect similar levels of p23 in all tissues tested and cross-react with a protein of the same size in mice, rabbits, guinea pigs, humans, and Saccharomyces cerevisiae, indicating that p23 is a conserved protein of broad tissue distribution. These antibodies were used to screen a chicken brain cDNA library, resulting in the isolation of a 468-bp partial cDNA clone encoding a sequence containing four sequences corresponding to peptide fragments isolated from chicken p23. This partial clone was subsequently used to isolate a full-length human cDNA clone. The human cDNA encodes a protein of 160 amino acids that does not show homology to previously identified proteins. The chicken and human cDNAs are 88% identical at the DNA level and 96.3% identical at the protein level. p23 is a highly acidic phosphoprotein with an aspartic acid-rich carboxy-terminal domain. Bacterially overexpressed human p23 was used to raise several monoclonal antibodies to p23. These antibodies specifically immunoprecipitate p23 in complex with hsp90 in all tissues tested and can be used to immunoaffinity isolate progesterone receptor complexes from chicken oviduct cytosol.