Structure, composition, and mechanical properties of Australian orthodontic wires

Objective: To investigate the surface morphology, structure, elemental composition, and key mechanical properties of various sizes and tempers of Australian wires. Materials and Methods: Three types of Australian wire were used: 0.016" regular, 0.018" regular+, and 0.018" special+ (A.J. Wilcock, Whittlesea, Victoria, Australia). Each type of wire was subjected to scanning electron microscopy (SEM) analysis, x-ray energy dispersive spectroscopy (EDS) investigation, Vickers hardness testing, and tensile testing. The modulus of elasticity and ultimate tensile strength were determined. Hardness, modulus, and strength data were analyzed with one-way analysis of variance (ANOVA) and Tukey testing at the .05 level of significance. Results: All three types of Australian wire were found to possess considerably rough surfaces with striations, irregularities, and excessive porosity. All three wire types had high levels of carbon and a similar hardness, which ranged within 600 VHN (Vickers hardness number), and a similar modulus of elasticity (173 to 177 GPa). The 0.018" special+ had a significantly lower tensile strength (1632 MPa) than the 0.016" regular and the 0.018" regular+ wire (2100 MPa). Conclusions: Australian wires did not show variation implied by the size or temper of the wires. © 2009 by The EH Angle Education and Research Foundation, Inc

The flaky skin (fsn) mutation in mice: map location and description of the anemia.

Flaky skin (gene symbol fsn) is an autosomal recessive mutation that causes pleiotropic effects of anemia, papulosquamous skin disorder, and gastric forestomach hyperplasia. In this report, we assign fsn to distal chromosome 17 and characterize the anemia. The decrease in hematocrit levels and red blood cell counts is significant and persists throughout life in fsn/fsn mice. There is compensatory enlargement of the heart, liver, and spleen by 8 weeks of age, whereas the thymus is less than one half normal weight. Nucleated cell counts in the peripheral blood are increased 15- to 30-fold, primarily due to an increased percentage of normoblasts. The fsn/fsn mice examined at 8 weeks of age have significantly increased reticulocyte counts and protoporphyrin levels but reduced hemoglobin concentration, suggesting possible abnormalities of hemoglobin metabolism. Erythrocyte membrane fragility is normal. Compared with normal +/? littermates, fsn/fsn mice (1) lack splenic and hepatic stores of elemental iron, (2) have the ability to transport 59Fe across the duodenal cells and into the blood, (3) have increased levels of transferrin in serum, and (4) have acute loss of urinary 59Fe. Hemolysis is indicated by increased serum bilirubin and high blood reticulocyte numbers. Collectively, the genetic, hematologic, and pathologic data indicate a severe hematologic disorder caused by homozygosity for the fsn mutation that differs from other known hematologic mutations in the mouse. The mechanism whereby fsn induces the reported pleiotropic effects has yet to be elucidated

Lymphadenopathy, elevated serum IgE levels, autoimmunity, and mast cell accumulation in flaky skin mutant mice.

The autosomal recessive mutation flaky skin (fsn) causes pleiotropic abnormalities in the immune and hematopoietic systems accompanied by pathologic changes in the skin. Homozygotes (fsn/fsn) showed increased size and histological alterations in the spleen and lymph nodes. Abnormalities in lymphoid architecture of the spleen in fsn/fsn mice were accompanied by marked increases in total numbers of B cells, macrophages, and immature erythroid cells. Splenic B cells displayed elevated MHC class II expression. Serum IgE levels were greater than 100 microg/ml by 10 weeks of age, representing \u3e 7000-fold increase compared with normal littermates. This increased IgE level was associated with elevated IL-4 production by spleen cells and with increased amounts of serum IL-4. Serum IgM, IgG1, and IgG2b levels were also increased in fsn/fsn mice while IgG3 was decreased. Autoimmunity in fsn/fsn mice was evidenced by glomerulonephritis accompanied by immune complex deposition in the kidneys, increased serum blood urea nitrogen levels, and the presence of circulating anti-double-stranded DNA autoantibodies. Pathological changes in the skin of fsn/fsn mice were characterized by epidermal hyperplasia and mixed dermal inflammation. Increased numbers of mast cells were also observed in the dermis of the truncal skin as well as in the epithelial stomach. These marked immunological abnormalities suggest that the fsn locus encodes a major immunoregulatory molecule important in multiple immune and hematopoietic functions

Isolation and characterization of a monoclonal anti-quadruplex DNA antibody from autoimmune viable motheaten mice.

A cell line that produces an autoantibody specific for DNA quadruplex structures has been isolated and cloned from a hybridoma library derived from 3-month-old nonimmunized autoimmune, immunodeficient viable motheaten mice. This antibody has been tested extensively in vitro and found to bind specifically to DNA quadruplex structures formed by two biologically relevant sequence motifs. Scatchard and nonlinear regression analyses using both one- and two-site models were used to derive association constants for the antibody-DNA binding reactions. In both cases, quadruplexes had higher association constants than triplex and duplex molecules. The anti-quadruplex antibody binds to the quadruplex formed by the promoter-region-derived oligonucleotide d(CGCG4GCG) (Ka = 3.3 x 10(6) M-1), and has enhanced affinity for telomere-derived quadruplexes formed by the oligonucleotides d(TG4) and d(T2G4T2G4T2G4T2G4) (Ka = 5.38 x 10(6) and 1.66 x 10(7) M-1, respectively). The antibody binds both types of quadruplexes but has preferential affinity for the parallel four-stranded structure. In vitro radioimmunofilter binding experiments demonstrated that purified anti-DNA quadruplex antibodies from anti-quadruplex antibody-producing tissue culture supernatants have at least 10-fold higher affinity for quadruplexes than for triplex and duplex DNA structures of similar base composition and length. The antibody binds intramolecular DNA triplexes formed by d(G4T3G4T3C4) and d(C4T3G4T3G4), and the duplex d(CGCGCGCGCG)2 with an affinities of 6. 76 x 10(5), 5.59 x 10(5), and 8.26 x 10(5) M-1, respectively. Competition experiments showed that melted quadruplexes are not effective competitors for antibody binding when compared to native structures, confirming that the quadruplex is bound structure-specifically. To our knowledge, this is the first immunological reagent known to specifically recognize quadruplex structures. Subsequent sequence analysis demonstrates homologies between the antibody complementarity determining regions and sequences from Myb family telomere binding proteins, which are hypothesized to control cell aging via telomeric DNA interactions. The presence of this antibody in the autoimmune repertoire suggests a possible linkage between autoimmunity, telomeric DNA binding proteins, and aging

The Tetratricopeptide repeat domain 7 gene is mutated in flaky skin mice: a model for psoriasis, autoimmunity, and anemia.

The flaky skin (fsn) mutation in mice causes pleiotropic abnormalities including psoriasiform dermatitis, anemia, hyper-IgE, and anti-dsDNA autoantibodies resembling those detected in systemic lupus erythematosus. The fsn mutation was mapped to an interval of 3.9 kb on chromosome 17 between D17Mit130 and D17Mit162. Resequencing of known and predicted exons and regulatory sequences from this region in fsn/fsn and wild-type mice indicated that the mutation is due to the insertion of an endogenous retrovirus (early transposon class) into intron 14 of the Tetratricopeptide repeat (TPR) domain 7 (Ttc7) gene. The insertion leads to reduced levels of wild-type Ttc7 transcripts in fsn mice and the insertion of an additional exon derived from the retrovirus into the majority of Ttc7 mRNAs. This disrupts one of the TPRs within TTC7 and may affect its interaction with an as-yet unidentified protein partner. The Ttc7 is expressed in multiple types of tissue including skin, kidney, spleen, and thymus, but is most abundant in germinal center B cells and hematopoietic stem cells, suggesting an important role in the development of immune system cells. Its role in immunologic and hematologic disorders should be further investigated