A B S T R A C T A specific and reproducible double antibody radioimmunoassay for the measurement of thyroglobulin (HTg) in human serum has been developed. Since antithyroglobulin autoantibodies combine with the ["3'I] HTg tracer, antibody-positive sera were rejected for measurement. Specificity is demonstrated in that thyroid analogous such as thyroxine (T4), triiodothyronine (T3) monoiodotyrosine (MIT) and diiodotyrosine (DIT) did not crossreact. Sera previously reacted with anti-HTg-Sepharose contained no immunoassayable HTg. Finally, sera obtained from patients after total thyroid ablation for thyroid carcinoma did not contain demonstrable HTg. The sensitivity of the assay is 1.6 ng/ml, and HTg was detectable in 74% of 95 normal subjects. The mean concentration was 5.1 ng/ml ±0.49 SEM (range < 1.6-20.7 ng/ml). Day to day variation in HTg levels is large in some euthyroid subjects and nearly absent in others. HTg was detectable in 90% of the sera obtained in 23 pregnant women at delivery in whom a mean concentration of 10.1 ng/ml ±1.3 SEM was observed. The mean level for the corresponding newborn infants at birth was 29.3 ng/ml ±4.7 SEM a value significantly higher than the mean maternal HTg concentration (P < 0.001). A group of 17 thyrotoxic individuals all had elevated HTg levels; the mean for this group was 344.8 ng/ml ±90.7 SEM. In the acute phase of subacute thyroiditis HTg was also elevated in all of 12 patients, and the mean for this group was 136.8 ng/ml ±74.6 SEM.
The aim of this work was to design and utilize a bifunctional peptide inhibitor called glutamic acid decarboxylase-bifunctional peptide inhibitor to suppress the progression of type 1 diabetes in non-obese diabetic mice. The hypothesis is that glutamic acid decarboxylase-bifunctional peptide inhibitor binds simultaneously to major histocompatibility complex-II and intercellular adhesion molecule type 1 on antigen-presenting cell and inhibits the immunological synapse formation during T-cell-antigen-presenting cell interactions. Glutamic acid decarboxylase-bifunctional peptide inhibitor was composed of a major epitope of the type 1 diabetes-associated antigen, glutamic acid decarboxylase 65 kDa, covalently linked to a peptide derived from CD11a of lymphocyte function-associated antigen-1. The suppression of insulitis and type 1 diabetes was evaluated using non-obese diabetic and non-obese diabetic severe combined immunodeficiency mice. Glutamic acid decarboxylase-bifunctional peptide inhibitor had the capacity to suppress invasive insulitis in non-obese diabetic mice. CD4+ T-cells isolated from glutamic acid decarboxylase-bifunctional peptide inhibitor treated mice also suppressed insulitis and hyperglycemia when transferred with diabetogenic non-obese diabetic spleen cells into non-obese diabetic severe combined immunodeficiency recipients. As predicted, the glutamic acid decarboxylase-bifunctional peptide inhibitor cross-linked a significant fraction of major histocompatibility complex class-II molecules to intercellular adhesion molecule type 1 molecules on the surface of live antigen-presenting cell. Intravenous injection of the glutamic acid decarboxylase-bifunctional peptide inhibitor elicited interleukin-4-producing T-cells in non-obese diabetic mice primed against the glutamic acid decarboxylase-epitope peptide. Together, the results indicate that glutamic acid decarboxylase-bifunctional peptide inhibitor induces interleukin-4-producing regulatory cells but does not expand the glutamic acid decarboxylase-specific Th2 population. Given that Th2 effector cells can cause pathology, the glutamic acid decarboxylase-bifunctional peptide inhibitor may represent a novel mechanism to induce interleukin-4 without Th2-associated pathology.
The mitochondrial distribution pattern has been monitored in normally cleaving and developmentally arrested preimplantation mouse embryos in vitro and compared with the distribution found immediately after flushing from the oviduct in vivo. Mitochondria in normally cleaving embryos in vitro and in vivo were found to be homogeneously distributed throughout the cytoplasm of the blastomeres during interphase. In developmentally arrested embryos in vitro the mitochondria became progressively aggregated and localized in the perinuclear region and the area of the cytocortex immediately adjacent to the plasma membrane. Injection of G2 cell cycle cytoplasmic factor(s) from a cycling 2-cell embryo into an arrested embryo resulted in the re-initiation of normal cleavage. Concomitant with the re-initiation of cleavage, a re-distribution of the aggregated mitochondria to the pattern, associated with normally cycling embryos, was observed. Specific mitochondrial translocations to the mitotic spindle were observed during cleavage. The results have shown that observation of the mitochondrial distribution using the vital stain Rhodamine 123, provides an accurate and reliable prediction of an embryo's ability to proceed through the next cleavage stage and develop in vitro and suggests that the specific association of mitochondria with the mitotic spindle is a prerequisite for normal cleavage.
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