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O Tarutani

Publications and source records attributed to O Tarutani.

At least 55 records · Page 3Linked to original sources
PubMed1984

Structural changes of carbohydrate chains of human thyroglobulin accompanying malignant transformations of thyroid glands.

Carbohydrate moieties were released from human thyroglobulins prepared from normal and transformed, thyroid tissues by hydrazinolysis. The oligosaccharides thus prepared were fractionated by DEAE-cellulose, Bio-Gel P-4, concanavalin-A--Sepharose and Ricinus-communis-agglutinin--Sepharose columns and were characterized by exo-glycosidase and endo-glycosidase digestions, methylation analysis and 400-MHz 1H-NMR spectroscopy. These studies showed that the alterations accompanying malignancy occurred in complex-type carbohydrate chains and exhibited the following structural features: (a) a complex-type carbohydrate chain containing 1 phosphate in a diester linkage was present in all the malignant thyroglobulins. (b) Asialo-carbohydrate chains with biosynthetically incomplete structures were found in all of the malignant thyroglobulins. (c) Carbohydrate chains of higher molecular mass, which have repeating Gal-GlcNAc disaccharides and peripheral alpha-fucosyl residues were present in metastatic papillary carcinoma.

Carbohydrate Conformation↗
PubMed1984

[Investigations on the mechanism(s) of the production of anti-thyroid hormone antibodies 3:Production of anti-rabbit thyroglobulin and anti-thyroid hormone antibodies in rabbits immunized with rabbit thyroglobulin].

Recently, the presence of anti-thyroid hormone antibodies has been reported in many cases of thyroidal and non-thyroidal disorders. In order to elucidate the immunological mechanism(s) in the production of anti-thyroid hormone antibodies, we immunized outbred rabbits and mice with different H-2 and Igh allotypes with human thyroglobulin (HTg) and showed that the production of both anti-HTg and anti-thyroid hormone antibodies is genetically controlled. In our present study, rabbit thyroglobulin (RTg) was purified from 4 rabbit thyroid glands and was immunized in two rabbits (RG-I, RG-2). The two rabbits were then serially bled and tested for the presence of anti-RTg and anti-thyroid hormone antibodies. In both rabbits, the production of anti-RTg and anti-thyroid hormone antibodies was observed. The binding constant of anti-RTg, anti-T4 and anti-T3 antibodies in RG-1 were 6 X 10(9)M-1, 9.5 X 10(8)M-1, 4.6 X 10(8)M-1, and those in RG-2 were 6.5 X 10(9)M-1, 5.6 X 10(8)M-1, 1.6 X 10(8)M-1, respectively. These results further strengthen the possibility that the antigen of the anti-thyroid hormone antibodies observed in various disorders so far reported is the HTg molecule. In addition, the fact that anti-RTg antibodies had a higher binding constant and capacity than anti-thyroid hormone antibodies suggests that the antigenic site(s) of RTg, which contains thyroid hormones, is not highly immunogenic.

Animals↗
PubMed1983

[Production of antithyroid hormone antibodies. 2. Genetic control of the production of anti-human thyroglobulin and antithyroid hormone antibodies in mice immunized with human thyroglobulin].

Recently anti-thyroid hormone antibodies have been found in many cases of thyroidal and non-thyroidal disorders. However, the exact mechanism(s) of production of anti-thyroid hormone antibodies in these patients is so far obscure. Thyroxine (T4) and triiodothyronine (T3) are haptens and are not immunogenic in free form. In this respect, human thyroglobulin (HTg) has long been suggested as an antigen of the anti-thyroid hormone antibodies observed in them because it carries thyroid hormones on its surface. In our previous communication, we reported the production of anti-HTg antibodies and anti-thyroid hormone antibodies in two rabbits and various strains of mice immunized with HTg. In order to elucidate the gene(s) which controls the production of anti-HTg and anti-thyroid hormone antibodies, various strains of mice which have different H-2 and Igh allotypes were immunized with HTg. The titers of anti-HTg and anti-thyroid hormone antibodies were measured, and the locus (loci) which controls the immune response against them was determined. Our present investigation has revealed that the Ir-gene(s) which controls the production of anti-HTg and anti-T4 antibodies is located in the I-A subregion. Concerning the production of anti-T4 antibodies in mice, the presence of Ir-gene(s) outside of H-2 is also suggested. The significance of the genetic mechanisms controlling the immune response against thyroid hormones in various thyroidal disorders is discussed.

Animals↗
PubMed1983

Genetic control of mouse antibody production to human thyroglobulin.

Genetic control of immune responses in mice against human thyroglobulin was studied using the enzyme-linked immunosorbent assay and passive haemagglutination test. Our results revealed that mice of H-2a, H-2d, H-2q, H-2k and H-2r haplotypes were high responders for antibody production to human thyroglobulin, while mice of H-2b and H-2s haplotypes were low responders. High responsiveness to human thyroglobulin was transmitted to F1 mice in a dominant fashion. Study of the genetic mapping of the immune responses to human thyroglobulin using various congenic mice showed that I-A subregion gene(s) control the immune response to human thyroglobulin.

Animals↗
PubMed1981

Electrophoretic analysis of thyroid iodoproteins in highly cross-linked polyacrylamide gels.

The electrophoretic behavior of thyroglobulin and larger thyroglobulin-like iodoproteins prepared from the hog thyroid was studied in polyacrylamide gels over a wide range of cross-linking degrees (C%). When examined at a constant total acrylamide monomer concentration (T%) of 5%, the mobility of 19S thyroglobulin decreased with increase in C below C = 5%, whereas above C = 5%, it increased markedly with increase in C, giving a minimum mobility at C = 5%. Similar biphasic mobility curves were obtained with 27S and 37S thyroid iodoproteins. Furthermore, in a region above C = 15%, at least two additional larger components which escaped detection in the gels with lower degrees of cross-linking appeared as separate bands. Ferguson plots constructed for thyroid iodoproteins at a higher constant C of 20% gave straight lines intersecting at a common point at T = 0%. From the calculated slopes of the Ferguson plots, it has been established that the thyroid contains a series of multimers of 19S thyroglobulin as constituent iodoproteins. Structural parameters of highly cross-linked gels were estimated under the assumption that the gels would be predominantly composed of a random meshwork of gel beads.

Animals↗
PubMed1978

Isolation and properties of thyroglobulin-related 4S protein in the soluble fraction of thyroid tissue.

A 4S protein which is thyroglobulin-related and which is immunologically distinguished from unusually iodinated albumin-like proteins or impaired substances of thyroglobulin synthesis, was found in the thyroid-soluble fraction even in the normal gland, though in minute amounts. In the present study, purification and characterization of the substance has been carried out using human and hog thyroid glands. This protein contains some of the immunospecific determinants of thyroglobulin, although the amino acid composition of the protein differs from that of thyroglobulin. The 4S protein has a molecular weight of about 58,500 as determined by the sedimentation equilibrium method. Interestingly, the present 4S protein is eluted just in front of, or together with, thyroglobulin by gradient elution chromatography on a DEAE-cellulose column, and it is precipitated with thyroglobulin at 1.9 M ammonium sulfate. Therefore, it was concluded that a molecular-sieving process is necessary for the purification of thyroglobulin, in addition to a complex procedure which consists of ammonium sulfate fractionation and DEAE-cellulose chromatography.

Amino Acids↗
PubMed1977

Properties of carbohydrate-stripped thyroglobulin. III. Solubility characteristics of thyroglobulin.

In studying the solubility characteristics of thyroglobulin, it was found that the removal of sialic acid residues from either human or hog thyroglobulin by treatment with neuraminidase markedly decreased the solubility in salt solutions. On the other hand, naturally sialic acid-rich thyroglobulin obtained from human diffuse goiter was slightly more soluble than thyroglobulin in which sialic acid content was within the normal range. However, the desialized preparations prepared from both normal and sialic acid-rich thyroglobulin showed markedly lower solubility and further, showed no significant difference in solubility between them. These results indicate that the surface charge of thyroglobulin which influenced the salting-out property depends largely on the number of sialic acid residues in a thyroglobulin molecule, not on the degree of iodination of thyroglobulin.

Amino Acids↗
PubMed1977

Subunit structure of 27 S thyroid iodoprotein.

The dissociation of thyroid 27 S iodoprotein by sodium dodecyl sulfate (SDS) and by succinic anhydride was investigated by means of ultracentrifugation and polyacrylamide gel electrophoresis. The iodoprotein obtained from either a human or hog was dissociated into three kinds of subunits (S-19, S-17 and S-12) by SDS treatment. At increased concentrations of SDS, the S-12 subunit was predominant among the dissociation products. The succinylation of 27 S iodoprotein showed essentially the same dissociation pattern as in the case of SDS treatment. The dissociation products of the protein preparations of different animals were qualitatively the same as those of thyroglobulin of the respective animals, confirming the hypothesis that 27 S iodoprotein was composed of two molecules of thyroglobulin. However, the extent of dissociation of 27 S iodoprotein measured by S-12 formation showed higher resistancy of the protein to the dissociating agents than that of thyroglobulin. The contents of sialic acid and hexose as well as iodoamino acids of 27 S iodoprotein were found to be the same as, or not far from, those of thyroglobulin. The dissociability and chemical composition of 27 S iodoprotein was discussed with reference to the subunit structure of the protein.

Anhydrides↗
PubMed1976

Subunit structure of 27 S thyroid iodoprotein.

The dissociation of thyroid 27 S iodoprotein by sodium dodecyl sulfate (SDS) and by succinic anhydride was investigated by means of ultracentrifugation and polyacrylamide gel electrophoresis. The iodoprotein obtained from either a human or hog was dissociated into three kinds of subunits (S-19, S-17 and S-12) by SDS treatment. At increased concentrations of SDS, the S-12 subunit was predominant among the dissociation products. The succinylation of 27 S iodoprotein showed essentially the same dissociation pattern as in the case of SDS treatment. This dissociation products of the protein preparations of different animals were qualitatively the same as those of thyroglobulin of the respective animals, confirming the hypothesis that 27 S iodoprotein was composed of two molecules of thyroglobulin. However, the extent of dissociation of 27 S iodoprotein measured by S-12 formation showed higher resistancy of the protein to the dissociating agents than that of thyroglobulin. The contents of sialic acid and hexose as well as iodoamino acids of 27 S iodoprotein were found to be the same as, or not far from, those of thyroglobulin; The dissociability and chemical composition of 27 S iodoprotein was discussed with reference to the subunit structure of the protein.

Amino Acids↗
PubMed1975

The effect of iodide administration on hog thyroid gland and the composition of thyroglobulin and 27-S iodoprotein.

The effect of excess iodide on hog thyroid gland has been examined with regard to the change in the chemical composition of thyroglobulin and in the accumulation of 27-S iodoprotein by the in vivo treatment of hogs with iodide for various lengths of time. The iodine content of thyroglobulin was either unchanged by short term administration of excess iodide, or somewhat lowered. However, the iodine content as well as the total amount of thyroglobulin increased in the glands enlarged by prolonged treatment with iodide. The iodine highest reached 1.17% of the protein on an average. On the other hand, 27-S iodoprotein decreased and finally disappeared after the chronic treatment. Monoiodotyrosine and diiodotyrosine increased in parallel with the increase in the iodine content (0.15 to 1.17%) caused by the iodide treatment, while thyroxine increased but reached a plateau at the level of three residues per mole of thyroglobulin, and no change was observed even in the proteins with the higher iodine content than 0.75%. Proteolytic activity measured by amino acid release from the thyroid protein was depressed by the chronic treatment. On the other hand, the amount of iodocompound released by the autoproteolysis, which may reflect hormone secretion, increased, possibly because of the marked increase in the iodine content of thyroglobulin.

Animals↗