Occurrence of sym-homospermidine in the Japanese newt, Cynops pyrrhogaster pyrrhogaster.
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Biomedical subjects
Publications and source records attributed to K Hamana.
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High mobility group (HMG) nonhistone chromosomal proteins have been shown to exist also in the ciliated protozoan Tetrahymena pyriformis. One or two histone-like components were extracted with 0.25 M HCl from the chromatin, in addition to five histone species. These proteins were also extracted selectively with 0.5 M HClO4, 0.35 M NaCl, or 4 mM spermidine, together with H1 histone, and were characterized as HMG proteins on the basis of the following criteria: high mobilities on polyacrylamide gel electrophoresis, relatively low molecular weights, amino acid compositions rich in lysine and glutamic acid, and relative contents in chromatin. This extends the distribution of the HMG proteins to all four eukaryotic kingdoms, and suggests the possibility that they have some universal role in chromatin structure and function.
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The concentrations of polyamines (putrescine, spermidine, and spermine) and of histamine in normal and diseased thyroids were determined with an automated amino acid analyzer. A total of 39 specimens was investigated: 7 specimens of normal tissue, 6 adenocarcinomas, 2 specimens of tissues adjacent to adenocarcinoma, 13 specimens from treated Graves' disease, 7 follicular adenomas, 2 adenomatous goiters, and 2 specimens of Hashimoto's thyroiditis. Mean putrescine levels in tissues from normal thyroid, adenocarcinomas, Graves' disease, and follicular adenoma were 26, 143, 20, and 12 nmol/g wet tissue, respectively. The mean levels of both spermidine and spermine were slightly but significantly higher in adenocarcinomas than in other thyroid tissues. The molar ratio of spermidine to spermine was about 0.5 both in the normal and diseased thyroid tissues, except for specimens of thyroiditis. Histamine was detected in 3 of the 6 cases of thyroid carcinomas, and in case of adenomatous goiter. The data suggest that measurement of polyamines, especially putrescine, may be useful for diagnosis of thyroid adenocarcinomas.
Changes in ornithine decarboxylase (ODC) activity and in polyamine contents of the rat thyroid were studied under various experimental conditions. Methylthiouracil (MTU) treatment produced several-fold increases in the thyroid ODC activity and in the content of putrescine, spermidine and spermine within a week. While serum thyrotropin (TSH) levels increased gradually up to 3 weeks, the content of both putrescine and spermidine tended to reach a plateau after 2 weeks of the goitrogen treatment; spermine content continued to increase progressively for 3 weeks. Discontinuance of MTU at 7 days resulted in a rapid decline in the elevated thyroid ODC activity, followed by a diminution of putrescine, spermidine and RNA contents. Thyroidal putrescine, spermidine and RNA responded more sensitively to both introduction and withdrawal of TSH stimulation than thyroidal spermine and DNA. Excess iodide, having no effect on the basal level of thyroid ODC, suppressed the MTU-induced increase in this enzyme activity without affecting circulating TSH, thyroxine (T4) and triiodothyronine (T3) levels. There was a significant negative correlation between the ODC activity and intrathyroidal concentration of iodine in MTU-pretreated rats. Theophylline increased the thyroid weight and ODC activity when given to rats fed with a subeffective dose of MTU. Analyses of serum TSH, T4, T3 and of thyroidal iodine revealed that TSH-induced thyroid ODC activity was suppressed by increased circulating thyroid hormones and/or intrathyroidal iodine. Furthermore, it was suggested that thyroid hormones and excess iodide acted directly on the thyroid to alter polyamine biosynthesis, possibly by changing the responsiveness of the gland to TSH.
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Adenosine 3':5'-monophosphate-dependent protein kinase (protein kinase A) purified from silkworm pupae phosphorylated five major fractions of calf thymus histone, whereas guanosine 3':5'-monophosphate-dependent protein kinase (protein kinase G) purified from the same organism reacted preferentially with H1, H2A, and H2B histones. Amino acid analysis of the phosphopeptides which were obtained by proteolytic digestion revealed that both protein kinases A and G showed the abilities to phosphorylate the same serine hydroxyl groups in H1 and H2B histones. Both protein kinases reacted with Ser-38 in H1 histone. With H2B histone as substrate protein kinase A phosphorylated Ser-32 as well as Ser-36, whereas protein kinase G reacted preferentially with Ser-32 and the reaction with Ser-36 was very slow. H3 and H4 histones were practically inactive substrates for protein kinase G. Although H2A histone has not been analyzed, the evidence has raised a possibility that protein kinase G utilizes a portion of the substrate proteins for protein kinase A.
Polyacrylamide gel electrophoresis of whole histones of calf thymus, chicken erythrocytes, and Tetrahymena was carried out in the absence or presence of a nonionic surfactant, Triton X-100 (up to 6 mM), in 0.9 M acetic acid and 6.25 M urea-0.9 M acetic acid. Calf thymus whole histone was also chromatographed on Bio-Gel P-200 in the absence or presence of 6 mM Triton in 0.01 M HCl and 8 M urea-0.9 M acetic acid. Triton reduced the electrophoretic mobility and distribution coefficient of various histone species in the following order of decreasing effect; H2A greater than H3, H4 greater than H2B greater than H1 in the absence of urea. H1 and specific histones for chicken erythrocytes and Tetrahymena were almost unaffected. Urea antagonized the surfactant effect more for H4 and H2B, and less for H2A and H3. Such surfactant effects can be correlated with the helical contents of histone species under the experimental conditions used, rather than their total hydrophobicites, suggesting that Triton binds to helical regions.
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