[A case of pulmonary aspergillosis with massive hemoptysis and tumor-like shadow, in healed tuberculosis complicated by diabetes mellitus].
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Biomedical subjects
Publications and source records attributed to M Hatakeyama.
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Tac antigen, the receptor for human interleukin 2 (IL-2), contains in its intracytoplasmic region a serine residue (Ser-247) that is seemingly the predominant site of protein kinase C-mediated phosphorylation. A number of studies on growth factor receptors have suggested the importance of phosphorylation in receptor structure, function, and regulation. In this study, we generated site-directed mutations in the Tac antigen cDNA to generate mutant receptors in which Ser-247 or Thr-250, a probable site of minor phosphorylation, was replaced with another amino acid that is not accessible to phosphorylation. Study of the expression of these mutant genes in a T-lymphoid cell line has provided no evidence as to the essential role of the above-mentioned residues in determining the degree of receptor affinity, its ability for signal transduction, and phorbol ester-mediated regulation of the receptor. Our results strongly suggest the existence of an IL-2 receptor "complex" in which the Tac antigen is associated with another molecule(s) that is involved in receptor structure, function, and regulation.
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High-resolution computed tomographic scans of 19 patients with pulmonary asbestosis revealed a subpleural curvilinear shadow (SCLS) parallel to the inner chest wall in the lungs of 15 (78.9%) patients. Most (46.7%) SCLS measured greater than 5 cm but less than 10 cm in length and occurred less than 1 cm from the inner chest wall in all cases. SCLS was distributed mainly in the lower lobe in patients with mild pulmonary fibrosis and in segments where fibrosis was mild in patients with honeycomb shadows. This may reflect initiation of pulmonary fibrosis leading to the formation of a honeycomb shadow. Radiologic-pathologic correlation, achieved in one postmortem specimen, seemed to indicate that SCLS was associated with the initial change of fibrosing bronchioloalveolitis, which is characteristic of pulmonary asbestosis.
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Interleukin 2(IL-2), a lymphokine that is produced by helper T cells, plays a key role in the proliferation of T lymphocytes by interacting with a specific cell surface receptor. Recent studies demonstrated that the IL-2 receptor exists in two forms having different affinities to the ligand and the growth signal seems to be delivered by IL-2 bound to the high affinity, but not the low affinity, receptor. In man, both forms of the IL-2 receptor can be recognized by a monoclonal antibody, anti-Tac. Using this antibody, a cDNA that encodes Tac antigen has been cloned from ATL-derived T cell line. Transfection of the cloned cDNA into mammalian non-T cells, however, resulted in the expression of only a non-functional, low affinity IL-2 receptor. This observation raised a question whether or not the cloned cDNA for Tac antigen actually encodes the functional, high affinity IL-2 receptor. In order to clarify this problem, Tac antigen cDNA was obtained from human PBL cDNA library. This cDNA was connected to RSV-LTR and was transfected into mouse thymoma derived T-cell line EL4, and L929 fibroblast. Then transformants that constitutively express Tac antigen were established. IL-2 binding assay demonstrated that EL4 transformants expressed high affinity as well as low affinity human IL-2 receptor. In contrast, L929 transformants expressed only a low affinity receptor. The growth of the EL4 transformants harboring the high affinity human IL-2 receptor was inhibited by virtue of the specific interaction of the receptor with human, but not mouse, recombinant IL-2. These results demonstrate: the cloned cDNA dose encode a functional IL-2 receptor, the affinity of the IL-2 receptor is variably modified by post-translational events and 3. IL-2/receptor interaction leads to the reversal of the cell growth in EL4 cells. The reconstitution system described here will be of great use in elucidating the mechanism of T cell growth.
The hepatic arteries of 122 patients were analysed on angiography to identify the left medial segment of the liver. Left medial arterial branches were classified into three types: type I arising from the left hepatic artery on the umbilical portion of the portal vein; type II arising from proximal portion of left hepatic artery before reaching the umbilical portion of the portal vein; type III arising from right hepatic artery. Incidence of each type is 37.2%, 35.8% and 27.0%, respectively. The artery frequently kinks at the right side of the umbilical portion of the portal vein and a total of incidence is 68% and that of each type is 23.5%, 89.8% and 100%, respectively. We call this characteristic kinking point of the left medial arterial branches, the "M-point".
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Immune complex induced the release of thioltransferase from rabbit peritoneal exudates polymorphonuclear leucocytes in vitro. The release of thioltransferase occurs from viable cells and does not depend on a cytolysis. The catalytic activity of the released enzyme with S-sulfocysteine and glutathione as substrates had a distinct optimum pH at 7.6. On the contrary, opsonized zymosan was not effective as a stimulus for the liberation of thioltransferase from polymorphonuclear leucocytes. Thioltransferase liberated by the stimulation with immune complex was inhibited by chloramphenicol, but not by bacitracin. The inhibition was non-competitive (apparent Ki of 0.2 mM).
Thioltransferase was purified 650-fold from rabbit liver by procedures including acid treatment, heat treatment, gel filtration on Sephadex G-50, column chromatography on DEAE-cellulose, isoelectric focusing (pH 3.5-10) and gel filtration on Sephadex G-75. The final enzyme preparation was almost homogeneous in polyacrylamide gel electrophoretic analysis. Only one active peak with an apparent molecular weight (Mr) of 13,000 was detected by gel filtration on Sephadex G-50 and only a single protein band with a molecular weight of 12,400 was detected by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. Isoelectric focusing revealed only one enzyme species, having an isoelectric point (pI) of 5.3. The enzyme has an optimum pH about 3.0 with S-sulfocysteine and GSH as substrates. The purified enzyme utilized some disulfides including S-sulfocysteine, alpha-chymotrypsin, trypsin, bovine serum albumin, and insulin as substrates in the presence of GSH. The enzyme does not act as a protein : disulfide isomerase (the activity of which can be measured in terms of reactivation of randomly reoxidized soybean Kunitz trypsin inhibitor). The enzyme activity was inhibited by chloramphenicol, but not by bacitracin. The inhibition by chloramphenicol was non-competitive (apparent K1 of 0.5 mM). Thioltransferase activity was found in the cytosol of various rabbit tissues.
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A cytosol thioltransferase was purified 37,000-fold from bovine liver by essentially the same procedure as reported for rat liver enzyme by Axelsson et al. [1978) Biochemistry 17, 2978-2984). The purified enzyme appears to be homogeneous on sodium dodecyl sulfate (SDS)-gel electrophoresis and has a molecular weight (Mr) of 11,000, an isoelectric point (pI) of 8.1, and an optimum pH with S-sulfocysteine and GSH as substrates of 8.5. It is specific for disulfides including L-cystine, S-sulfocysteine, ribonuclease A, trypsin, soybean kunitz trypsin inhibitor, soybean Bowman Birk trypsin inhibitor and insulin, and converts Bowman Birk trypsin inhibitor to an inactive form. The enzyme does not act as a protein : disulfide isomerase, as measured by reactivation of "scramble" ribonuclease and Kunitz soybean trypsin inhibitor. Thioltransferase activity was found in cytosol of various bovine tissues.
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Radiation chimeras in mice were induced by intrasplenic injection of allogeneic bone marrow cells instead of intravenous injection. Interestingly, the survival time in X-irradiated BALB/c mice inoculated intrasplenically (i.s.) with bone marrow cells from C3H/He mice was markedly prolonged as compared with that in X-irradiated BALB/c mice inoculated i.v. with bone marrow cells from C3H/He mice. However, when C57BL/6 mice were used as donors, a significant difference between i.s. injection and i.v. injection has not been found in survival time at 60 days after X irradiation. On the contrary, when bone marrow cells from BALB/c or C57BL/6 mice were injected into X-irradiated C3H/He mice, i.s. injection gave longer survival days to recipients than did i.v. injection. Based on testing their chimerism, it was suggested that lymphoid cells of donor origin were predominantly identified in almost all BALB/c or C3H/He recipients which were inoculated i.s. with bone marrow cells from C57BL/6 mice. However, somewhat incomplete chimerism was observed when the C3H/He to BALB/c donor-recipient combination was used and vice versa.