Interleukin-10 containing normal human serum inhibits granzyme B release but not perforin release from alloreactive and EBV-specific T cell clones

Interleukin-10 (IL-10), also known as cytokine synthesis inhibitory factor, has pleiotropic effects in immunoregulation and inflammation. It is capable of inhibiting synthesis of pro-inflammatory cytokines like interferon γ (IFNγ), IL-2, IL-3, tumor necrosis factor α(TNFα) and granulocyte macrophage colony stimulating factor (GM-CSF) made by cells such as macrophages and T helper Type 1 cells. We observed that normal human serum, derived from a healthy individual but containing large amounts of IL-10 (arbitrarily designated as "IL-10 serum"), inhibited cytotoxic activity and interfered with granzyme B release from alloreactive cytotoxic T cell (CTL) clones _in vitro_, but did not affect perforin release. The addition of normal human serum containing high levels of anti-IL-10 IgG (arbitrarily designated as "anti-IL-10 IgG serum") neutralized the inhibitory effects of IL-10 serum. Moreover, we have identified that cytotoxic activity and granzyme B release from an Epstein-Barr virus (EBV)-specific CTL clone was similarly inhibited in the presence of IL-10 serum, while perforin release was unaffected. Anti-IL-10 IgG serum also appeared to neutralize the inhibitory effect of IL-10 serum on an EBV-specific CTL clone

The Pathogenesis of Tuberculous Meningitis. A Criticism of Rich's Focus-theory

この論文は国立情報学研究所の学術雑誌公開支援事業により電子化されました。1) The pathogenesis of tuberculous meningitis was studied by the preparation of the spreading specimens of meninges. 2) The tuberculous meningitis in infant succeeded to primary tuberculosis will break out by the cerebrospinal fluid infection from multiple caseous foci in meninges, which were formed in the walls of meningeal arteriols in the early dissemination. 3) Sometimes caseous foci in brains and choroid plexuses were found, but these foci are not essential as the cause of meningitis. 4) There will be rarely some cases, in which bacilli will be discharged in the subarachnoid space from the caseous foci in brains. In such cases tuberculous meningitis apt to be chronic and to relapse in spite of the adequate therapy

ステロイド投与家兎における大腿骨頭内血液循環に関する研究

取得学位 : 博士（医学）, 学位授与番号 : 医博乙第1207号, 学位授与年月日：平成4年12月2日,学位授与年：199

FFC Ceramic Water(TM) Enhances Plant Apyrase Activity

The FFC ceramics(TM) from FFC Japan Co., Ltd. are now widely used in the fields of agriculture, fishery and food industry in Japan. Recently the FFC ceramic beads-based technology has been also applied to meet several environmental problems including pollution in sea, lakes and rivers. In this study the FFC ceramic water was tested for effect on plant enzyme, potato apyrase (EC 3.6.1.5; ATP-diphosphohydrolase), which hydrolyses nucleoside triphosphate (NTP) and -diphosphate (NDP) to produce corresponding nucleoside monophosphate (NMP) and inorganic phosphate (Pi). Addition of the FFC ceramic water to the enzyme reaction mixture markedly enhanced ATP-hydrolyzing activity, when used as ATP as substrate. However, the concomitant presence of Ca(2+) chelator, EGTA (O,O'-bis(2-aminoethyl)ethyleneglycol-N,N,N',N'-tetraacetic acid) with the FFC ceramic water, completely abolished the enzyme activation. In fact, exogenous calcium ion such as CaSO4 mimicked the FFC ceramic water. These results indicate that apyrase activation by the FFC ceramic water largely depends on calcium ions. On the other hand, when the FFC ceramic water prepared from "used" ceramics was tested for the apyrase activity, the enhanced effect on apyrase was decreased compared to the FFC ceramic water from "new" ones. This result, consistent with our present data covering concentration of calcium ions and conductivity, indicates that long and/or successive usage of the ceramic beads results in decrease of contents of released minerals, especially calcium ions. The apyrase-based enzyme assay presented here is probably applicable to estimate and quantify the effect of FFC ceramic water.本報は，FFC セラミックス(TM)（㈱エフエフシー・ジャパン）で調製した FFC セラミック水（FFC 水）の植物アピラーゼ（EC 3.6.1.5）の活性に及ぼす直接的な作用について調べたものである．FFC 水はアピラーゼがもつ ATP加水分解活性を促進し，その作用は反応液への添加量に依存した．先の無機元素分析結果から，FFC 水に含まれる主要な塩類はCa(2＋)であることが判明している．そこで，Ca(2＋)キレート剤EGTAを反応液へ加え，その影響について調べたところ，FFC 水による活性化作用は消失することが明らかとなった．また，FFC 水と類似の作用は，硫酸カルシウム，塩化カルシウムまたは硝酸カルシウムの添加で認められ，陰イオンの種類によって明確な違いはなかった．これらの結果から，FFC 水が植物アピラーゼに及ぼす活性化作用の一因は，セラミックスから遊離する Ca(2＋)に依存しているものと推察された．一方，アピラーゼ活性を指標として，使用済のセラミックスから調製した FFC 水の効果について検討したところ，未使用からの水と比べて，カルシウム濃度ならびに活性化作用の顕著な低下が認められた．このことは，継続的な使用によってセラミックスから遊離する塩類，特にカルシウムの溶出量が大きく変わることを意味し，アピラーゼを用いた本検定が，FFC 水の効果を定量的に確かめる方法の一つとして利用できると考えられた．以上，これらの結果を総合して，FFC水の植物酵素への直接的作用，ならびに植物への施用によって効果が現れる耐病性獲得作用との関連について考察した

Spatial distribution of lipid headgroups and water molecules at membrane/water interfaces visualized by three-dimensional scanning force microscopy

At biological interfaces, flexible surface structures and mobile water interact with each other to present non-uniform three-dimensional (3D) distributions. In spite of their impact on biological functions, molecular-scale understanding of such phenomena has remained elusive. Here we show direct visualization of such interfacial structures with subnanometer-scale resolution by 3D scanning force microscopy (3D-SFM). We measured a 3D force distribution at an interface between a model biological membrane and buffer solution by scanning a sharp tip within the 3D interfacial space. We found that vertical cross sections of the 3D image taken along a specific lateral direction show characteristic molecular-scale contrasts tilted at 30° to the membrane surface. Detailed analysis of the 3D image reveals that the tilted contrast corresponds to the time-averaged conformation of fluctuating lipid headgroups. On the basis of the obtained results, we discuss the relationships among the hydration structure, headgroup fluctuation, molecular fluidity, and mechanical strength of the membrane. The results demonstrate that 3D-SFM is capable of visualizing averaged 3D distribution of fluctuating surface structures as well as that of mobile water (i.e., hydration structure) at interfaces between biological systems and water. © 2012 American Chemical Society