1989-12 http://hdl.handle.net/10564/2091 2026-04-10T15:28:05Z 2026-04-10T15:28:05Z http://hdl.handle.net/10564/2106 2017-05-29T06:08:13Z 1989-12-30T15:00:00Z

タイトル: 第110回奈良医学会 : 学会記事

1989-12-30T15:00:00Z 藤森, 由佳子 http://hdl.handle.net/10564/2105 2017-05-29T06:08:08Z 1989-12-30T15:00:00Z

タイトル: アルコールの肝における高比重リポ蛋白代謝に及ぼす影響に関する研究 著者: 藤森, 由佳子 抄録: The effect of alcohol intake on the serum levels of high-density lipoprotein cholesterol (HDL-ch), apolipoprotein A-Ⅰ (apo. A-Ⅰ), and apolipoprotein A-Ⅱ (apo. A-Ⅱ) was investigated in 19 habitual alcohol drinkers without liver disfunction (Group A), 35 with mild hepatic damage (Group B), and 7 with advanced liver disease (Group C). The serum level of HDL-ch was higher in Group A than in 10 non-drinkers (control group) (P＜0.001). But it was lower in Group B (P＜0.01) and significantly lower in Group C (P＜0.001) than in the controls. The level of apo. A-Ⅰ was also higher in Group A (P＜0.005) than in the controls, although the level of apo. A-Ⅱ was not. To elucidate the effects of alcohol on apo. A-Ⅰ production by hepatocytes, the author investgated the synthesis of apo. A-Ⅰ and albumin by cultured rat liver cells in the presence of ethanol. Ethanol enhanced the production of apo. A-Ⅰ but not that of albumin. These results suggest that the elevation of serum HDL in habitual alcohol drinkers without liver disturbance is mainly attributable to the increase of apo. A-Ⅰ synthesis in the liver.

1989-12-30T15:00:00Z 新家, 興 西尾, 健治 中井, 寛明 嶋, 緑倫 高瀬, 俊夫 金田, 美喜夫 吉岡, 章 福井, 弘 藤村, 吉博 http://hdl.handle.net/10564/2104 2017-06-11T23:20:26Z 1989-12-30T15:00:00Z

タイトル: Ristocetin血小板凝集を抑制する抗von Willebrand因子モノクローナル抗体の多様性 著者: 新家, 興; 西尾, 健治; 中井, 寛明; 嶋, 緑倫; 高瀬, 俊夫; 金田, 美喜夫; 吉岡, 章; 福井, 弘; 藤村, 吉博 抄録: The epitopes of four anti-vWF monoclonal antibodies (MoAbs), which inhibit antibiotic ristocetin induced vWF binding to GPⅠb, were investigated and compared with each other. MoAb NMC-4 completely inhibited both the vWF bindings to GPⅠb expressed by ristocetin and snake venom botrocetin at the final concentrations of 10 μg/ml. Another MoAb RFF-VⅢ RAG : 1 also completely inhibited ristocetin-induced vWF binding at the IgG concentration of 10 μg/ml, but showed a partial inhibition (75% at the IgG concentlation of 100 μg/ml) on botrocetin-induced binding. Two other MoAbs, RG46 and 52-K8, inhibited ristocetin-induced vWF binding at the inhibition constant by 50% of 90 μg/ml and 30 μg/ml respectively, but without effect on botrocetin-induced vWF binding. Using the radiolabelled NMC-4 and its binding to vWF immobilized to plastic tubes, the competitive binding assay was performed. In this assay, cold NMC-4 clearly displaced (¹²⁵Ⅰ) NMC-4 binding to solid-phase vWF, and RFF-VⅢRAG : 1 partially blocked the binding (60% at the IgG concentration of 100 μg/ml), whereas neither RG46 nor 52K-8 blocked this binding. These results indicated that the epitopes of NMC-4 and RFF-VⅢRAG : 1 are in close proximity, but those of RG46 and 52K-8 are different, suggesting the epitope heterogeneity of anti-vWF MoAbs which inhibit ristocetin-induced vWF binding.

1989-12-30T15:00:00Z 新家, 興 武田, 以知郎 中井, 寛明 西尾, 健治 宮田, 茂樹 嶋, 緑倫 吉岡, 章 福井, 弘 藤村, 吉博 http://hdl.handle.net/10564/2102 2017-06-11T23:20:26Z 1989-12-30T15:00:00Z

タイトル: von Willebrand因子(vWF)フラグメント(97 kDa，52/48 kDa，及びFⅢ-T2) と抗vWFモノクローナル抗体NMC-4の免疫反応性 著者: 新家, 興; 武田, 以知郎; 中井, 寛明; 西尾, 健治; 宮田, 茂樹; 嶋, 緑倫; 吉岡, 章; 福井, 弘; 藤村, 吉博 抄録: We have shown that an anti-von Willebrand factor (vWF) monoclonal antibody designated as NMC-4 blocks both the ristocetin- and botrocetin-induced (¹²⁵Ⅰ) vWF bindings to platelet glycoprotein (GP)Ⅰb. Using NMC-4 coupled Sepharose 4B column or electroelution apparatus, a 97 kDa fragment and a 130 kDa fragment were distinctively purified from a whole tryptic digest of vWF. The 97 kDa fragment, which was shown to be a homodimer of the amino acid residue 449-728 of vWF subunit, retained the activity to inhibit both the ristocetin- and botrocetin-induced (¹²⁵Ⅰ) vWF binding to GPⅠb as found in the parent molecule. Another vWF fragment, the FⅢ-T2 fragment, which is a twin heterodimer composed of two H-chains (residue 273-511) and two L-chains (residue 674-728) held together by disulfide-bonds, was also purified by high pressure liquid chromatography. FⅢ-T2 fragment showed no inhibitory effect on botrocetin-induced vWF binding to GPⅠb, whereas it blocked the ristocetin-induced vWF binding. On Western blotting analysis and dot blot assay, NMC-4 failed to react with both the reduced and nonreduced FⅢ-T2 fragment. These results indicate that the vWF binding domains to GPⅠb expressed by either ristocetin or botrocetin are different and the amino acid residue Leu512-Lys673 is important for both botrocetin-induced vWF binding and NMC-4 binding.

1989-12-30T15:00:00Z