雪莲对小鼠腹腔巨噬细胞Fc和C_(3b)受体及红细胞免疫粘附功能的影响

检测巨噬细胞膜F_c和C_(3b)受体的活性及红细胞免疫粘附功能是选一步研究补益药增强机体免疫功能的重要手段。为探讨雪莲增强免疫作用的机制,本实验采用EA、YC花环形成以及红细胞C(3b)受体花环和免疫复合物花环形成等方法分别检测了雪莲和雪莲多糖对脾虚模型和氢化可的松琥珀酸钠(HCSS)抑制的小鼠腹腔巨噬细胞F_c和C_(3b)受体及红细胞免疫粘附功能的影响以及对胰酶损伤的小鼠腹腔巨噬细胞F_c和C_(3b)受体的修复作用。结果表明雪莲和雪莲多糖能提高脾虚模型和HCSS抑制的小鼠腹腔巨噬细胞EA和YC花环形成率及红细胞C_(3b)受体花环形成率和免疫复合物花环形成率,但二者在体外作用一小时,对胰酶损伤的小鼠腹腔巨噬细胞EA和YC花环形成率无显著影响,说明雪莲和雪莲多糖能增强脾虚模型和HCSS抑制的小鼠腹腔巨噬细胞膜F_c和C_(3b)受体及红细胞免疫粘附功能,对胰酶损伤的小鼠腹腔巨噬细胞F_c和C_(3b)受体,则无明显的修复作用。     

红细胞免疫功能研究进展

1981年,Siegel等人首次提出“红细胞免疫系统”的概念,并从红细胞免疫粘附以及与之有关的循环复合物(CIC)清除、促进吞噬细胞吞噬功能、效应细胞样作用等方面论述了红细胞的免疫功能。而且设计出了检测红细胞免疫粘附受体活性的“标准的红细胞免疫粘附试验”。此后,国外学者从各方面展开了深入研究。在国内,郭峰在siegel标准试验的基础上,于1982年建立了红细胞C_3b受体花环试验和红细胞免疫复合物花环试验,分别测定红细胞C_3b受体活性和红细胞膜上吸附免疫复合物的情况。在此基础上,国内学     

雏鸡与青年鸡红细胞免疫粘附功能的比较

对刚出壳雏鸡与青年鸡的红细胞免疫粘附功能进行了比较，结果表明：刚出壳雏鸡红细胞免疫粘附功能明显低于青年鸡；健康青年鸡红细胞免疫复合物花环率明显低于红细胞受体花环率。     

应用流式细胞仪检测斑点叉尾鮰红细胞免疫粘附功能

制备荧光标记的致敏酵母及未致敏酵母,应用流式细胞仪检测斑点叉尾鮰全血体系与洗涤红细胞体系下红细胞C3b受体(erythrocyte C3breceptors,E-C3bR)与红细胞免疫复合物(erythrocyte immune complexes,E-IC)花环率,同时检测未灭活血清与灭活血清(58℃处理30min)对洗涤红细胞免疫粘附功能的调控作用.结果显示,斑点叉尾鮰红细胞能有效粘附致敏酵母及未致敏酵母,其灭活血清组E-C3bR与E-IC花环率(分别为16.78%和13.51%)明显高于未灭活血清组(分别为5.99%和6.99%)与生理盐水组(分别为8.59%和8.30%);未灭活血清组E-C3bR与E-IC花环率明显低于生理盐水组.试验结果表明斑点叉尾鮰红细胞具有免疫粘附功能,并且血清中存在促进红细胞免疫粘附功能的热稳定因子及抑制其免疫粘附功能的热不稳定因子.该试验不仅从技术上促进了红细胞免疫功能的研究,而且有助于全面客观地了解鱼类的红细胞免疫功能,为鱼类的病害监测及其防治奠定基础.     

存放时间对爱拔益加鸡红细胞免疫吸附性能的影响

为进一步检验体外存放时间对爱拔益加鸡红细胞免疫吸附性能的影响,应用红细胞C3b受体花环(C3b Receptor Rosette,C3bRR)和免疫复合物花环(Immune Complex Rosette,ICR)实验,以12 h为时间梯度进行测定,结果表明爱拔益加鸡红细胞的免疫吸附性能随体外存放时间延长而略有下降趋势.     

硒对新城疫免疫雏鸡红细胞免疫功能的影响

采用鸡红细胞免疫复合物RBC-IC花环、鸡红细胞受体（RBC-CR1）花环及RBC-CR1花环促进试验，通过饮水给硒的方式，探讨硒对新城疫免疫雏鸡红细胞免疫粘附功能及其免疫粘附促进因子活性的影响。试验结果表明：各组平均血清硒含量变化与给硒剂量一致；各试验组红细胞免疫粘附功能及其血清中的免疫粘附促进因子的活性均较对照组为高。     

绵羊自然感染附红细胞体对绵羊红细胞的影响

选择1岁左右自然感染附红细胞体的杂交育肥绵羊为试验动物,采血,观察红细胞的形态,并测定RBC、Hb、PCV、红细胞脆性（最小脆性和最大脆性）、红细胞ATPase和SOD活性、红细胞C3b受体（E-C3bRR）花环率和红细胞免疫复合物（E-ICR）花环率.检测结果显示：与对照组相比,急性感染组绵羊红细胞脆性、RBC、Hb、PCV、红细胞ATPase和SOD活性及E-C3bRR率和E-ICR率呈降低趋势;但隐性感染组所测定指标变化不明显.表明附红细胞体侵袭红细胞后,感染越强,红细胞就易破裂而溶血、红细胞内外阳离子平衡失调、红细胞抗氧化能力降低,同时,破坏了红细胞膜表面的C3b受体,红细胞膜表面游离状态的C3b受体数量明显减少,机体红细胞的免疫黏附活性降低,红细胞免疫功能低下.     

高住低练对红细胞免疫功能影响的研究分析

对红细胞免疫概念的发展以及运动和低氧对其的影响进行了总结,着重就高住低练训练法对红细胞天然免疫分子如CR1,CD55,CD59和RBC-C3bRR(红细胞C3b受体花环率)、RBC-ICR(红细胞免疫复合物花环率)等指标的影响进行分析,以期为竞技体育的训练提供理论依据.     

大学生体育课中补液对红细胞免疫功能的影响

探讨了大学生体育课中补液对红细胞免疫功能的影响.10名男性大学生实验前一周作为安静状态对照,测试三堂课,隔周进行,分别为不补液课、补凉开水课和补运动饮料课.在体育课中使用遥测心率仪监测和询问自我运动感觉状况.课后即刻取血,测定红细胞SOD活力;采用郭峰法测定红细胞C3b受体花环率(RBC.C3bRR)和红细胞免疫复合物花环率(RBC.ICR).结果显示:各体育课后即刻RBC.C3bRR都比安静状态时低,不补液课、补凉开水课和补运动饮料课RBC.C3bRR有逐渐升高的趋势;而RBC.ICR的变化与RBC.C3bRR相反,却与红细胞SOD活力变化相同.由此可见,体育课后,红细胞免疫功能下降;在课中补液,出现红细胞免疫“节省化”现象,尤其是补充运动饮料.     

芦荟多糖对S180小鼠免疫调节因子活性的影响

研究库拉索芦荟多糖对S180小鼠红细胞免疫调节因子活性的影响．采用郭峰法测定．库拉索芦荟多糖可显著提高S180小鼠红细胞G3b受体花环促进率,降低其抑制率,因而从红细胞免疫角度,来揭示芦荟多糖具有抗肿瘤及提高机体免疫的功能．     

猪红细胞免疫功能初步研究

本实验通过对35例猪红细胞 C_3b 受体花环和免疫复合物花环的检测,证明猪红细胞亦有C_3b 受体(即 Complement receptortype I,CR_1),表明猪红细胞不但具有传统医学观念上的功能,而且还可借助 CR_1进行免疫粘附,并以此为基础,表现出各种重要的免疫功能。     

Ge-132对荷瘤小鼠NK细胞活性及红细胞免疫功能的影响

为探讨Ｇｅ－１３２抗癌作用机制,进行了Ｇｅ－１３２对荷瘤小鼠脾脏ＮＫ细胞活性和红细胞免疫粘附功能影响的体内实验研究,结果表明,Ｇｅ－１３２对小鼠移植瘤（Ｓ１８０）的生长具有显著的抑制效应,抑制率达５５％,荷瘤小鼠脾脏ＮＫ细胞活性明显低于正常对照组,Ｇｅ－１３２能使其恢复;荷瘤小鼠ＲＢＣ－Ｃ３ｂ受体花环率和肿瘤ＲＢＣ花环率明显低于正常对照组（Ｐ〈０．０１）,ＲＢＣ－ＩＣ花环率则高于正常对照组（Ｐ〈０     

肝炎患者红细胞免疫功能及与体液免疫功能的关系

检测１２１例各型肝炎患者红细胞免疫功能，以及大部分患者的体液免疫功能指标，并探讨两者间的相关性。结果显示：（１）各型肝炎患者及慢性乙肝病毒携带者ＲＢＣＣ３ｂＲＲ均明显低于正常人。急性肝炎急性期和中－重度慢性肝炎患者ＲＢＣ－ＩＣＲ均明显高于正常人。中－重度慢性肝炎患者ＲＢＣＣ３ｂＲＲ明显低于轻度患者，前者ＲＢＣ－ＩＣＲ明显高于后者；急性肝炎恢复期患者ＲＢＣＣ３ｂＲＲ明显高于急性期患者，前者的ＲＢＣ－ＩＣＲ却明显低于后者；（２）急性和慢性肝炎患者血清ＣＩＣ水平均明显升高，急性肝炎恢复期患者血清ＣＩＣ水平较急性期降低。慢性肝炎患者血清ＩｇＭ、ＩｇＧ、ＩｇＡ水平均有不同程度的升高。中－重度慢性肝炎患者血清Ｃ３、Ｃ４水平均明显下降；（３）急性肝炎急性期和恢复期患者ＲＢＣＣ３ｂＲＲ与血清ＣＩＣ水平均呈负相关，而他们的ＲＢＣ－ＩＣＲ与之呈正相关。中－重度慢性肝炎患者ＲＢＣＣ３ｂＲＲ与血清ＣＩＣ水平呈负相关，与血清Ｃ３、Ｃ４水平呈正相关。相反，其ＲＢＣ－ＩＣＲ与血清ＣＩＣ水平呈正相关，与Ｃ３、Ｃ４水平呈负相关。故临床上动态观察肝炎患者的红细胞免疫功能变化，有助于评估病情转归和病变程度。     

加味犀角地黄汤作用机理初探

利用兔“热毒血瘀”病理模型研究了加味犀角地黄汤的作用机理．结果表明,该方能降低模型兔的体温、全血粘度、全血还原粘度和血浆粘度,提高其红细胞Ｃ３ｂ 受体酵母花环率和ＩＣ酵母花环率,从而使“热毒血瘀”模型的血液高粘滞和红细胞兔疫粘附功能低下状态得到改善     

软件无线电中CIC滤波器的性能改进

由于传统的CIC滤波器调谐参数固定且受限,频谱响应不理想,不能灵活运用于软件无线电中.通过分析传统的CIC滤波器结构和功率谱密度,提出一种改进型的CIC滤波器.改进型CIC滤波器每级采用不同延时,使其灵活调谐.通过MATLAB进行仿真,并调节参数,由于折叠进入通带,可使改进型的CIC滤波器在零点附近区域引起的镜像混叠减至最小,得到较好的旁瓣抑制和镜像衰减,证明其性能更优.     

Glycoprotein C of herpes simplex virus 1 acts as a receptor for the C3b complement component on infected cells

Receptors for the Fc portion of immunoglobulins or for the third component of complement (C3) are present on a variety of circulating and fixed tissue cells including granulocytes, monocytes, lymphocytes and glomerular epithelial cells. Cells which lack Fc receptors may express them after infection by herpes simplex virus (HSV)-1, HSV-2, cytomegalovirus or varicella zoster virus. We recently reported that infection by HSV-1 induces both Fc and C3 receptors on human endothelial cells. Glycoprotein E of HSV-1 has been shown to function as an Fc receptor. We now demonstrate that glycoprotein C (gC) of HSV-1 functions as a C3b receptor. This receptor appears following HSV-1, but not HSV-2, infection. Detection of the C3b receptor is blocked by monoclonal antibodies to glycoprotein C (gC) of HSV-1, but not by monoclonal antibodies to other HSV-1 glycoproteins. In addition, the MP mutant of HSV-1, which lacks gC, fails to express a C3b receptor. These results assign a new function of gC of HSV-1 and demonstrate potentially important differences between HSV-1 and HSV-2 glycoproteins.     

The structure of complement C3b provides insights into complement activation and regulation

The human complement system is an important component of innate immunity. Complement-derived products mediate functions contributing to pathogen killing and elimination. However, inappropriate activation of the system contributes to the pathogenesis of immunological and inflammatory diseases. Complement component 3 (C3) occupies a central position because of the manifold biological activities of its activation fragments, including the major fragment, C3b, which anchors the assembly of convertases effecting C3 and C5 activation. C3 is converted to C3b by proteolysis of its anaphylatoxin domain, by either of two C3 convertases. This activates a stable thioester bond, leading to the covalent attachment of C3b to cell-surface or protein-surface hydroxyl groups through transesterification. The cleavage and activation of C3 exposes binding sites for factors B, H and I, properdin, decay accelerating factor (DAF, CD55), membrane cofactor protein (MCP, CD46), complement receptor 1 (CR1, CD35) and viral molecules such as vaccinia virus complement-control protein. C3b associates with these molecules in different configurations and forms complexes mediating the activation, amplification and regulation of the complement response. Structures of C3 and C3c, a fragment derived from the proteolysis of C3b, have revealed a domain configuration, including six macroglobulin domains (MG1-MG6; nomenclature follows ref. 5) arranged in a ring, termed the beta-ring. However, because neither C3 nor C3c is active in complement activation and regulation, questions about function can be answered only through direct observations on C3b. Here we present a structure of C3b that reveals a marked loss of secondary structure in the CUB (for 'complement C1r/C1s, Uegf, Bmp1') domain, which together with the resulting translocation of the thioester domain provides a molecular basis for conformational changes accompanying the conversion of C3 to C3b. The total conformational changes make many proposed ligand-binding sites more accessible and create a cavity that shields target peptide bonds from access by factor I. A covalently bound N-acetyl-l-threonine residue demonstrates the geometry of C3b attachment to surface hydroxyl groups.     

Transfer of diabetes in mice prevented by blockade of adhesion-promoting receptor on macrophages

Insulin-dependent diabetes mellitus (IDDM) is a disease with an autoimmune aetiology. The non-obese diabetic mouse is a good spontaneous animal model of the human disease, with IDDM developing in 50-80% of female mice by the age of 6 months. The disease can be transferred by splenic T cells from diabetic donors and is prevented by T-cell depletion. The mechanism(s) by which the beta cell is specifically destroyed is not known, but T cells and macrophages have both been implicated, based on the presence of macrophages in the infiltrated islet and the ability of chronic silica treatment to prevent disease. The monoclonal antibody 5C6 is specific for the myelomonocytic adhesion-promoting type-3 complement receptor (CR3 or CD11b/CD18) and does not bind to T cells. Here we show that blockade of macrophage CR3 in vivo prevents intra-islet infiltration by both macrophages and T cells and inhibits development of IDDM. We conclude that both T cells and macrophages have an essential role in the onset of IDDM.     

Structure of C3b reveals conformational changes that underlie complement activity

Resistance to infection and clearance of cell debris in mammals depend on the activation of the complement system, which is an important component of innate and adaptive immunity. Central to the complement system is the activated form of C3, called C3b, which attaches covalently to target surfaces to amplify complement response, label cells for phagocytosis and stimulate the adaptive immune response. C3b consists of 1,560 amino-acid residues and has 12 domains. It binds various proteins and receptors to effect its functions. However, it is not known how C3 changes its conformation into C3b and thereby exposes its many binding sites. Here we present the crystal structure at 4-A resolution of the activated complement protein C3b and describe the conformational rearrangements of the 12 domains that take place upon proteolytic activation. In the activated form the thioester is fully exposed for covalent attachment to target surfaces and is more than 85 A away from the buried site in native C3 (ref. 5). Marked domain rearrangements in the alpha-chain present an altered molecular surface, exposing hidden and cryptic sites that are consistent with known putative binding sites of factor B and several complement regulators. The structural data indicate that the large conformational changes in the proteolytic activation and regulation of C3 take place mainly in the first conversion step, from C3 to C3b. These insights are important for the development of strategies to treat immune disorders that involve complement-mediated inflammation.