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101.
102.
目的:建立以紫外分光光度法测定支扩养阴颗粒中二氢黄酮含量的方法。方法:以橙皮苷为对照品,四氢硼钠为还原剂,在紫外吸收光谱283nm波长处测定二氢黄酮的含量。结果:供试品与对照品有相近的特征紫外吸收光谱;二氢黄酮以橙皮苷计,进样量在100~710μg范围内与吸光度呈良好线性关系(r=0.9999),平均加样回收率为99.89%,RSD=0.66%(n=9)。结论:本方法简易、可行、精密度好,可用于支扩养阴颗粒的质量控制。 相似文献
103.
目的:建立结肠炎奇效颗粒中京尼平苷酸的HPLC测定方法。方法:色谱柱:Kromasil C18柱(250 mm×4.6 mm,5μm),以甲醇-1%醋酸溶液(10:90)为流动相,检测波长为254 nm,柱温为30℃,流速为1 ml·min-1。结果:京尼平苷酸在0.306~3.666μg范围内线性关系良好,相关系数为r=0.9991,平均回收率为100.0%,RSD=1.91%(n=6)。结论:方法简便,结果准确,可用于结肠炎奇效颗粒的质量控制。 相似文献
104.
目的 建立小儿氨酚黄那敏颗粒中对乙酰氨基酚的测定方法.方法 采用Eclipse XDB-C18(4.6 mm× 150 mm,5 μm)色谱柱,以甲醇-水(40:60)为流动相,流速1.0 ml·min-1,检测波长275 nm,进样量为20 μl.结果 对乙酰氨基酚在5.84~58.4 mg·L-1(r=0.9... 相似文献
105.
106.
中药配方颗粒是通过现代制药技术将符合规范的中药饮片制成的一种不需要煎煮的颗粒剂,自投放市场以来受到了广泛的关注与好评。本文从不同方面、不同层次分析它的优势,并根据传统中医药理论来分析它在今后的发展趋势,为广大医务人员提供用药参考。 相似文献
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108.
Zhen-Chang Wang Shan Yang Jing-Jing Huang Song-Lin Chen Quan-Qiang Li Yuan Li 《Asian Pacific journal of tropical medicine》2014,7(7):576-581
Objective:To observe the effect of Rougan Huaqian granules combined with human mesenchymal stem cell(hMSC)transplantation on the liver fibrosis in carbon tetrachlorideinduced cirrhosis rats.Methods:Sixty SD rats were randomly divided into live groups.The rats in control group received intraperitoneal injection of saline,while those in model control group,treatment group A,group B and group C received intraperitoneal injection of carbon tetrachloride oily solution to induce liver cirrhosis within 8 weeks.Then,the rats in the model control group,treatment group A,treatment group B,treatment group C received vein tail injection of saline,Rougan Huaqian granules,hMSC suspension and Rougan Huaqian granules combined with hMSC suspension.Results:The treatment groups had significantly different liver function(AST levels),liver fibrosis index(laminin and HA),hepatic sinusoidal wallsα-smooth muscle actin,Ⅳcollagen and laminin protein expression andⅠ,Ⅲcollagen from the model group(P0.05).The transplanted cells showed human hepatocyte-like cells differentiation trend in the liver.Conclusions:The Rougan Huaqian granules combined with hMSC transplantation can alleviate liver fibrosis in cirrhosis rats. 相似文献
109.
Aravinth Kumar Jayabalan Srivathsan Adivarahan Aakash Koppula Rachy Abraham Mona Batish Daniel Zenklusen Diane E. Griffin Anthony K. L. Leung 《Proceedings of the National Academy of Sciences of the United States of America》2021,118(6)
While biomolecular condensates have emerged as an important biological phenomenon, mechanisms regulating their composition and the ways that viruses hijack these mechanisms remain unclear. The mosquito-borne alphaviruses cause a range of diseases from rashes and arthritis to encephalitis, and no licensed drugs are available for treatment or vaccines for prevention. The alphavirus virulence factor nonstructural protein 3 (nsP3) suppresses the formation of stress granules (SGs)—a class of cytoplasmic condensates enriched with translation initiation factors and formed during the early stage of infection. nsP3 has a conserved N-terminal macrodomain that hydrolyzes ADP-ribose from ADP-ribosylated proteins and a C-terminal hypervariable domain that binds the essential SG component G3BP1. Here, we show that macrodomain hydrolase activity reduces the ADP-ribosylation of G3BP1, disassembles virus-induced SGs, and suppresses SG formation. Expression of nsP3 results in the formation of a distinct class of condensates that lack translation initiation factors but contain G3BP1 and other SG-associated RNA-binding proteins. Expression of ADP-ribosylhydrolase–deficient nsP3 results in condensates that retain translation initiation factors as well as RNA-binding proteins, similar to SGs. Therefore, our data reveal that ADP-ribosylation controls the composition of biomolecular condensates, specifically the localization of translation initiation factors, during alphavirus infection.Biomolecular condensates are prevalent in cells and critical for a range of cellular functions, including RNA metabolism, embryonic cell fate specification, and neuronal activity (1–3). While condensates often dynamically exchange components with the surrounding milieu, the overall composition of these cellular structures remains distinct (4). How cells control the specific composition of these condensates remains unclear. Stress granules (SGs), one of the best characterized biomolecular condensates, are RNA–protein assemblies formed in response to a variety of environmental cues (1). While SG composition can vary with the type of stress cue (5), certain common components, such as Ras GTP-activating protein-binding proteins G3BP1/2, are essential for formation of SGs (6, 7). Dysregulation of SG formation and disassembly is implicated in the pathogenesis of diseases, including viral infection, cancer, and neurodegeneration (2, 8–10).SG formation and disassembly are tightly regulated during viral infection, often reflecting cellular translation status (11–14). In the early phase of many viral infections, the presence of double-stranded viral RNAs (vRNAs) activate protein kinase R (PKR), resulting in eIF2α phosphorylation, messenger RNA (mRNA) translation inhibition, and formation of SGs enriched with translation initiation factors such as eIF3b. However, in later infection stages, many viruses instead suppress SG formation or disassemble SGs altogether. The mechanisms underlying this switch, and its physiological function, remain unclear.SG formation and disassembly are regulated by posttranslational modifications of proteins, including those that conjugate simple chemical groups, attach polypeptides, and add nucleotides as in the case of ADP-ribosylation (15–21). ADP-ribosylation refers to the addition of one or more ADP-ribose units onto proteins (22–24). In humans, ADP-ribosylation is accomplished primarily by a family of 17 ADP-ribosyltransferases, commonly known as poly(ADP-ribose) polymerases (PARPs). SG components are specifically ADP-ribosylated, and ADP-ribose polymers [i.e., poly(ADP-ribose) or PAR], five PARPs and two isoforms of the degradative enzyme PAR glycohydrolase (PARG) have been localized to these condensates (17, 25–27). Overexpression of these PARPs and PARG isoforms induces and suppresses SG formation, respectively, while PARG knockdown delays SG disassembly (17, 26). The noncovalent interaction between PAR and proteins facilitates SG targeting (25–27). For example, PAR-mediated targeting regulates TDP-43 localization to SGs and prevents the formation of pathological aggregates in amyotrophic lateral sclerosis (26, 27).The mosquito-borne alphaviruses, which cause a range of diseases from rashes and arthritis to encephalitis, induce SG formation early in infection and later initiate SG disassembly (11, 14, 28, 29). Previous studies have identified the alphaviral nonstructural protein 3 (nsP3), a key factor for virus replication and virulence (30–32), as able to suppress SG formation (28, 33–35). The alphaviral nsP3 is a tripartite protein composed of a highly conserved macrodomain (MD) in the N terminus, a central zinc-binding domain (ZBD), and a C-terminal hypervariable domain (HVD; ref. 30). Recent studies indicate that the HVD, which is of low complexity, directs alphaviral nsP3 binding to host SG proteins (30, 36). For example, the HVD of chikungunya virus (CHIKV) binds the essential SG components G3BP1 and G3BP2 (33, 37). Given that nsP3 expression increases over the course of viral infection, it has been proposed that nsP3 sequesters G3BP1/2, resulting in the suppression of SG formation during the late phase of infection (28, 29, 34).Here, we report that the expression of the G3BP-binding HVD alone does not suppress SG formation; rather, expression of the N-terminal MD alone can trigger the suppression of this biomolecular condensate. The structural integrity of SGs is dependent on ADP-ribosylation (17), and we and others recently found that the viral MD can remove single ADP-ribose groups, and possibly PAR, from ADP-ribosylated proteins (31, 38–40). We therefore hypothesized that MD ADP-ribosylhydrolase activity is required to suppress SG formation across stress conditions, with G3BP1 being a key target substrate. Indeed, we find that MD ADP-ribosylhydrolase activity is critical for disassembling SGs formed by G3BP1 expression and during viral infection. Consistent with this premise, live cell imaging revealed that SGs persist in cells infected with a hydrolase-deficient recombinant CHIKV. ADP-ribosylhydrolase activity is required for altering the composition of biomolecular condensates in nsP3-expressing or virus-infected cells and specifically regulates translation factor localization. Together, these data argue that nsP3 ADP-ribosylhydrolase activity modulates SG formation, disassembly, and composition. 相似文献
110.
《Ultrastructural pathology》2013,37(2):131-138
Two cases of small cell “undifferentiated” carcinoma (oat cell carcinoma) of the lung with dual neurosecretory and squamous differentiation are reported. One was treated with various regimens of chemotherapy and radiotherapy; the other was untreated at the time of biopsy. By electron microscopy, the same tumor cells showed membrane-bound, dense-core, neurosecretory-type granules and bundles of tonofibrils denoting squamous differentiation. This dual differentiation underlies the difficulty of ascribing an exclusively neural histogenesis to small cell carcinomas with neurosecretory-type granules. It is possible that entoderm-associated neuroectodermal tumors develop features of autochthonous entodermal tumors as a result of microenvironmental influences. An alternative hypothesis would be that small cell tumors are derived from basal reserve bronchoepithelial cells with pluripotentialities. 相似文献