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The Acute Phase Complement Proteins
Published in Andrzej Mackiewicz, Irving Kushner, Heinz Baumann, Acute Phase Proteins, 2020
The complement system consists of a set of more than 20 effector and regulatory proteins that mediate inflammation initiated by tissue injury, microbial infection, and/or interaction between specific antibodies and corresponding antigens. Other nonhost defense-related functions of the complement system have also been recognized. The complement cascade is activated by limited proteolysis of the classical (antibody-dependent) pathway and alternative (antibody-independent) pathway proteins. The interaction of antigens with antibodies of immunoglobulin class IgM and several IgG subclasses initiates binding and activation of the classical complement pathway. The specificity of this reaction is imposed by the antibody. Under some conditions, however, viral agents,1-4 DNA, C-reactive protein,5,6 and mitochondrial membranes7,8 can activate the classical pathway in the absence of antibody. Activation of the alternative complement pathway always involves antibody-independent recognition of structures that are highly represented among pathogenic microorganisms. This activation therefore involves relatively nonspecific binding. Localization of the alternative pathway reaction is accomplished by permissive propagation of the cascade, i.e., conditions limiting control protein inactivation of the effector proteins. Amplification is an important feature of both pathways, since deposition of one or a few molecules results in enzymatic cleavage of thousands of later components in the cascade and the appearance of complement-dependent biological activities. Further amplification results from the positive activation loop involving the proteins of the alternative pathway. The proteins of the classical pathway include Cl (a macromolecular complex comprised of the products of five genes and the fourth [C4] and second [C2] components). The latter two are encoded by genes within the major histocompatibility complex along with one of the alternative pathway proteins, factor B. The other alternative pathway constituents include factor D and C3. Two distinct unstable enzymes capable of cleaving the third component of complement (C3) are generated by complexing active fragments of the proteins of the two pathways.
The promising potentials of capped gold nanoparticles for drug delivery systems
Published in Journal of Drug Targeting, 2018
Kamyar Khoshnevisan, Maryam Daneshpour, Mohammad Barkhi, Morteza Gholami, Hadi Samadian, Hassan Maleki
The specific nature of oligonucleotides makes them an ideal option for sensitive and targeted delivery objectives. Therefore, synthesis, characterisation and application of DNA-capped GNPs have been considered the most attractive fields of research during the past decades [2]. It has been documented that the internalisation of DNA-C-GNPs would increase by augmentation of DNA molecules on the surface and lead to better intracellular targeting [55]. Most researchers believe that DNA-C-GNPs cannot enter the cells due to their negative charge. However, numerous investigations reported surprising results about the ability of these nanostructures to enter different cell types [2,56]. Mirkin et al. reported the successful use of DNA-C-GNPs for gene regulation followed by protein expression in cells [57].
Intrauterine Bacterial Colonization and Endometrial MicroRNA-17-5p Levels in Association to Endometriosis: A Study in an Egyptian Population
Published in Immunological Investigations, 2020
Yasmin Nabiel, Heba ELshahawy, Alaa Mosbah
RNA extraction kits Direct-zol RNA MiniPreP (Zymo research) were used to extract total RNA from collected endometrial tissue samples (each of 100 mg) by applying the manufacturer’s instructions. The resulting RNA strands were assessed using gel electrophoresis and their purity was measured using a spectrophotometer. One µg of total RNA was reversely transcribed to synthetize its complementary DNA (c-DNA) by the SensiFAST c-DNA synthesis Kit (Bioline).