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Complement C5a acts as molecular adjuvant in fish by enhancing antibody response to soluble antigen
C5a, the most potent anaphylatoxin generated during complement activation, has important proinflammatory actions and has also been shown to enhance antigen-specific antibody response in mammals, thereby acting as a molecular adjuvant.
Oriol Sunyer, Yong-An Zhang
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Pharmacological activity of C5a and peptide analogues of C5a [PDF]
The activation of the blood borne complement system results in the production of the anaphylatoxin C5a. The interaction of C5a with its receptor leads to activation of inflammatory cells. The inappropriate and excessive production of C5a has been implicated in numerous inflammatory disease states, including arthritis and Alzheimer's disease. At present
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Role of C5a and C5a Receptor in Sepsis
2006In experimental sepsis (after cecal ligation and puncture, CLP) there is convincing evidence of complement activation, as there is in human sepsis. In addition, in sepsis involving rodents and humans, blood neutrophils have lost innate immune functions (chemotaxis, phagocytosis, the ability to produce H2O2).
F. S. Zetoune +2 more
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A cyclic peptide, Phe-[Orn-Pro-D-Cyclohexylalanine-Trp-Arg] (F-[OPdChaWR]), was recently shown in vitro to antagonise the binding of C5a to its receptor (CD88) on human polymorphonuclear leukocytes (PMNs) and in vivo to inhibit the neutropenia associated
Damien Harkin +2 more
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Human T Cells Express the C5a Receptor and Are Chemoattracted to C5a
The Journal of Immunology, 1999Abstract The anaphylatoxin C5a is a potent mediator of inflammation that exerts a broad range of activity on cells of the myeloid lineage. In this study, we present the first evidence that human T cells express the C5a receptor (C5aR) and are chemotactic to C5a.
S, Nataf +3 more
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Modeling Molecular Mechanisms of Binding of the Anaphylatoxin C5a to the C5a Receptor
Biochemistry, 2008This study presents the 3D model of the complex between the anaphylatoxin C5a and its specific receptor, C5aR. This is the first 3D model of a G-protein-coupled receptor (GPCR) complex with a peptide ligand deduced by a molecular modeling procedure analyzing various conformational possibilities of the extracellular loops and the N-terminal segment of ...
Gregory V, Nikiforovich +2 more
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The Human Mast Cell Line HMC‐1 Expresses C5a Receptors and Responds to C5a but not to C5a(desArg)
Scandinavian Journal of Immunology, 1996The expression of the receptor for the anaphylatoxin C5a (C5aR, CD88) on the human mast cell line HMC‐1 was studied with four anti‐C5aR monoclonal antibodies directed to the N‐terminal domain of the receptor. All antibodies bound to the human mast cell line HMC‐1.
T, Werfel +6 more
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particularly neutrophil chemoattraction. Herein, the role of C5a in the genesis of inflammatory hypernociception was investigated in rats and mice using the specific C5a receptor antagonist PMX53 (AcF-[OP(D-Cha)WR])
Thiago Mattar Cunha +2 more
exaly +2 more sources
1978
Publisher Summary This chapter discusses the structural and functional characterization of anaphylatoxins, spasmogenic substances released during complement activation. These low molecular weight peptide fragments of C3 and C5 elicit a variety of cellular responses, which implies that they play a significant role in inflammation and acute allergic ...
T E, Hugli, H J, Müller-Eberhard
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Publisher Summary This chapter discusses the structural and functional characterization of anaphylatoxins, spasmogenic substances released during complement activation. These low molecular weight peptide fragments of C3 and C5 elicit a variety of cellular responses, which implies that they play a significant role in inflammation and acute allergic ...
T E, Hugli, H J, Müller-Eberhard
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Gene, 1997
Binding and effector domains of the human anaphylatoxin C5a have been determined by either site directed mutagenesis or synthetic peptide studies. However, the lack of specific selection methods, which allow direct investigation of C5a-C5a-receptor interaction made these studies laborious.
M, Hennecke +6 more
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Binding and effector domains of the human anaphylatoxin C5a have been determined by either site directed mutagenesis or synthetic peptide studies. However, the lack of specific selection methods, which allow direct investigation of C5a-C5a-receptor interaction made these studies laborious.
M, Hennecke +6 more
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