Results 201 to 210 of about 53,790 (237)
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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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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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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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Human T Cells Express the C5a Receptor and Are Chemoattracted to C5a
The Journal of Immunology, 1999AbstractThe 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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Acta Crystallographica Section D Biological Crystallography, 2010
The anaphylatoxin C5a is derived from the complement component C5 during activation of the complement cascade. It is an important component in the pathogenesis of a number of inflammatory diseases. NMR structures of human and porcine C5a have been reported; these revealed a four-helix bundle stabilized by three disulfide bonds. The crystal structure of
William J, Cook +4 more
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The anaphylatoxin C5a is derived from the complement component C5 during activation of the complement cascade. It is an important component in the pathogenesis of a number of inflammatory diseases. NMR structures of human and porcine C5a have been reported; these revealed a four-helix bundle stabilized by three disulfide bonds. The crystal structure of
William J, Cook +4 more
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Immunology & Cell Biology, 2013
Receptors for C5a have an important role in innate immunity and inflammation where their expression and activation is tightly regulated. There are two known receptors for C5a: the C5a receptor (C5aR) and the C5a receptor like‐2 (C5L2) receptor. Here we hypothesized that activation of C5aR might lead to heteromer formation with C5L2, as a downregulatory
Croker, Daniel E. +3 more
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Receptors for C5a have an important role in innate immunity and inflammation where their expression and activation is tightly regulated. There are two known receptors for C5a: the C5a receptor (C5aR) and the C5a receptor like‐2 (C5L2) receptor. Here we hypothesized that activation of C5aR might lead to heteromer formation with C5L2, as a downregulatory
Croker, Daniel E. +3 more
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Current pharmaceutical design, 1999
The anaphylatoxin C5a is an extremely potent proinflammatory peptide produced during activation of the complement system. The structure of C5a includes a core region (N-terminal residues 1-63) consisting of four, antiparallel alpha-helices held together by three disulfide linkages and a structured C-terminal tail (residues 64-74).
T C, Pellas, L P, Wennogle
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The anaphylatoxin C5a is an extremely potent proinflammatory peptide produced during activation of the complement system. The structure of C5a includes a core region (N-terminal residues 1-63) consisting of four, antiparallel alpha-helices held together by three disulfide linkages and a structured C-terminal tail (residues 64-74).
T C, Pellas, L P, Wennogle
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Mediators of C5a-induced bronchoconstriction
Agents and Actions, 1987Previous studies had suggested that histamine and products of arachidonate metabolism were mediators of the bronchoconstriction induced in guinea pigs by the complement cleavage product C5a. The present study was conducted to further define the arachidonate metabolite(s) involved.
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