rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1994-6-14
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pubmed:abstractText |
The anaphylatoxic peptide C5a is an important inflammatory mediator of the complement system. We have generated human C5a-receptor (hC5aR) mutants with truncation of its cytosolic carboxyl-terminus (C-terminus). Both mutants were analysed for C5a-binding in transiently expressing COS cells, and one mutant additionally for GTP-binding regulatory protein (G-protein) coupling in cRNA-injected Xenopus oocytes. Our data suggest that (a) amino acids (aa) 314 to 326 as part of the C-terminus are necessary for proper receptor folding or expression and (b) the receptor C-terminus distal from position 327 is not critical for receptor expression, folding, binding and G-protein coupling.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
May
|
pubmed:issn |
0014-5793
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
9
|
pubmed:volume |
344
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
79-82
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:8181569-Animals,
pubmed-meshheading:8181569-Base Sequence,
pubmed-meshheading:8181569-Binding, Competitive,
pubmed-meshheading:8181569-Cell Line,
pubmed-meshheading:8181569-Complement C5a,
pubmed-meshheading:8181569-Female,
pubmed-meshheading:8181569-GTP-Binding Proteins,
pubmed-meshheading:8181569-Gene Expression,
pubmed-meshheading:8181569-Humans,
pubmed-meshheading:8181569-Kinetics,
pubmed-meshheading:8181569-Molecular Sequence Data,
pubmed-meshheading:8181569-Oocytes,
pubmed-meshheading:8181569-Peptide Fragments,
pubmed-meshheading:8181569-Receptor, Anaphylatoxin C5a,
pubmed-meshheading:8181569-Receptors, Complement,
pubmed-meshheading:8181569-Signal Transduction,
pubmed-meshheading:8181569-Structure-Activity Relationship,
pubmed-meshheading:8181569-Transfection,
pubmed-meshheading:8181569-Xenopus laevis
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pubmed:year |
1994
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pubmed:articleTitle |
Amino acids 327-350 of the human C5a-receptor are not essential for [125I]C5a binding in COS cells and signal transduction in Xenopus oocytes.
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pubmed:affiliation |
Institut für Medizinische Mikrobiologie, Medizinische Hochschule Hannover, Germany.
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pubmed:publicationType |
Journal Article
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