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- Title
Biological properties of human C5a: selected in vitro and in vivo studies.
- Authors
Yancey, K. B.
- Abstract
The article presents a study related to human C5a. During the activation of complement, a variety of cleavage fragments are produced which display potent inflammatory, immunomodulatory, and immunological properties. One of these fragments is C5a, a 74-residue glycopeptide produced by cleavage of the amino terminal end of the C5 alpha chain. In man, serum carboxypeptidase N rapidly converts C5a to the less potent though biologically active derivative, C5a des Arg, by removal ofthe carboxy terminal arginine. C5a and C5a des Arg have a variety of important biological properties which are mediated through the interaction of these glycopeptides with peripheral blood leucocytes and specific cells resident in tissue. This cellular interaction is mediated by the binding of C5a or C5a des Arg to plasma membrane receptors on these effector cells.
- Subjects
BLOOD plasma; AMINO acids; PEPTIDES; BLOOD cells; LEUCOCYTES; CELL membranes
- Publication
Clinical & Experimental Immunology, 1988, Vol 71, Issue 2, p207
- ISSN
0009-9104
- Publication type
Article