Attachment of human C5a des Arg to its cochemotaxin is required for maximum expression of chemotactic activity
| Autor: | I M Goldstein, H D Perez, D E Chenoweth |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
Anaphylatoxins
Complement C5a chemical and pharmacologic phenomena Iodine Radioisotopes chemistry.chemical_compound Humans Polyacrylamide gel electrophoresis Complement component 5 chemistry.chemical_classification Chemotactic Factors Complement C5a des-Arginine Chemotaxis Complement C5 hemic and immune systems Blood Proteins General Medicine respiratory system Oligosaccharide Blood Physiological Phenomena Blood proteins Molecular biology N-Acetylneuraminic Acid Sialic acid Molecular Weight chemistry Biochemistry Chromatography Gel Sialic Acids Electrophoresis Polyacrylamide Gel Density gradient ultracentrifugation Peptides N-Acetylneuraminic acid Research Article |
| Zdroj: | Journal of Clinical Investigation. 78:1589-1595 |
| ISSN: | 0021-9738 |
| DOI: | 10.1172/jci112751 |
| Popis: | The chemotactic activity of human C5a des Arg is enhanced significantly by an anionic polypeptide (cochemotaxin) in normal human serum and plasma. We have found that the cochemotaxin attaches to the oligosaccharide chain of native C5a des Arg to form a complex with potent chemotactic activity for human polymorphonuclear leukocytes. Although capable of enhancing the chemotactic activity of native C5a des Arg, the cochemotaxin had no effect on the chemotactic activity of either deglycosylated C5a des Arg, native C5a, or N-formyl-methionyl-leucyl-phenylalanine. Of the known components of the oligosaccharide chain, only sialic acid prevented enhancement by the cochemotaxin of the chemotactic activity exhibited by native C5a des Arg. Sialic acid also prevented the formation of C5a des Arg-cochemotaxin complexes, detected by acid polyacrylamide gel electrophoresis, molecular sieve chromatography on polyacrylamide gels, and sucrose density gradient ultracentrifugation. |
| Databáze: | OpenAIRE |
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