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Functional analysis of chemically synthesized derivatives of the human CC chemokine CCL15/HCC‐2, a high affinity CCR1 ligand by S.E. Escher; J. Vakili; U. Forssmann; A. Frimpong‐Boateng; H. Sticht; M. Detheux; K. Adermann is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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**Abstract:** The CCL15 is a human CC chemokine that activates the receptors, CCR1 and CCR3. Unlike other chemokines, it contains an unusually long N‐terminal domain of 31 amino acids preceding the first cysteine residue and a third disulfide bond. To elucidate the functional role of distinct structural determinants, a series of sequential amino‐terminal truncated and point‐mutated CCL15 derivatives as well as mutants lacking the third disulfide bond and the carboxy‐terminal __α__‐helix were synthesized using 9‐fluorenylmethoxycarbonyl (Fmoc) chemistry. We demonstrate that a truncation of 24 amino acid residues (Δ24‐CCL15) converts the slightly active 92‐residue Δ0‐CCL15 into a potent agonist of CC chemokine receptor 1 (CCR1) and a weak agonist of CCR3 in cell‐based assays. The biological activity decreases from Δ24‐CCL15 to Δ29‐CCL15, and re‐increases from Δ29‐CCL15 to Δ30‐CCL15. Thus, an exocyclic N‐terminal region of only one amino acid residue is sufficient for efficient CCR1 activation. As none of the peptides investigated except for Δ24‐CCL15 activates CCR3, we suggest that CCR1 is the major receptor for CCL15 in vivo. Further we demonstrate that the third disulfide bond of C

Who reads Functional analysis of chemically synthesized derivatives of the human CC chemokine CCL15/HCC‐2, a high affinity CCR1 ligand?

Author

S.E. Escher; J. Vakili; U. Forssmann; A. Frimpong‐Boateng; H. Sticht; M. Detheux; K. Adermann

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 1397-002X)

Published

2004

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)