کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2431649 | 1106767 | 2014 | 6 صفحه PDF | دانلود رایگان |

• A secretory recombinant protein of Japanese flounder IL-8 was produced using a human cell line.
• The N-terminal amino acid sequence of rIL-8 was identified as VSLRSLGV.
• rIL-8 specifically induced the migration of neutrophils.
• rIL-8 with mutated SLH residues displayed no reduction in its chemotaxis-inducing activity.
• N-terminally truncated rIL-8, deleting the first six or more residues, significantly reduced neutrophil chemotactic activity.
The objective of this study was to locate the functional region responsible for the chemotaxis-inducing activity of flounder interleukin 8 (IL-8), which lacks the glutamic acid–leucine–arginine (ELR) motif essential for the induction of neutrophil migration by mammalian IL-8. Using a human cell line, we produced a secretory recombinant protein of flounder IL-8, and analyzed its chemotaxis-inducing activity on leukocytes collected from the flounder kidney. The recombinant IL-8 induced significant migration in neutrophils, which were morphologically and functionally characterized. Using the Edman degradation method, the N-terminal amino acid sequence of rIL-8 was identified as VSLRSLGV. To examine the significance of the N-terminal region for the bioactivity of flounder IL-8, we prepared several recombinant proteins that containing mutations at the N-terminus. Modification of three residues (residues 9–11: serine–leucine–histidine) corresponding in position to the ELR motif in mammalian IL-8 did not reduce its chemotaxis-inducing activity. However, deletion of the first six or more residues significantly reduced its chemotaxis-inducing activity. We propose that residue 6 (leucine) at the N-terminus is important for the chemotaxis-inducing activity of flounder IL-8.
Journal: Fish & Shellfish Immunology - Volume 38, Issue 2, June 2014, Pages 361–366