ArticleBMC immunology2008
Cloning and bioactivity analysis of a CXC ligand in black seabream Acanthopagrus schlegeli: the evolutionary clues of ELR+CXC chemokines.
Article in BMC immunology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 37 citations in OpenAlex.
- Identification, Expression and Antimicrobial Functional Analysis of Interleukin-8 (IL-8) in Response toAnimals : an open access journal from MDPI · 2024Article
- Comparative Characterization of TwoBiomolecules · 2020Article
- Molecular Characterization and Chemotactic Function of CXCL8 in Northeast Chinese Lamprey (Frontiers in immunology · 2020Article
- Effects of chronic cortisol administration on global expression of GR and the liver transcriptome in Sparus aurata.Marine biotechnology (New York, N.Y.) · 2013Article
- CXCL8 chemokines in teleost fish: two lineages with distinct expression profiles during early phases of inflammation.PloS one · 2010Article
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5 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundThe ELR+CXC chemokines are multifunctional mediators that are mainly responsible for the recruitment of leucocytes to sites of inflammation and infection. Because of their high sequence identity with mammalian IL-8, fish IL-8-like CXCs have been named as piscine 'IL-8' and included in the ELR+ subgroup, even though there is no reliable functional or evolutionary evidence to support this classification.
resultsIn this investigation, a homologue of piscine 'IL-8' from black seabream (Acanthopagrus schlegeli), called BS CXC, has been cloned and analyzed. The results revealed that BS CXC has a high gene similarity and tertiary structure similarity with piscine and mammalian CXC chemokines, both ELR-CXC and ELR+CXC, although it has a lower identity with ELR-CXC, compared with ELR+CXC chemokines. Like other piscine IL-8, BS CXC has only an incomplete ELR motif, which is essential for the mammalian ELR+CXC ability to attract granulocytes. Bioactivity assay demonstrated that the BS rCXC produced in E. coli significantly stimulated migration of fish neutrophils and macrophages, but had no effect on rat neutrophils and macrophages, whereas hrIL-8 induced strong chemotaxis of fish neutrophils but did not affect fish macrophages. BS CXC seems show some structural and functional properties of the intermediate between ELR-CXC and ELR+CXC.
conclusionAs an incomplete ELR+CXC chemokine from a modern fish, BS CXC provides some clues on the evolution from ancient ELR-CXC to ELR+CXC by retaining some properties of the intermediate stage in evolution, and it may be more appropriate to call this molecule 'piscine CXC with an incomplete ELR', instead of terming it fish 'IL-8'.
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