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The N- and C-terminal peptides of hIL8/CXCL8 are ligands for hCXCR1 and hCXCR2.

Publication ,  Journal Article
Li, Q-J; Yao, M; Wong, W; Parpura, V; Martins-Green, M
Published in: FASEB J
April 2004

Chemokines are small cytokines that function in immune responses, wound healing, and pathological conditions such as chronic inflammation and tumorigenesis. This multifunctionality has been attributed primarily to ligand interaction with multiple or dimerized receptors. However, multifunctionality could also result from interactions of the receptors with small peptides produced by processing of the chemokines. Chemokine peptides are functional in vivo, but it is not yet known whether they can interact with and activate their receptors. The work presented here examines the interactions between the two forms of human interleukin 8 (hIL-8), and its N- and C-peptides, with the chemokine receptors hCXCR1 and hCXCR2. We used a Tet-on retroviral system to introduce CXCR1 into mouse NIH 3T3 cells (that lack endogenous CXCR1) and monitored activation of this receptor by the ligands by using quantitative Ca2+ imaging and mitogen-activated protein kinase (MAPK) activation. We found that the N and C termini of the chemokine can stimulate the respective CXCR1 to induce intracellular Ca2+ release and MAPK activation independent of the other regions of the molecules. Furthermore, we showed that these peptides can also stimulate chemotaxis of several cell types, including primary human microvascular endothelial cells, and that this function is specific and mediated by hCXCR1 and/or hCXCR2. These findings advance understanding of the multifunctionality exhibited by chemokines, reveal a new mode of functional regulation, and may serve as the basis for therapeutic targeting.

Duke Scholars

Published In

FASEB J

DOI

EISSN

1530-6860

Publication Date

April 2004

Volume

18

Issue

6

Start / End Page

776 / 778

Location

United States

Related Subject Headings

  • Receptors, Interleukin-8B
  • Receptors, Interleukin-8A
  • Protein Structure, Tertiary
  • Peptides
  • NIH 3T3 Cells
  • Models, Biological
  • Mitogen-Activated Protein Kinases
  • Mice
  • Ligands
  • Interleukin-8
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Li, Q.-J., Yao, M., Wong, W., Parpura, V., & Martins-Green, M. (2004). The N- and C-terminal peptides of hIL8/CXCL8 are ligands for hCXCR1 and hCXCR2. FASEB J, 18(6), 776–778. https://doi.org/10.1096/fj.02-1175fje
Li, Qi-Jing, Min Yao, William Wong, Vladimir Parpura, and Manuela Martins-Green. “The N- and C-terminal peptides of hIL8/CXCL8 are ligands for hCXCR1 and hCXCR2.FASEB J 18, no. 6 (April 2004): 776–78. https://doi.org/10.1096/fj.02-1175fje.
Li Q-J, Yao M, Wong W, Parpura V, Martins-Green M. The N- and C-terminal peptides of hIL8/CXCL8 are ligands for hCXCR1 and hCXCR2. FASEB J. 2004 Apr;18(6):776–8.
Li, Qi-Jing, et al. “The N- and C-terminal peptides of hIL8/CXCL8 are ligands for hCXCR1 and hCXCR2.FASEB J, vol. 18, no. 6, Apr. 2004, pp. 776–78. Pubmed, doi:10.1096/fj.02-1175fje.
Li Q-J, Yao M, Wong W, Parpura V, Martins-Green M. The N- and C-terminal peptides of hIL8/CXCL8 are ligands for hCXCR1 and hCXCR2. FASEB J. 2004 Apr;18(6):776–778.

Published In

FASEB J

DOI

EISSN

1530-6860

Publication Date

April 2004

Volume

18

Issue

6

Start / End Page

776 / 778

Location

United States

Related Subject Headings

  • Receptors, Interleukin-8B
  • Receptors, Interleukin-8A
  • Protein Structure, Tertiary
  • Peptides
  • NIH 3T3 Cells
  • Models, Biological
  • Mitogen-Activated Protein Kinases
  • Mice
  • Ligands
  • Interleukin-8