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Cloning of the human eosinophil chemoattractant, eotaxin. Expression, receptor binding, and functional properties suggest a mechanism for the selective recruitment of eosinophils.

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Ponath, P D, Qin, S, Ringler, D J, Clark-Lewis, I, Wang, J, Kassam, N, Smith, H, Shi, X, Gonzalo, J A, Newman, W, Gutierrez-Ramos, J C, Mackay, C R·1996·Journal of Clinical Investigation

Abstract

The CC chemokine eotaxin, identified in guinea pigs and also recently in mice, may be a key element for the selective recruitment of eosinophils to certain inflamed tissues. Using a partial mouse eotaxin CDNA probe, the human eotaxin gene was cloned and found to be 61.8 and 63.2% identical at the amino acid level to guinea pig and mouse eotaxin. Human eotaxin protein was a strong and specific eosinophil chemoattractant in vitro and was an effective eosinophil chemoattractant when injected into the skin of a rhesus monkey. Radiolabeled eotaxin was used to identify a high affinity receptor on eosinophils (0.52 nM Kd), expressed at 4.8 x 10(4) sites per cell. This receptor also bound RANTES and monocyte chemotactic protein-3 with lower affinity, but not macrophage inflammatory protein-1 alpha. Eotaxin could desensitize calcium responses of eosinophils to RANTES and monocyte chemotactic protein-3, although RANTES was able to only partially desensitize eosinophil calcium responses to eotaxin. Immunohistochemistry on human nasal polyp with antieotaxin mAbs showed that certain leukocytes as well as respiratory epithelium were intensely immunoreactive, and eosinophil infiltration occurred at sites of eotaxin upregulation. Thus eotaxin in humans is a potent and selective eosinophil chemoattractant that is expressed by a variety cell types in certain inflammatory conditions.

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Authors
Ponath, P. D., Qin, S., Ringler, D. J., Clark-Lewis, I., Wang, J., Kassam, N., Smith, H., Shi, X., Gonzalo, J. A., Newman, W., Gutierrez-Ramos, J. C., & Mackay, C. R.
Venue
Journal of Clinical Investigation
Published
1996-02-01
Volume
97
Issue
3
Pages
604-612
ISSN
0021-9738 (ISSN-L)
OpenAlex
W2023520187
Cited by
697
References
0
FWCI
48.58
Type
journal article
Language
en
Open access
bronze

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