Human Mig chemokine

Biochemical and functional characterization

Fang Liao, Ronald L. Rabin, John R. Yannelli, Leonidas Koniaris, Padmavathy Vanguri, Joshua M. Farber

Research output: Contribution to journalArticle

319 Citations (Scopus)

Abstract

Mig is a chemokine of the CXC subfamily that was discovered by differential screening of a cDNA library prepared from lymphokine-activated macrophages. The mig gene is inducible in macrophages and in other cells in response to interferon (IFN)-γ. We have transfected Chinese hamster ovary (CHO) cells with cDNA encoding human Mig and we have derived CHO cell lines from which we have purified recombinant human Mig (rHuMig). rHuMig induced the transient elevation of [Ca2+](i) in human tumor-infiltrating T lymphocytes (TIL) and in cultured, activated human peripheral blood-derived lymphocytes. No responses were seen in human neutrophils, monocytes, or Epstein-Barr virus-transformed B lymphoblastoid cell lines rHuMig was chemotactic for TIL by a modified Boyden chamber assay but rHuMig was not chemotactic for neutrophils or monocytes. The CHO cell lines, IFN-γ-treated human peripheral-blood monocytes, and IFN-γ-treated cells of the human monocytic cell line THP-1 all secreted multiple and identical HuMig species as revealed by SDS-PAGE. Using the CHO-derived rHuMig, we have shown that the species' heterogeneity is due to proteolytic cleavage at basic carboxy- terminal residues, and that the proteolysis occurs before and not after rHuMig secretion by the CHO cells. The major species of secreted rHuMig ranged from 78 to 103 amino acids in length, the latter corresponding to the full-length secreted protein predicted from the HuMig cDNA. Carboxy-terminal- truncated forms of rHuMig were of lower specific activity compared to full- length rHuMig in the calcium flux assay, and the truncated species did not block the activity of the full-length species. It is likely that HuMig plays a role in T cell trafficking and perhaps in other aspects of the physiology of activated T cells.

Original languageEnglish (US)
Pages (from-to)1301-1314
Number of pages14
JournalJournal of Experimental Medicine
Volume182
Issue number5
DOIs
StatePublished - Nov 1 1995
Externally publishedYes

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Chemokine CXCL9
Cricetulus
Ovary
Interferons
T-Lymphocytes
Tumor-Infiltrating Lymphocytes
Monocytes
Cell Line
Neutrophils
Complementary DNA
Macrophages
CXC Chemokines

ASJC Scopus subject areas

  • Immunology

Cite this

Liao, F., Rabin, R. L., Yannelli, J. R., Koniaris, L., Vanguri, P., & Farber, J. M. (1995). Human Mig chemokine: Biochemical and functional characterization. Journal of Experimental Medicine, 182(5), 1301-1314. https://doi.org/10.1084/jem.182.5.1301

Human Mig chemokine : Biochemical and functional characterization. / Liao, Fang; Rabin, Ronald L.; Yannelli, John R.; Koniaris, Leonidas; Vanguri, Padmavathy; Farber, Joshua M.

In: Journal of Experimental Medicine, Vol. 182, No. 5, 01.11.1995, p. 1301-1314.

Research output: Contribution to journalArticle

Liao, F, Rabin, RL, Yannelli, JR, Koniaris, L, Vanguri, P & Farber, JM 1995, 'Human Mig chemokine: Biochemical and functional characterization', Journal of Experimental Medicine, vol. 182, no. 5, pp. 1301-1314. https://doi.org/10.1084/jem.182.5.1301
Liao, Fang ; Rabin, Ronald L. ; Yannelli, John R. ; Koniaris, Leonidas ; Vanguri, Padmavathy ; Farber, Joshua M. / Human Mig chemokine : Biochemical and functional characterization. In: Journal of Experimental Medicine. 1995 ; Vol. 182, No. 5. pp. 1301-1314.
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