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The Journal of Immunology, Vol 159, Issue 6 2554-2558, Copyright © 1997 by American Association of Immunologists

CUTTING EDGE

Isolation and characterization of Exodus-2, a novel C-C chemokine with a unique 37-amino acid carboxyl-terminal extension

R Hromas, CH Kim, M Klemsz, M Krathwohl, K Fife, S Cooper, C Schnizlein-Bick and HE Broxmeyer
Department of Medicine, Indiana University Medical Center, Indianapolis 46202, USA. robertvhromas@iucc.iupui.edu

Chemokines are a group of small, homologous proteins that regulate leukocyte migration, hemopoiesis, and HIV-1 absorption. We report here the cloning and characterization of a novel murine and human C-C chemokine termed Exodus-2 for its similarity to Exodus-1/MIP- 3alpha/LARC, and its chemotactic ability. This novel chemokine has a unique 36 or 37 (murine and human, respectively) amino acid carboxyl- terminal extension not seen in any other chemokine family member. Purified recombinant Exodus-2 was found to have two activities classically associated with chemokines: inhibiting hemopoiesis and stimulating chemotaxis. However, Exodus-2 also had unusual characteristics for C-C chemokines. It selectively stimulated the chemotaxis of T-lymphocytes and was preferentially expressed in lymph node tissue. The combination of these characteristics may be a functional correlate for the unique carboxyl-terminal structure of Exodus-2.


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