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

Robert Hromas, Chang H. Kim, Michael Klemsz, Mitchell Krathwohl, Kenneth Fife, Scott Cooper, Carol Schnizlein-Bick, Hal E. Broxmeyer

Research output: Contribution to journalArticle

122 Scopus citations

Abstract

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-3a/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.

Original languageEnglish (US)
Pages (from-to)2554-2558
Number of pages5
JournalJournal of Immunology
Volume159
Issue number6
StatePublished - Dec 1 1997

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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