| First Author | Hromas R | Year | 1997 |
| Journal | J Immunol | Volume | 159 |
| Issue | 6 | Pages | 2554-8 |
| PubMed ID | 9300671 | Mgi Jnum | J:42623 |
| Mgi Id | MGI:1096048 | Doi | 10.4049/jimmunol.159.6.2554 |
| Citation | Hromas R, et al. (1997) Isolation and characterization of Exodus-2, a novel C-C chemokine with a unique 37-amino acid carboxyl-terminal extension. J Immunol 159(6):2554-8 |
| abstractText | 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. |
