Hromas R, Kim C H, Klemsz M, Krathwohl M, Fife K, Cooper S, Schnizlein-Bick C, Broxmeyer H E
Department of Medicine, Indiana University Medical Center, Indianapolis 46202, USA.
J Immunol. 1997 Sep 15;159(6):2554-8.
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.
趋化因子是一类小型同源蛋白，可调节白细胞迁移、造血作用以及HIV-1吸附。我们在此报告一种新型鼠源和人源C-C趋化因子的克隆及特性，因其与Exodus-1/MIP-3α/LARC相似且具有趋化能力，故而命名为Exodus-2。这种新型趋化因子具有独特的36或37个（分别为鼠源和人源）氨基酸的羧基末端延伸结构，这在其他任何趋化因子家族成员中都未见过。纯化的重组Exodus-2具有两种与趋化因子经典相关的活性：抑制造血作用和刺激趋化性。然而，Exodus-2对于C-C趋化因子也具有不同寻常的特性。它能选择性地刺激T淋巴细胞的趋化性，且在淋巴结组织中优先表达。这些特性的组合可能与Exodus-2独特的羧基末端结构存在功能关联。
