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Isolation and Characterization of Exodus-2, a Novel C-C Chemokine With a Unique 37-amino Acid Carboxyl-Terminal Extension

Isolation and Characterization of Exodus-2, a Novel C-C Chemokine With a Unique 37-amino Acid Carboxyl-Terminal Extension

R Hromas, C H Kim, M Klemsz, M Krathwohl, K Fife, S Cooper, C Schnizlein-Bick, H E Broxmeyer

J Immunol. 1997 Sep 15;159(6):2554-8.

PMID: 9300671

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-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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4248646	Exodus-2 (CCL21) human			Price

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