Molecular cloning and characterization of a novel human CC chemokine, SCYA26.

Abstract:

:By searching the Expressed Sequence Tag database, a full-length cDNA for a novel human CC chemokine was cloned. This cDNA encoded a 94-amino-acid protein with a putative signal peptide of 26 amino acids. The deduced mature protein had the four conserved cysteine residues characteristic of CC chemokines and showed 44% identity with MIP-1beta and 40% identity with MIP-1alpha, RANTES, and MCP-4. mRNA for this chemokine was expressed constitutively in human heart and liver and with lesser but detectable levels in skeletal muscle, kidney, and small intestine. To investigate its biological activity, the protein was expressed in mammalian cells and purified by affinity chromatography. The recombinant protein demonstrated chemotactic activity in vitro for T cells and monocytes but not for neutrophils. The gene was mapped to chromosome 7q11.2 by fluorescence in situ hybridization. Based on its structural identity with other CC chemokines and the chemotactic activity and chromosomal location of this chemokine, we designate this chemokine small inducible cytokine subfamily A, member 26 (SCYA26). This gene symbol has been approved by the HUGO Gene Nomenclature Committee.

journal_name

Genomics

journal_title

Genomics

authors

Guo RF,Ward PA,Hu SM,McDuffie JE,Huber-Lang M,Shi MM

doi

10.1006/geno.1999.5837

subject

Has Abstract

pub_date

1999-06-15 00:00:00

pages

313-7

issue

3

eissn

0888-7543

issn

1089-8646

pii

S0888-7543(99)95837-8

journal_volume

58

pub_type

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