An N-terminally Truncated Mutant of Human Chemokine CXCL14 has Biological Activity
2013
Chemokines are members of the superfamily of cytokines involved in: (i) cell migration to sites of infection; or
(ii) cellular stress during an immune response. Human CXCL14/BRAK is a monocyte-selective chemokine expressed in
all normal tissues, but is also involved in the development of several cancers. We describe the expression, structural characterization
and biological activity of an N-terminal truncated mutant of CXCL14, ΔCXCL14, where the first eleven residues
and the two disulphide bridges were removed. We designed this species in order to analyse the biological importance
of the disulphide bonds and the flexible N terminus of CXCL14 for its protein folding, stability and function. The mutant
ΔCXCL14 is biologically active, as suggested by the in vitro assays with migration of pancreatic cancer cells, but also its
structure is not well-fixed, as suggested by fluorescence, CD and NMR. We conclude that the disulphide bridges are important
in maintaining the structure of this chemokine, but they are not necessary for the biological activity of CXCL14
species.
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