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Blood, 1 December 2000, Vol. 96, No. 12, pp. 3696-3706
CHEMOKINES
Novel nuclear target for thrombin: activation of the Elk1
transcription factor leads to chemokine gene expression
Qi-Jing Li,
Sucheta Vaingankar,
Frances M. Sladek, and
Manuela Martins-Green
From the Department of Cell Biology and Neuroscience,
University of California, Riverside, CA.
Thrombin is primarily known for its role in homeostasis and
thrombosis. However, this enzyme also plays important roles in wound
healing and pathologic situations such as inflammation and tumorigenesis. Among the molecules stimulated by thrombin in these latter processes are the stress response proteins, chemokines. Chemokines are also known for their roles in inflammatory responses and
tumor development. These correlative observations strongly suggest that
chemokines may be mediators of some of thrombin's functions in these
processes. Elucidation of the molecular mechanisms of stimulation of
chemokines by thrombin may help to unravel the ways in which their
expression can be modulated. Up-regulation of the chemokine 9E3/cCAF by
thrombin occurs via its proteolytically activated receptor with
subsequent transactivation of the epidermal growth factor receptor
tyrosine kinase. This study shows that stimulation by thrombin very
rapidly activates this chemokine at the transcriptional level, that 2 Elk1 binding elements located between  534 and 483 bp of the
promoter are major thrombin response elements, that activation occurs
via the Elk1 transcription factor, and that the latter is directly
activated by MEK1/ERK2. The common occurrence of Elk1 binding domains
in the promoters of immediate early response genes suggests that it may
be characteristically involved in gene activation by
stress-inducing agents.
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