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An EGF-like peptide sequence from Dictyostelium enhances cell motility and chemotaxis.

Abstract：

:Dictyostelium discoideum possesses more EGF-like (EGFL) domains than any other sequenced eukaryote. Here we show that a synthetic EGFL peptide (DdEGFL1) based upon an amino acid sequence from a cysteine-rich Dictyostelium protein, functions extracellularly to enhance random cell motility and cAMP-mediated chemotaxis in Dictyostelium by 625% and 85%, respectively, in strain NC4 and by 620% and 80% in strain AX3. Quinacrine inhibited peptide-enhanced random motility but not chemotaxis in strain AX3 providing evidence that PLA2 is the predominant regulator of this process. While LY294002 alone had no significant effect on either event, in combination with quinacrine it dramatically inhibited both processes suggesting that both PI3K and PLA2-mediated signaling are required for EGFL peptide-enhanced cell movement. DdEGFL1 also sustained the threonine phosphorylation of a 210kDa protein that is dephosphorylated during Dictyostelium starvation. Taken together, these results suggest an important role for certain EGFL peptides in Dictyostelium cell movement.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Huber R,O'Day DH

doi

10.1016/j.bbrc.2008.12.081

subject

Has Abstract

pub_date

2009-02-06 00:00:00

pages

470-5

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(08)02498-4

journal_volume

379

pub_type

杂志文章

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