Protein Structure and Expression
The Egfl7 protein (29 kDa) is composed of several putative domains: a putative cleavable signal peptide at the N-terminal end, an EMI domain, found on extracellular matrix proteins, two EGF-like domains and a leucine and valine rich C-terminal region. The first EGF-like domain has a region similar to the DSL (Delta/Serrate/Lag-2) domain found in ligands of the Notch receptors family, the second EGF-like domain is predicted to bind Ca2+. The Eglf7 protein is secreted and associates with the blood vessel extracellular matrix.
Endothelial cell lines naturally express egfl7, on the contrary to non-endothelial cells. In endothelial cells, expression is controlled by the Erg and GATA2 transcription factors and, indirectly by Fli-1. The expression pattern of the egfl7 gene is conserved across species. Egfl7 is expressed in endothelial progenitors and in endothelial cells during embryonic and neonatal development. Expression is down-regulated in adults but is still detectable in blood vessels of lung, heart and kidney. An up-regulation of egfl7 is observed in endothelial cells during vascular remodelling tissues, such as in reproductive organs during pregnancy, in regenerating endothelium following arterial injury, in atherosclerotic plaques, and in growing tumours. Expression of egfl7 has also been reported in primordial germ cells and in adult ovaries and testes and in neurons.
Read more about this topic: EGFL7
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