Similarities between the N-terminal regions of the three subunits of the clotting protein fibrinogen - (αβγ)2 - suggest that they evolved from a common progenitor. However, to date no human a chain has been found with the strong C-terminal homology shared by the β and γ chains. Here we examine the natural product of a novel fibrinogen α chain transcript bearing a separate open reading frame that supplies the missing C-terminal homology to the other chains. Additional splicing leads to the use of this extra sequence as a sixth exon elongating the a chain by 35%. Since the extended α chain (αE) is assembled into fibrinogen molecules and its synthesis is enhanced by interleukin-6, it suggests participation in both the acute phase response and normal physiology.
|Original language||English (US)|
|Number of pages||5|
|State||Published - 1992|
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