Abstract
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) |
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Pages (from-to) | 11968-11972 |
Number of pages | 5 |
Journal | Biochemistry® |
Volume | 31 |
Issue number | 48 |
State | Published - 1992 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry