Summary
FactorVIII acts as an essential compound of the tenase complex of the coagulation
system. Herein we report the cDNA of the rat factor VIII. The rat cDNA comprises 6777
nucleotides and encodes a protein of 2258 amino acids, 61 amino acids less than mouse
and 92 amino acids less than human factor VIII. The overall identity compared to human
cDNA is 61% on the cDNA and 51% on the amino acid level. In cDNA, highest levels of
sequence identity can be observed in the A and C domains (ranging between 68% and
73%), whereas B domain and the small acidic regions are more divergent (34%-49%).
Compared to mouse and human most sites for posttranslational modifications such as
sulfatation and glycosylation as well as thrombin and protein C cleavage sites are
conserved in rat. Alternative transcripts lacking exon 17 and/or comprising additional
26 bp due to alternative splicing of exon 20 were found. Furthermore, 13 polymorphisms
(seven in exon 14, one in exon 20, 23, 24, and 25, two in the 3’UTR) three of which
lead to an amino acid exchange could be detected. Our findings might provide new insights
into the structure-function analysis of the factor VIII protein and might prove useful
for future animal models addressing the function of factor VIII.
Keywords
Factor VIII - rat - cDNA - alternative splicing - exon skipping
