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J. Biol. Chem., Vol. 266, Issue 18, 11575-11581, Jun, 1991
H Maekawa, K Yamazumi, S Muramatsu, M Kaneko, H Hirata, N Takahashi, NB de Bosch, Z Carvajal, A Ojeda and CL Arocha-Pinango
We have identified a unique N-glycosylated Asn substitution for a Ser at
position 434 of the A alpha chain of an abnormal fibrinogen designated
fibrinogen Caracas II. This dysfibrinogen was characterized by impaired
fibrin monomer aggregation. Since there were 4 Thr residues immediately
following the mutation, a new Asn-X-Thr/Ser-type consensus sequence,
Asn-Thr-Thr arose for N-glycosylation of the Asn. The extra oligosaccharide
was found to consist mainly of a disialylated biantennary structure
comprising 81.9%, while a neutral and a monosialylated biantennary
oligosaccharide represented only 3.6% and 14.5%, respectively. The mutation
resides in the carboxyl-terminal region of the A alpha chain, which could
fold back to form an extra small globular region located near the central
region of the molecule (Erickson, H.P., and Fowler, W.E. (1983) Ann. N. Y.
Acad. Sci. 408, 146- 163; Weisel, H.P., Stauffacher, C.V., Bullitt, E., and
Cohen, C. (1985) Science 230, 3124-3133). Therefore, the participation of
this region, referred to as an additional central domain or an alpha
domain, in fibrin gel formation is strongly implicated.
An A alpha Ser-434 to N-glycosylated Asn substitution in a dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin gel formation
Division of Hemostasis and Thrombosis Research, Jichi Medical School, Tochigi, Japan.
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