Fibrinogen Osaka IV: a congenital dysfibrinogenemia found in a patient originally reported in relation to surgery, now defined to have an A alpha arginine-16 to histidine substitution.

Abstract

We discovered a congenital heterozygous dysfibrinogen in a patient and reported this case in relation to surgery some time ago (Jpn J Surg (1988) 18:43-46). Further studies on the isolated abnormal population of fibrinogen derived from this patient have revealed that fibrinopeptide A was not cleaved by ancrod, a snake venom-derived thrombin-like enzyme, but by thrombin, slowly but completely. The released fibrinopeptide A components, being the A, AY, and AP peptides, were all found to be abnormal, as evidenced by slightly earlier elution positions on high-performance liquid chromatography, compared with the normal counterparts. By analyzing their amino acid sequence, we have identified an arginine to histidine substitution at position 16 of the A alpha chain, the thrombin cleavage site. Utilizing insolubilized abnormal fibrinogen, we confirmed that the polymerization site assigned to the central E domain, the "A" site, was exposed by thrombin, but not by ancrod. This dysfibrinogen, designated as fibrinogen Osaka IV, is the second abnormal molecule with an A alpha arginine-16 to histidine substitution identified among Japanese families.

• Authors: K Yamazumi, S Terukina, M Matsuda, J Kanbayashi, M Sakon, T Tsujinaka
• Journal: Surgery today (Surg Today) Vol. 23 Issue 1 Pg. 45-50 ( 1993) ISSN: 0941-1291 [Print] Japan
• PMID: 8461606 (Publication Type: Case Reports, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Fibrinogens, Abnormal
• fibrinogen Osaka IV
• Fibrinopeptide A
• Histidine
• Arginine
• Ancrod

Topics

• Afibrinogenemia (congenital, genetics)
• Amino Acid Sequence
• Ancrod
• Arginine (chemistry)
• Chromatography, High Pressure Liquid
• Fibrinogens, Abnormal (chemistry)
• Fibrinopeptide A (chemistry)
• Histidine (chemistry)
• Humans
• Male
• Middle Aged
• Molecular Sequence Data