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A novel fibrinogen variant (fibrinogen Seoul II; AαGln328Pro) characterized by impaired fibrin α-chain cross-linking

Authors
 Rojin Park  ;  Hyun-Ju Doh  ;  Seong-Soo A. An  ;  Jong-Rak Choi  ;  Kwang-Hoe Chung  ;  Kyung-Soon Song 
Citation
 Blood, Vol.108(6) : 1919-1924, 2006 
Journal Title
 Blood 
ISSN
 0006-4971 
Issue Date
2006
Abstract
We report a novel fibrinogen variant (fibrinogen Seoul II), which has a heterozygous point mutation from CAA to CCA leading to AαGln328Pro. The mutation site is among several glutamine residues that serve as α-chain cross-linking acceptor sites. Fibrinogen Seoul II was found in a 51-year-old male patient and his family in Seoul, Korea. The patient was diagnosed with myocardial infarction at age 43. Eight years later he was admitted to the emergency room due to recurrence of the disease, where he expired under treatment with tissue plasminogen activator (t-PA). Fibrin polymerization curves, made using purified fibrinogen from the patient's relatives, showed a decreased final turbidity, suggesting Seoul II fibrin clots are composed of thinner fibers. This supposition was verified using scanning electron microscopy. Alpha-polymer formation by the mutant fibrinogen upon thrombin treatment in the presence of factor XIII and calcium was distinctly impaired. This result confirms that the residue Aα328 plays a pivotal role in α-chain cross-linking.
Files in This Item:
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DOI
10.1182/blood-2005-11-007591
Appears in Collections:
1. Journal Papers (연구논문) > 1. College of Medicine (의과대학) > Dept. of Laboratory Medicine (진단검사의학교실)
Yonsei Authors
송경순(Song, Kyung Soon)
최종락(Choi, Jong Rak) ORCID logo https://orcid.org/0000-0002-0608-2989
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URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/109073
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