Molecular basis for the fibrinogen structure and functions - Analysls of hereditary dysfibrinogens and their application to the study

Studies on two hereditary dysfibrinogens were conducted in collaboration with Dr. Michael W。Mosesson专注于电子显微镜分析。（1） Fbg Niigata发现有一个独特的Bβ Asn-160与一个额外的寡乙酰N-链接到Bβ Asn-150的替代品，也就是说，双链纤维原型是正常形成的，他们的长期联系是无效的，很可能会附着到额外的寡乙酰Indeed， enzymatic Deglycosylation resulted in hancement of fibrin monomer polymerization to a great extent。Scanning electron microscopic analyses of fibrin clots revealed an abnormal architecture， being composed of curvilinear fibrin fibers。在脱糖基化之后，纤维蛋白纤维几乎成为正常的，是直的，适当的分支。与生物化学和基因分析数据一起的结果现在处于血液修订的状态之下。从德国Marburg发现了一位20岁的老妇女，她在20岁的第一次交货时了解凯撒尼亚部分。严重流血和成功的循环性循环性的象征性复杂性是特征性的。这种分子具有Aα-链的150-氨基酸溶液断裂，并在Aα-Cys-442上与血清专辑进行了部分干扰性桥接。Marburg纤维布是相当脆弱的，但完全抵抗力对塑料过度疲劳，因素XIIIa-crosslining概况由SDS-PAGE管理的几种α·β-异量剂，在正常样本中没有观察到。要注意的是，Aα-链连接的血清专辑被交叉链接到另一个纤维分子的g链，创造了无序的纤维克隆。Scanning electron microscopy showed Compact fibrin gels consisting of extremely thin but highly branched fibrin fibers。这些发现似乎有资格为经常性的后操作ethrombo-embolic Compplications帐户。这些结果的部分出现在血液（91 ： 3282-3288， 1998）中，留下的人现在正在准备出版。

Studies on two hereditary dysfibrinogens were conducted in collaboration with Dr. Michael W. Mosesson focusing on electron microscopic analyses. 1) Fbg Niigata was found to have a unique Bβ Asn-160 to Ser substitution with an extra oligosaccharide N-linked to Bβ Asn-150.Although the double-stranded fibrin protofibrils are normally formed, their lateral association is impaired, most probably due to the extra oligosaccharide attached to the coiled-coil region. Indeed, enzymatic deglycosylation resulted in enhancement of fibrin monomer polymerization to a great extent. Scanning electron microscopic analyses of fibrin clots revealed an abnormal architecture, being composed of curvilinear fibrin fibers. After deglycosylation, the fibrin fibers became nearly normal, being straight and appropriately branched. The result together with biochemical and gene analysis data is now under the status of revision in BLOOD. Fibrinogen Marburg from Germany was found in a 20-year-old woman who underwent a Caesarian section on her first delivery at the age of 20.Severe bleeding and successive recurrent thrombo-embolic complications were characteristic. This molecule has a 150-amino acid residue truncation of the Aα-chain, and is partly disulfide-bridged with serum albumin at Aα Cys-442. The Marburg fibrin clots are apparently fragile but totally resistant against plasmin Furthermore, factor XIIIa-crosslinking profiles analyzed by SDS-PAGE manifested several α・β- heteromultimers, not observed in the normal sample. To be noted is that the Aα-chain-linked serum albumin was crosslinked to the g-chain of another fibrin molecules, creating disordered fibrin clots. Scanning electron microscopy showed compact fibrin gels consisting of extremely thin but highly branched fibrin fibers. These findings seem to account for recurrent postoperativethrombo-embolic complications. Part of these results appeared in BLOOD (91 : 3282-3288, 1998) and the remainder is now in preparation for publication.