课题基金 / 基金详情

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

Molecular basis for the fibrinogen structure and functions - Analysls of hereditary dysfibrinogens and their application to the study
纤维蛋白原结构和功能的分子基础 - 遗传性异常纤维蛋白原的分析及其在研究中的应用
批准号:
10044316
负责人:
MATSUDA Michio
金额:
$1.15万
依托单位:
依托单位国家:
日本
项目类别:
Grant-in-Aid for international Scientific Research
财政年份:
1998
资助国家:
日本
项目状态:
已结题
起止时间:
1998 至 --

项目摘要

项目成果

MATSUDA Michio的其他基金

相似基金

相关文献

中文摘要
翻译
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 BβAsn-160 to Ser substitution with an extra oligosaccharide N-linked to BβAsn-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 a20-year-old woman who underwent a Caesarian section on her first delivery at the age of20.Severe bleeding and successive recurrent thrombo-embolic complications were characteristic。This molecule has a150-amino acid residue truncation of the Aα-chain,and is partly disulfide-bridged with serum albumin at AαCys-442。The Marburg fibrin clots are apparently fragile but totally resistant against plasmin Furthermore,factor XIIIa-crosslinking profiles analyzed by SDS-PAGE manifested severalα·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.
英文摘要
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.
期刊论文(0)
专著(0)
科研奖励(0)
会议论文
Sugo T, akamikawa C, Takebe M, Kohno I, Egbring R, Matsuda M: "The disulfide-linked albumin to the Marburg fibrinogen Aα-chain serves as substrate for factor XIIIa : Possible relevance to the resistance against plasmin of cross-linked fibrin"Blood. 91(9).
Sugo T、akamikawa C、Takebe M、Kohno I、Egbring R、Matsuda M:“马尔堡纤维蛋白原 Aα 链上的二硫键连接的白蛋白充当因子 XIIIa 的底物:可能与交联纤维蛋白的纤溶酶抗性相关“血。91(9)。
DOI: --
发表时间:
期刊:
影响因子: --
作者: []
通讯作者:
YANG, Wei: "Two-step spreading mode of human glioma cells on fibrin monomer : interaction of αVβ3 with the substratum followed by interaction of α5β1 with endogenous cellular fibronectin secreted in the extracellular matrix"Thromb. Res.. (in press.). (199
杨伟:“人胶质瘤细胞在纤维蛋白单体上的两步扩散模式:αVβ3与基质相互作用,然后α5β1与细胞外基质中分泌的内源性细胞纤连蛋白相互作用”《Thromb》。 (199
DOI: --
发表时间:
期刊:
影响因子: --
作者: []
通讯作者:
DOI: --
发表时间:
期刊:
影响因子: --
作者: []
通讯作者:
MADOIWA, Seiji: "Effect of carbohydrate side chain of tissue-type plasminogen activator on its interaction with plasminogen inhibitor-1"Fibrinolysis & Proteolysis. 12(1). 17-22 (1998)
MADOIWA,Seiji:“组织型纤溶酶原激活剂碳水化合物侧链对其与纤溶酶原抑制剂-1 相互作用的影响”纤维蛋白溶解
DOI: --
发表时间:
期刊:
影响因子: --
作者: []
通讯作者:
Molecular basis for the fibrinogen structure and functions-Analysis Of hereditary dysfibrinogens and their application to the study
  • 批准号:
    11694308
  • 项目类别:
    Grant-in-Aid for Scientific Research (B).
  • 资助金额:
    $2.11万
  • 财政年份:
    1999
  • 负责人:
    MATSUDA Michio
  • 依托单位:
STUDIES ON THE PATHOPHYSIOLOGY OF THROMBOEMBOLIC DISEASES WITH SPECIAL REFERENCE TO THE UNDERLYING IMPAIRED BLOOD COAGULATION AND ITS REGULATION
  • 批准号:
    11470250
  • 项目类别:
    Grant-in-Aid for Scientific Research (B).
  • 资助金额:
    $7.81万
  • 财政年份:
    1999
  • 负责人:
    MATSUDA Michio
  • 依托单位:
Molecular basis for the fibrinogen structure and functions-Analysis of hereditary dysfibrinogens and their application to the study
  • 批准号:
    09044329
  • 项目类别:
    Grant-in-Aid for international Scientific Research
  • 资助金额:
    $1.66万
  • 财政年份:
    1997
  • 负责人:
    MATSUDA Michio
  • 依托单位:
Etiology and pathophysiology of thrombosis : A molecular biological aproach to elucidate disturbed mechanisms of blood coagulation and its inhibition.
  • 批准号:
    08407034
  • 项目类别:
    Grant-in-Aid for Scientific Research (A)
  • 资助金额:
    $15.23万
  • 财政年份:
    1996
  • 负责人:
    MATSUDA Michio
  • 依托单位:
海外基金