A New Type of Congenital Dysfibrinogen, Fibrinogen Bremen, with an Aα Gly-17 to Val Substitution Associated with Hemorrhagic Diathesis and Delayed Wound Healing
A New Type of Congenital Dysfibrinogen, Fibrinogen Bremen, with an Aα Gly-17 to Val Substitution Associated with Hemorrhagic Diathesis and Delayed Wound Healing
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一种新型先天性纤维蛋白原异常，纤维蛋白原 Bremen，Aα Gly-17 被 Val 取代，与出血素质和伤口愈合延迟相关
DOI：
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发表时间：
1993
影响因子：
6.7
通讯作者：
M. Matsuda
中科院分区：
文献类型：
--
作者：
Y. Wada;K. Niwa;Hisato Meakawa;S. Asakura;T. Sugo;M. Nakanishi;G. Auerswald;Manfred Popp;M. Matsuda
总结我们在先天性纤维蛋白原异常（纤维蛋白原不莱梅）中发现了一种新型的Aα Gly-17替换为瓦尔，该纤维蛋白原来源于一名15岁男孩，表现为易瘀伤和伤口愈合延迟。功能异常的特点是改变纤维蛋白单体聚合，这变得明显，通过增加盐浓度和pH值。合成四肽与正常纤维蛋白α链，Gly-Pro-Arg-Val的氨基末端片段的序列，基本上抑制正常和患者来源的纤维蛋白单体的聚合。具有Val-Pro-Arg-Val的不莱梅型序列的合成四肽在肽：纤维蛋白单体摩尔比为4，000：1时部分抑制患者的纤维蛋白单体的聚合，并且在10，000：1的高得多的比率时抑制正常的纤维蛋白单体的聚合。同样地，用另一种脂肪族氨基酸Ala取代Gly残基的合成肽Ala-Pro-Arg-Val类似地抑制患者的纤维蛋白单体聚合。因此，由氨基末端Gly的α-氨基和正常纤维蛋白α链3位Arg的胍基组成的假定的两叉插座样结构似乎在低离子强度和pH值下在突变型纤维蛋白α链中显著恢复，尽管氨基末端Gly被另一种脂肪族氨基酸瓦尔取代。
Summary We have identified a new type of Aα Gly-17 to Val substitution in a congenital dysfibrinogen, fibrinogen Bremen, derived from a 15-year-old boy having manifested easy bruising and delayed wound healing. The functional abnormality was characterized by altered fibrin monomer polymerization, which became evident by increasing the salt concentration and pH. A synthetic tetrapeptide with a sequence of the amino-terminal segment of normal fibrin α-chain, Gly-Pro-Arg-Val, substantially inhibited polymerization of both normal and the patient-derived fibrin monomers. A synthetic tetrapeptide with the Bremen type sequence of Val-Pro-Arg-Val inhibited polymerization of the patient’s fibrin monomers partially at a peptide: fibrin monomer molar ratio of 4,000:1, and that of normal one at a much higher ratio of 10,000:1. Likewise, a synthetic peptide Ala-Pro-Arg-Val with a replacement of the Gly residue by another aliphatic amino acid Ala inhibited similarly the patient’s fibrin monomer polymerization. Thus, the hypothetical two-pronged socket-like structure consisting of the α-amino group of the amino-terminal Gly and the guanidino group of an Arg at position 3 of the normal fibrin α-chain seems to be restored considerably in the mutant fibrin α-chain at low ionic strengths and pH’s, despite the replacement of the amino-terminal Gly by another aliphatic amino acid Val.
影响因子：
3.4
作者：
J. Weisel
通讯作者：
J. Weisel
人纤维蛋白原伽玛链中聚合和钙结合所必需的片段的定位。
影响因子：
2.9
作者：
Váradi,A;Scheraga,HA
通讯作者：
Scheraga,HA
人纤维蛋白结构 D 和 E 结构域中互补聚合位点之间的相互作用。
DOI：
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发表时间：
1992
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Ugarova,TP;Budzynski,AZ
通讯作者：
Budzynski,AZ